Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures
Basic Information
Protein Name :  Serum albumin  

UniProtKB / Swiss-Prot ID :  ALBU_HUMAN

Gene Name (Synonyms) : 
ALBGIG20, GIG42, PRO0903, PRO1708, PRO2044, PRO2619, PRO2675,UNQ696/PRO1341  

Species :  Homo sapiens (Human). 

Subcellular Localization :  Secreted. 

Protein Function :  Serum albumin, the main protein of plasma, has a good binding capacity for water, Ca(2+), Na(+), K(+), fatty acids, hormones, bilirubin and drugs. Its main function is the regulation of the colloidal osmotic pressure of blood. Major zinc transporter in plasma, typically binds about 80% of all plasma zinc. 

Protein Sequence MKWVTFISLLFLFSSAYSRGVFRRDAHKSEVAHRFKDLGEENFKALVLIAFAQYLQQCPFEDHVKLVNEV...
Predicted Secondary Structure CHHHHHHHHHHHHHHHHHCCCCCCHHHHHHHHHHHHCCCHHHHHHHHHHHHHHHHCCCCHHHHHHHHHHH...
Protein Variant
LocationDescription
23R -> C (in Redhill/Malmo-I/Tradate;associated with T-344 in Redhill).
23R -> H (in Fukuoka-2/Lille/Taipei/Varese/Komagome-3).
24R -> L (in Jaffna). VAR_000501
24R -> P (in Takefu/Honolulu-1). VAR_000502
24R -> Q (in Christchurch/Honolulu-2). VAR_000503
25D -> V (in Bleinheim/Iowa city-2). VAR_000504
27H -> Q (in Nagasaki-3). VAR_000505
27H -> Y (in Larino). VAR_000506
73F -> Y. VAR_010657
84E -> K (in Torino). VAR_000507
87D -> N (in Malmo-95/Dalakarlia). VAR_000508
90L -> P (in FDH). VAR_013011
106E -> K (in Vibo Valentia). VAR_000509
121E -> G. VAR_014290
138R -> G (in Yanomama-2). VAR_000510
143E -> K (in Nagoya). VAR_000511
146V -> E (in Tregasio). VAR_013012
152H -> R (in Komagome-2). VAR_000512
201C -> F (in Hawkes bay). VAR_000513
215A -> T (in dbSNP:rs3210154). VAR_014291
215A -> V (in dbSNP:rs3204504). VAR_014292
220Q -> L (in dbSNP:rs3210163). VAR_014293
242R -> H (in FDH). VAR_000514
242R -> P (in FDH). VAR_013013
249K -> Q (in Tradate-2). VAR_000515
264K -> E (in Herborn). VAR_000516
292Q -> R (in Malmo-10). VAR_000517
293D -> G (in Nagasaki-1). VAR_000518
300K -> N (in Caserta). VAR_000519
337K -> N (in Canterbury/New Guinea/Tagliacozzo/Cuneo/Cooperstown).
338D -> G (in Bergamo). VAR_013014
338D -> V (in Brest). VAR_013015
342N -> K (in Malmo-47). VAR_000521
344A -> T (in Redhill; associated with C-23).
345E -> K (in Roma). VAR_000523
357E -> K (in Sondrio). VAR_000524
378E -> K (in Hiroshima-1). VAR_000525
382E -> K (in Coari I/Porto Alegre). VAR_000526
383K -> N (in Trieste). VAR_013016
389D -> H (in Parklands). VAR_000527
389D -> V (in Iowa city-1). VAR_000528
396K -> E (in Naskapi/Mersin/Komagome-1). VAR_000529
399D -> N (in Nagasaki-2). VAR_000530
400E -> K (in Tochigi). VAR_000531
400E -> Q (in Malmo-5). VAR_000532
406E -> K (in Hiroshima-2). VAR_000533
420E -> K. VAR_014294
434R -> C (in Liprizzi). VAR_013017
490K -> E (in dbSNP:rs1063469). VAR_014295
503E -> K (in Dublin). VAR_000534
518D -> N (in Casebrook). VAR_000535
525E -> K (in Manaus-1/Adana/Lambadi/Vancouver).
529E -> K (in Ortonovo). VAR_000537
557V -> M (in Maddaloni). VAR_013018
560K -> E (in Castel di Sangro). VAR_000538
565K -> E (in Maku). VAR_000539
574D -> A (in Malmo-61). VAR_000541
574D -> G (in Mexico). VAR_000540
584K -> E (in Church bay). VAR_013019
587D -> N (in Fukuoka-1/Paris-2). VAR_000542
589E -> K (in Osaka-1). VAR_000543
594E -> K (in Osaka-2/Phnom Phen/albumin B/Verona).
596GKKLVAASQAALGL -> PTMRIRERK (in Venezia). VAR_000547
597K -> E (in Gent/Milano Fast). VAR_000545
598K -> N (in Vanves). VAR_000546
599LVAASQAALGL -> TCCCKSSCLRLITSHLKASQPTMRIRERK (in Kenitra).
