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Protein

RNA polymerase-associated protein CTR9 homolog

Gene

CTR9

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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 KMT2A/MLL1; it promotes leukemogenesis through association with KMT2A/MLL1-rearranged oncoproteins, such as KMT2A/MLL1-MLLT3/AF9 and KMT2A/MLL1-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 (By similarity).By similarity7 Publications

GO - Molecular functioni

GO - Biological processi

  • blastocyst growth Source: Ensembl
  • cellular response to lipopolysaccharide Source: UniProtKB
  • endodermal cell fate commitment Source: UniProtKB
  • histone H2B ubiquitination Source: UniProtKB
  • histone H3-K4 trimethylation Source: UniProtKB
  • histone monoubiquitination Source: UniProtKB
  • inner cell mass cell differentiation Source: Ensembl
  • interleukin-6-mediated signaling pathway Source: UniProtKB
  • JAK-STAT cascade Source: UniProtKB
  • negative regulation of mRNA polyadenylation Source: UniProtKB
  • negative regulation of myeloid cell differentiation Source: UniProtKB
  • negative regulation of transcription from RNA polymerase II promoter Source: UniProtKB
  • positive regulation of histone H2B ubiquitination Source: UniProtKB
  • positive regulation of histone H3-K4 methylation Source: UniProtKB
  • positive regulation of histone H3-K79 methylation Source: UniProtKB
  • positive regulation of transcription elongation from RNA polymerase II promoter Source: UniProtKB
  • positive regulation of transcription from RNA polymerase II promoter Source: UniProtKB
  • regulation of genetic imprinting Source: Ensembl
  • stem cell population maintenance Source: UniProtKB
  • transcription, DNA-templated Source: UniProtKB-KW
  • trophectodermal cell differentiation Source: Ensembl
  • Wnt signaling pathway Source: UniProtKB-KW
Complete GO annotation...

Keywords - Biological processi

Transcription, Transcription regulation, Wnt signaling pathway

Enzyme and pathway databases

BioCyciZFISH:G66-32640-MONOMER.
ReactomeiR-HSA-112382. Formation of RNA Pol II elongation complex.
R-HSA-112387. Elongation arrest and recovery.
R-HSA-674695. RNA Polymerase II Pre-transcription Events.
R-HSA-75955. RNA Polymerase II Transcription Elongation.

Names & Taxonomyi

Protein namesi
Recommended name:
RNA polymerase-associated protein CTR9 homolog
Alternative name(s):
SH2 domain-binding protein 1
Gene namesi
Name:CTR9
Synonyms:KIAA0155, SH2BP1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 11

Organism-specific databases

HGNCiHGNC:16850. CTR9.

Subcellular locationi

GO - Cellular componenti

  • Cdc73/Paf1 complex Source: UniProtKB
  • nuclear speck Source: UniProtKB-SubCell
  • transcriptionally active chromatin Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Organism-specific databases

DisGeNETi9646.
OpenTargetsiENSG00000198730.
PharmGKBiPA134896774.

Polymorphism and mutation databases

BioMutaiCTR9.
DMDMi74758318.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002315881 – 1173RNA polymerase-associated protein CTR9 homologAdd BLAST1173

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei925PhosphothreonineCombined sources1
Modified residuei932PhosphoserineCombined sources1
Modified residuei941PhosphoserineCombined sources1
Modified residuei943PhosphoserineCombined sources1
Modified residuei970PhosphoserineCombined sources1
Modified residuei1020PhosphoserineCombined sources1
Modified residuei1021PhosphoserineCombined sources1
Modified residuei1039PhosphoserineBy similarity1
Modified residuei1041PhosphoserineBy similarity1
Modified residuei1043PhosphoserineBy similarity1
Modified residuei1081PhosphoserineBy similarity1
Modified residuei1085PhosphoserineBy similarity1
Modified residuei1087PhosphoserineCombined sources1
Modified residuei1097PhosphoserineCombined sources1
Modified residuei1102PhosphoserineCombined sources1

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiQ6PD62.
MaxQBiQ6PD62.
PaxDbiQ6PD62.
PeptideAtlasiQ6PD62.
PRIDEiQ6PD62.

