Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures
Basic Information
Protein Name :  La-related protein 1  

UniProtKB / Swiss-Prot ID :  LARP1_HUMAN

Gene Name (Synonyms) : 
LARP1, KIAA0731, LARP  

Species :  Homo sapiens (Human). 

Subcellular Localization :   

Protein Function :   

Protein Sequence MATQVEPLLPGGATLLQAEEHGGLVRKKPPPAPEGKGEPGPNDVRGGEPDGSARRPRPPCAKPHKEGTGQ...
Predicted Secondary Structure CCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCC...
Protein Variant -
- top -

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
- top -

Experimental Post-Translational Modification Sites Download
Locations
Modification
Substrate Sites
&
Secondary Structure
Accessible Surface Area (%)
Resource
Reference
Structural Characterization
Orthologous
Protein Cluster
2N-acetylalanine.---MATQVE
---CCCCCC
20.31UniProtKB
Link-
68PhosphothreonineHKEGTGQQE
CCCCCCCCC
32.67HPRD
Link-
68PhosphothreonineHKEGTGQQE
CCCCCCCCC
32.67PhosphoELM
Link-
68PhosphothreonineHKEGTGQQE
CCCCCCCCC
32.67Phosphositeplus
Link-
68PhosphothreonineHKEGTGQQE
CCCCCCCCC
32.67SysPTM
Link-
75PhosphoserineQERESPRPL
CCCCCCCCC
32.22HPRD
Link-
75PhosphoserineQERESPRPL
CCCCCCCCC
32.22PhosphoELM
Link-
75PhosphoserineQERESPRPL
CCCCCCCCC
32.22Phosphositeplus
Link-
75PhosphoserineQERESPRPL
CCCCCCCCC
32.22SysPTM
Link-
75Phosphoserine.QERESPRPL
CCCCCCCCC
32.22UniProtKB
Link-
90PhosphoserineGPAISDGEE
CCCCCCCCC
41.49HPRD
Link-
90PhosphoserineGPAISDGEE
CCCCCCCCC
41.49PhosphoELM
Link-
90PhosphoserineGPAISDGEE
CCCCCCCCC
41.49Phosphositeplus
Link-
90PhosphoserineGPAISDGEE
CCCCCCCCC
41.49SysPTM
Link-
90Phosphoserine.GPAISDGEE
CCCCCCCCC
41.49UniProtKB
Link-
138PhosphothreoninePVLTTVNGQ
CCCCCCCCC
14.07HPRD
Link-
143PhosphoserineVNGQSPPEH
CCCCCCCCC
43.77HPRD
Link-
143PhosphoserineVNGQSPPEH
CCCCCCCCC
43.77HPRD
Link-
143PhosphoserineVNGQSPPEH
CCCCCCCCC
43.77PhosphoELM
Link-
143PhosphoserineVNGQSPPEH
CCCCCCCCC
43.77Phosphositeplus
Link-
143PhosphoserineVNGQSPPEH
CCCCCCCCC
43.77SysPTM
Link-
143Phosphoserine.VNGQSPPEH
CCCCCCCCC
43.77UniProtKB
Link-
148PhosphoserinePPEHSAPAK
CCCCCCCCC
34.00HPRD
Link-
165PhosphoserineQRKGSKVGD
CCCCCCCCC
27.48HPRD
Link-
165PhosphoserineQRKGSKVGD
CCCCCCCCC
27.48PhosphoELM
Link-
165PhosphoserineQRKGSKVGD
CCCCCCCCC
27.48Phosphositeplus
Link-
165PhosphoserineQRKGSKVGD
CCCCCCCCC
27.48SysPTM
Link-
165Phosphoserine.QRKGSKVGD
CCCCCCCCC
27.48UniProtKB
Link-
172Caspase cleavage aspartic acidGDFGDAINW
CCCCCCCCC
44.24Phosphositeplus
Link-
215PhosphoserineKGEGSDSKE
CCCCCCCCC
34.11HPRD
Link-
215PhosphoserineKGEGSDSKE
CCCCCCCCC
34.11Phosphositeplus
Link-
217PhosphoserineEGSDSKESP
CCCCCCCCC
39.77HPRD