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Overview of Protein Modification Sites with Functional and Structural Information
Accessible Surface Area (ASA)
Pred. Secondary
Real Secondary
Disorder Prediction
Protein Domain
&
Experimental PTM Sites
Predicted PTM Sites
Protein Variant
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Experimental Post-Translational Modification Sites Download
Locations
Modification
Substrate Sites
&
Secondary Structure
Accessible Surface Area (%)
Resource
Reference
Structural Characterization
Orthologous
Protein Cluster
36N-linked (Glc) (glycation)AHRFKDLGE
HHHHHCCCH
52.58HPRD
Link
36N6-acetyllysineAHRFKDLGE
HHHHHCCCH
52.58HPRD
Link
75N-linked (Glc) (glycation); in vitro.TEFAKTCVA
HHHHHHHCC
48.02UniProtKB
Link
77S-cysteinyl 3-(oxidosulfanyl)alanine (Cys-Cys)FAKTCVADE
HHHHHCCCC
2.04HPRD
Link
82PhosphoserineVADESAENC
CCCCCCCCC
41.24HPRD
Link
82PhosphoserineVADESAENC
CCCCCCCCC
41.24Phosphositeplus
Link
82Phosphoserine.VADESAENC
CCCCCCCCC
41.24UniProtKB
Link
86S-cysteinyl 3-(oxidosulfanyl)alanine (Cys-Cys)SAENCDKSL
CCCCCCCCH
5.40HPRD
Link
97N6-acetyllysineLFGDKLCTV
HHHHHHHCC
45.93HPRD
Link
99S-cysteinyl 3-(oxidosulfanyl)alanine (Cys-Cys)GDKLCTVAT
HHHHHCCCC
3.37HPRD
Link
108PhosphotyrosineLRETYGEMA
CCCCCCCCH
13.31PhosphoELM
Link
108PhosphotyrosineLRETYGEMA
CCCCCCCCH
13.31Phosphositeplus
Link
108Phosphotyrosine.LRETYGEMA
CCCCCCCCH
13.31UniProtKB
Link
114S-cysteinyl 3-(oxidosulfanyl)alanine (Cys-Cys)EMADCCAKQ
CCHHHHCCC
1.44HPRD
Link
115S-cysteinyl 3-(oxidosulfanyl)alanine (Cys-Cys)MADCCAKQE
CHHHHCCCC
5.65HPRD
Link
117N6-acetyllysineDCCAKQEPE
HHHCCCCCH
41.08HPRD
Link
125S-cysteinyl 3-(oxidosulfanyl)alanine (Cys-Cys)ERNECFLQH
HHHHHHHHC
4.75HPRD
Link
130N6-acetyllysineFLQHKDDNP
HHHCCCCCC
54.54HPRD
Link
148S-cysteinyl 3-(oxidosulfanyl)alanine (Cys-Cys)VDVMCTAFH
HHHHHHHHH
2.20HPRD
Link
160N6-acetyllysineETFLKKYLY
HHHHHHHHH
34.87HPRD
Link
161N-linked (Glc) (glycation); in vitro.TFLKKYLYE
HHHHHHHHH
42.51UniProtKB
Link
161N6-acetyllysineTFLKKYLYE
HHHHHHHHH
42.51HPRD
Link
162PhosphotyrosineFLKKYLYEI
HHHHHHHHH
16.96HPRD
Link
162PhosphotyrosineFLKKYLYEI
HHHHHHHHH
16.96Phosphositeplus
Link
164PhosphotyrosineKKYLYEIAR
HHHHHHHHH
11.38HPRD
Link
164PhosphotyrosineKKYLYEIAR
HHHHHHHHH
11.38PhosphoELM
Link
164PhosphotyrosineKKYLYEIAR
HHHHHHHHH
11.38Phosphositeplus
Link
164Phosphotyrosine.KKYLYEIAR
HHHHHHHHH
11.38UniProtKB
Link
172PhosphotyrosineRRHPYFYAP
HHCCCCCHH
11.78Phosphositeplus
Link
174PhosphotyrosineHPYFYAPEL
CCCCCHHHH
18.53Phosphositeplus
Link
183N6-acetyllysineLFFAKRYKA
HHHHHHHHH
51.62HPRD
Link
186N-linked (Glc) (glycation); in vitro.AKRYKAAFT
HHHHHHHHH
36.95UniProtKB
Link
186N6-acetyllysineAKRYKAAFT
HHHHHHHHH
36.95HPRD
Link
192S-cysteinyl 3-(oxidosulfanyl)alanine (Cys-Cys)AFTECCQAA
HHHHHCCCC
1.57HPRD
Link
193S-cysteinyl 3-(oxidosulfanyl)alanine (Cys-Cys)FTECCQAAD
HHHHCCCCC
2.22HPRD
Link
198N6-acetyllysineQAADKAACL
CCCCHHHHH
32.91HPRD
Link
201S-cysteinyl 3-(oxidosulfanyl)alanine (Cys-Cys)DKAACLLPK
CHHHHHHHH
4.85HPRD
Link
223N-linked (Glc) (glycation)KQRLKCASL
HHHHHHHHH
29.91HPRD
Link
223N-linked (Glc) (glycation); in vitro.KQRLKCASL
HHHHHHHHH
29.91UniProtKB
Link
223N6-acetyllysineKQRLKCASL
HHHHHHHHH
29.91HPRD
Link
223N6-acetyllysineKQRLKCASL
HHHHHHHHH
29.91HPRD
Link
223N6-acetyllysineKQRLKCASL
HHHHHHHHH
29.91Phosphositeplus
Link
224S-cysteinyl 3-(oxidosulfanyl)alanine (Cys-Cys)QRLKCASLQ
HHHHHHHHH