PTM databases

iPTMnetiQ6PD62.
PhosphoSitePlusiQ6PD62.

Miscellaneous databases

PMAP-CutDBQ6PD62.

Expressioni

Tissue specificityi

Widely expressed.1 Publication

Gene expression databases

BgeeiENSG00000198730.
CleanExiHS_CTR9.
ExpressionAtlasiQ6PD62. baseline and differential.
GenevisibleiQ6PD62. HS.

Organism-specific databases

HPAiHPA068122.

Interactioni

Subunit structurei

Component of the mammalian PAF1 complex, which consists of CDC73, PAF1, LEO1, CTR9, RTF1 and WDR61. Interacts with KMT2A/MLL1. Interacts with STAT3 (By similarity).By similarity

Binary interactionsi

WithEntry#Exp.IntActNotes
CDC73Q6P1J917EBI-1019583,EBI-930143
KMT2AQ031645EBI-1019583,EBI-591370
PAF1Q8N7H523EBI-1019583,EBI-2607770
WDR61Q9GZS310EBI-1019583,EBI-358545

GO - Molecular functioni

Protein-protein interaction databases

BioGridi115004. 105 interactors.
DIPiDIP-31693N.
IntActiQ6PD62. 86 interactors.
MINTiMINT-1182366.
STRINGi9606.ENSP00000355013.

Structurei

3D structure databases

ProteinModelPortaliQ6PD62.
SMRiQ6PD62.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Repeati41 – 75TPR 1Add BLAST35
Repeati129 – 162TPR 2Add BLAST34
Repeati163 – 196TPR 3Add BLAST34
Repeati198 – 231TPR 4Add BLAST34
Repeati235 – 268TPR 5Add BLAST34
Repeati306 – 339TPR 6Add BLAST34
Repeati341 – 374TPR 7Add BLAST34
Repeati412 – 444TPR 8Add BLAST33
Repeati451 – 484TPR 9Add BLAST34
Repeati497 – 530TPR 10Add BLAST34
Repeati531 – 564TPR 11Add BLAST34
Repeati566 – 598TPR 12Add BLAST33
Repeati613 – 646TPR 13Add BLAST34
Repeati647 – 680TPR 14Add BLAST34
Repeati681 – 714TPR 15Add BLAST34
Repeati717 – 750TPR 16Add BLAST34

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi844 – 1011Lys-richAdd BLAST168
Compositional biasi904 – 908Poly-Gly5
Compositional biasi933 – 936Poly-Lys4
Compositional biasi956 – 959Poly-Lys4
Compositional biasi1015 – 1172Ser-richAdd BLAST158

Sequence similaritiesi

Contains 16 TPR repeats.PROSITE-ProRule annotation

Keywords - Domaini

Repeat, TPR repeat

Phylogenomic databases

eggNOGiKOG2002. Eukaryota.
COG0457. LUCA.
GeneTreeiENSGT00390000005097.
HOGENOMiHOG000246926.
HOVERGENiHBG081372.
InParanoidiQ6PD62.
KOiK15176.
OMAiRNDPKNL.
OrthoDBiEOG091G01GC.
PhylomeDBiQ6PD62.
TreeFamiTF314342.

Family and domain databases

Gene3Di1.25.40.10. 5 hits.
InterProiIPR031101. Ctr9.
IPR013026. TPR-contain_dom.
IPR011990. TPR-like_helical_dom.
IPR019734. TPR_repeat.
[Graphical view]
PANTHERiPTHR14027:SF2. PTHR14027:SF2. 1 hit.
PfamiPF13181. TPR_8. 3 hits.
[Graphical view]
SMARTiSM00028. TPR. 10 hits.
[Graphical view]
SUPFAMiSSF48452. SSF48452. 3 hits.
PROSITEiPS50005. TPR. 10 hits.
PS50293. TPR_REGION. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q6PD62-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSRGSIEIPL RDTDEVIELD FDQLPEGDEV ISILKQEHTQ LHIWIALALE
60 70 80 90 100
YYKQGKTEEF VKLLEAARID GNLDYRDHEK DQMTCLDTLA AYYVQQARKE
110 120 130 140 150
KNKDNKKDLI TQATLLYTMA DKIIMYDQNH LLGRACFCLL EGDKMDQADA
160 170 180 190 200
QFHFVLNQSP NNIPALLGKA CISFNKKDYR GALAYYKKAL RTNPGCPAEV
210 220 230 240 250
RLGMGHCFVK LNKLEKARLA FSRALELNSK CVGALVGLAV LELNNKEADS
260 270 280 290 300
IKNGVQLLSR AYTIDPSNPM VLNHLANHFF FKKDYSKVQH LALHAFHNTE
310 320 330 340 350
VEAMQAESCY QLARSFHVQE DYDQAFQYYY QATQFASSSF VLPFFGLGQM
360 370 380 390 400
YIYRGDKENA SQCFEKVLKA YPNNYETMKI LGSLYAASED QEKRDIAKGH
410 420 430 440 450
LKKVTEQYPD DVEAWIELAQ ILEQTDIQGA LSAYGTATRI LQEKVQADVP
460 470 480 490 500
PEILNNVGAL HFRLGNLGEA KKYFLASLDR AKAEAEHDEH YYNAISVTTS
510 520 530 540 550
YNLARLYEAM CEFHEAEKLY KNILREHPNY VDCYLRLGAM ARDKGNFYEA
560 570 580 590 600
SDWFKEALQI NQDHPDAWSL IGNLHLAKQE WGPGQKKFER ILKQPSTQSD
610 620 630 640 650
TYSMLALGNV WLQTLHQPTR DREKEKRHQD RALAIYKQVL RNDAKNLYAA
660 670 680 690 700
NGIGAVLAHK GYFREARDVF AQVREATADI SDVWLNLAHI YVEQKQYISA
710 720 730 740 750
VQMYENCLRK FYKHQNTEVV LYLARALFKC GKLQECKQTL LKARHVAPSD
760 770 780 790 800
TVLMFNVALV LQRLATSVLK DEKSNLKEVL NAVKELELAH RYFSYLSKVG
810 820 830 840 850
DKMRFDLALA ATEARQCSDL LSQAQYHVAR ARKQDEEERE LRAKQEQEKE
860 870 880 890 900
LLRQKLLKEQ EEKRLREKEE QKKLLEQRAQ YVEKTKNILM FTGETEATKE
910 920 930 940 950
KKRGGGGGRR SKKGGEFDEF VNDDTDDDLP ISKKKKRRKG SGSEQEGEDE
960 970 980 990 1000
EGGERKKKKR RRHPKGEEGS DDDETENGPK PKKRRPPKAE KKKAPKPERL
1010 1020 1030 1040 1050
PPSMKGKIKS KAIISSSDDS SDEDKLKIAD EGHPRNSNSN SDSDEDEQRK
1060 1070 1080 1090 1100
KCASSESDSD ENQNKSGSEA GSPRRPRRQR SDQDSDSDQP SRKRRPSGSE
1110 1120 1130 1140 1150
QSDNESVQSG RSHSGVSEND SRPASPSAES DHESERGSDN EGSGQGSGNE
1160 1170
SEPEGSNNEA SDRGSEHGSD DSD
Length:1,173
Mass (Da):133,502
Last modified:July 5, 2004 - v1
Checksum:i4B5AC22A5C5573C6
GO

Sequence cautioni

The sequence BAA09925 differs from that shown. Reason: Erroneous initiation.Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D63875 mRNA. Translation: BAA09925.2. Different initiation.
CH471064 Genomic DNA. Translation: EAW68557.1.
CH471064 Genomic DNA. Translation: EAW68558.1.
BC058914 mRNA. Translation: AAH58914.1.
CCDSiCCDS7805.1.
RefSeqiNP_055448.1. NM_014633.4.
UniGeneiHs.725151.

Genome annotation databases

EnsembliENST00000361367; ENSP00000355013; ENSG00000198730.
GeneIDi9646.
KEGGihsa:9646.
UCSCiuc001mja.4. human.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D63875 mRNA. Translation: BAA09925.2. Different initiation.
CH471064 Genomic DNA. Translation: EAW68557.1.
CH471064 Genomic DNA. Translation: EAW68558.1.
BC058914 mRNA. Translation: AAH58914.1.
CCDSiCCDS7805.1.
RefSeqiNP_055448.1. NM_014633.4.
UniGeneiHs.725151.

3D structure databases

ProteinModelPortaliQ6PD62.
SMRiQ6PD62.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi115004. 105 interactors.
DIPiDIP-31693N.
IntActiQ6PD62. 86 interactors.
MINTiMINT-1182366.
STRINGi9606.ENSP00000355013.

PTM databases

iPTMnetiQ6PD62.
PhosphoSitePlusiQ6PD62.

Polymorphism and mutation databases

BioMutaiCTR9.
DMDMi74758318.

Proteomic databases

EPDiQ6PD62.
MaxQBiQ6PD62.
PaxDbiQ6PD62.
PeptideAtlasiQ6PD62.
PRIDEiQ6PD62.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000361367; ENSP00000355013; ENSG00000198730.
GeneIDi9646.
KEGGihsa:9646.
UCSCiuc001mja.4. human.

Organism-specific databases

CTDi9646.
DisGeNETi9646.
GeneCardsiCTR9.
HGNCiHGNC:16850. CTR9.
HPAiHPA068122.
MIMi609366. gene.
neXtProtiNX_Q6PD62.
OpenTargetsiENSG00000198730.
PharmGKBiPA134896774.
HUGEiSearch...
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG2002. Eukaryota.
COG0457. LUCA.
GeneTreeiENSGT00390000005097.
HOGENOMiHOG000246926.
HOVERGENiHBG081372.
InParanoidiQ6PD62.
KOiK15176.
OMAiRNDPKNL.
OrthoDBiEOG091G01GC.
PhylomeDBiQ6PD62.
TreeFamiTF314342.

Enzyme and pathway databases

BioCyciZFISH:G66-32640-MONOMER.
ReactomeiR-HSA-112382. Formation of RNA Pol II elongation complex.
R-HSA-112387. Elongation arrest and recovery.
R-HSA-674695. RNA Polymerase II Pre-transcription Events.
R-HSA-75955. RNA Polymerase II Transcription Elongation.

Miscellaneous databases

ChiTaRSiCTR9. human.
GeneWikiiCTR9.
GenomeRNAii9646.
PMAP-CutDBQ6PD62.
PROiQ6PD62.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000198730.
CleanExiHS_CTR9.
ExpressionAtlasiQ6PD62. baseline and differential.
GenevisibleiQ6PD62. HS.

Family and domain databases

Gene3Di1.25.40.10. 5 hits.
InterProiIPR031101. Ctr9.
IPR013026. TPR-contain_dom.
IPR011990. TPR-like_helical_dom.
IPR019734. TPR_repeat.
[Graphical view]
PANTHERiPTHR14027:SF2. PTHR14027:SF2. 1 hit.
PfamiPF13181. TPR_8. 3 hits.
[Graphical view]
SMARTiSM00028. TPR. 10 hits.
[Graphical view]
SUPFAMiSSF48452. SSF48452. 3 hits.
PROSITEiPS50005. TPR. 10 hits.
PS50293. TPR_REGION. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiCTR9_HUMAN
AccessioniPrimary (citable) accession number: Q6PD62
Secondary accession number(s): D3DQV8, Q15015
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 4, 2006
Last sequence update: July 5, 2004
Last modified: November 30, 2016
This is version 129 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 11
    Human chromosome 11: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.