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Protein Page:
SH2BP1 (human)
p Phosphorylation
ac Acetylation
me Methylation
m1 Mono-methylation
m2 Di-methylation
m3 Tri-methylation
ub Ubiquitination
sm Sumoylation
ne Neddylation
gl O-GlcNAc
ga O-GalNAc
pa Palmitoylation
ad Adenylylation
sn S-Nitrosylation
ca Caspase cleavage
sc Succinylation

Overview
SH2BP1 Component of the PAF1 complex (PAF1C) which has multiple functions during transcription by RNA polymerase II and is implicated in regulation of development and maintenance of embryonic stem cell pluripotency. PAF1C associates with RNA polymerase II through interaction with POLR2A CTD non- phosphorylated and 'Ser-2'- and 'Ser-5'-phosphorylated forms and is involved in transcriptional elongation, acting both indepentently and synergistically with TCEA1 and in cooperation with the DSIF complex and HTATSF1. PAF1C is required for transcription of Hox and Wnt target genes. PAF1C is involved in hematopoiesis and stimulates transcriptional activity of MLL1; it promotes leukemogenesis though association with MLL-rearranged oncoproteins, such as MLL-MLLT3/AF9 and MLL-MLLT1/ENL. PAF1C is involved in histone modifications such as ubiquitination of histone H2B and methylation on histone H3 'Lys-4' (H3K4me3). PAF1C recruits the RNF20/40 E3 ubiquitin-protein ligase complex and the E2 enzyme UBE2A or UBE2B to chromatin which mediate monoubiquitination of 'Lys-120' of histone H2B (H2BK120ub1); UB2A/B-mediated H2B ubiquitination is proposed to be coupled to transcription. PAF1C is involved in mRNA 3' end formation probably through association with cleavage and poly(A) factors. In case of infection by influenza A strain H3N2, PAF1C associates with viral NS1 protein, thereby regulating gene transcription. Required for mono- and trimethylation on histone H3 'Lys-4' (H3K4me3) and dimethylation on histone H3 'Lys-79' (H3K4me3). Required for Hox gene transcription. Required for the trimethylation of histone H3 'Lys-4' (H3K4me3) on genes involved in stem cell pluripotency; this function is synergistic with CXXC1 indicative for an involvement of the SET1 complex. Involved in transcriptional regulation of IL6-responsive genes and in JAK-STAT pathway; may regulate DNA-association of STAT3. Note: This description may include information from UniProtKB.
Protein type: Transcription regulation
Cellular Component: nuclear speck
Molecular Function: protein binding; SH2 domain binding
Biological Process: histone monoubiquitination; negative regulation of myeloid cell differentiation; Wnt receptor signaling pathway; endodermal cell fate commitment; transcription, DNA-dependent; positive regulation of RNA elongation from RNA polymerase II promoter; stem cell maintenance; histone H2B ubiquitination; positive regulation of transcription from RNA polymerase II promoter; negative regulation of transcription from RNA polymerase II promoter; positive regulation of histone H3-K4 methylation; JAK-STAT cascade
Reference #:  Q6PD62 (UniProtKB)
Alt. Names/Synonyms: CTR9; Ctr9, Paf1/RNA polymerase II complex component, homolog (S. cerevisiae); KIAA0155; p150; p150TSP; RNA polymerase-associated protein CTR9 homolog; SH2 domain binding protein 1 (tetratricopeptide repeat containing); SH2 domain-binding protein 1; SH2BP1; TPR-containing, SH2-binding phosphoprotein; TSBP
Gene Symbols: CTR9
Molecular weight: 133,502 Da
Basal Isoelectric point: 6.32  Predict pI for various phosphorylation states
Protein-Specific Antibodies or siRNAs from Cell Signaling Technology® Total Proteins
Select Structure to View Below

SH2BP1

Protein Structure Not Found.


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Modification Sites and Domains Show Modification Legend
Click here to view phosphorylation modifications only

Modification Sites in Parent Protein, Orthologs, and Isoforms Show Modification Legend
 

Show Multiple Sequence Alignment


 SS 

SS: The number of records in which this modification site was determined using site-specific methods. SS methods include amino acid sequencing, site-directed mutagenesis, modification site-specific antibodies, specific MS strategies, etc.


 MS 

MS: The number of records in which this modification site was assigned using ONLY proteomic discovery-mode mass spectrometry.


       human

 
0 2 S5 ___MSRGSIEIPLRD
0 2 K62-ub GKTEEFVkLLEAARI
0 1 Y92-p CLDTLAAyyVQQARK
0 2 Y93-p LDTLAAyyVQQARKE
0 1 Y117-p ITQATLLyTMADKII
0 1 S173 LLGKACISFNKKDYR
0 1 K252-ub NKEADSIkNGVQLLS
0 1 S361-p RGDKENAsQCFEKVL
0 1 K366 NAsQCFEKVLkAYPN
0 1 K369-ub QCFEKVLkAYPNNYE
0 1 K379-ub PNNYETMkILGSLYA
0 1 K393-ub AASEDQEkRDIAKGH
0 1 K472-ub GNLGEAKkYFLASLD
0 1 K544-ub LGAMARDkGNFYEAS
0 1 T597 RILKQPSTQSDTYSM
0 1 S599 LKQPSTQSDTYSMLA
0 1 K645-ub QVLRNDAkNLYAANG
0 1 K660-ub IGAVLAHkGYFREAR
0 1 K770-ub RLATSVLkDEKSNLK
0 1 K784-ub KEVLNAVkELELAHR
0 2 K798-ub RYFSYLSkVGDKMRF
0 1 R804 SkVGDKMRFDLALAA
0 1 T812-p FDLALAAtEARQCSD
0 1 R815 ALAAtEARQCSDLLS
0 1 K844-m2 EERELRAkQEQEkEL
0 1 K844-ub EERELRAkQEQEkEL
0 1 K849-ub RAkQEQEkELLRQKL
0 1 S911-p GGGGGRRsKKGGEFD
0 83 T925-p DEFVNDDtDDDLPIs
0 4 S932-p tDDDLPIsKKKKRRK
0 21 S941-p KKKRRKGsGsEQEGE
0 19 S943-p KRRKGsGsEQEGEDE
0 27 S970-p HPKGEEGsDDDEtEN
0 2 T975-p EGsDDDEtENGPKPK
0 8 S1015-p IKSKAIIsssDDssD
0 7 S1016-p KSKAIIsssDDssDE
0 7 S1017-p SKAIIsssDDssDED
0 14 S1020-p IIsssDDssDEDKLK
0 13 S1021-p IsssDDssDEDKLKI
0 20 S1037-p DEGHPRNsNsNsDsD
0 20 S1039-p GHPRNsNsNsDsDED
0 7 S1041-p PRNsNsNsDsDEDEQ
0 21 S1043-p NsNsNsDsDEDEQRK
0 2 S1059-p CASSESDsDENQNKs
0 2 S1066-p sDENQNKsGsEAGsP
0 3 S1068-p ENQNKsGsEAGsPRR
0 5 S1072-p KsGsEAGsPRRPRRQ
1 18 S1081-p RRPRRQRsDQDsDsD
0 20 S1085-p RQRsDQDsDsDQPsR
0 22 S1087-p RsDQDsDsDQPsRKR
0 13 S1091-p DsDsDQPsRKRRPsG
0 3 S1097-p PsRKRRPsGsEQsDN
0 2 S1099-p RKRRPsGsEQsDNES
0 2 S1102-p RPsGsEQsDNESVQS
0 1 S1112-p ESVQSGRsHSGVsEN
0 1 S1117-p GRsHSGVsENdSRPA
0 1 D1120-ca HSGVsENdSRPASPS
0 3 S1121 SGVsENdSRPASPSA
0 3 S1125 ENdSRPASPSAEsDH
0 4 S1130-p PASPSAEsDHESERG
0 1 S1138-p DHESERGsDNEGSGQ
0 1 S1147-p NEGSGQGsGNEsEPE
0 1 S1151-p GQGsGNEsEPEGsNN
0 1 S1156-p NEsEPEGsNNEASDR
  mouse

 
S5-p ___MSRGsIEIPLRD
K62 GKTEEFVKLLEAARI
Y92 CLDTLAAYYVQQARK
Y93 LDTLAAYYVQQARKE
Y117 ITQATLLYTMADKII
S173 LLGKACISFNKKDYR
K252 NKEADSIKNGVQLLS
S361 RGDKENASQCFEkVL
K366-ub NASQCFEkVLKAYPN
K369 QCFEkVLKAYPNNYE
K379 PNNYETMKILGSLYA
K393 AASEDQEKRDIAKGH
K472 GNLGEAKKYFLASLD
K544 LGAMARDKGNFYEAS
T597-p RILKQPAtQsDTYSM
S599-p LKQPAtQsDTYSMLA
K645 QVLRNDAKNLYAANG
K660 IGAVLAHKGYFREAR
K770 RLATSVLKDEKSNLK
K784 KEVLNAVKELELAHR
K798 RYFSYLSKVGDKMrF
R804-m2 SKVGDKMrFDLALAA
S812 FDLALAASEArQCSD
R815-m2 ALAASEArQCSDLLS
K844 EERELRAKQEQEKEL
K844 EERELRAKQEQEKEL
K849 RAKQEQEKELLRQKL
S911 GGGGGRRSKKGGEFD
T925-p DEFVNDDtDDDLPVs
S932-p tDDDLPVsKKKKRRK
S941-p KKKRRKGsGsEQEGE
S943-p KRRKGsGsEQEGEEE
S970-p PPKGEEGsEEEEtEN
T975-p EGsEEEEtENGPKPK
S1015-p IKSKAIIsssDDssD
S1016-p KSKAIIsssDDssDE
S1017-p SKAIIsssDDssDED
S1020-p IIsssDDssDEDKLK
S1021-p IsssDDssDEDKLKI
S1037-p DEGHPRNsNsDsDDD
S1039-p GHPRNsNsDsDDDER
- gap
S1041-p PRNsNsDsDDDERPN
S1057-p RASSESDsDDNQNKS
S1064 sDDNQNKSGsEAGsP
S1066-p DNQNKSGsEAGsPRR
S1070-p KSGsEAGsPRRSGRQ
S1079-p RRSGRQEsDEDsDsD
S1083-p RQEsDEDsDsDQPSR
S1085-p EsDEDsDsDQPSRKR
S1089 DsDsDQPSRKRRRSG
S1095 PSRKRRRSGSEQSDN
S1097 RKRRRSGSEQSDNES
S1100 RRSGSEQSDNESVQS
S1110 ESVQSGRSPSGASEN
S1115 GRSPSGASENENDsR
D1120 GASENENDsRPAsPS
S1121-p ASENENDsRPAsPSA
S1125-p ENDsRPAsPSAEsDH
S1130-p PAsPSAEsDHESEQG
S1138 DHESEQGSDNEGSGQ
S1147 NEGSGQGSGNESEPE
S1151 GQGSGNESEPEGSNN
S1156 NESEPEGSNNEASDR
  rat

 
S5 ___MSRGSIEIPLRD
K62 GKTEEFVKLLEAARI
Y92 CLDTLAAYYVQQARK
Y93 LDTLAAYYVQQARKE
Y117 ITQATLLYTMADKII
S173-p LLGKACIsFNKKDYR
K252 NKEADSIKNGVQLLS
S361 RGDKENASQCFEKVL
K366 NASQCFEKVLKAYPN
K369 QCFEKVLKAYPNNYE
K379 PNNYETMKILGSLYA
K393 AASEDQEKRDIAKGH
K472 GNLGEAKKYFLASLD
K544 LGAMARDKGNFYEAS
A567 INQDHPDAWSLIGNL
S599 LKQPATQSDTYSMLA
K645 QVLRNDAKNLYAANG
K660 IGAVLAHKGYFREAR
K770 RLATSVLKDEKSNLK
K784 KEVLNAVKELELAHR
K798 RYFSYLSKVGDKMRF
R804 SKVGDKMRFDLALAA
S812 FDLALAASEARQCSD
R815 ALAASEARQCSDLLS
K844 EERELRAKQEQEKEL
K844 EERELRAKQEQEKEL
K849 RAKQEQEKELLRQKL
S911 GGGGGRRSKKGGEFD
T925-p DEFVNDDtDDDLPIS
S932 tDDDLPISKKKKKRK
S941-p KKKKRKGsGsEQEGE
S943-p KKRKGsGsEQEGEEE
S970-p PPKGEEGsDDDETEN
T975 EGsDDDETENGPKPK
S1015 IKSKAIISSSDDssD
S1016 KSKAIISSSDDssDE
S1017 SKAIISSSDDssDED
S1020-p IISSSDDssDEDKLK
S1021-p ISSSDDssDEDKLKI
S1037-p DEGHPRNsNsDsDDD
S1039-p GHPRNsNsDsDDDER
- gap
S1041-p PRNsNsDsDDDERPN
S1057-p RASSESDsDDNQNKS
S1064 sDDNQNKSGSEAGsP
S1066 DNQNKSGSEAGsPRR
S1070-p KSGSEAGsPRRSGRQ
S1079 RRSGRQESDEDsDSD
S1083-p RQESDEDsDSDQPSR
S1085 ESDEDsDSDQPSRKR
S1089 DsDSDQPSRKRRRsG
S1095-p PSRKRRRsGSEQSDN
S1097 RKRRRsGSEQSDNES
S1100 RRsGSEQSDNESAQS
S1110 ESAQSGRSPSGGSEN
S1115 GRSPSGGSENENDSR
D1120 GGSENENDSRPVSPS
S1121 GSENENDSRPVSPSA
S1125 ENDSRPVSPSAESDH
S1130 PVSPSAESDHESEQG
S1138 DHESEQGSDNEGSGQ
S1147 NEGSGQGSGNESEPE
S1151 GQGSGNESEPEGSNN
S1156 NESEPEGSNNEASDR
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