Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures
Basic Information
Protein Name :  Nuclear pore complex protein Nup153  

UniProtKB / Swiss-Prot ID :  NU153_HUMAN

Gene Name (Synonyms) : 
NUP153  

Species :  Homo sapiens (Human). 

Subcellular Localization :  Nucleus, nuclear pore complex. Note=Located to the terminal ring structure of the nucleoplasmic cage. Tightly associated with the nuclear membrane and lamina (By similarity). 

Protein Function :  Possible DNA-binding subunit of the nuclear pore complex (NPC). The repeat-containing domain may be involved in anchoring components of the pore complex to the pore membrane. 

Protein Sequence MASGAGGVGGGGGGKIRTRRCHQGPIKPYQQGRQQHQGILSRVTESVKNIVPGWLQRYFNKNEDVCSCST...
Predicted Secondary Structure CCCCCCCCCCCCCCCEEEEECCCCCCCHHHHCCHHHHHHHHHHHHHHHHHHHHHHHHHHCCCCCEEEECC...
Protein Variant
LocationDescription
90D -> N (in dbSNP:rs16879902). VAR_046554
248I -> V (in dbSNP:rs2228375). VAR_046555
402N -> K (in dbSNP:rs6906499). VAR_046556
821P -> L (in dbSNP:rs6905654). VAR_046557
827A -> T (in dbSNP:rs2274136). VAR_046558
1388T -> A (in dbSNP:rs45475293). VAR_046559
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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
2N-acetylalanine.---MASGAG
---CCCCCC
28.16UniProtKB
Link-
3Phosphoserine--MASGAGG
--CCCCCCC
40.82HPRD
Link-
3Phosphoserine--MASGAGG
--CCCCCCC
40.82Phosphositeplus
Link-
18PhosphothreonineGKIRTRRCH
CCEEEEECC
26.41HPRD
Link-
48Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)TESVKNIVP
HHHHHHHHH
50.68Phosphositeplus
Link-
93PhosphoserineADEESSNIT
EECCCCCCC
27.00HPRD
Link-
93PhosphoserineADEESSNIT
EECCCCCCC
27.00SysPTM
Link-
102PhosphothreonineDGRITPEPA
CCEECCCCC
21.90HPRD
Link-
102PhosphothreonineDGRITPEPA
CCEECCCCC
21.90Phosphositeplus
Link-
110PhosphothreonineAVSNTEEPS
CCCCCCCCC
33.93HPRD
Link-
110PhosphothreonineAVSNTEEPS
CCCCCCCCC
33.93SysPTM
Link-
115PhosphothreonineEEPSTTSTA
CCCCCCCCC
35.17HPRD
Link-
115PhosphothreonineEEPSTTSTA
CCCCCCCCC
35.17SysPTM
Link-
116PhosphothreonineEPSTTSTAS
CCCCCCCCC
28.55HPRD
Link-
116PhosphothreonineEPSTTSTAS
CCCCCCCCC
28.55SysPTM
Link-
117PhosphoserinePSTTSTASN
CCCCCCCCC
23.28HPRD
Link-
117PhosphoserinePSTTSTASN
CCCCCCCCC
23.28SysPTM
Link-
118PhosphothreonineSTTSTASNY
CCCCCCCCC
31.82HPRD
Link-
118PhosphothreonineSTTSTASNY
CCCCCCCCC
31.82SysPTM
Link-
120PhosphoserineTSTASNYPD
CCCCCCCCH
36.66HPRD
Link-
120PhosphoserineTSTASNYPD
CCCCCCCCH
36.66SysPTM
Link-
122PhosphotyrosineTASNYPDVL
CCCCCCHHH
9.79HPRD
Link-
122PhosphotyrosineTASNYPDVL
CCCCCCHHH
9.79SysPTM
Link-
130PhosphoserineLTRPSLHRS
HCCCCHHHH
33.25HPRD
Link-
130PhosphoserineLTRPSLHRS
HCCCCHHHH
33.25SysPTM
Link-
172PhosphoserineEIKDSTSQH
HHHHHHHCC
25.59HPRD
Link-
173PhosphothreonineIKDSTSQHD
HHHHHHCCC
42.41HPRD
Link-
174PhosphoserineKDSTSQHDD
HHHHHCCCC
29.48HPRD
Link-
182PhosphoserineDDNISTTSG
CCCCCCCCC
31.70HPRD
Link-
182PhosphoserineDDNISTTSG
CCCCCCCCC
31.70Phosphositeplus
Link-
188PhosphoserineTSGFSSRAS
CCCCCCCCC
23.57Phosphositeplus
Link-
189PhosphoserineSGFSSRASD
CCCCCCCCC
29.60Phosphositeplus
Link-
192PhosphoserineSSRASDKDI
CCCCCCCCE
44.05HPRD
Link-
192PhosphoserineSSRASDKDI
CCCCCCCCE
44.05Phosphositeplus
Link-
192PhosphoserineSSRASDKDI
CCCCCCCCE
44.05SysPTM
Link-
200Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)ITVSKNTSL
EEEECCCCC
60.97Phosphositeplus
Link-
202PhosphothreonineVSKNTSLPP
EECCCCCCC
35.06HPRD
Link-
203PhosphoserineSKNTSLPPL
ECCCCCCCC
48.55HPRD
Link-
203PhosphoserineSKNTSLPPL
ECCCCCCCC
48.55PhosphoELM
Link-
203PhosphoserineSKNTSLPPL
ECCCCCCCC
48.55Phosphositeplus
Link-
209PhosphoserinePPLWSPEAE
CCCCCCCCH
22.12HPRD
Link-
209PhosphoserinePPLWSPEAE
CCCCCCCCH
22.12PhosphoELM
Link-
209PhosphoserinePPLWSPEAE
CCCCCCCCH
22.12Phosphositeplus
Link-
209PhosphoserinePPLWSPEAE
CCCCCCCCH
22.12SysPTM
Link-
209Phosphoserine.PPLWSPEAE
CCCCCCCCH
22.12UniProtKB
Link-
217PhosphoserineERSHSLSQH
HHHHHHHHH
30.84HPRD
Link-
217PhosphoserineERSHSLSQH
HHHHHHHHH
30.84Phosphositeplus
Link-
219PhosphoserineSHSLSQHTA
HHHHHHHHC
23.95HPRD
Link-
219PhosphoserineSHSLSQHTA
HHHHHHHHC
23.95PhosphoELM
Link-
219PhosphoserineSHSLSQHTA
HHHHHHHHC
23.95Phosphositeplus
Link-
224PhosphothreonineQHTATSSKK
HHHCCCCCC
34.39HPRD
Link-
224PhosphothreonineQHTATSSKK
HHHCCCCCC
34.39PhosphoELM
Link-
225PhosphoserineHTATSSKKP
HHCCCCCCC
37.38HPRD
Link-
238PhosphothreonineSAFGTLSPS
EECCCCCCC
20.01HPRD
Link-
238PhosphothreonineSAFGTLSPS
EECCCCCCC
20.01SysPTM
Link-
240PhosphoserineFGTLSPSLG
CCCCCCCCC
16.57HPRD
Link-
240PhosphoserineFGTLSPSLG
CCCCCCCCC
16.57PhosphoELM
Link-
240PhosphoserineFGTLSPSLG
CCCCCCCCC
16.57Phosphositeplus
Link-
240PhosphoserineFGTLSPSLG
CCCCCCCCC
16.57SysPTM
Link-
240Phosphoserine.FGTLSPSLG
CCCCCCCCC
16.57UniProtKB
Link-
242PhosphoserineTLSPSLGNS
CCCCCCCCC
45.60PhosphoELM
Link-
257PhosphoserineQLGDSPFYP
HCCCCCCCC
18.34HPRD
Link-
257PhosphoserineQLGDSPFYP
HCCCCCCCC
18.34PhosphoELM
Link-
257PhosphoserineQLGDSPFYP
HCCCCCCCC
18.34Phosphositeplus
Link-
257PhosphoserineQLGDSPFYP
HCCCCCCCC
18.34SysPTM
Link-
257Phosphoserine.QLGDSPFYP
HCCCCCCCC
18.34UniProtKB
Link-
260PhosphotyrosineDSPFYPGKT
CCCCCCCCC
17.92Phosphositeplus
Link-
260Phosphotyrosine.DSPFYPGKT
CCCCCCCCC
17.92UniProtKB
Link-
263Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)FYPGKTTYG
CCCCCCCCC
32.94Phosphositeplus
Link-
281PhosphothreonineKLRNTPYQA
HHHCCCCCC
19.55PhosphoELM
Link-
281PhosphothreonineKLRNTPYQA
HHHCCCCCC
19.55Phosphositeplus
Link-
281Phosphothreonine.KLRNTPYQA
HHHCCCCCC
19.55UniProtKB
Link-
304PhosphothreonineSYGVTSSTA
HCCCCCHHH
16.76HPRD
Link-
306PhosphoserineGVTSSTARR
CCCCHHHHH
19.40HPRD
Link-
307PhosphothreonineVTSSTARRI
CCCHHHHHH
24.77HPRD
Link-
317Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)QSLEKMSSP
HHHHHHHCC
49.75Phosphositeplus
Link-
319PhosphoserineLEKMSSPLA
HHHHHCCCC
39.61HPRD
Link-
320PhosphoserineEKMSSPLAD
HHHHCCCCC
22.04HPRD
Link-
320PhosphoserineEKMSSPLAD
HHHHCCCCC
22.04Phosphositeplus
Link-
320Phosphoserine.EKMSSPLAD
HHHHCCCCC
22.04UniProtKB
Link-
330PhosphoserineKRIPSIVSS
CCCHHHHHC
33.00HPRD
Link-
330PhosphoserineKRIPSIVSS
CCCHHHHHC
33.00PhosphoELM
Link-
330PhosphoserineKRIPSIVSS
CCCHHHHHC
33.00Phosphositeplus
Link-
330PhosphoserineKRIPSIVSS
CCCHHHHHC
33.00SysPTM
Link-
330Phosphoserine.KRIPSIVSS
CCCHHHHHC
33.00UniProtKB
Link-
333PhosphoserinePSIVSSPLN
HHHHHCCCC
25.27HPRD
Link-
333PhosphoserinePSIVSSPLN
HHHHHCCCC
25.27PhosphoELM
Link-
333PhosphoserinePSIVSSPLN
HHHHHCCCC
25.27Phosphositeplus
Link-
334PhosphoserineSIVSSPLNS
HHHHCCCCC
23.63HPRD
Link-
334PhosphoserineSIVSSPLNS
HHHHCCCCC
23.63PhosphoELM
Link-
334PhosphoserineSIVSSPLNS
HHHHCCCCC
23.63Phosphositeplus
Link-
334PhosphoserineSIVSSPLNS
HHHHCCCCC
23.63SysPTM
Link-
334Phosphoserine.SIVSSPLNS
HHHHCCCCC
23.63UniProtKB
Link-
338PhosphoserineSPLNSPLDR
CCCCCCCCC
34.23HPRD
Link-
338PhosphoserineSPLNSPLDR
CCCCCCCCC
34.23PhosphoELM
Link-
338PhosphoserineSPLNSPLDR
CCCCCCCCC
34.23Phosphositeplus
Link-
338PhosphoserineSPLNSPLDR
CCCCCCCCC
34.23SysPTM
Link-
338Phosphoserine.SPLNSPLDR
CCCCCCCCC
34.23UniProtKB
Link-
343PhosphoserinePLDRSGIDI
CCCCCCCCC
39.50HPRD
Link-
343PhosphoserinePLDRSGIDI
CCCCCCCCC
39.50PhosphoELM
Link-
343PhosphoserinePLDRSGIDI
CCCCCCCCC
39.50Phosphositeplus
Link-
343PhosphoserinePLDRSGIDI
CCCCCCCCC
39.50SysPTM
Link-
343Phosphoserine.PLDRSGIDI
CCCCCCCCC
39.50UniProtKB
Link-
348PhosphothreonineGIDITDFQA
CCCCEECCH
27.32Phosphositeplus
Link-
369PhosphothreonineQRLMTPKPV
HHHCCCCCC
32.52HPRD
Link-
369PhosphothreonineQRLMTPKPV
HHHCCCCCC
32.52PhosphoELM
Link-
369PhosphothreonineQRLMTPKPV
HHHCCCCCC
32.52Phosphositeplus
Link-
369PhosphothreonineQRLMTPKPV
HHHCCCCCC
32.52SysPTM
Link-
369Phosphothreonine.QRLMTPKPV
HHHCCCCCC
32.52UniProtKB
Link-
377PhosphothreonineVSIATNRSV
CEEEECCEE
29.51HPRD
Link-
384Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)SVYFKPSLT
EEEECCCCC
18.93Phosphositeplus
Link-
384N6-acetyllysineSVYFKPSLT
EEEECCCCC
18.93HPRD
Link-
384N6-acetyllysineSVYFKPSLT
EEEECCCCC
18.93Phosphositeplus
Link-
384N6-acetyllysine.SVYFKPSLT
EEEECCCCC
18.93UniProtKB
Link-
386PhosphoserineYFKPSLTPS
EECCCCCCC
45.53Phosphositeplus
Link-
388PhosphothreonineKPSLTPSGE
CCCCCCCCC
21.53HPRD
Link-
388PhosphothreonineKPSLTPSGE
CCCCCCCCC
21.53PhosphoELM
Link-
388PhosphothreonineKPSLTPSGE
CCCCCCCCC
21.53Phosphositeplus
Link-
413PhosphothreonineEKNMTPGQN
CCCCCCCCC
33.39Phosphositeplus
Link-
460Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)FVASKPLEE
CCCCCCCCH
43.83Phosphositeplus
Link-
490PhosphoserineTFNFSSPEI
CCCCCCCCE
46.19HPRD
Link-
491PhosphoserineFNFSSPEIT
CCCCCCCEE
23.55HPRD
Link-
498PhosphoserineITTSSPSPI
EECCCCCCC
27.57HPRD
Link-
500PhosphoserineTSSPSPINS
CCCCCCCCC
40.12HPRD
Link-
500PhosphoserineTSSPSPINS
CCCCCCCCC
40.12Phosphositeplus
Link-
515PhosphothreonineKVQMTSPSS
CEEEECCCC
22.01HPRD
Link-
515PhosphothreonineKVQMTSPSS
CEEEECCCC
22.01PhosphoELM
Link-
515PhosphothreonineKVQMTSPSS
CEEEECCCC
22.01Phosphositeplus
Link-
516PhosphoserineVQMTSPSST
EEEECCCCC
19.90HPRD
Link-
516PhosphoserineVQMTSPSST
EEEECCCCC
19.90PhosphoELM
Link-
516PhosphoserineVQMTSPSST
EEEECCCCC
19.90Phosphositeplus
Link-
516PhosphoserineVQMTSPSST
EEEECCCCC
19.90SysPTM
Link-
516Phosphoserine.VQMTSPSST
EEEECCCCC
19.90UniProtKB
Link-
518PhosphoserineMTSPSSTGS
EECCCCCCC
40.06HPRD
Link-
518PhosphoserineMTSPSSTGS
EECCCCCCC
40.06PhosphoELM
Link-
518PhosphoserineMTSPSSTGS
EECCCCCCC
40.06Phosphositeplus
Link-
518PhosphoserineMTSPSSTGS
EECCCCCCC
40.06SysPTM
Link-
518Phosphoserine.MTSPSSTGS
EECCCCCCC
40.06UniProtKB
Link-
519PhosphoserineTSPSSTGSP
ECCCCCCCC
39.92HPRD
Link-
519PhosphoserineTSPSSTGSP
ECCCCCCCC
39.92PhosphoELM
Link-
519PhosphoserineTSPSSTGSP
ECCCCCCCC
39.92Phosphositeplus
Link-
519PhosphoserineTSPSSTGSP
ECCCCCCCC
39.92SysPTM
Link-
520PhosphothreonineSPSSTGSPM
CCCCCCCCC
46.12HPRD
Link-
520PhosphothreonineSPSSTGSPM
CCCCCCCCC
46.12PhosphoELM
Link-
520PhosphothreonineSPSSTGSPM
CCCCCCCCC
46.12Phosphositeplus
Link-
522PhosphoserineSSTGSPMFK
CCCCCCCEE
17.18HPRD
Link-
522PhosphoserineSSTGSPMFK
CCCCCCCEE
17.18PhosphoELM
Link-
522PhosphoserineSSTGSPMFK
CCCCCCCEE
17.18Phosphositeplus
Link-
522PhosphoserineSSTGSPMFK
CCCCCCCEE
17.18SysPTM
Link-
522Phosphoserine.SSTGSPMFK
CCCCCCCEE
17.18UniProtKB
Link-
529PhosphoserineFKFSSPIVK
EEECCCEEE
23.06HPRD
Link-
529PhosphoserineFKFSSPIVK
EEECCCEEE
23.06PhosphoELM
Link-
529PhosphoserineFKFSSPIVK
EEECCCEEE
23.06Phosphositeplus
Link-
529PhosphoserineFKFSSPIVK
EEECCCEEE
23.06SysPTM
Link-
529Phosphoserine.FKFSSPIVK
EEECCCEEE
23.06UniProtKB
Link-
534O-linked (GalNAc...)PIVKSTEAN
CEEECCCCC
22.15HPRD
Link-
534O-linked (GlcNAc)PIVKSTEAN
CEEECCCCC
22.15Phosphositeplus
Link-
544O-linked (GalNAc...)LPPSSIGFT
CCCCCCCCC
32.29HPRD
Link-
544O-linked (GlcNAc)LPPSSIGFT
CCCCCCCCC
32.29Phosphositeplus
Link-
588PhosphothreonineNCKKTPPED
HHCCCCCCC
29.57HPRD
Link-
588PhosphothreonineNCKKTPPED
HHCCCCCCC
29.57PhosphoELM
Link-
588PhosphothreonineNCKKTPPED
HHCCCCCCC
29.57Phosphositeplus
Link-
588PhosphothreonineNCKKTPPED
HHCCCCCCC
29.57SysPTM
Link-
588Phosphothreonine.NCKKTPPED
HHCCCCCCC
29.57UniProtKB
Link-
607PhosphoserineLKEGSVLDI
HCCCCCCCC
22.16Phosphositeplus
Link-
613Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)LDILKSPGF
CCCCCCCCC
55.74Phosphositeplus
Link-
614PhosphoserineDILKSPGFA
CCCCCCCCC
27.15HPRD
Link-
614PhosphoserineDILKSPGFA
CCCCCCCCC
27.15PhosphoELM
Link-
614PhosphoserineDILKSPGFA
CCCCCCCCC
27.15Phosphositeplus
Link-
614PhosphoserineDILKSPGFA
CCCCCCCCC
27.15SysPTM
Link-
614Phosphoserine.DILKSPGFA
CCCCCCCCC
27.15UniProtKB
Link-
619PhosphoserinePGFASPKID
CCCCCCCCC
25.19HPRD
Link-
619PhosphoserinePGFASPKID
CCCCCCCCC
25.19PhosphoELM
Link-
619PhosphoserinePGFASPKID
CCCCCCCCC
25.19Phosphositeplus
Link-
619PhosphoserinePGFASPKID
CCCCCCCCC
25.19SysPTM
Link-
619Phosphoserine.PGFASPKID
CCCCCCCCC
25.19UniProtKB
Link-
632PhosphothreonineQPTATSPVV
CCCCCCCCC
35.72HPRD
Link-
632PhosphothreonineQPTATSPVV
CCCCCCCCC
35.72Phosphositeplus
Link-
633PhosphoserinePTATSPVVY
CCCCCCCCE
17.15HPRD
Link-
633PhosphoserinePTATSPVVY
CCCCCCCCE
17.15PhosphoELM
Link-
633PhosphoserinePTATSPVVY
CCCCCCCCE
17.15Phosphositeplus
Link-
633Phosphoserine.PTATSPVVY
CCCCCCCCE
17.15UniProtKB
Link-
687PhosphoserineAAKLSPRDT
CCCCCCCCC
19.72HPRD
Link-
687PhosphoserineAAKLSPRDT
CCCCCCCCC
19.72PhosphoELM
Link-
687PhosphoserineAAKLSPRDT
CCCCCCCCC
19.72Phosphositeplus
Link-
687PhosphoserineAAKLSPRDT
CCCCCCCCC
19.72SysPTM
Link-
687Phosphoserine.AAKLSPRDT
CCCCCCCCC
19.72UniProtKB
Link-
695PhosphothreonineTAKQTGIET
CCCCCCCCC
39.15HPRD
Link-
699PhosphothreonineTGIETPNKS
CCCCCCCCC
30.18HPRD
Link-
699PhosphothreonineTGIETPNKS
CCCCCCCCC
30.18Phosphositeplus
Link-
718N6-acetyllysineGFGDKFKPV
CCCEECCCC
56.52HPRD
Link-
718N6-acetyllysineGFGDKFKPV
CCCEECCCC
56.52Phosphositeplus
Link-
718N6-acetyllysine.GFGDKFKPV
CCCEECCCC
56.52UniProtKB
Link-
886Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)KSGFKGFDT
CCCCCCCCC
63.29Phosphositeplus
Link-
908O-linked (GalNAc...)KFGVSSSSS
CCCCCCCCC
25.53HPRD
Link-
908O-linked (GlcNAc)KFGVSSSSS
CCCCCCCCC
25.53Phosphositeplus
Link-
909O-linked (GalNAc...)FGVSSSSSG
CCCCCCCCC
31.65HPRD
Link-
909O-linked (GlcNAc)FGVSSSSSG
CCCCCCCCC
31.65Phosphositeplus
Link-
925Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)TGNFKFGDQ
CCCCCCCCC
53.06Phosphositeplus
Link-
954Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)FKFSKPIGD
CCCCCCCCC
43.73Phosphositeplus
Link-
954N6-acetyllysineFKFSKPIGD
CCCCCCCCC
43.73HPRD
Link-
954N6-acetyllysineFKFSKPIGD
CCCCCCCCC
43.73Phosphositeplus
Link-
954N6-acetyllysine.FKFSKPIGD
CCCCCCCCC
43.73UniProtKB
Link-
960Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)IGDFKFGVS
CCCEECCCC
46.04Phosphositeplus
Link-
968Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)SSESKPEEV
CCCCCCCCC
53.01Phosphositeplus
Link-
973Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)PEEVKKDSK
CCCCCCCCC
54.89Phosphositeplus
Link-
982Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)NDNFKFGLS
CCCCCCCCC
44.79Phosphositeplus
Link-
1010Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)GQEEKKEEL
CCCCCCEEC
65.81Phosphositeplus
Link-
1106Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)RTEEKQQEP
CCCCCCCCC
51.56Phosphositeplus
Link-
1113O-linked (GalNAc...)EPVTSTSLV
CCCCCCCCC
19.08HPRD
Link-
1113O-linked (GlcNAc)EPVTSTSLV
CCCCCCCCC
19.08Phosphositeplus
Link-
1120Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)LVFGKKADN
CCCCCCCCC
33.07Phosphositeplus
Link-
1120N6-acetyllysineLVFGKKADN
CCCCCCCCC
33.07HPRD
Link-
1148Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)ENSSKSTFS
CCCCCCCCC
54.02Phosphositeplus
Link-
1156O-linked (GalNAc...)SFSMTKPSE
CCCEECCCC
38.31HPRD
Link-
1156O-linked (GlcNAc)SFSMTKPSE
CCCEECCCC
38.31Phosphositeplus
Link-
1157Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)FSMTKPSEK
CCEECCCCC
37.59Phosphositeplus
Link-
1161Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)KPSEKESEQ
CCCCCCCCC
71.52Phosphositeplus
Link-
1179O-linked (GlcNAc)AQTSTTADQ
CCCCCCCCC
29.41Phosphositeplus
Link-
1180O-linked (GlcNAc)QTSTTADQG
CCCCCCCCC
28.18Phosphositeplus
Link-
1457PhosphoserineNVFSSSGTS
CCCCCCCCC
22.71HPRD
Link-
1457PhosphoserineNVFSSSGTS
CCCCCCCCC
22.71PhosphoELM
Link-
1457PhosphoserineNVFSSSGTS
CCCCCCCCC
22.71Phosphositeplus
Link-
1457PhosphoserineNVFSSSGTS
CCCCCCCCC
22.71SysPTM
Link-
1457Phosphoserine.NVFSSSGTS
CCCCCCCCC
22.71UniProtKB
Link-
1460PhosphothreonineSSSGTSFSG
CCCCCCCCC
28.66HPRD
Link-
1460PhosphothreonineSSSGTSFSG
CCCCCCCCC
28.66Phosphositeplus
Link-
1461PhosphoserineSSGTSFSGR
CCCCCCCCC
22.42HPRD
Link-
1461PhosphoserineSSGTSFSGR
CCCCCCCCC
22.42PhosphoELM
Link-
1463PhosphoserineGTSFSGRKI
CCCCCCCEE
37.14HPRD
Link-
1463PhosphoserineGTSFSGRKI
CCCCCCCEE
37.14PhosphoELM
Link-
1463PhosphoserineGTSFSGRKI
CCCCCCCEE
37.14Phosphositeplus
Link-
1463PhosphoserineGTSFSGRKI
CCCCCCCEE
37.14SysPTM
Link-
1463Phosphoserine.GTSFSGRKI
CCCCCCCEE
37.14UniProtKB
Link-
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Protein-Protein Interactions
      Interacting Protein      
Interaction type
Source ID
      Resource      
      Pubmed ID      
Domain-Domain Interactions
NU133_HUMANphysical interactionMINT-4788188MINT17363900
NXF2_HUMANin vitroHPRD:04899HPRD11073998
RAN_HUMANin vitroHPRD:04899HPRD10202161
TNPO1_HUMANin vitroHPRD:04899HPRD10202161
IMB3_HUMANin vitro
in vivo
HPRD:04899HPRD9114010
NU153_HUMANin vitro
in vivo
HPRD:04899HPRD10668806
9114010
XPO1_HUMANin vitroHPRD:04899HPRD10202161
XPOT_HUMANin vitroHPRD:04899HPRD12138183
NXF1_HUMANin vitroHPRD:04899HPRD10668806
IMB1_HUMANin vitroHPRD:04899HPRD10749866
SMAD2_HUMANin vivo
yeast 2-hybrid
HPRD:04899HPRD12191473
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Disease Reference
Kegg disease
There are no disease associations of PTM sites.
Drug Reference
There are no disease associations of PTM sites.
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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT SER-209; TYR-260; SER-320; SER-334; SER-338;SER-516; SER-518; SER-522; SER-529; SER-619 AND SER-1463, AND MASSSPECTROMETRY.
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions.";
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.;
Science 325:834-840(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-384; LYS-718 AND LYS-954,AND MASS SPECTROMETRY.
Phosphorylation
ReferencePubMed
"Kinase-selective enrichment enables quantitative phosphoproteomics ofthe kinome across the cell cycle.";
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,Greff Z., Keri G., Stemmann O., Mann M.;
Mol. Cell 31:438-448(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-209, AND MASSSPECTROMETRY.
"A quantitative atlas of mitotic phosphorylation.";
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-209; SER-240; SER-257;SER-330; SER-334; SER-338; SER-343; THR-369; SER-516; SER-522;SER-529; SER-614; SER-619; SER-687; SER-1457 AND SER-1463, AND MASSSPECTROMETRY.
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT SER-209; TYR-260; SER-320; SER-334; SER-338;SER-516; SER-518; SER-522; SER-529; SER-619 AND SER-1463, 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-209; SER-257; TYR-260;SER-320; SER-334; SER-338; SER-516; SER-522 AND SER-1463, AND MASSSPECTROMETRY.
"Large-scale characterization of HeLa cell nuclear phosphoproteins.";
Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J.,Li J., Cohn M.A., Cantley L.C., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-529, AND MASSSPECTROMETRY.
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks.";
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.;
Cell 127:635-648(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-334; SER-338 ANDTHR-588, AND MASS SPECTROMETRY.
"A probability-based approach for high-throughput proteinphosphorylation analysis and site localization.";
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
Nat. Biotechnol. 24:1285-1292(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-209; SER-619 ANDSER-633, AND MASS SPECTROMETRY.
"Improved titanium dioxide enrichment of phosphopeptides from HeLacells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra.";
Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.;
J. Proteome Res. 6:4150-4162(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-687, AND MASSSPECTROMETRY.
"Combining protein-based IMAC, peptide-based IMAC, and MudPIT forefficient phosphoproteomic analysis.";
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,Yates J.R. III;
J. Proteome Res. 7:1346-1351(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-257; THR-281; SER-334AND SER-338, 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