Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures
Basic Information
Protein Name :  Serine/threonine-protein kinase PRP4 homolog  

UniProtKB / Swiss-Prot ID :  PRP4B_HUMAN

Gene Name (Synonyms) : 
PRPF4B, KIAA0536, PRP4, PRP4H, PRP4K  

Species :  Homo sapiens (Human). 

Subcellular Localization :  Nucleus. 

Protein Function :  Has a role in pre-mRNA splicing. Phosphorylates SF2/ASF. 

Protein Sequence MAAAETQSLREQPEMEDANSEKSINEENGEVSEDQSQNKHSRHKKKKHKHRSKHKKHKHSSEEDKDKKHK...
Predicted Secondary Structure CCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCHHHHCCCCCCCCCCCCCCCCCHHHCCCCCCCHHHCCC...
Protein Variant
LocationDescription
83I -> V (in dbSNP:rs9503893). VAR_046969
584I -> V. VAR_047798
658F -> L (in a breast cancer sample;somatic mutation).
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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.---MAAAET
---CCCCCC
27.04UniProtKB
Link-
6PhosphothreonineAAAETQSLR
CCCCCCCCC
20.80HPRD
Link-
6Phosphothreonine.AAAETQSLR
CCCCCCCCC
20.80UniProtKB
Link-
8PhosphoserineAETQSLREQ
CCCCCCCCC
36.49HPRD
Link-
8Phosphoserine.AETQSLREQ
CCCCCCCCC
36.49UniProtKB
Link-
20PhosphoserineEDANSEKSI
CCCCCCCCC
48.39HPRD
Link-
20PhosphoserineEDANSEKSI
CCCCCCCCC
48.39HPRD
Link-
20PhosphoserineEDANSEKSI
CCCCCCCCC
48.39PhosphoELM
Link-
20PhosphoserineEDANSEKSI
CCCCCCCCC
48.39Phosphositeplus
Link-
20PhosphoserineEDANSEKSI
CCCCCCCCC
48.39SysPTM
Link-
20Phosphoserine.EDANSEKSI
CCCCCCCCC
48.39UniProtKB
Link-
23PhosphoserineNSEKSINEE
CCCCCCCCC
26.96HPRD
Link-
23PhosphoserineNSEKSINEE
CCCCCCCCC
26.96HPRD
Link-
23PhosphoserineNSEKSINEE
CCCCCCCCC
26.96PhosphoELM
Link-
23PhosphoserineNSEKSINEE
CCCCCCCCC
26.96Phosphositeplus
Link-
23PhosphoserineNSEKSINEE
CCCCCCCCC
26.96SysPTM
Link-
23Phosphoserine.NSEKSINEE
CCCCCCCCC
26.96UniProtKB
Link-
32PhosphoserineNGEVSEDQS
CCCCCCHHH
31.02HPRD
Link-
32PhosphoserineNGEVSEDQS
CCCCCCHHH
31.02HPRD
Link-
32PhosphoserineNGEVSEDQS
CCCCCCHHH
31.02PhosphoELM
Link-
32PhosphoserineNGEVSEDQS
CCCCCCHHH
31.02Phosphositeplus
Link-
32PhosphoserineNGEVSEDQS
CCCCCCHHH
31.02SysPTM
Link-
32Phosphoserine.NGEVSEDQS
CCCCCCHHH
31.02UniProtKB
Link-
36PhosphoserineSEDQSQNKH
CCHHHHCCC
48.30HPRD
Link-
36PhosphoserineSEDQSQNKH
CCHHHHCCC
48.30HPRD
Link-
36PhosphoserineSEDQSQNKH
CCHHHHCCC
48.30PhosphoELM
Link-
36PhosphoserineSEDQSQNKH
CCHHHHCCC
48.30Phosphositeplus
Link-
36PhosphoserineSEDQSQNKH
CCHHHHCCC
48.30SysPTM
Link-
36Phosphoserine.SEDQSQNKH
CCHHHHCCC