3.53HPRD
Link
229Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)ASLQKFGER
HHHHHHCHH
61.71Phosphositeplus
Link
229N6-acetyllysineASLQKFGER
HHHHHHCHH
61.71HPRD
Link
236N6-acetyllysineERAFKAWAV
HHHHHHHHH
41.87HPRD
Link
249N-linked (Glc) (glycation); in vitro.QRFPKAEFA
HHCCCCCHH
58.81UniProtKB
Link
249N6-acetyllysineQRFPKAEFA
HHCCCCCHH
58.81HPRD
Link
257N-linked (Glc) (glycation)AEVSKLVTD
HHHHHHHHH
52.75HPRD
Link
257N6-acetyllysineAEVSKLVTD
HHHHHHHHH
52.75Phosphositeplus
Link
269S-cysteinyl 3-(oxidosulfanyl)alanine (Cys-Cys)VHTECCHGD
HHHHCCCCC
1.87HPRD
Link
270S-cysteinyl 3-(oxidosulfanyl)alanine (Cys-Cys)HTECCHGDL
HHHCCCCCH
3.06HPRD
Link
277S-cysteinyl 3-(oxidosulfanyl)alanine (Cys-Cys)DLLECADDR
CHHHHHHHH
5.19HPRD
Link
286N6-acetyllysineADLAKYICE
HHHHHHHHH
42.31HPRD
Link
289S-cysteinyl 3-(oxidosulfanyl)alanine (Cys-Cys)AKYICENQD
HHHHHHHHH
3.49HPRD
Link
294PhosphoserineENQDSISSK
HHHHHHHHH
18.01HPRD
Link
294Phosphoserine.ENQDSISSK
HHHHHHHHH
18.01UniProtKB
Link
297PhosphoserineDSISSKLKE
HHHHHHHHH
40.10HPRD
Link
297Phosphoserine.DSISSKLKE
HHHHHHHHH
40.10UniProtKB
Link
300N-linked (Glc) (glycation); in vitro.SSKLKECCE
HHHHHHHHC
53.06UniProtKB
Link
302S-cysteinyl 3-(oxidosulfanyl)alanine (Cys-Cys)KLKECCEKP
HHHHHHCCC
3.29HPRD
Link
303S-cysteinyl 3-(oxidosulfanyl)alanine (Cys-Cys)LKECCEKPL
HHHHHCCCC
8.70HPRD
Link
305N-linked (Glc) (glycation)ECCEKPLLE
HHHCCCCCC
27.35HPRD
Link
305N-linked (Glc) (glycation).ECCEKPLLE
HHHCCCCCC
27.35UniProtKB
Link
305N6-acetyllysineECCEKPLLE
HHHCCCCCC
27.35HPRD
Link
313S-cysteinyl 3-(oxidosulfanyl)alanine (Cys-Cys)EKSHCIAEV
CHHHHHHHC
3.99HPRD
Link
332noneSLAADFVES
CCCCCCCCC
42.38HPRD
Link
337N-linked (Glc) (glycation); in vitro.FVESKDVCK
CCCCHHHHC
40.45UniProtKB
Link
340S-cysteinyl 3-(oxidosulfanyl)alanine (Cys-Cys)SKDVCKNYA
CHHHHCCCC
3.20HPRD
Link
341N-linked (Glc) (glycation)KDVCKNYAE
HHHHCCCCC
53.49HPRD
Link
342N-linked (GlcNAc...); in variant Redhill./FTId=CAR_000226.DVCKNYAEA
HHHCCCCCC
35.80UniProtKB
Link
343PhosphotyrosineVCKNYAEAK
HHCCCCCCC
7.42Phosphositeplus
Link
347N-linked (Glc) (glycation); in vitro.YAEAKDVFL
CCCCCHHHH
46.02UniProtKB
Link
347N6-acetyllysineYAEAKDVFL
CCCCCHHHH
46.02HPRD
Link
365PhosphotyrosineRHPDYSVVL
HCCCCCHHH
14.07Phosphositeplus
Link
375N-linked (Glc) (glycation)LRLAKTYET
HHHHHHHHH
57.12HPRD
Link
375N6-acetyllysineLRLAKTYET
HHHHHHHHH
57.12HPRD
Link
377PhosphotyrosineLAKTYETTL
HHHHHHHHH
15.57Phosphositeplus
Link
384S-cysteinyl 3-(oxidosulfanyl)alanine (Cys-Cys)TLEKCCAAA
HHHHHHCCC
1.08HPRD
Link
385S-cysteinyl 3-(oxidosulfanyl)alanine (Cys-Cys)LEKCCAAAD
HHHHHCCCC
4.23HPRD
Link
393S-cysteinyl 3-(oxidosulfanyl)alanine (Cys-Cys)DPHECYAKV
CCHHHHHHH
3.49HPRD
Link
394PhosphotyrosinePHECYAKVF
CHHHHHHHH
13.38Phosphositeplus
Link
402N-linked (Glc) (glycation); in vitro.FDEFKPLVE
HHHHHHHHH
35.08UniProtKB
Link
402N6-acetyllysineFDEFKPLVE
HHHHHHHHH
35.08HPRD
Link
402N6-acetyllysineFDEFKPLVE
HHHHHHHHH
35.08Phosphositeplus
Link
416S-cysteinyl 3-(oxidosulfanyl)alanine (Cys-Cys)IKQNCELFE
HHHHHHHHH
4.44HPRD
Link
426N6-acetyllysineLGEYKFQNA
HCHHHHHHH
35.85HPRD
Link
437N-linked (Glc) (glycation); in vitro.VRYTKKVPQ
HHHHHHCCC
42.72UniProtKB
Link
437N6-acetyllysineVRYTKKVPQ
HHHHHHCCC
42.72HPRD
Link
438N6-acetyllysineRYTKKVPQV
HHHHHCCCC
51.88HPRD
Link
443PhosphoserineVPQVSTPTL
CCCCCCHHH
24.34Phosphositeplus
Link
443Phosphoserine.VPQVSTPTL
CCCCCCHHH
24.34UniProtKB
Link
444PhosphothreoninePQVSTPTLV
CCCCCHHHH
22.80Phosphositeplus
Link
444Phosphothreonine.PQVSTPTLV
CCCCCHHHH
22.80UniProtKB
Link
446PhosphothreonineVSTPTLVEV
CCCHHHHHH
43.45Phosphositeplus
Link
446Phosphothreonine.VSTPTLVEV
CCCHHHHHH
43.45UniProtKB
Link
447noneSTPTLVEVS
CCHHHHHHH
3.05HPRD
Link
461S-cysteinyl 3-(oxidosulfanyl)alanine (Cys-Cys)VGSKCCKHP
HHHHHCCCC
3.91HPRD
Link
462S-cysteinyl 3-(oxidosulfanyl)alanine (Cys-Cys)GSKCCKHPE
HHHHCCCCC
5.36HPRD
Link
463N-linked (Glc) (glycation)SKCCKHPEA
HHHCCCCCC
72.21HPRD
Link
463N-linked (Glc) (glycation).SKCCKHPEA
HHHCCCCCC
72.21UniProtKB
Link
468N-linked (Glc) (glycation); in vitro.HPEAKRMPC
CCCCCCCCC
47.79UniProtKB
Link
472S-cysteinyl 3-(oxidosulfanyl)alanine (Cys-Cys)KRMPCAEDY
CCCCCHHHH
4.78HPRD
Link
485S-cysteinyl 3-(oxidosulfanyl)alanine (Cys-Cys)LNQLCVLHE
HHHHHHHCC
1.89HPRD
Link
500S-cysteinyl 3-(oxidosulfanyl)alanine (Cys-Cys)RVTKCCTES
HHHHHHHHH
2.25HPRD
Link
501S-cysteinyl 3-(oxidosulfanyl)alanine (Cys-Cys)VTKCCTESL
HHHHHHHHH
5.15HPRD
Link
511S-cysteinyl 3-(oxidosulfanyl)alanine (Cys-Cys)NRRPCFSAL
HHHHHHHHC
3.90HPRD
Link
518N-linked (GlcNAc...); in variantALEVDETYV
HCCCCCCCC
32.90UniProtKB
Link
521PhosphotyrosineVDETYVPKE
CCCCCCCCC
16.83HPRD
Link
538S-cysteinyl 3-(oxidosulfanyl)alanine (Cys-Cys)HADICTLSE
CCHHCCCCH
3.01HPRD
Link
543N6-acetyllysineTLSEKERQI
CCCHHHHHH
55.62HPRD
Link
549N-linked (Glc) (glycation)RQIKKQTAL
HHHHHHHHH
55.28HPRD
Link
549N-linked (Glc) (glycation).RQIKKQTAL
HHHHHHHHH
55.28UniProtKB
Link
549N6-acetyllysineRQIKKQTAL
HHHHHHHHH
55.28HPRD
Link
558N-linked (Glc) (glycation)VELVKHKPK
HHHHHHCCC
59.54HPRD
Link
560N-linked (Glc) (glycation); in vitro.LVKHKPKAT
HHHHCCCCC
42.36UniProtKB
Link
565N6-acetyllysinePKATKEQLK
CCCCHHHHH
48.61HPRD
Link
569N-linked (Glc) (glycation); in vitro.KEQLKAVMD
HHHHHHHHH
38.33UniProtKB
Link
569N6-acetyllysineKEQLKAVMD
HHHHHHHHH
38.33HPRD
Link
581N6-acetyllysineAFVEKCCKA
HHHHHHHCC
39.36HPRD
Link
582S-cysteinyl 3-(oxidosulfanyl)alanine (Cys-Cys)FVEKCCKAD
HHHHHHCCC
1.50HPRD
Link
583S-cysteinyl 3-(oxidosulfanyl)alanine (Cys-Cys)VEKCCKADD
HHHHHCCCC
6.36HPRD
Link
591S-cysteinyl 3-(oxidosulfanyl)alanine (Cys-Cys)DKETCFAEE
CCCCCCCCC
2.97HPRD
Link
597N-linked (Glc) (glycation); in vitro.AEEGKKLVA
CCCCHHHHH
46.33UniProtKB
Link
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Protein-Protein Interactions
      Interacting Protein      
Interaction type
Source ID
      Resource      
      Pubmed ID      
Domain-Domain Interactions
ALBU_HUMANphysical interactionEBI-1224020
intact15174051
PF4V_HUMANphysical interactionEBI-1224020
intact15174051
CFAH_HUMANphysical interactionEBI-1224020
intact15174051
QTRD1_HUMANphysical interaction
physical interaction
EBI-1224020
EBI-1222961
intact15174051
15174051
GELS_HUMANphysical interactionEBI-1224020
intact15174051
CXCL7_HUMANphysical interactionEBI-1224020
intact15174051
FA7_HUMANphysical interactionEBI-1224020
intact15174051
CHKB_HUMANphysical interactionEBI-1224020
intact15174051
NOPE_HUMANphysical interactionEBI-1224020
intact15174051
TLN2_HUMANphysical interaction
physical interaction
physical interaction
EBI-1224020
EBI-1222961
EBI-1
intact15174051
15174051
15174051
FINC_HUMANphysical interaction
physical interaction
physical interaction
EBI-1224020
EBI-1223494
EBI-1
intact15174051
15174051
15174051
CO4A_HUMANphysical interactionEBI-1224020
intact15174051
F10A1_HUMANphysical interactionEBI-1224020
intact15174051
TIAM1_HUMANphysical interaction
physical interaction
EBI-1224020
EBI-1222961
intact15174051
15174051
CTGE5_HUMANphysical interactionEBI-1224020
intact15174051
OR3A2_HUMANphysical interactionEBI-1224020
intact15174051
K2C5_HUMANphysical interactionEBI-1224020
intact15174051
ASPG_HUMANphysical interactionEBI-1224020
intact15174051
ZN292_HUMANphysical interactionEBI-1224020
intact15174051
APOC2_HUMANphysical interactionEBI-1224020
intact15174051
APOA2_HUMANphysical interaction
physical interaction
EBI-1224020
EBI-1222961
intact15174051
15174051
FETUA_HUMANphysical interaction
physical interaction
EBI-1224020
EBI-1223494
intact15174051
15174051
ITIH1_HUMANphysical interactionEBI-1224020
intact15174051
TRY3_HUMANphysical interactionEBI-1224020
intact15174051
CFAB_HUMANphysical interactionEBI-1224020
intact15174051
GFAP_HUMANphysical interaction
physical interaction
EBI-1224020
EBI-1223494
intact15174051
15174051
DERL1_HUMANphysical interactionEBI-1224020
intact15174051
K2C6A_HUMANphysical interaction
physical interaction
EBI-1224020
EBI-1223494
intact15174051
15174051
APOC3_HUMANphysical interaction
physical interaction
physical interaction
EBI-1224020
EBI-1223494
EBI-1
intact15174051
15174051
15174051
AP1M1_HUMANphysical interactionEBI-1224020
intact15174051
K0232_HUMANphysical interactionEBI-1224020
intact15174051
Q8NHM4_HUMANphysical interactionEBI-1224020
intact15174051
K2C1_HUMANphysical interaction
physical interaction
physical interaction
physical interaction
EBI-1224020
EBI-1223494
EBI-1
intact15174051
15174051
15174051
15174051
NCOA3_HUMANphysical interactionEBI-1224020
intact15174051
SACS_HUMANphysical interactionEBI-1224020
intact15174051
K1C14_HUMANphysical interaction
physical interaction
EBI-1224020
EBI-1220884
intact15174051
15174051
F71E2_HUMANphysical interactionEBI-1224020
intact15174051
3BP5_HUMANphysical interactionEBI-1224020
intact15174051
APOA1_HUMANphysical interaction
physical interaction
physical interaction
physical interaction
EBI-1224020
EBI-1223494
EBI-1
intact15174051
15174051
15174051
15174051
TTHY_HUMANphysical interaction
physical interaction
physical interaction
EBI-1224020
EBI-1223494
EBI-1
intact15174051
15174051
15174051
K1C9_HUMANphysical interaction
physical interaction
physical interaction
EBI-1224020
EBI-1223494
EBI-1
intact15174051
15174051
15174051
RYR2_HUMANphysical interactionEBI-1224020
intact15174051
K1C13_HUMANphysical interactionEBI-1224020
intact15174051
CFAD_HUMANphysical interactionEBI-1224020
intact15174051
Q8IUP3_HUMANphysical interactionEBI-1224020
intact15174051
PHC3_HUMANphysical interactionEBI-1224020
intact15174051
DCD_HUMANphysical interactionEBI-1224020
intact15174051
AMPD3_HUMANphysical interactionEBI-1224020
intact15174051
ERF1_HUMANphysical interactionEBI-1224020
intact15174051
APOC1_HUMANphysical interaction
physical interaction
physical interaction
EBI-1224020
EBI-1222961
EBI-1
intact15174051
15174051
15174051
K1C10_HUMANphysical interaction
physical interaction
physical interaction
EBI-1224020
EBI-1222961
EBI-1
intact15174051
15174051
15174051
RBP2_HUMANphysical interactionEBI-1224020
intact15174051
APOA4_HUMANphysical interaction
physical interaction
physical interaction
EBI-1224020
EBI-1223494
EBI-1
intact15174051
15174051
15174051
K1C16_HUMANphysical interactionEBI-1224020
intact15174051
FIBA_HUMANphysical interaction
physical interaction
EBI-1224020
EBI-1220884
intact15174051
15174051
PCDH1_HUMANphysical interactionEBI-1224020
intact15174051
OR8D2_HUMANphysical interaction
physical interaction
EBI-1224020
EBI-1220884
intact15174051
15174051
K2C6B_HUMANphysical interactionEBI-1224020
intact15174051
CYTC_HUMANphysical interactionEBI-1224020
intact15174051
HEMO_HUMANphysical interactionEBI-1224020
intact15174051
IGHG1_HUMANphysical interaction
physical interaction
physical interaction
physical interaction
EBI-1224020
EBI-1223494
EBI-1
intact15174051
15174051
15174051
15174051
OBSL1_HUMANphysical interactionEBI-1224020
intact15174051
CT121_HUMANphysical interactionEBI-1223494
intact15174051
Q8N355_HUMANphysical interactionEBI-1223494
intact15174051
KAC_HUMANphysical interactionEBI-1223494
intact15174051
EXOC6_HUMANphysical interactionEBI-1223494
intact15174051
CRUM1_HUMANphysical interactionEBI-1223494
intact15174051
SETX_HUMANphysical interaction
physical interaction
physical interaction
EBI-1223494
EBI-1222961
EBI-1
intact15174051
15174051
15174051
KV201_HUMANphysical interaction
physical interaction
EBI-1223494
EBI-1220884
intact15174051
15174051
SFR19_HUMANphysical interactionEBI-1223494
intact15174051
ITB5_HUMANphysical interactionEBI-1223494
intact15174051
THRB_HUMANphysical interaction
physical interaction
EBI-1223494
EBI-1222961
intact15174051
15174051
Q8NCN1_HUMANphysical interactionEBI-1223494
intact15174051
IC1_HUMANphysical interactionEBI-1223494
intact15174051
APOE_HUMANphysical interactionEBI-1222961
intact15174051
CMTA1_HUMANphysical interactionEBI-1222961
intact15174051
Q9UQC9_HUMANphysical interactionEBI-1222961
intact15174051
LAT_HUMANphysical interactionEBI-1222961
intact15174051
SCN5A_HUMANphysical interactionEBI-1222961
intact15174051
CNOT1_HUMANphysical interactionEBI-1222961
intact15174051
CMC2_HUMANphysical interactionEBI-1222961
intact15174051
DMD_HUMANphysical interactionEBI-1222961
intact15174051
SPAST_HUMANphysical interactionEBI-1222961
intact15174051
MYLK3_HUMANphysical interactionEBI-1222961
intact15174051
TR150_HUMANphysical interactionEBI-1222961
intact15174051
DICER_HUMANphysical interactionEBI-1222961
intact15174051
TRY1_HUMANphysical interactionEBI-1222961
intact15174051
Q9H0L1_HUMANphysical interactionEBI-1222961
intact15174051
OCTC_HUMANphysical interactionEBI-1222961
intact15174051
DCC_HUMANphysical interactionEBI-1222961
intact15174051
SL9A8_HUMANphysical interactionEBI-1222961
intact15174051
K1712_HUMANphysical interactionEBI-1222961
intact15174051
PEG3_HUMANphysical interactionEBI-1222961
intact15174051
PALB2_HUMANphysical interactionEBI-1222961
intact15174051
CABL1_HUMANphysical interactionEBI-1222961
intact15174051
VINEX_HUMANphysical interactionEBI-1222961
intact15174051
Q96B20_HUMANphysical interactionEBI-1222961
intact15174051
CL035_HUMANphysical interactionEBI-1222961
intact15174051
DGKG_HUMANphysical interactionEBI-1222961
intact15174051
ITA2_HUMANphysical interactionEBI-1222961
intact15174051
TITIN_HUMANphysical interactionEBI-1222961
intact15174051
LDB3_HUMANphysical interactionEBI-1222961
intact15174051
RANB3_HUMANphysical interactionEBI-1222961
intact15174051
AAAT_HUMANphysical interactionEBI-1222961
intact15174051
SLAP2_HUMANphysical interactionEBI-1222961
intact15174051
GRAP2_HUMANphysical interactionEBI-1222961
intact15174051
F75A7_HUMANphysical interactionEBI-1222961
intact15174051
BBC3_HUMANphysical interactionEBI-1222961
intact15174051
AP4E1_HUMANphysical interactionEBI-1222961
intact15174051
PZRN4_HUMANphysical interactionEBI-1222961
intact15174051
MYL4_HUMANphysical interactionEBI-1222961
intact15174051
NPHN_HUMANphysical interactionEBI-1222961
intact15174051
GCN1L_HUMANphysical interactionEBI-1222961
intact15174051
JARD2_HUMANphysical interactionEBI-1222961
intact15174051
CDCP1_HUMANphysical interactionEBI-1220884
intact15174051
CATL1_HUMANphysical interactionEBI-1220884
intact15174051
PLAG1_HUMANphysical interactionEBI-1220884
intact15174051
ATM_HUMANphysical interactionEBI-1220884
intact15174051
HPT_HUMANphysical interactionEBI-1220884
intact15174051
CAC1I_HUMANphysical interactionEBI-1220884
intact15174051
CXG2_HUMANphysical interactionEBI-1220884
intact15174051
OR2T6_HUMANphysical interactionEBI-1220884
intact15174051
ADA1B_HUMANphysical interactionEBI-1220884
intact15174051
GABR1_HUMANphysical interactionEBI-1220884
intact15174051
RLF_HUMANphysical interactionEBI-1220884
intact15174051
DDB1_HUMANphysical interactionEBI-1220884
intact15174051
IGHG2_HUMANphysical interactionEBI-1220884
intact15174051
ZN232_HUMANphysical interactionEBI-1220884
intact15174051
KCMA1_HUMANphysical interactionEBI-1220884
intact15174051
KLK3_HUMANphysical interactionEBI-1220884
intact15174051
PDE4B_HUMANphysical interactionEBI-1220884
intact15174051
CC45L_HUMANphysical interactionEBI-1220884
intact15174051
LC7L2_HUMANphysical interactionEBI-731176
intact16169070
LC7L2_HUMANyeast 2-hybridHPRD:00062HPRD16169070
NTCP_HUMANENSP00000295897STRING
NTCP_HUMANENSP00000295897STRING
FCGRN_HUMANENSP00000295897STRING
FCGRN_HUMANENSP00000295897STRING
CD79A_HUMANENSP00000295897STRING
CD79A_HUMANENSP00000295897STRING
CD79A_HUMANENSP00000295897STRING
CD79A_HUMANENSP00000295897STRING
SIAL_HUMANENSP00000295897STRING
SIAL_HUMANENSP00000295897STRING
TTHY_HUMANENSP00000295897STRING
TTHY_HUMANENSP00000295897STRING
OPSB_HUMANENSP00000295897STRING
OPSB_HUMANENSP00000295897STRING
INS_HUMANENSP00000295897STRING
INS_HUMANENSP00000295897STRING
INS_HUMANENSP00000295897STRING
INS_HUMANENSP00000295897STRING
APOE_HUMANENSP00000295897STRING
APOE_HUMANENSP00000295897STRING
SO1B1_HUMANENSP00000295897STRING
SO1B1_HUMANENSP00000295897STRING
HNF1A_HUMANENSP00000295897STRING
HNF1A_HUMANENSP00000295897STRING
SO1B3_HUMANENSP00000295897STRING
SO1B3_HUMANENSP00000295897STRING
LRP2_HUMANENSP00000295897STRING
LRP2_HUMANENSP00000295897STRING
TRFE_HUMANENSP00000295897STRING
TRFE_HUMANENSP00000295897STRING
RB_HUMANENSP00000295897STRING
RB_HUMANENSP00000295897STRING
PTHY_HUMANENSP00000295897STRING
PTHY_HUMANENSP00000295897STRING
MRP3_HUMANENSP00000295897STRING
MRP3_HUMANENSP00000295897STRING
IL8_HUMANENSP00000295897STRING
IL8_HUMANENSP00000295897STRING
FABP6_HUMANENSP00000295897STRING
FABP6_HUMANENSP00000295897STRING
VEGFA_HUMANENSP00000295897STRING
VEGFA_HUMANENSP00000295897STRING
A1AT_HUMANENSP00000295897STRING
A1AT_HUMANENSP00000295897STRING
A1AT_HUMANENSP00000295897STRING
A1AT_HUMANENSP00000295897STRING
A1AT_HUMANENSP00000295897STRING
A1AT_HUMANENSP00000295897STRING
A1AT_HUMANENSP00000295897STRING
A1AT_HUMANENSP00000295897STRING
A1AT_HUMANENSP00000295897STRING
A1AT_HUMANENSP00000295897STRING
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Disease Reference
Kegg disease
OMIM disease
615999Hyperthyroxinemia, familial dysalbuminemic (FDAH)
616000Analbuminemia (ANALBA)
Drug Reference
There are no disease associations of PTM sites.
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Related Literatures of Post-Translational Modification
N-linked Glycosylation
ReferencePubMed
"Enzymatic digestion and mass spectrometry in the study of advancedglycation end products/peptides.";
Lapolla A., Fedele D., Reitano R., Arico N.C., Seraglia R., Traldi P.,Marotta E., Tonani R.;
J. Am. Soc. Mass Spectrom. 15:496-509(2004).
Cited for: PROTEIN SEQUENCE OF 250-264, GLYCATION AT LYS-75; LYS-161; LYS-186;LYS-249; LYS-257; LYS-300; LYS-337; LYS-347; LYS-375; LYS-402;LYS-437; LYS-468; LYS-560; LYS-549; LYS-569 AND LYS-597, LACK OFGLYCATION AT LYS-28; LYS-44; LYS-65; LYS-88; LYS-97; LYS-117; LYS-130;LYS-160; LYS-183; LYS-198; LYS-205; LYS-214; LYS-219; LYS-229;LYS-236; LYS-264; LYS-286; LYS-298; LYS-310; LYS-383; LYS-396;LYS-413; LYS-426; LYS-438; LYS-456; LYS-460; LYS-490; LYS-499;LYS-524; LYS-543; LYS-548; LYS-562; LYS-565; LYS-581; LYS-584; LYS-588AND LYS-598, AND MASS SPECTROMETRY.
"The principal site of nonenzymatic glycosylation of human serumalbumin in vivo.";
Garlick R.L., Mazer J.S.;
J. Biol. Chem. 258:6142-6146(1983).
Cited for: GLYCATION AT LYS-223 AND LYS-549.
"Nonenzymatic glycosylation of human serum albumin alters itsconformation and function.";
Shaklai N., Garlick R.L., Bunn H.F.;
J. Biol. Chem. 259:3812-3817(1984).
Cited for: GLYCATION AT LYS-549.
"Nonenzymatic glycosylation of albumin in vivo. Identification ofmultiple glycosylated sites.";
Iberg N., Fluckiger R.;
J. Biol. Chem. 261:13542-13545(1986).
Cited for: GLYCATION AT LYS-36; LYS-223; LYS-257; LYS-305; LYS-341; LYS-375;LYS-463; LYS-549 AND LYS-558.
Phosphorylation
ReferencePubMed
"Global survey of phosphotyrosine signaling identifies oncogenickinases in lung cancer.";
Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J.,Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L.,Mitchell J., Wetzel R., Macneill J., Ren J.M., Yuan J.,Bakalarski C.E., Villen J., Kornhauser J.M., Smith B., Li D., Zhou X.,Gygi S.P., Gu T.-L., Polakiewicz R.D., Rush J., Comb M.J.;
Cell 131:1190-1203(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-108 AND TYR-164, ANDMASS SPECTROMETRY.
"Large-scale phosphoproteome analysis of human liver tissue byenrichment and fractionation of phosphopeptides with strong anionexchange chromatography.";
Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D.,Zou H., Gu J.;
Proteomics 8:1346-1361(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-82, AND MASSSPECTROMETRY.
"An initial characterization of the serum phosphoproteome.";
Zhou W., Ross M.M., Tessitore A., Ornstein D., Vanmeter A.,Liotta L.A., Petricoin E.F. III;
J. Proteome Res. 8:5523-5531(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-294 AND SER-297, TISSUESPECIFICITY, AND MASS SPECTROMETRY.
"An extensive survey of tyrosine phosphorylation revealing new sitesin human mammary epithelial cells.";
Heibeck T.H., Ding S.-J., Opresko L.K., Zhao R., Schepmoes A.A.,Yang F., Tolmachev A.V., Monroe M.E., Camp D.G. II, Smith R.D.,Wiley H.S., Qian W.-J.;
J. Proteome Res. 8:3852-3861(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-164, AND MASSSPECTROMETRY.
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions.";
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.;
Sci. Signal. 2:RA46-RA46(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-443; THR-444 ANDTHR-446, AND MASS SPECTROMETRY.
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Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures