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

UniProtKB / Swiss-Prot ID :  TPR_HUMAN

Gene Name (Synonyms) : 
TPR  

Species :  Homo sapiens (Human). 

Subcellular Localization :  Nucleus, nuclear pore complex. Nucleus membrane; Peripheral membrane protein; Cytoplasmic side. Chromosome, centromere, kinetochore. Note=The assembly of the NPC is a stepwise process in which Trp-containing peripheral structures assemble after other com 

Protein Function :  Component of the cytoplasmic fibrils of the nuclear pore complex implicated in nuclear protein import. Its N-terminus is involved in activation of oncogenic kinases. Plays a role in the mitotic spindle checkpoint. 

Protein Sequence MAAVLQQVLERTELNKLPKSVQNKLEKFLADQQSEIDGLKGRHEKFKVESEQQYFEIEKRLSHSQERLVN...
Predicted Secondary Structure CHHHHHHHHHHHHHHHHHHHHHHHHHHHHHHHHHHHHHHHHHHHHHCCCHHHHHHHHHHHHHHHHHHHHH...
Protein Variant
LocationDescription
960S -> N (in dbSNP:rs3753565). VAR_020429
1428V -> G (in dbSNP:rs35550453). VAR_047289
1707T -> A (in dbSNP:rs35766045). VAR_047290
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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.---MAAVLQ
---CHHHHH
19.99UniProtKB
Link-
40Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)IDGLKGRHE
HHHHHHHHH
60.47Phosphositeplus
Link-
59Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)FEIEKRLSH
HHHHHHHHH
65.39Phosphositeplus
Link-
62PhosphoserineEKRLSHSQE
HHHHHHHHH
25.73HPRD
Link-
135PhosphoserineNERLSQELE
HHHHHHHHH
28.03HPRD
Link-
135PhosphoserineNERLSQELE
HHHHHHHHH
28.03Phosphositeplus
Link-
177Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)DVSVKYREK
HHHHHHHHH
30.96Phosphositeplus
Link-
252N6-acetyllysineEHLQKHVED
HHHHHHHHH
56.85HPRD
Link-
252N6-acetyllysineEHLQKHVED
HHHHHHHHH
56.85Phosphositeplus
Link-
252N6-acetyllysine.EHLQKHVED
HHHHHHHHH
56.85UniProtKB
Link-
270PhosphoserineEQQASMEEK
HHHHHHHHH
23.53HPRD
Link-
270PhosphoserineEQQASMEEK
HHHHHHHHH
23.53Phosphositeplus
Link-
290Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)SNLYKSAAD
HHHHHHHHH
36.46Phosphositeplus
Link-
299Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)DSEAKSNEL
HHHHHHHHH
50.16Phosphositeplus
Link-
312N6-acetyllysineEELHKLLKE
HHHHHCCCH
69.05HPRD
Link-
312N6-acetyllysineEELHKLLKE
HHHHHCCCH
69.05Phosphositeplus
Link-
312N6-acetyllysine.EELHKLLKE
HHHHHCCCH
69.05UniProtKB
Link-
315Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)HKLLKEAGE
HHCCCHHHH
56.82Phosphositeplus
Link-
345N6-acetyllysineEMLEKIGRL
HHHHHHHHH
46.64HPRD
Link-
345N6-acetyllysineEMLEKIGRL
HHHHHHHHH
46.64Phosphositeplus
Link-
345N6-acetyllysine.EMLEKIGRL
HHHHHHHHH
46.64UniProtKB
Link-
351Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)GRLEKELEN
HHHHHHHHH
72.66Phosphositeplus
Link-
364Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)LSATKRKGA
HHHHHHHCC
52.40Phosphositeplus
Link-
366Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)ATKRKGAIL
HHHHHCCCC
55.01Phosphositeplus
Link-
379PhosphoserineLAAMSPTAA
HHHCCHHHH
17.86HPRD
Link-
379PhosphoserineLAAMSPTAA
HHHCCHHHH
17.86PhosphoELM
Link-
379PhosphoserineLAAMSPTAA
HHHCCHHHH
17.86Phosphositeplus
Link-
379Phosphoserine.LAAMSPTAA
HHHCCHHHH
17.86UniProtKB
Link-
381PhosphothreonineAMSPTAAAV
HCCHHHHHH
22.94HPRD
Link-
381PhosphothreonineAMSPTAAAV
HCCHHHHHH
22.94Phosphositeplus
Link-
381Phosphothreonine.AMSPTAAAV
HCCHHHHHH
22.94UniProtKB
Link-
421Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)KRINKYLDE
HHHHHHHHH
44.83Phosphositeplus
Link-
428N6-acetyllysineDEIVKEVEA
HHHHHHHHH
62.80HPRD
Link-
428N6-acetyllysineDEIVKEVEA
HHHHHHHHH
62.80Phosphositeplus
Link-
428N6-acetyllysine.DEIVKEVEA
HHHHHHHHH
62.80UniProtKB
Link-
433Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)EVEAKAPIL
HHHHCCHHH
40.98Phosphositeplus
Link-
457N6-acetyllysineSLSVKLEQA
HHHHHHHHH
42.82HPRD
Link-
457N6-acetyllysineSLSVKLEQA
HHHHHHHHH
42.82Phosphositeplus
Link-
457N6-acetyllysine.SLSVKLEQA
HHHHHHHHH
42.82UniProtKB
Link-
463Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)EQAMKEIQR
HHHHHHHHH
55.47Phosphositeplus
Link-
477Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)DKANKQSSV
HHHHHHHHH
57.31Phosphositeplus
Link-
494Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)EIQVKDLSQ
HHHHHHHHH
36.25Phosphositeplus
Link-
522PhosphoserineDEEVSSADI
HHHHHHHCC
24.08HPRD
Link-
523PhosphoserineEEVSSADIS
HHHHHHCCC
34.83HPRD
Link-
527PhosphoserineSADISSSSE
HHCCCCHHH
25.39HPRD
Link-
528PhosphoserineADISSSSEV
HCCCCHHHH
37.91HPRD
Link-
529PhosphoserineDISSSSEVI
CCCCHHHHH
24.59HPRD
Link-
530PhosphoserineISSSSEVIS
CCCHHHHHH
37.52HPRD
Link-
575Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)TTSSKITEL
HHHHHHHHH
54.11Phosphositeplus
Link-
582Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)ELQLKLESA
HHHHHHHHH
36.93Phosphositeplus
Link-
631PhosphoserinePLHASSLDD
CCCHHHHHH
22.23Phosphositeplus
Link-
632PhosphoserineLHASSLDDV
CCHHHHHHH
36.28Phosphositeplus
Link-
641PhosphothreonineSLASTPKRP
HHHHCCCCC
27.50HPRD
Link-
641PhosphothreonineSLASTPKRP
HHHHCCCCC
27.50Phosphositeplus
Link-
646PhosphoserinePKRPSTSQT
CCCCCHHHH
44.73HPRD
Link-
646PhosphoserinePKRPSTSQT
CCCCCHHHH
44.73PhosphoELM
Link-
646PhosphoserinePKRPSTSQT
CCCCCHHHH
44.73Phosphositeplus
Link-
646Phosphoserine.PKRPSTSQT
CCCCCHHHH
44.73UniProtKB
Link-
647PhosphothreonineKRPSTSQTV
CCCCHHHHH
27.77HPRD
Link-
648PhosphoserineRPSTSQTVS
CCCHHHHHH
28.35HPRD
Link-
648PhosphoserineRPSTSQTVS
CCCHHHHHH
28.35PhosphoELM
Link-
650PhosphothreonineSTSQTVSTP
CHHHHHHCC
19.05HPRD
Link-
652PhosphoserineSQTVSTPAP
HHHHHCCCC
31.87HPRD
Link-
652PhosphoserineSQTVSTPAP
HHHHHCCCC
31.87PhosphoELM
Link-
652PhosphoserineSQTVSTPAP
HHHHHCCCC
31.87Phosphositeplus
Link-
653PhosphothreonineQTVSTPAPV
HHHHCCCCC
21.09HPRD
Link-
653PhosphothreonineQTVSTPAPV
HHHHCCCCC
21.09PhosphoELM
Link-
663PhosphothreonineVIESTEAIE
HCHHHHHHC
19.35HPRD
Link-
673Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)KAALKQLQE
HHHHHHHHH
44.21Phosphositeplus
Link-
691Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)AENEKIQNE
HHHHHHHHH
62.26Phosphositeplus
Link-
699Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)EQLEKLQEQ
HHHHHHHHH
65.15Phosphositeplus
Link-
713Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)SQNTKISTQ
HHHHCCHHH
42.06Phosphositeplus
Link-
713N6-acetyllysineSQNTKISTQ
HHHHCCHHH
42.06HPRD
Link-
713N6-acetyllysineSQNTKISTQ
HHHHCCHHH
42.06Phosphositeplus
Link-
713N6-acetyllysine.SQNTKISTQ
HHHHCCHHH
42.06UniProtKB
Link-
723Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)DFASKRYEM
HHHHHHHHH
56.41Phosphositeplus
Link-
723N6-acetyllysineDFASKRYEM
HHHHHHHHH
56.41HPRD
Link-
723N6-acetyllysineDFASKRYEM
HHHHHHHHH
56.41Phosphositeplus
Link-
723N6-acetyllysine.DFASKRYEM
HHHHHHHHH
56.41UniProtKB
Link-
740PhosphothreonineRREITSLHE
HHHHHHHHH
22.08HPRD
Link-
748N6-acetyllysineERNQKLTAT
HHHHHHHHH
51.89HPRD
Link-
748N6-acetyllysineERNQKLTAT
HHHHHHHHH
51.89Phosphositeplus
Link-
748N6-acetyllysine.ERNQKLTAT
HHHHHHHHH
51.89UniProtKB
Link-
755Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)ATTQKQEQI
HHHHHHHHH
54.43Phosphositeplus
Link-
755N6-acetyllysineATTQKQEQI
HHHHHHHHH
54.43HPRD
Link-
755N6-acetyllysineATTQKQEQI
HHHHHHHHH
54.43Phosphositeplus
Link-
755N6-acetyllysine.ATTQKQEQI
HHHHHHHHH
54.43UniProtKB
Link-
877Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)LLDTKRQLD
HHHHHHHHH
37.50Phosphositeplus
Link-
920PhosphoserineASQSSQRTG
HHHHHHHCC
18.95HPRD
Link-
920PhosphoserineASQSSQRTG
HHHHHHHCC
18.95PhosphoELM
Link-
920PhosphoserineASQSSQRTG
HHHHHHHCC
18.95Phosphositeplus
Link-
920Phosphoserine.ASQSSQRTG
HHHHHHHCC
18.95UniProtKB
Link-
952Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)VNDLKERLK
HHHHHHHHH
43.59Phosphositeplus
Link-
965PhosphotyrosineNVEQYQAMV
HHHHHHHHH
5.68Phosphositeplus
Link-
1038Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)SELKKTLSS
HHHHHHHHH
68.28Phosphositeplus
Link-
1173PhosphoserineKVVASVKEG
HHHHHHHHH
23.32Phosphositeplus
Link-
1185PhosphoserinePLNVSLSEE
HHHHHHHHH
25.71HPRD
Link-
1185PhosphoserinePLNVSLSEE
HHHHHHHHH
25.71PhosphoELM
Link-
1185PhosphoserinePLNVSLSEE
HHHHHHHHH
25.71Phosphositeplus
Link-
1185PhosphoserinePLNVSLSEE
HHHHHHHHH
25.71SysPTM
Link-
1185Phosphoserine.PLNVSLSEE
HHHHHHHHH
25.71UniProtKB
Link-
1192PhosphoserineEEGKSQEQI
HHHHHHHHH
50.21Phosphositeplus
Link-
1252PhosphothreonineKVQVTAKTM
HHHHHHHHH
12.82HPRD
Link-
1254Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)QVTAKTMAQ
HHHHHHHHH
29.48Phosphositeplus
Link-
1255PhosphothreonineVTAKTMAQH
HHHHHHHHH
18.44HPRD
Link-
1255PhosphothreonineVTAKTMAQH
HHHHHHHHH
18.44Phosphositeplus
Link-
1265N6-acetyllysineELMKKTETM
HHHHHHHHH
37.31Phosphositeplus
Link-
1277N6-acetyllysineMETNKMLRE
HHHHHHHHH
46.89Phosphositeplus
Link-
1296Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)QMQAKVRKL
HHHHHHHHH
26.19Phosphositeplus
Link-
1385PhosphoserineEIARSNASL
HHHHHHHHH
27.94HPRD
Link-
1390PhosphothreonineNASLTNNQN
HHHHHHHHH
29.63HPRD
Link-
1398PhosphoserineNLIQSLKED
HHHHHHHHH
34.12HPRD
Link-
1400Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)IQSLKEDLN
HHHHHHHHH
55.20Phosphositeplus
Link-
1449Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)YEELKAQQD
HHHHHHHHH
47.64Phosphositeplus
Link-
1458PhosphothreonineKVMETSAQS
HCCCCCCCC
15.97HPRD
Link-
1459PhosphoserineVMETSAQSS
CCCCCCCCC
15.82HPRD
Link-
1459PhosphoserineVMETSAQSS
CCCCCCCCC
15.82PhosphoELM
Link-
1462PhosphoserineTSAQSSGDH
CCCCCCCCC
35.68HPRD
Link-
1462PhosphoserineTSAQSSGDH
CCCCCCCCC
35.68PhosphoELM
Link-
1491Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)ETKSKSLES
HCCCCCHHH
61.69Phosphositeplus
Link-
1637Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)EPSNKVPEQ
CCCCCCCCC
64.60Phosphositeplus
Link-
1666PhosphothreonineSDPPTANIK
CCCCCCCCC
37.41HPRD
Link-
1666PhosphothreonineSDPPTANIK
CCCCCCCCC
37.41PhosphoELM
Link-
1666PhosphothreonineSDPPTANIK
CCCCCCCCC
37.41Phosphositeplus
Link-
1670Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)TANIKPTPV
CCCCCCCCC
42.52Phosphositeplus
Link-
1676O-linked (GalNAc...)TPVVSTPSK
CCCCCCCCC
34.53HPRD
Link-
1676O-linked (GlcNAc)TPVVSTPSK
CCCCCCCCC
34.53Phosphositeplus
Link-
1676PhosphoserineTPVVSTPSK
CCCCCCCCC
34.53HPRD
Link-
1676PhosphoserineTPVVSTPSK
CCCCCCCCC
34.53PhosphoELM
Link-
1676PhosphoserineTPVVSTPSK
CCCCCCCCC
34.53Phosphositeplus
Link-
1677PhosphothreoninePVVSTPSKV
CCCCCCCCC
21.70HPRD
Link-
1677PhosphothreoninePVVSTPSKV
CCCCCCCCC
21.70PhosphoELM
Link-
1677PhosphothreoninePVVSTPSKV
CCCCCCCCC
21.70Phosphositeplus
Link-
1677Phosphothreonine.PVVSTPSKV
CCCCCCCCC
21.70UniProtKB
Link-
1679PhosphoserineVSTPSKVTA
CCCCCCCCC
39.59Phosphositeplus
Link-
1690Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)MAGNKSTPR
CCCCCCCCC
55.58Phosphositeplus
Link-
1691PhosphoserineAGNKSTPRA
CCCCCCCCC
47.87HPRD
Link-
1691PhosphoserineAGNKSTPRA
CCCCCCCCC
47.87PhosphoELM
Link-
1691PhosphoserineAGNKSTPRA
CCCCCCCCC
47.87Phosphositeplus
Link-
1692PhosphothreonineGNKSTPRAS
CCCCCCCCC
20.57HPRD
Link-
1692PhosphothreonineGNKSTPRAS
CCCCCCCCC
20.57Phosphositeplus
Link-
1712PhosphothreonineNPTTTPTAT
CCCCCCCCC
22.56Phosphositeplus
Link-
1725PhosphoserineTQVESQEAM
CCCCCCCCC
34.17HPRD
Link-
1725Phosphoserine.TQVESQEAM
CCCCCCCCC
34.17UniProtKB
Link-
1804PhosphoserineVVQSSPVER
CCCCCCCCC
18.84HPRD
Link-
1804Phosphoserine.VVQSSPVER
CCCCCCCCC
18.84UniProtKB
Link-
1838PhosphoserineEEEDSTIEA
CCCCCCCCC
34.27HPRD
Link-
1838PhosphoserineEEEDSTIEA
CCCCCCCCC
34.27PhosphoELM
Link-
1839PhosphothreonineEEDSTIEAS
CCCCCCCCC
34.85HPRD
Link-
1839PhosphothreonineEEDSTIEAS
CCCCCCCCC
34.85PhosphoELM
Link-
1847PhosphoserineSDQVSDDTV
CCCCCCCCC
24.92HPRD
Link-
2034PhosphoserineRAADSQNSG
CCCCCCCCC
26.91HPRD
Link-
2034PhosphoserineRAADSQNSG
CCCCCCCCC
26.91PhosphoELM
Link-
2034PhosphoserineRAADSQNSG
CCCCCCCCC
26.91Phosphositeplus
Link-
2034Phosphoserine.RAADSQNSG
CCCCCCCCC
26.91UniProtKB
Link-
2037PhosphoserineDSQNSGEGN
CCCCCCCCC
30.50HPRD
Link-
2037PhosphoserineDSQNSGEGN
CCCCCCCCC
30.50Phosphositeplus
Link-
2037PhosphoserineDSQNSGEGN
CCCCCCCCC
30.50SysPTM
Link-
2037Phosphoserine.DSQNSGEGN
CCCCCCCCC
30.50UniProtKB
Link-
2047PhosphoserineGAAESSFSQ
CCCCCCCCC
31.77HPRD
Link-
2047PhosphoserineGAAESSFSQ
CCCCCCCCC
31.77Phosphositeplus
Link-
2048PhosphoserineAAESSFSQE
CCCCCCCCC
22.03HPRD
Link-
2048PhosphoserineAAESSFSQE
CCCCCCCCC
22.03Phosphositeplus
Link-
2048Phosphoserine.AAESSFSQE
CCCCCCCCC
22.03UniProtKB
Link-
2050PhosphoserineESSFSQEVS
CCCCCCCCC
27.64HPRD
Link-
2050PhosphoserineESSFSQEVS
CCCCCCCCC
27.64PhosphoELM
Link-
2050PhosphoserineESSFSQEVS
CCCCCCCCC
27.64Phosphositeplus
Link-
2050Phosphoserine.ESSFSQEVS
CCCCCCCCC
27.64UniProtKB
Link-
2054PhosphoserineSQEVSREQQ
CCCCCCCCC
29.37HPRD
Link-
2073PhosphoserineRAPQSPRRP
CCCCCCCCC
21.22HPRD
Link-
2073PhosphoserineRAPQSPRRP
CCCCCCCCC
21.22Phosphositeplus
Link-
2073Phosphoserine.RAPQSPRRP
CCCCCCCCC
21.22UniProtKB
Link-
2116PhosphothreonineGLQLTPGIG
CCCCCCCCC
13.40Phosphositeplus
Link-
2146PhosphothreonineVPHRTDGFA
CCCCCCCCC
37.12Phosphositeplus
Link-
2147Caspase cleavage aspartic acidPHRTDGFAE
CCCCCCCCC
50.61Phosphositeplus
Link-
2155PhosphoserineEAIHSPQVA
CCCCCCCCC
15.77HPRD
Link-
2155PhosphoserineEAIHSPQVA
CCCCCCCCC
15.77PhosphoELM
Link-
2155PhosphoserineEAIHSPQVA
CCCCCCCCC
15.77Phosphositeplus
Link-
2155Phosphoserine.EAIHSPQVA
CCCCCCCCC
15.77UniProtKB
Link-
2175PhosphothreonineDMPQTSSSH
CCCCCCCCC
25.38HPRD
Link-
2178PhosphoserineQTSSSHSDL
CCCCCCCCC
27.12HPRD
Link-
2180PhosphoserineSSSHSDLGQ
CCCCCCCCC
36.16HPRD
Link-
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Protein-Protein Interactions
      Interacting Protein      
Interaction type
Source ID
      Resource      
      Pubmed ID      
Domain-Domain Interactions
MK01_HUMANin vitro
in vivo
HPRD:08927HPRD12594221
IF16_HUMANyeast 2-hybridHPRD:08927HPRD12513910
SHC1_HUMANin vitroHPRD:08927HPRD11896612
NUP98_HUMANin vivoHPRD:08927HPRD11248057
NU153_HUMANin vitro
in vivo
yeast 2-hybrid
HPRD:08927HPRD12802065
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Disease Reference
Kegg disease
H00032 Thyroid cancer
OMIM disease
188550Thyroid papillary carcinoma (TPC)
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-379; THR-381; SER-1185 AND THR-1677, 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-252; LYS-312; LYS-345;LYS-428; LYS-457; LYS-713; LYS-723; LYS-748 AND LYS-755, AND MASSSPECTROMETRY.
Phosphorylation
ReferencePubMed
"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-1185, AND MASSSPECTROMETRY.
"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-2155, AND MASSSPECTROMETRY.
"Global proteomic profiling of phosphopeptides using electron transferdissociation tandem mass spectrometry.";
Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A.;
Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-646; SER-1185 ANDSER-2155, AND MASS SPECTROMETRY.
"ATM and ATR substrate analysis reveals extensive protein networksresponsive to DNA damage.";
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.;
Science 316:1160-1166(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-920; SER-2034 ANDSER-2050, AND MASS SPECTROMETRY.
"Evaluation of the low-specificity protease elastase for large-scalephosphoproteome analysis.";
Wang B., Malik R., Nigg E.A., Korner R.;
Anal. Chem. 80:9526-9533(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1725 AND SER-1804, ANDMASS SPECTROMETRY.
"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-2155, 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-379; SER-1185; SER-2048AND SER-2155, AND MASS SPECTROMETRY.
"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-379; THR-381; SER-1185 AND THR-1677, 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-1185; SER-2050 ANDSER-2155, AND MASS SPECTROMETRY.
"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-2037, 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-2073 AND SER-2155, ANDMASS SPECTROMETRY.
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