48.30UniProtKB
Link-
87PhosphoserineIIDASDKEG
CCCCCCCCC
45.53HPRD
Link-
87PhosphoserineIIDASDKEG
CCCCCCCCC
45.53PhosphoELM
Link-
87PhosphoserineIIDASDKEG
CCCCCCCCC
45.53Phosphositeplus
Link-
87PhosphoserineIIDASDKEG
CCCCCCCCC
45.53SysPTM
Link-
87Phosphoserine.IIDASDKEG
CCCCCCCCC
45.53UniProtKB
Link-
93PhosphoserineKEGMSPAKR
CCCCCCCCC
32.34HPRD
Link-
93PhosphoserineKEGMSPAKR
CCCCCCCCC
32.34PhosphoELM
Link-
93PhosphoserineKEGMSPAKR
CCCCCCCCC
32.34Phosphositeplus
Link-
93PhosphoserineKEGMSPAKR
CCCCCCCCC
32.34SysPTM
Link-
93Phosphoserine.KEGMSPAKR
CCCCCCCCC
32.34UniProtKB
Link-
131PhosphoserineGKVQSGMGL
HHCCCCCCC
33.46HPRD
Link-
131PhosphoserineGKVQSGMGL
HHCCCCCCC
33.46SysPTM
Link-
140PhosphotyrosineILQGYESGS
CCCCCCCCC
8.25HPRD
Link-
140PhosphotyrosineILQGYESGS
CCCCCCCCC
8.25PhosphoELM
Link-
140PhosphotyrosineILQGYESGS
CCCCCCCCC
8.25Phosphositeplus
Link-
140PhosphotyrosineILQGYESGS
CCCCCCCCC
8.25SysPTM
Link-
140Phosphotyrosine.ILQGYESGS
CCCCCCCCC
8.25UniProtKB
Link-
142PhosphoserineQGYESGSEE
CCCCCCCCC
38.85HPRD
Link-
142PhosphoserineQGYESGSEE
CCCCCCCCC
38.85PhosphoELM
Link-
142PhosphoserineQGYESGSEE
CCCCCCCCC
38.85Phosphositeplus
Link-
142PhosphoserineQGYESGSEE
CCCCCCCCC
38.85SysPTM
Link-
142Phosphoserine.QGYESGSEE
CCCCCCCCC
38.85UniProtKB
Link-
144PhosphoserineYESGSEEEG
CCCCCCCCC
51.63HPRD
Link-
144PhosphoserineYESGSEEEG
CCCCCCCCC
51.63PhosphoELM
Link-
144PhosphoserineYESGSEEEG
CCCCCCCCC
51.63Phosphositeplus
Link-
144PhosphoserineYESGSEEEG
CCCCCCCCC
51.63SysPTM
Link-
144Phosphoserine.YESGSEEEG
CCCCCCCCC
51.63UniProtKB
Link-
239PhosphoserineQARKSKSPT
HHHHHCCCC
32.58HPRD
Link-
239PhosphoserineQARKSKSPT
HHHHHCCCC
32.58PhosphoELM
Link-
239PhosphoserineQARKSKSPT
HHHHHCCCC
32.58Phosphositeplus
Link-
239PhosphoserineQARKSKSPT
HHHHHCCCC
32.58SysPTM
Link-
239Phosphoserine.QARKSKSPT
HHHHHCCCC
32.58UniProtKB
Link-
241PhosphoserineRKSKSPTLR
HHHCCCCCC
30.15HPRD
Link-
241PhosphoserineRKSKSPTLR
HHHCCCCCC
30.15PhosphoELM
Link-
241PhosphoserineRKSKSPTLR
HHHCCCCCC
30.15Phosphositeplus
Link-
241PhosphoserineRKSKSPTLR
HHHCCCCCC
30.15SysPTM
Link-
241Phosphoserine.RKSKSPTLR
HHHCCCCCC
30.15UniProtKB
Link-
243PhosphothreonineSKSPTLRRR
HCCCCCCCC
39.73HPRD
Link-
243PhosphothreonineSKSPTLRRR
HCCCCCCCC
39.73Phosphositeplus
Link-
257PhosphoserineGKARSPTDD
CCCCCCCCC
36.69HPRD
Link-
257PhosphoserineGKARSPTDD
CCCCCCCCC
36.69PhosphoELM
Link-
257PhosphoserineGKARSPTDD
CCCCCCCCC
36.69Phosphositeplus
Link-
257PhosphoserineGKARSPTDD
CCCCCCCCC
36.69SysPTM
Link-
257Phosphoserine.GKARSPTDD
CCCCCCCCC
36.69UniProtKB
Link-
259PhosphothreonineARSPTDDKV
CCCCCCCCC
59.06HPRD
Link-
259PhosphothreonineARSPTDDKV
CCCCCCCCC
59.06PhosphoELM
Link-
259PhosphothreonineARSPTDDKV
CCCCCCCCC
59.06Phosphositeplus
Link-
259PhosphothreonineARSPTDDKV
CCCCCCCCC
59.06SysPTM
Link-
277PhosphoserineDRKKSPIIN
CCCCCCCCC
25.11HPRD
Link-
277PhosphoserineDRKKSPIIN
CCCCCCCCC
25.11PhosphoELM
Link-
277PhosphoserineDRKKSPIIN
CCCCCCCCC
25.11Phosphositeplus
Link-
277PhosphoserineDRKKSPIIN
CCCCCCCCC
25.11SysPTM
Link-
277Phosphoserine.DRKKSPIIN
CCCCCCCCC
25.11UniProtKB
Link-
283PhosphoserineIINESRSRD
CCCCCCCCC
30.94HPRD
Link-
283PhosphoserineIINESRSRD
CCCCCCCCC
30.94Phosphositeplus
Link-
283PhosphoserineIINESRSRD
CCCCCCCCC
30.94SysPTM
Link-
292PhosphoserineRGKKSRSPV
CCCCCCCCC
41.29HPRD
Link-
292PhosphoserineRGKKSRSPV
CCCCCCCCC
41.29PhosphoELM
Link-
292PhosphoserineRGKKSRSPV
CCCCCCCCC
41.29Phosphositeplus
Link-
292PhosphoserineRGKKSRSPV
CCCCCCCCC
41.29SysPTM
Link-
292Phosphoserine.RGKKSRSPV
CCCCCCCCC
41.29UniProtKB
Link-
294PhosphoserineKKSRSPVDL
CCCCCCCCC
36.04HPRD
Link-
294PhosphoserineKKSRSPVDL
CCCCCCCCC
36.04PhosphoELM
Link-
294PhosphoserineKKSRSPVDL
CCCCCCCCC
36.04Phosphositeplus
Link-
294PhosphoserineKKSRSPVDL
CCCCCCCCC
36.04SysPTM
Link-
294Phosphoserine.KKSRSPVDL
CCCCCCCCC
36.04UniProtKB
Link-
328PhosphoserineKPIKSPSKD
CCCCCCCCC
34.82HPRD
Link-
328PhosphoserineKPIKSPSKD
CCCCCCCCC
34.82PhosphoELM
Link-
328PhosphoserineKPIKSPSKD
CCCCCCCCC
34.82Phosphositeplus
Link-
328PhosphoserineKPIKSPSKD
CCCCCCCCC
34.82SysPTM
Link-
328Phosphoserine.KPIKSPSKD
CCCCCCCCC
34.82UniProtKB
Link-
330PhosphoserineIKSPSKDAS
CCCCCCCCC
50.70HPRD
Link-
330PhosphoserineIKSPSKDAS
CCCCCCCCC
50.70Phosphositeplus
Link-
349PhosphoserineRPGRSPKRR
HCCCCCCCC
40.46HPRD
Link-
349PhosphoserineRPGRSPKRR
HCCCCCCCC
40.46Phosphositeplus
Link-
354PhosphoserinePKRRSLSPK
CCCCCCCCC
36.91HPRD
Link-
354PhosphoserinePKRRSLSPK
CCCCCCCCC
36.91HPRD
Link-
354PhosphoserinePKRRSLSPK
CCCCCCCCC
36.91PhosphoELM
Link-
354PhosphoserinePKRRSLSPK
CCCCCCCCC
36.91Phosphositeplus
Link-
354PhosphoserinePKRRSLSPK
CCCCCCCCC
36.91SysPTM
Link-
354Phosphoserine.PKRRSLSPK
CCCCCCCCC
36.91UniProtKB
Link-
356PhosphoserineRRSLSPKPR
CCCCCCCCC
31.93HPRD
Link-
356PhosphoserineRRSLSPKPR
CCCCCCCCC
31.93HPRD
Link-
356PhosphoserineRRSLSPKPR
CCCCCCCCC
31.93PhosphoELM
Link-
356PhosphoserineRRSLSPKPR
CCCCCCCCC
31.93Phosphositeplus
Link-
356PhosphoserineRRSLSPKPR
CCCCCCCCC
31.93SysPTM
Link-
356Phosphoserine.RRSLSPKPR
CCCCCCCCC
31.93UniProtKB
Link-
358N6-acetyllysineSLSPKPRDK
CCCCCCCCC
49.67HPRD
Link-
358N6-acetyllysineSLSPKPRDK
CCCCCCCCC
49.67Phosphositeplus
Link-
358N6-acetyllysine.SLSPKPRDK
CCCCCCCCC
49.67UniProtKB
Link-
366PhosphoserineKSRRSRSPL
CCCCCCCCC
35.68HPRD
Link-
366PhosphoserineKSRRSRSPL
CCCCCCCCC
35.68HPRD
Link-
366PhosphoserineKSRRSRSPL
CCCCCCCCC
35.68PhosphoELM
Link-
366PhosphoserineKSRRSRSPL
CCCCCCCCC
35.68Phosphositeplus
Link-
366PhosphoserineKSRRSRSPL
CCCCCCCCC
35.68SysPTM
Link-
366Phosphoserine.KSRRSRSPL
CCCCCCCCC
35.68UniProtKB
Link-
368PhosphoserineRRSRSPLLN
CCCCCCCCH
22.58HPRD
Link-
368PhosphoserineRRSRSPLLN
CCCCCCCCH
22.58PhosphoELM
Link-
368PhosphoserineRRSRSPLLN
CCCCCCCCH
22.58Phosphositeplus
Link-
368PhosphoserineRRSRSPLLN
CCCCCCCCH
22.58SysPTM
Link-
368Phosphoserine.RRSRSPLLN
CCCCCCCCH
22.58UniProtKB
Link-
381PhosphoserineKQSKSPSRT
CCCCCCCCC
33.10HPRD
Link-
381PhosphoserineKQSKSPSRT
CCCCCCCCC
33.10Phosphositeplus
Link-
381PhosphoserineKQSKSPSRT
CCCCCCCCC
33.10SysPTM
Link-
381Phosphoserine.KQSKSPSRT
CCCCCCCCC
33.10UniProtKB
Link-
383PhosphoserineSKSPSRTLS
CCCCCCCCC
45.01HPRD
Link-
383PhosphoserineSKSPSRTLS
CCCCCCCCC
45.01Phosphositeplus
Link-
385PhosphothreonineSPSRTLSPG
CCCCCCCCC
35.61HPRD
Link-
385PhosphothreonineSPSRTLSPG
CCCCCCCCC
35.61Phosphositeplus
Link-
385PhosphothreonineSPSRTLSPG
CCCCCCCCC
35.61SysPTM
Link-
385Phosphothreonine.SPSRTLSPG
CCCCCCCCC
35.61UniProtKB
Link-
387PhosphoserineSRTLSPGRR
CCCCCCCCC
25.37HPRD
Link-
387PhosphoserineSRTLSPGRR
CCCCCCCCC
25.37HPRD
Link-
387PhosphoserineSRTLSPGRR
CCCCCCCCC
25.37PhosphoELM
Link-
387PhosphoserineSRTLSPGRR
CCCCCCCCC
25.37Phosphositeplus
Link-
387PhosphoserineSRTLSPGRR
CCCCCCCCC
25.37SysPTM
Link-
387Phosphoserine.SRTLSPGRR
CCCCCCCCC
25.37UniProtKB
Link-
394PhosphoserineRRAKSRSLE
CCCCCCCCC
26.56HPRD
Link-
394PhosphoserineRRAKSRSLE
CCCCCCCCC
26.56Phosphositeplus
Link-
396PhosphoserineAKSRSLERK
CCCCCCCCC
41.49HPRD
Link-
396PhosphoserineAKSRSLERK
CCCCCCCCC
41.49Phosphositeplus
Link-
410PhosphoserineRRRLSSPRT
HHHCCCCCC
36.16HPRD
Link-
410PhosphoserineRRRLSSPRT
HHHCCCCCC
36.16PhosphoELM
Link-
410PhosphoserineRRRLSSPRT
HHHCCCCCC
36.16Phosphositeplus
Link-
410PhosphoserineRRRLSSPRT
HHHCCCCCC
36.16SysPTM
Link-
410Phosphoserine.RRRLSSPRT
HHHCCCCCC
36.16UniProtKB
Link-
411PhosphoserineRRLSSPRTR
HHCCCCCCC
24.00HPRD
Link-
411PhosphoserineRRLSSPRTR
HHCCCCCCC
24.00PhosphoELM
Link-
411PhosphoserineRRLSSPRTR
HHCCCCCCC
24.00Phosphositeplus
Link-
411PhosphoserineRRLSSPRTR
HHCCCCCCC
24.00SysPTM
Link-
411Phosphoserine.RRLSSPRTR
HHCCCCCCC
24.00UniProtKB
Link-
427PhosphoserineRRERSKDAS
CCCCCCCCC
30.09HPRD
Link-
427PhosphoserineRRERSKDAS
CCCCCCCCC
30.09PhosphoELM
Link-
427PhosphoserineRRERSKDAS
CCCCCCCCC
30.09Phosphositeplus
Link-
427PhosphoserineRRERSKDAS
CCCCCCCCC
30.09SysPTM
Link-
427Phosphoserine.RRERSKDAS
CCCCCCCCC
30.09UniProtKB
Link-
431PhosphoserineSKDASPINR
CCCCCCCCC
36.12HPRD
Link-
431PhosphoserineSKDASPINR
CCCCCCCCC
36.12HPRD
Link-
431PhosphoserineSKDASPINR
CCCCCCCCC
36.12PhosphoELM
Link-
431PhosphoserineSKDASPINR
CCCCCCCCC
36.12Phosphositeplus
Link-
431PhosphoserineSKDASPINR
CCCCCCCCC
36.12SysPTM
Link-
431Phosphoserine.SKDASPINR
CCCCCCCCC
36.12UniProtKB
Link-
437PhosphoserineINRWSPTRR
CCCCCCCCC
17.10HPRD
Link-
437PhosphoserineINRWSPTRR
CCCCCCCCC
17.10HPRD
Link-
437PhosphoserineINRWSPTRR
CCCCCCCCC
17.10PhosphoELM
Link-
437PhosphoserineINRWSPTRR
CCCCCCCCC
17.10Phosphositeplus
Link-
437PhosphoserineINRWSPTRR
CCCCCCCCC
17.10SysPTM
Link-
437Phosphoserine.INRWSPTRR
CCCCCCCCC
17.10UniProtKB
Link-
439PhosphothreonineRWSPTRRRS
CCCCCCCCC
31.15HPRD
Link-
439PhosphothreonineRWSPTRRRS
CCCCCCCCC
31.15Phosphositeplus
Link-
439PhosphothreonineRWSPTRRRS
CCCCCCCCC
31.15SysPTM
Link-
443PhosphoserineTRRRSRSPI
CCCCCCCCC
34.99PhosphoELM
Link-
443PhosphoserineTRRRSRSPI
CCCCCCCCC
34.99Phosphositeplus
Link-
445PhosphoserineRRSRSPIRR
CCCCCCCCC
26.40PhosphoELM
Link-
445PhosphoserineRRSRSPIRR
CCCCCCCCC
26.40Phosphositeplus
Link-
458PhosphoserinePLRRSRSPR
CHHHHCCCC
30.58PhosphoELM
Link-
458PhosphoserinePLRRSRSPR
CHHHHCCCC
30.58Phosphositeplus
Link-
460PhosphoserineRRSRSPRRR
HHHCCCCCC
24.81PhosphoELM
Link-
460PhosphoserineRRSRSPRRR
HHHCCCCCC
24.81Phosphositeplus
Link-
518PhosphoserineVEQESSSDD
CCCCCCCCC
34.53HPRD
Link-
518PhosphoserineVEQESSSDD
CCCCCCCCC
34.53PhosphoELM
Link-
518PhosphoserineVEQESSSDD
CCCCCCCCC
34.53Phosphositeplus
Link-
518PhosphoserineVEQESSSDD
CCCCCCCCC
34.53SysPTM
Link-
518Phosphoserine.VEQESSSDD
CCCCCCCCC
34.53UniProtKB
Link-
519PhosphoserineEQESSSDDN
CCCCCCCCC
36.71HPRD
Link-
519PhosphoserineEQESSSDDN
CCCCCCCCC
36.71PhosphoELM
Link-
519PhosphoserineEQESSSDDN
CCCCCCCCC
36.71Phosphositeplus
Link-
519PhosphoserineEQESSSDDN
CCCCCCCCC
36.71SysPTM
Link-
519Phosphoserine.EQESSSDDN
CCCCCCCCC
36.71UniProtKB
Link-
520PhosphoserineQESSSDDNL
CCCCCCCCC
59.26HPRD
Link-
520PhosphoserineQESSSDDNL
CCCCCCCCC
59.26PhosphoELM
Link-
520PhosphoserineQESSSDDNL
CCCCCCCCC
59.26Phosphositeplus
Link-
520PhosphoserineQESSSDDNL
CCCCCCCCC
59.26SysPTM
Link-
520Phosphoserine.QESSSDDNL
CCCCCCCCC
59.26UniProtKB
Link-
554PhosphotyrosineQKYKYLAED
CCHHHCCCH
14.19HPRD
Link-
559PhosphoserineLAEDSNMSV
CCCHHHCCC
26.41HPRD
Link-
562PhosphoserineDSNMSVPSE
HHHCCCCCC
34.82HPRD
Link-
565PhosphoserineMSVPSEPSS
CCCCCCCCC
61.04HPRD
Link-
565PhosphoserineMSVPSEPSS
CCCCCCCCC
61.04PhosphoELM
Link-
565PhosphoserineMSVPSEPSS
CCCCCCCCC
61.04Phosphositeplus
Link-
568PhosphoserinePSEPSSPQS
CCCCCCCCC
51.07HPRD
Link-
569PhosphoserineSEPSSPQSS
CCCCCCCCC
37.36HPRD
Link-
569PhosphoserineSEPSSPQSS
CCCCCCCCC
37.36HPRD
Link-
569PhosphoserineSEPSSPQSS
CCCCCCCCC
37.36PhosphoELM
Link-
569PhosphoserineSEPSSPQSS
CCCCCCCCC
37.36Phosphositeplus
Link-
569PhosphoserineSEPSSPQSS
CCCCCCCCC
37.36SysPTM
Link-
569Phosphoserine.SEPSSPQSS
CCCCCCCCC
37.36UniProtKB
Link-
572PhosphoserineSSPQSSTRT
CCCCCCCCC
36.74HPRD
Link-
573PhosphoserineSPQSSTRTR
CCCCCCCCC
19.36HPRD
Link-
574PhosphothreoninePQSSTRTRS
CCCCCCCCC
41.11HPRD
Link-
574PhosphothreoninePQSSTRTRS
CCCCCCCCC
41.11Phosphositeplus
Link-
576PhosphothreonineSSTRTRSPS
CCCCCCCCC
35.27HPRD
Link-
576PhosphothreonineSSTRTRSPS
CCCCCCCCC
35.27PhosphoELM
Link-
576PhosphothreonineSSTRTRSPS
CCCCCCCCC
35.27Phosphositeplus
Link-
576Phosphothreonine.SSTRTRSPS
CCCCCCCCC
35.27UniProtKB
Link-
578PhosphoserineTRTRSPSPD
CCCCCCCCC
29.17HPRD
Link-
578PhosphoserineTRTRSPSPD
CCCCCCCCC
29.17HPRD
Link-
578PhosphoserineTRTRSPSPD
CCCCCCCCC
29.17PhosphoELM
Link-
578PhosphoserineTRTRSPSPD
CCCCCCCCC
29.17Phosphositeplus
Link-
578PhosphoserineTRTRSPSPD
CCCCCCCCC
29.17SysPTM
Link-
578Phosphoserine.TRTRSPSPD
CCCCCCCCC
29.17UniProtKB
Link-
580PhosphoserineTRSPSPDDI
CCCCCCCCH
42.05HPRD
Link-
580PhosphoserineTRSPSPDDI
CCCCCCCCH
42.05HPRD
Link-
580PhosphoserineTRSPSPDDI
CCCCCCCCH
42.05PhosphoELM
Link-
580PhosphoserineTRSPSPDDI
CCCCCCCCH
42.05Phosphositeplus
Link-
580PhosphoserineTRSPSPDDI
CCCCCCCCH
42.05SysPTM
Link-
580Phosphoserine.TRSPSPDDI
CCCCCCCCH
42.05UniProtKB
Link-
622PhosphoserineQNNGSSQKK
CCCCCCCCC
31.55HPRD
Link-
623PhosphoserineNNGSSQKKL
CCCCCCCCC
47.63HPRD
Link-
636PhosphoserineMFTESDDMF
CCCCCCCCC
35.53Phosphositeplus
Link-
717N6-acetyllysineEVAVKIIRN
EEEEEEECC
23.76HPRD
Link
717N6-acetyllysineEVAVKIIRN
EEEEEEECC
23.76Phosphositeplus
Link
717N6-acetyllysine.EVAVKIIRN
EEEEEEECC
23.76UniProtKB
Link
837PhosphoserineCDFGSASHV
EECCEEEEC
26.96Phosphositeplus
Link
847PhosphothreonineDNDITPYLV
CCCEEEEEE
14.56HPRD
Link
847PhosphothreonineDNDITPYLV
CCCEEEEEE
14.56PhosphoELM
Link
847PhosphothreonineDNDITPYLV
CCCEEEEEE
14.56Phosphositeplus
Link
849PhosphotyrosineDITPYLVSR
CEEEEEECC
15.87HPRD
Link
849PhosphotyrosineDITPYLVSR
CEEEEEECC
15.87HPRD
Link
849PhosphotyrosineDITPYLVSR
CEEEEEECC
15.87PhosphoELM
Link
849PhosphotyrosineDITPYLVSR
CEEEEEECC
15.87Phosphositeplus
Link
849PhosphotyrosineDITPYLVSR
CEEEEEECC
15.87SysPTM
Link
849Phosphotyrosine.DITPYLVSR
CEEEEEECC
15.87UniProtKB
Link
852PhosphoserinePYLVSRFYR
EEEECCCCC
17.68HPRD
Link
852PhosphoserinePYLVSRFYR
EEEECCCCC
17.68PhosphoELM
Link
852PhosphoserinePYLVSRFYR
EEEECCCCC
17.68Phosphositeplus
Link
855PhosphotyrosineVSRFYRAPE
ECCCCCCHH
12.54Phosphositeplus
Link
905N6-acetyllysineAMDLKGKMP
HHHHCCCCC
52.82HPRD
Link
905N6-acetyllysineAMDLKGKMP
HHHHCCCCC
52.82Phosphositeplus
Link
907N6-acetyllysineDLKGKMPNK
HHCCCCCHH
49.99HPRD
Link
907N6-acetyllysineDLKGKMPNK
HHCCCCCHH
49.99Phosphositeplus
Link
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Protein-Protein Interactions
      Interacting Protein      
Interaction type
Source ID
      Resource      
      Pubmed ID      
Domain-Domain Interactions
KLF13_HUMANphysical interaction
phosphorylation
colocalization
physical interaction
physical interaction
EBI-1255904
EBI-1255970
EBI-1
intact17513757
17513757
17513757
17513757
17513757
SFRS1_HUMANin vitroHPRD:09087HPRD11418604
PININ_HUMANin vivo
yeast 2-hybrid
HPRD:09087HPRD12077342
1433G_HUMANin vivoHPRD:09087HPRD15324660
HSPB3_HUMANyeast 2-hybridHPRD:09087HPRD16169070
RPC6_HUMANyeast 2-hybridHPRD:09087HPRD16169070
KLF13_HUMANin vivo
yeast 2-hybrid
HPRD:09087HPRD17513757
NCOR1_HUMANENSP00000283003STRING
KLF13_HUMANENSP00000283003STRING
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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
"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-6 AND SER-8, ACETYLATION[LARGE SCALE ANALYSIS] AT ALA-2, 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-20; SER-23; SER-32; SER-87; SER-93; SER-142 ANDSER-144, AND MASS SPECTROMETRY.
"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-358 AND LYS-717, AND MASSSPECTROMETRY.
Phosphorylation
ReferencePubMed
"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-20; SER-23; SER-32;SER-36; SER-277; SER-294; SER-354; SER-356; SER-366; SER-368; SER-387;SER-431; SER-437; SER-569; SER-578 AND SER-580, AND MASS SPECTROMETRY.
"Time-resolved mass spectrometry of tyrosine phosphorylation sites inthe epidermal growth factor receptor signaling network reveals dynamicmodules.";
Zhang Y., Wolf-Yadlin A., Ross P.L., Pappin D.J., Rush J.,Lauffenburger D.A., White F.M.;
Mol. Cell. Proteomics 4:1240-1250(2005).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-849, AND MASSSPECTROMETRY.
"Immunoaffinity profiling of tyrosine phosphorylation in cancercells.";
Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,Zha X.-M., Polakiewicz R.D., Comb M.J.;
Nat. Biotechnol. 23:94-101(2005).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-849, 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-20; SER-23; SER-32;SER-87; SER-93; SER-239; SER-241; SER-257; SER-277; SER-292; SER-294;SER-328; SER-366; SER-368; SER-381; THR-385; SER-387; SER-410;SER-411; SER-431; SER-437; THR-576; SER-578; SER-580 AND TYR-849, 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 SER-292 AND SER-294, ANDMASS SPECTROMETRY.
"Phosphoproteome analysis of the human mitotic spindle.";
Nousiainen M., Sillje H.H.W., Sauer G., Nigg E.A., Koerner R.;
Proc. Natl. Acad. Sci. U.S.A. 103:5391-5396(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-578, AND MASSSPECTROMETRY.
"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-849, 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-277; SER-366 ANDSER-368, AND MASS SPECTROMETRY.
"Multiple reaction monitoring for robust quantitative proteomicanalysis of cellular signaling networks.";
Wolf-Yadlin A., Hautaniemi S., Lauffenburger D.A., White F.M.;
Proc. Natl. Acad. Sci. U.S.A. 104:5860-5865(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-849, AND MASSSPECTROMETRY.
"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-6 AND SER-8, ACETYLATION[LARGE SCALE ANALYSIS] AT ALA-2, AND MASS SPECTROMETRY.
"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-20; SER-23; SER-32;SER-87; SER-93; TYR-140; SER-142; SER-144; SER-257; SER-277; SER-292;SER-294; SER-427; SER-431; SER-437; SER-518; SER-519; SER-520;SER-569; SER-578; SER-580 AND TYR-849, 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-20; SER-23; SER-32; SER-87; SER-93; SER-142 ANDSER-144, 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-849, 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-20; SER-23; SER-32;TYR-140; SER-142; SER-144; SER-518; SER-519; SER-520; SER-578 ANDSER-580, 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