Link-
220PhosphoserineDSKESPKTK
CCCCCCCCC
35.12HPRD
Link-
220PhosphoserineDSKESPKTK
CCCCCCCCC
35.12Phosphositeplus
Link-
225PhosphoserinePKTKSDESG
CCCCCCCCC
52.41Phosphositeplus
Link-
228PhosphoserineKSDESGEEK
CCCCCCCCC
57.40Phosphositeplus
Link-
303PhosphothreonineVAPPTPAWQ
CCCCCCCCC
25.28Phosphositeplus
Link-
322PhosphothreonineDQDETSSVK
CCCCCCCCC
34.29HPRD
Link-
322PhosphothreonineDQDETSSVK
CCCCCCCCC
34.29Phosphositeplus
Link-
324PhosphoserineDETSSVKSD
CCCCCCCCC
40.77HPRD
Link-
324PhosphoserineDETSSVKSD
CCCCCCCCC
40.77Phosphositeplus
Link-
327PhosphoserineSSVKSDGAG
CCCCCCCCC
38.84Phosphositeplus
Link-
361PhosphotyrosineTHFDYQFGY
CEEECCCCC
12.56Phosphositeplus
Link-
365PhosphotyrosineYQFGYRKFD
CCCCCCCCC
16.36Phosphositeplus
Link-
376PhosphothreonineEGPRTPKYM
CCCCCCHHH
27.54HPRD
Link-
376PhosphothreonineEGPRTPKYM
CCCCCCHHH
27.54Phosphositeplus
Link-
376PhosphothreonineEGPRTPKYM
CCCCCCHHH
27.54SysPTM
Link-
379PhosphotyrosineRTPKYMNNI
CCCHHHHHC
13.28HPRD
Link-
379PhosphotyrosineRTPKYMNNI
CCCHHHHHC
13.28PhosphoELM
Link-
393PhosphothreonineNVSSTELYS
CCCCCCCCH
23.62HPRD
Link-
393PhosphothreonineNVSSTELYS
CCCCCCCCH
23.62PhosphoELM
Link-
462Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)FAALKDSKV
HHHHHCCCC
56.05Phosphositeplus
Link-
473Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)IVDEKVRRR
EECCCCEEC
36.26Phosphositeplus
Link-
515PhosphothreonineYQKETESAP
CCCCCCCCC
42.13HPRD
Link-
515PhosphothreonineYQKETESAP
CCCCCCCCC
42.13Phosphositeplus
Link-
515PhosphothreonineYQKETESAP
CCCCCCCCC
42.13SysPTM
Link-
517PhosphoserineKETESAPGS
CCCCCCCCC
47.38HPRD
Link-
517PhosphoserineKETESAPGS
CCCCCCCCC
47.38PhosphoELM
Link-
517PhosphoserineKETESAPGS
CCCCCCCCC
47.38Phosphositeplus
Link-
517PhosphoserineKETESAPGS
CCCCCCCCC
47.38SysPTM
Link-
517PhosphoserineKETESAPGS
CCCCCCCCC
47.38SysPTM
Link-
517Phosphoserine.KETESAPGS
CCCCCCCCC
47.38UniProtKB
Link-
521PhosphoserineSAPGSPRAV
CCCCCCCCC
15.34HPRD
Link-
521PhosphoserineSAPGSPRAV
CCCCCCCCC
15.34PhosphoELM
Link-
521PhosphoserineSAPGSPRAV
CCCCCCCCC
15.34Phosphositeplus
Link-
521PhosphoserineSAPGSPRAV
CCCCCCCCC
15.34SysPTM
Link-
521PhosphoserineSAPGSPRAV
CCCCCCCCC
15.34SysPTM
Link-
521Phosphoserine.SAPGSPRAV
CCCCCCCCC
15.34UniProtKB
Link-
526PhosphothreoninePRAVTPVPT
CCCCCCCCC
19.99HPRD
Link-
526PhosphothreoninePRAVTPVPT
CCCCCCCCC
19.99PhosphoELM
Link-
526PhosphothreoninePRAVTPVPT
CCCCCCCCC
19.99Phosphositeplus
Link-
526PhosphothreoninePRAVTPVPT
CCCCCCCCC
19.99SysPTM
Link-
526PhosphothreoninePRAVTPVPT
CCCCCCCCC
19.99SysPTM
Link-
526Phosphothreonine.PRAVTPVPT
CCCCCCCCC
19.99UniProtKB
Link-
530PhosphothreonineTPVPTKTEE
CCCCCCHHH
51.32HPRD
Link-
530PhosphothreonineTPVPTKTEE
CCCCCCHHH
51.32Phosphositeplus
Link-
530PhosphothreonineTPVPTKTEE
CCCCCCHHH
51.32SysPTM
Link-
539Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)VSNLKTLPK
HHHHHHHHH
52.87Phosphositeplus
Link-
546PhosphoserinePKGLSASLP
HHHHCCCCC
25.20HPRD
Link-
546PhosphoserinePKGLSASLP
HHHHCCCCC
25.20PhosphoELM
Link-
546PhosphoserinePKGLSASLP
HHHHCCCCC
25.20Phosphositeplus
Link-
546PhosphoserinePKGLSASLP
HHHHCCCCC
25.20SysPTM
Link-
546PhosphoserinePKGLSASLP
HHHHCCCCC
25.20SysPTM
Link-
546Phosphoserine.PKGLSASLP
HHHHCCCCC
25.20UniProtKB
Link-
548PhosphoserineGLSASLPDL
HHCCCCCCC
36.74HPRD
Link-
548PhosphoserineGLSASLPDL
HHCCCCCCC
36.74PhosphoELM
Link-
548PhosphoserineGLSASLPDL
HHCCCCCCC
36.74Phosphositeplus
Link-
548PhosphoserineGLSASLPDL
HHCCCCCCC
36.74SysPTM
Link-
548PhosphoserineGLSASLPDL
HHCCCCCCC
36.74SysPTM
Link-
548Phosphoserine.GLSASLPDL
HHCCCCCCC
36.74UniProtKB
Link-
554PhosphoserinePDLDSENWI
CCCCCCCHH
39.88HPRD
Link-
554PhosphoserinePDLDSENWI
CCCCCCCHH
39.88HPRD
Link-
554PhosphoserinePDLDSENWI
CCCCCCCHH
39.88SysPTM
Link-
580PhosphoserineESRFSHLTS
CCHHHHHHH
19.24HPRD
Link-
580PhosphoserineESRFSHLTS
CCHHHHHHH
19.24Phosphositeplus
Link-
580PhosphoserineESRFSHLTS
CCHHHHHHH
19.24SysPTM
Link-
596PhosphoserineQQLMSKDQD
HHHHHCCCH
41.49HPRD
Link-
596PhosphoserineQQLMSKDQD
HHHHHCCCH
41.49Phosphositeplus
Link-
596PhosphoserineQQLMSKDQD
HHHHHCCCH
41.49SysPTM
Link-
622PhosphothreonineGRKNTFTAW
CCCCCCCCC
25.95HPRD
Link-
622PhosphothreonineGRKNTFTAW
CCCCCCCCC
25.95PhosphoELM
Link-
622PhosphothreonineGRKNTFTAW
CCCCCCCCC
25.95Phosphositeplus
Link-
622PhosphothreonineGRKNTFTAW
CCCCCCCCC
25.95SysPTM
Link-
622Phosphothreonine.GRKNTFTAW
CCCCCCCCC
25.95UniProtKB
Link-
624PhosphothreonineKNTFTAWSD
CCCCCCCCC
25.77HPRD
Link-
624PhosphothreonineKNTFTAWSD
CCCCCCCCC
25.77PhosphoELM
Link-
624PhosphothreonineKNTFTAWSD
CCCCCCCCC
25.77Phosphositeplus
Link-
624PhosphothreonineKNTFTAWSD
CCCCCCCCC
25.77SysPTM
Link-
624Phosphothreonine.KNTFTAWSD
CCCCCCCCC
25.77UniProtKB
Link-
627PhosphoserineFTAWSDEES
CCCCCCCCC
32.45HPRD
Link-
627PhosphoserineFTAWSDEES
CCCCCCCCC
32.45PhosphoELM
Link-
627PhosphoserineFTAWSDEES
CCCCCCCCC
32.45Phosphositeplus
Link-
627PhosphoserineFTAWSDEES
CCCCCCCCC
32.45SysPTM
Link-
627PhosphoserineFTAWSDEES
CCCCCCCCC
32.45SysPTM
Link-
627Phosphoserine.FTAWSDEES
CCCCCCCCC
32.45UniProtKB
Link-
631PhosphoserineSDEESDYEI
CCCCCCCCC
43.37HPRD
Link-
631PhosphoserineSDEESDYEI
CCCCCCCCC
43.37PhosphoELM
Link-
631PhosphoserineSDEESDYEI
CCCCCCCCC
43.37Phosphositeplus
Link-
631PhosphoserineSDEESDYEI
CCCCCCCCC
43.37SysPTM
Link-
631Phosphoserine.SDEESDYEI
CCCCCCCCC
43.37UniProtKB
Link-
633PhosphotyrosineEESDYEIDD
CCCCCCCCC
24.86HPRD
Link-
633PhosphotyrosineEESDYEIDD
CCCCCCCCC
24.86PhosphoELM
Link-
633PhosphotyrosineEESDYEIDD
CCCCCCCCC
24.86Phosphositeplus
Link-
633PhosphotyrosineEESDYEIDD
CCCCCCCCC
24.86SysPTM
Link-
633Phosphotyrosine.EESDYEIDD
CCCCCCCCC
24.86UniProtKB
Link-
647PhosphothreonineILIVTQTPH
EEEEECCCC
21.52HPRD
Link-
647PhosphothreonineILIVTQTPH
EEEEECCCC
21.52HPRD
Link-
649PhosphothreonineIVTQTPHYM
EEECCCCCC
11.58HPRD
Link-
649PhosphothreonineIVTQTPHYM
EEECCCCCC
11.58PhosphoELM
Link-
649PhosphothreonineIVTQTPHYM
EEECCCCCC
11.58Phosphositeplus
Link-
649PhosphothreonineIVTQTPHYM
EEECCCCCC
11.58SysPTM
Link-
649PhosphothreonineIVTQTPHYM
EEECCCCCC
11.58SysPTM
Link-
649Phosphothreonine.IVTQTPHYM
EEECCCCCC
11.58UniProtKB
Link-
652PhosphotyrosineQTPHYMRRH
CCCCCCCCC
8.10HPRD
Link-
699PhosphotyrosineFEPEYSQIK
CCCHHHHHH
19.32Phosphositeplus
Link-
716PhosphoserineVNMISREQF
HHHHHHHHH
20.99Phosphositeplus
Link-
722PhosphothreonineEQFDTLTPE
HHHHHHCCC
33.54HPRD
Link-
722PhosphothreonineEQFDTLTPE
HHHHHHCCC
33.54PhosphoELM
Link-
724PhosphothreonineFDTLTPEPP
HHHHCCCCC
27.91HPRD
Link-
724PhosphothreonineFDTLTPEPP
HHHHCCCCC
27.91PhosphoELM
Link-
724PhosphothreonineFDTLTPEPP
HHHHCCCCC
27.91Phosphositeplus
Link-
724PhosphothreonineFDTLTPEPP
HHHHCCCCC
27.91SysPTM
Link-
724Phosphothreonine.FDTLTPEPP
HHHHCCCCC
27.91UniProtKB
Link-
753Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)ALANKLFGA
HHHHHHCCC
39.32Phosphositeplus
Link-
761PhosphoserineAPEPSTIAR
CCCCHHHHH
30.68HPRD
Link-
766PhosphoserineTIARSLPTT
HHHHHCCCC
29.67HPRD
Link-
766PhosphoserineTIARSLPTT
HHHHHCCCC
29.67PhosphoELM
Link-
766PhosphoserineTIARSLPTT
HHHHHCCCC
29.67Phosphositeplus
Link-
766PhosphoserineTIARSLPTT
HHHHHCCCC
29.67SysPTM
Link-
766PhosphoserineTIARSLPTT
HHHHHCCCC
29.67SysPTM
Link-
766Phosphoserine.TIARSLPTT
HHHHHCCCC
29.67UniProtKB
Link-
769PhosphothreonineRSLPTTVPE
HHCCCCCCC
45.80HPRD
Link-
769PhosphothreonineRSLPTTVPE
HHCCCCCCC
45.80PhosphoELM
Link-
769PhosphothreonineRSLPTTVPE
HHCCCCCCC
45.80Phosphositeplus
Link-
770PhosphothreonineSLPTTVPES
HCCCCCCCC
31.93HPRD
Link-
770PhosphothreonineSLPTTVPES
HCCCCCCCC
31.93PhosphoELM
Link-
774PhosphoserineTVPESPNYR
CCCCCCCCC
16.63HPRD
Link-
774PhosphoserineTVPESPNYR
CCCCCCCCC
16.63HPRD
Link-
774PhosphoserineTVPESPNYR
CCCCCCCCC
16.63PhosphoELM
Link-
774PhosphoserineTVPESPNYR
CCCCCCCCC
16.63Phosphositeplus
Link-
774PhosphoserineTVPESPNYR
CCCCCCCCC
16.63SysPTM
Link-
774PhosphoserineTVPESPNYR
CCCCCCCCC
16.63SysPTM
Link-
774Phosphoserine.TVPESPNYR
CCCCCCCCC
16.63UniProtKB
Link-
777PhosphotyrosineESPNYRNTR
CCCCCCCCC
14.50HPRD
Link-
777PhosphotyrosineESPNYRNTR
CCCCCCCCC
14.50PhosphoELM
Link-
777PhosphotyrosineESPNYRNTR
CCCCCCCCC
14.50Phosphositeplus
Link-
777PhosphotyrosineESPNYRNTR
CCCCCCCCC
14.50SysPTM
Link-
780PhosphothreonineNYRNTRTPR
CCCCCCCCC
27.24Phosphositeplus
Link-
782PhosphothreonineRNTRTPRTP
CCCCCCCCC
18.32HPRD
Link-
782PhosphothreonineRNTRTPRTP
CCCCCCCCC
18.32SysPTM
Link-
785PhosphothreonineRTPRTPRTP
CCCCCCCCC
20.51HPRD
Link-
785PhosphothreonineRTPRTPRTP
CCCCCCCCC
20.51PhosphoELM
Link-
785PhosphothreonineRTPRTPRTP
CCCCCCCCC
20.51Phosphositeplus
Link-
785PhosphothreonineRTPRTPRTP
CCCCCCCCC
20.51SysPTM
Link-
785PhosphothreonineRTPRTPRTP
CCCCCCCCC
20.51SysPTM
Link-
785Phosphothreonine.RTPRTPRTP
CCCCCCCCC
20.51UniProtKB
Link-
788PhosphothreonineRTPRTPQLK
CCCCCCCCC
19.31HPRD
Link-
788PhosphothreonineRTPRTPQLK
CCCCCCCCC
19.31HPRD
Link-
788PhosphothreonineRTPRTPQLK
CCCCCCCCC
19.31PhosphoELM
Link-
788PhosphothreonineRTPRTPQLK
CCCCCCCCC
19.31Phosphositeplus
Link-
788PhosphothreonineRTPRTPQLK
CCCCCCCCC
19.31SysPTM
Link-
788PhosphothreonineRTPRTPQLK
CCCCCCCCC
19.31SysPTM
Link-
788Phosphothreonine.RTPRTPQLK
CCCCCCCCC
19.31UniProtKB
Link-
805Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)YPVVKEGRT
EEECCCCCC
55.47Phosphositeplus
Link-
823PhosphoserineKTRHSSNPP
HHCCCCCCC
28.64HPRD
Link-
823PhosphoserineKTRHSSNPP
HHCCCCCCC
28.64PhosphoELM
Link-
823PhosphoserineKTRHSSNPP
HHCCCCCCC
28.64Phosphositeplus
Link-
823Phosphoserine.KTRHSSNPP
HHCCCCCCC
28.64UniProtKB
Link-
824PhosphoserineTRHSSNPPL
HCCCCCCCH
47.43HPRD
Link-
824PhosphoserineTRHSSNPPL
HCCCCCCCH
47.43PhosphoELM
Link-
824PhosphoserineTRHSSNPPL
HCCCCCCCH
47.43Phosphositeplus
Link-
824PhosphoserineTRHSSNPPL
HCCCCCCCH
47.43SysPTM
Link-
824PhosphoserineTRHSSNPPL
HCCCCCCCH
47.43SysPTM
Link-
824Phosphoserine.TRHSSNPPL
HCCCCCCCH
47.43UniProtKB
Link-
830PhosphoserinePPLESHVGW
CCHHHHHHH
31.02HPRD
Link-
830PhosphoserinePPLESHVGW
CCHHHHHHH
31.02PhosphoELM
Link-
830PhosphoserinePPLESHVGW
CCHHHHHHH
31.02Phosphositeplus
Link-
838PhosphoserineWVMDSREHR
HHHHHHHCC
22.82PhosphoELM
Link-
838PhosphoserineWVMDSREHR
HHHHHHHCC
22.82Phosphositeplus
Link-
845PhosphothreonineHRPRTASIS
CCCCCCCCC
27.69HPRD
Link-
845PhosphothreonineHRPRTASIS
CCCCCCCCC
27.69PhosphoELM
Link-
845PhosphothreonineHRPRTASIS
CCCCCCCCC
27.69Phosphositeplus
Link-
845PhosphothreonineHRPRTASIS
CCCCCCCCC
27.69SysPTM
Link-
845PhosphothreonineHRPRTASIS
CCCCCCCCC
27.69SysPTM
Link-
845Phosphothreonine.HRPRTASIS
CCCCCCCCC
27.69UniProtKB
Link-
847PhosphoserinePRTASISSS
CCCCCCCCC
23.53HPRD
Link-
847PhosphoserinePRTASISSS
CCCCCCCCC
23.53PhosphoELM
Link-
847PhosphoserinePRTASISSS
CCCCCCCCC
23.53Phosphositeplus
Link-
847PhosphoserinePRTASISSS
CCCCCCCCC
23.53SysPTM
Link-
847Phosphoserine.PRTASISSS
CCCCCCCCC
23.53UniProtKB
Link-
849PhosphoserineTASISSSPS
CCCCCCCCC
23.44HPRD
Link-
849PhosphoserineTASISSSPS
CCCCCCCCC
23.44PhosphoELM
Link-
849PhosphoserineTASISSSPS
CCCCCCCCC
23.44Phosphositeplus
Link-
849PhosphoserineTASISSSPS
CCCCCCCCC
23.44SysPTM
Link-
849PhosphoserineTASISSSPS
CCCCCCCCC
23.44SysPTM
Link-
849Phosphoserine.TASISSSPS
CCCCCCCCC
23.44UniProtKB
Link-
850PhosphoserineASISSSPSE
CCCCCCCCC
44.60HPRD
Link-
850PhosphoserineASISSSPSE
CCCCCCCCC
44.60PhosphoELM
Link-
850PhosphoserineASISSSPSE
CCCCCCCCC
44.60Phosphositeplus
Link-
850PhosphoserineASISSSPSE
CCCCCCCCC
44.60SysPTM
Link-
850Phosphoserine.ASISSSPSE
CCCCCCCCC
44.60UniProtKB
Link-
851PhosphoserineSISSSPSEG
CCCCCCCCC
26.17HPRD
Link-
851PhosphoserineSISSSPSEG
CCCCCCCCC
26.17PhosphoELM
Link-
851PhosphoserineSISSSPSEG
CCCCCCCCC
26.17Phosphositeplus
Link-
851PhosphoserineSISSSPSEG
CCCCCCCCC
26.17SysPTM
Link-
851Phosphoserine.SISSSPSEG
CCCCCCCCC
26.17UniProtKB
Link-
853PhosphoserineSSSPSEGTP
CCCCCCCCC
51.08HPRD
Link-
853PhosphoserineSSSPSEGTP
CCCCCCCCC
51.08PhosphoELM
Link-
853PhosphoserineSSSPSEGTP
CCCCCCCCC
51.08Phosphositeplus
Link-
853PhosphoserineSSSPSEGTP
CCCCCCCCC
51.08SysPTM
Link-
853PhosphoserineSSSPSEGTP
CCCCCCCCC
51.08SysPTM
Link-
853Phosphoserine.SSSPSEGTP
CCCCCCCCC
51.08UniProtKB
Link-
856PhosphothreoninePSEGTPTVG
CCCCCCCCC
16.25Phosphositeplus
Link-
858PhosphothreonineEGTPTVGSY
CCCCCCCCC
37.02HPRD
Link-
858PhosphothreonineEGTPTVGSY
CCCCCCCCC
37.02Phosphositeplus
Link-
858PhosphothreonineEGTPTVGSY
CCCCCCCCC
37.02SysPTM
Link-
861PhosphoserinePTVGSYGCT
CCCCCCCCC
17.64Phosphositeplus
Link-
861PhosphoserinePTVGSYGCT
CCCCCCCCC
17.64SysPTM
Link-
862PhosphotyrosineTVGSYGCTP
CCCCCCCCC
15.42HPRD
Link-
862PhosphotyrosineTVGSYGCTP
CCCCCCCCC
15.42PhosphoELM
Link-
862PhosphotyrosineTVGSYGCTP
CCCCCCCCC
15.42Phosphositeplus
Link-
862Phosphotyrosine.TVGSYGCTP
CCCCCCCCC
15.42UniProtKB
Link-
865PhosphothreonineSYGCTPQSL
CCCCCCCCC
21.72HPRD
Link-
865PhosphothreonineSYGCTPQSL
CCCCCCCCC
21.72PhosphoELM
Link-
865PhosphothreonineSYGCTPQSL
CCCCCCCCC
21.72Phosphositeplus
Link-
865PhosphothreonineSYGCTPQSL
CCCCCCCCC
21.72SysPTM
Link-
868PhosphoserineCTPQSLPKF
CCCCCCCCC
48.09HPRD
Link-
868PhosphoserineCTPQSLPKF
CCCCCCCCC
48.09PhosphoELM
Link-
868PhosphoserineCTPQSLPKF
CCCCCCCCC
48.09Phosphositeplus
Link-
881Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)HELLKENGF
HHHHHHCCC
62.85Phosphositeplus
Link-
892N6-acetyllysineHVYHKYRRR
HHHHHHHHH
23.82HPRD
Link-
892N6-acetyllysineHVYHKYRRR
HHHHHHHHH
23.82Phosphositeplus
Link-
892N6-acetyllysine.HVYHKYRRR
HHHHHHHHH
23.82UniProtKB
Link-
944Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)LEDAKEGYR
HHHHHHHHH
65.08Phosphositeplus
Link-
972Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)LDIFKDFQE
HHHHHHHHH
58.95Phosphositeplus
Link-
1017Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)EYLGKFRRL
HHHHHHHCH
32.86Phosphositeplus
Link-
1017N6-acetyllysineEYLGKFRRL
HHHHHHHCH
32.86HPRD
Link-
1017N6-acetyllysineEYLGKFRRL
HHHHHHHCH
32.86Phosphositeplus
Link-
1017N6-acetyllysine.EYLGKFRRL
HHHHHHHCH
32.86UniProtKB
Link-
1040PhosphoserineHKRHSVVAG
CCCCEEEEC
23.48Phosphositeplus
Link-
1056PhosphoserineKRCPSQSSS
CCCCCCCCC
46.44HPRD
Link-
1056PhosphoserineKRCPSQSSS
CCCCCCCCC
46.44PhosphoELM
Link-
1056PhosphoserineKRCPSQSSS
CCCCCCCCC
46.44Phosphositeplus
Link-
1056PhosphoserineKRCPSQSSS
CCCCCCCCC
46.44SysPTM
Link-
1056Phosphoserine.KRCPSQSSS
CCCCCCCCC
46.44UniProtKB
Link-
1058PhosphoserineCPSQSSSRP
CCCCCCCCC
34.32HPRD
Link-
1058PhosphoserineCPSQSSSRP
CCCCCCCCC
34.32Phosphositeplus
Link-
1067PhosphoserineAAMISQPPT
CCCCCCCCC
24.45HPRD
Link-
1067PhosphoserineAAMISQPPT
CCCCCCCCC
24.45Phosphositeplus
Link-
1071PhosphothreonineSQPPTPPTG
CCCCCCCCC
48.89HPRD
Link-
1071PhosphothreonineSQPPTPPTG
CCCCCCCCC
48.89PhosphoELM
Link-
1071PhosphothreonineSQPPTPPTG
CCCCCCCCC
48.89Phosphositeplus
Link-
1071PhosphothreonineSQPPTPPTG
CCCCCCCCC
48.89SysPTM
Link-
1071Phosphothreonine.SQPPTPPTG
CCCCCCCCC
48.89UniProtKB
Link-
1089PhosphoserineTSQHSNTQT
HHHCCCHHH
33.66HPRD
Link-
1091PhosphothreonineQHSNTQTLG
HCCCHHHCC
26.41Phosphositeplus
Link-
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Protein-Protein Interactions
      Interacting Protein      
Interaction type
Source ID
      Resource      
      Pubmed ID      
Domain-Domain Interactions
1433T_HUMANphysical interactionMINT-51000MINT15324660
1433Z_HUMANphysical interactionMINT-51028MINT15324660
1433Z_HUMANphysical interactionMINT-3307331MINT15161933
1433G_HUMANin vivoHPRD:11225HPRD15324660
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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-517; SER-521; THR-526; SER-548; THR-622;THR-624; SER-627; SER-631; TYR-633; THR-724; SER-766; SER-774;SER-847; SER-849; SER-850; SER-851; SER-853 AND TYR-862, 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-892 AND LYS-1017, AND MASSSPECTROMETRY.
Phosphorylation
ReferencePubMed
"Quantitative phosphoproteome profiling of Wnt3a-mediated signalingnetwork: indicating the involvement of ribonucleoside-diphosphatereductase M2 subunit phosphorylation at residue serine 20 in canonicalWnt signal transduction.";
Tang L.-Y., Deng N., Wang L.-S., Dai J., Wang Z.-L., Jiang X.-S.,Li S.-J., Li L., Sheng Q.-H., Wu D.-Q., Li L., Zeng R.;
Mol. Cell. Proteomics 6:1952-1967(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-90 AND THR-526, 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-517; SER-521; THR-526;THR-622; THR-624; SER-627; THR-785 AND THR-788, 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-1056 AND THR-1071, ANDMASS 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 THR-526; SER-847 ANDSER-851, AND MASS SPECTROMETRY.
"Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column.";
Imami K., Sugiyama N., Kyono Y., Tomita M., Ishihama Y.;
Anal. Sci. 24:161-166(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-526 AND SER-774, ANDMASS SPECTROMETRY.
"Phosphoproteome of resting human platelets.";
Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J.,Schuetz C., Walter U., Gambaryan S., Sickmann A.;
J. Proteome Res. 7:526-534(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-521, 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-75; SER-90; SER-766;SER-774; SER-823 AND SER-824, AND MASS SPECTROMETRY.
"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-548, 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-90; SER-143; SER-165;SER-517; SER-521; THR-526; SER-627; SER-631; THR-649; THR-724;SER-766; SER-774; SER-824; THR-845; SER-851 AND SER-853, 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-517; SER-521; THR-526; SER-548; THR-622;THR-624; SER-627; SER-631; TYR-633; THR-724; SER-766; SER-774;SER-847; SER-849; SER-850; SER-851; SER-853 AND TYR-862, AND MASSSPECTROMETRY.
"Large-scale proteomics analysis of the human kinome.";
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,Mann M., Daub H.;
Mol. Cell. Proteomics 8:1751-1764(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-90; SER-517; SER-521;THR-526; SER-546; SER-548; THR-622; SER-627; SER-631; SER-766 ANDSER-774, AND MASS SPECTROMETRY.
"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-75; SER-90; THR-526;SER-548; SER-627; SER-631; THR-724; SER-774 AND SER-824, 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 THR-526; SER-548; SER-627AND SER-774, AND MASS SPECTROMETRY.
"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-90; SER-517; SER-521;THR-526; SER-627; SER-631; SER-766; SER-774; SER-824 AND THR-1071, ANDMASS 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 THR-526; THR-785 ANDTHR-788, 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 THR-526 AND THR-649, ANDMASS SPECTROMETRY.
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Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures