UniProtKB - Q6PD62 (CTR9_HUMAN)

BLAST

>sp|Q6PD62|CTR9_HUMAN RNA polymerase-associated protein CTR9 homolog OS=Homo sapiens OX=9606 GN=CTR9 PE=1 SV=1
MSRGSIEIPLRDTDEVIELDFDQLPEGDEVISILKQEHTQLHIWIALALEYYKQGKTEEF
VKLLEAARIDGNLDYRDHEKDQMTCLDTLAAYYVQQARKEKNKDNKKDLITQATLLYTMA
DKIIMYDQNHLLGRACFCLLEGDKMDQADAQFHFVLNQSPNNIPALLGKACISFNKKDYR
GALAYYKKALRTNPGCPAEVRLGMGHCFVKLNKLEKARLAFSRALELNSKCVGALVGLAV
LELNNKEADSIKNGVQLLSRAYTIDPSNPMVLNHLANHFFFKKDYSKVQHLALHAFHNTE
VEAMQAESCYQLARSFHVQEDYDQAFQYYYQATQFASSSFVLPFFGLGQMYIYRGDKENA
SQCFEKVLKAYPNNYETMKILGSLYAASEDQEKRDIAKGHLKKVTEQYPDDVEAWIELAQ
ILEQTDIQGALSAYGTATRILQEKVQADVPPEILNNVGALHFRLGNLGEAKKYFLASLDR
AKAEAEHDEHYYNAISVTTSYNLARLYEAMCEFHEAEKLYKNILREHPNYVDCYLRLGAM
ARDKGNFYEASDWFKEALQINQDHPDAWSLIGNLHLAKQEWGPGQKKFERILKQPSTQSD
TYSMLALGNVWLQTLHQPTRDREKEKRHQDRALAIYKQVLRNDAKNLYAANGIGAVLAHK
GYFREARDVFAQVREATADISDVWLNLAHIYVEQKQYISAVQMYENCLRKFYKHQNTEVV
LYLARALFKCGKLQECKQTLLKARHVAPSDTVLMFNVALVLQRLATSVLKDEKSNLKEVL
NAVKELELAHRYFSYLSKVGDKMRFDLALAATEARQCSDLLSQAQYHVARARKQDEEERE
LRAKQEQEKELLRQKLLKEQEEKRLREKEEQKKLLEQRAQYVEKTKNILMFTGETEATKE
KKRGGGGGRRSKKGGEFDEFVNDDTDDDLPISKKKKRRKGSGSEQEGEDEEGGERKKKKR
RRHPKGEEGSDDDETENGPKPKKRRPPKAEKKKAPKPERLPPSMKGKIKSKAIISSSDDS
SDEDKLKIADEGHPRNSNSNSDSDEDEQRKKCASSESDSDENQNKSGSEAGSPRRPRRQR
SDQDSDSDQPSRKRRPSGSEQSDNESVQSGRSHSGVSENDSRPASPSAESDHESERGSDN
EGSGQGSGNESEPEGSNNEASDRGSEHGSDDSD

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History
Entry version 147 (07 Nov 2018)
Sequence version 1 (05 Jul 2004)
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Protein

RNA polymerase-associated protein CTR9 homolog

Gene

CTR9

Organism

Homo sapiens (Human)

Status

Reviewed-Annotation score: -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

RNA polymerase II complex binding
Source: GO_Central
Inferred from biological aspect of ancestorⁱ
- 21873635
SH2 domain binding Source: Ensembl

View the complete GO annotation on QuickGO ...

GO - Biological processⁱ

blastocyst growth Source: Ensembl
blastocyst hatching Source: Ensembl
cellular response to lipopolysaccharide Source: UniProtKB
endodermal cell fate commitment Source: UniProtKB
histone H2B ubiquitination
Source: UniProtKB
Inferred from direct assayⁱ
- 16307923
histone H3-K4 trimethylation
Source: UniProtKB
Inferred from mutant phenotypeⁱ
- 16024656
histone monoubiquitination
Source: UniProtKB
Inferred from direct assayⁱ
- 16307923
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
Inferred from mutant phenotypeⁱ
- 19575011
negative regulation of myeloid cell differentiation
Source: UniProtKB
Inferred from direct assayⁱ
- 20541477
negative regulation of transcription by RNA polymerase II Source: UniProtKB
positive regulation of histone H2B ubiquitination
Source: UniProtKB
Inferred from mutant phenotypeⁱ
- 19575011
positive regulation of histone H3-K4 methylation
Source: UniProtKB
Inferred from mutant phenotypeⁱ
- 16024656
positive regulation of histone H3-K79 methylation
Source: UniProtKB
Inferred from mutant phenotypeⁱ
- 16024656
positive regulation of transcription by RNA polymerase II
Source: UniProtKB
Inferred from direct assayⁱ
- 20178742
positive regulation of transcription elongation from RNA polymerase II promoter
Source: UniProtKB
Inferred from direct assayⁱ
- 20178742
protein ubiquitination Source: Reactome
regulation of genetic imprinting Source: Ensembl
regulation of histone H3-K4 methylation
Source: GO_Central
Inferred from biological aspect of ancestorⁱ
- 21873635
stem cell population maintenance
Source: UniProtKB
Inferred from direct assayⁱ
- 19345177
transcription by RNA polymerase II Source: Reactome
transcription elongation from RNA polymerase II promoter Source: Reactome
trophectodermal cell differentiation Source: Ensembl
Wnt signaling pathway Source: UniProtKB-KW

View the complete GO annotation on QuickGO ...

Keywordsⁱ

Biological process	Transcription, Transcription regulation, Wnt signaling pathway

Biological process

Transcription, Transcription regulation, Wnt signaling pathway

Enzyme and pathway databases

Reactomeⁱ	R-HSA-112382 Formation of RNA Pol II elongation complex R-HSA-674695 RNA Polymerase II Pre-transcription Events R-HSA-75955 RNA Polymerase II Transcription Elongation R-HSA-8866654 E3 ubiquitin ligases ubiquitinate target proteins

Reactomeⁱ

R-HSA-112382 Formation of RNA Pol II elongation complex
R-HSA-674695 RNA Polymerase II Pre-transcription Events
R-HSA-75955 RNA Polymerase II Transcription Elongation
R-HSA-8866654 E3 ubiquitin ligases ubiquitinate target proteins

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
Organismⁱ	Homo sapiens (Human)
Taxonomic identifierⁱ	9606 [NCBI]
Taxonomic lineageⁱ	cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Dipnotetrapodomorpha › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Boreoeutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo
Proteomesⁱ	UP000005640 Componentⁱ: Chromosome 11

Organism-specific databases

EuPathDBⁱ	HostDB:ENSG00000198730.7
Human Gene Nomenclature Database More...HGNCⁱ	HGNC:16850 CTR9
MIMⁱ	609366 gene
neXtProtⁱ	NX_Q6PD62

Keywords - Cellular componentⁱ

Nucleus

Pathology & Biotechⁱ

Organism-specific databases

DisGeNET More...DisGeNETⁱ	9646
Open Targets More...OpenTargetsⁱ	ENSG00000198730
PharmGKBⁱ	PA134896774

Polymorphism and mutation databases

BioMutaⁱ	CTR9
DMDMⁱ	74758318

PTM / Processingⁱ

Molecule processing

Feature key	Position(s)	DescriptionActions	Graphical view	Length
ChainⁱPRO_0000231588	1 – 1173	RNA polymerase-associated protein CTR9 homologAdd BLAST		1173

Amino acid modifications

Feature key	Position(s)	DescriptionActions	Length
Modified residueⁱ	925	PhosphothreonineCombined sources	1
Modified residueⁱ	932	PhosphoserineCombined sources	1
Modified residueⁱ	941	PhosphoserineCombined sources	1
Modified residueⁱ	943	PhosphoserineCombined sources	1
Modified residueⁱ	970	PhosphoserineCombined sources	1
Modified residueⁱ	1020	PhosphoserineCombined sources	1
Modified residueⁱ	1021	PhosphoserineCombined sources	1
Modified residueⁱ	1039	PhosphoserineBy similarity	1
Modified residueⁱ	1041	PhosphoserineBy similarity	1
Modified residueⁱ	1043	PhosphoserineBy similarity	1
Modified residueⁱ	1081	PhosphoserineBy similarity	1
Modified residueⁱ	1085	PhosphoserineBy similarity	1
Modified residueⁱ	1087	PhosphoserineCombined sources	1
Modified residueⁱ	1097	PhosphoserineCombined sources	1
Modified residueⁱ	1102	PhosphoserineCombined sources	1

Keywords - PTMⁱ

Phosphoprotein

Proteomic databases

EPDⁱ	Q6PD62
MaxQB - The MaxQuant DataBase More...MaxQBⁱ	Q6PD62
PaxDbⁱ	Q6PD62
PeptideAtlas More...PeptideAtlasⁱ	Q6PD62
PRIDEⁱ	Q6PD62
ProteomicsDBⁱ	67068

PTM databases

iPTMnetⁱ	Q6PD62
PhosphoSitePlusⁱ	Q6PD62

Miscellaneous databases

PMAP-CutDBⁱ	Q6PD62

PMAP-CutDBⁱ

Q6PD62

Expressionⁱ

Tissue specificityⁱ

Widely expressed.1 Publication

Gene expression databases

Bgeeⁱ	ENSG00000198730 Expressed in 242 organ(s), highest expression level in caput epididymis
CleanExⁱ	HS_CTR9
ExpressionAtlasⁱ	Q6PD62 baseline and differential
Genevisibleⁱ	Q6PD62 HS

Organism-specific databases

Human Protein Atlas More...HPAⁱ	HPA061027 HPA068122

HPAⁱ

HPA061027
HPA068122

Interactionⁱ

Subunit structureⁱ

Component of the PAF1 complex, which consists of CDC73, PAF1, LEO1, CTR9, RTF1 and WDR61 (PubMed:16024656, PubMed:19952111, PubMed:20178742). The PAF1 complex interacts with PHF5A (By similarity). Interacts with KMT2A/MLL1 (PubMed:20541477). Interacts with STAT3. Interacts with SETD5.By similarity4 Publications

Binary interactionsⁱ

With	Entry	#Exp.	IntAct
CDC73	Q6P1J9	19	EBI-1019583,EBI-930143
KMT2A	Q03164	5	EBI-1019583,EBI-591370
PAF1	Q8N7H5	23	EBI-1019583,EBI-2607770
WDR61	Q9GZS3	10	EBI-1019583,EBI-358545

GO - Molecular functionⁱ

RNA polymerase II complex binding
Source: GO_Central
Inferred from biological aspect of ancestorⁱ
- 21873635
SH2 domain binding Source: Ensembl

View the complete GO annotation on QuickGO ...

Protein-protein interaction databases

BioGridⁱ	115004, 110 interactors
CORUMⁱ	Q6PD62
Database of interacting proteins More...DIPⁱ	DIP-31693N
IntActⁱ	Q6PD62, 92 interactors
Molecular INTeraction database More...MINTⁱ	Q6PD62
STRINGⁱ	9606.ENSP00000355013

Structureⁱ

Secondary structure

Legend: HelixTurnBeta strandPDB Structure known for this area

Feature key	Position(s)	DescriptionActions	Length
Beta strandⁱ	302 – 304	Combined sources	3
Helixⁱ	307 – 318	Combined sources	12
Helixⁱ	322 – 335	Combined sources	14
Helixⁱ	337 – 339	Combined sources	3
Helixⁱ	341 – 354	Combined sources	14
Helixⁱ	357 – 370	Combined sources	14
Helixⁱ	375 – 388	Combined sources	14
Helixⁱ	391 – 407	Combined sources	17
Helixⁱ	412 – 424	Combined sources	13
Helixⁱ	430 – 447	Combined sources	18
Helixⁱ	451 – 464	Combined sources	14
Helixⁱ	467 – 479	Combined sources	13
Turnⁱ	482 – 486	Combined sources	5
Helixⁱ	491 – 493	Combined sources	3
Helixⁱ	494 – 509	Combined sources	16
Helixⁱ	513 – 526	Combined sources	14
Helixⁱ	531 – 543	Combined sources	13
Helixⁱ	547 – 560	Combined sources	14
Helixⁱ	565 – 577	Combined sources	13
Helixⁱ	581 – 591	Combined sources	11
Beta strandⁱ	592 – 594	Combined sources	3
Beta strandⁱ	597 – 600	Combined sources	4
Helixⁱ	601 – 615	Combined sources	15
Helixⁱ	620 – 626	Combined sources	7
Helixⁱ	628 – 640	Combined sources	13
Helixⁱ	647 – 659	Combined sources	13
Turnⁱ	660 – 662	Combined sources	3
Helixⁱ	663 – 675	Combined sources	13
Helixⁱ	681 – 693	Combined sources	13
Helixⁱ	697 – 711	Combined sources	15
Helixⁱ	719 – 725	Combined sources	7
Beta strandⁱ	728 – 731	Combined sources	4
Helixⁱ	739 – 743	Combined sources	5
Beta strandⁱ	748 – 750	Combined sources	3
Helixⁱ	756 – 772	Combined sources	17
Helixⁱ	779 – 796	Combined sources	18
Helixⁱ	809 – 890	Combined sources	82

Show more details

3D structure databases

ProteinModelPortalⁱ	Q6PD62
SMRⁱ	Q6PD62
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Family & Domainsⁱ

Domains and Repeats

Feature key	Position(s)	DescriptionActions	Length
Repeatⁱ	41 – 75	TPR 1Add BLAST	35
Repeatⁱ	129 – 162	TPR 2Add BLAST	34
Repeatⁱ	163 – 196	TPR 3Add BLAST	34
Repeatⁱ	198 – 231	TPR 4Add BLAST	34
Repeatⁱ	235 – 268	TPR 5Add BLAST	34
Repeatⁱ	306 – 339	TPR 6Add BLAST	34
Repeatⁱ	341 – 374	TPR 7Add BLAST	34
Repeatⁱ	412 – 444	TPR 8Add BLAST	33
Repeatⁱ	451 – 484	TPR 9Add BLAST	34
Repeatⁱ	497 – 530	TPR 10Add BLAST	34
Repeatⁱ	531 – 564	TPR 11Add BLAST	34
Repeatⁱ	566 – 598	TPR 12Add BLAST	33
Repeatⁱ	613 – 646	TPR 13Add BLAST	34
Repeatⁱ	647 – 680	TPR 14Add BLAST	34
Repeatⁱ	681 – 714	TPR 15Add BLAST	34
Repeatⁱ	717 – 750	TPR 16Add BLAST	34

Compositional bias

Feature key	Position(s)	DescriptionActions	Length
Compositional biasⁱ	844 – 1011	Lys-richAdd BLAST	168
Compositional biasⁱ	904 – 908	Poly-Gly	5
Compositional biasⁱ	933 – 936	Poly-Lys	4
Compositional biasⁱ	956 – 959	Poly-Lys	4
Compositional biasⁱ	1015 – 1172	Ser-richAdd BLAST	158

Keywords - Domainⁱ

Repeat, TPR repeat

Phylogenomic databases

eggNOGⁱ	KOG2002 Eukaryota COG0457 LUCA
Ensembl GeneTree More...GeneTreeⁱ	ENSGT00390000005097
HOGENOMⁱ	HOG000246926
HOVERGENⁱ	HBG081372
InParanoidⁱ	Q6PD62
KEGG Orthology (KO) More...KOⁱ	K15176
OMAⁱ	MLAAHYV
Database of Orthologous Groups More...OrthoDBⁱ	EOG091G01GC
PhylomeDBⁱ	Q6PD62
TreeFamⁱ	TF314342

Family and domain databases

Gene3Dⁱ	1.25.40.10, 3 hits
InterProⁱ	View protein in InterPro IPR031101 Ctr9 IPR013026 TPR-contain_dom IPR011990 TPR-like_helical_dom_sf IPR019734 TPR_repeat
PANTHERⁱ	PTHR14027 PTHR14027, 1 hit
Pfam protein domain database More...Pfamⁱ	View protein in Pfam PF13181 TPR_8, 4 hits
SMARTⁱ	View protein in SMART SM00028 TPR, 10 hits
SUPFAMⁱ	SSF48452 SSF48452, 3 hits
PROSITEⁱ	View protein in PROSITE PS50005 TPR, 10 hits PS50293 TPR_REGION, 1 hit

Sequence (1+)ⁱ

Sequence statusⁱ: Complete.

This entry has 1 described isoform and 2 potential isoforms that are computationally mapped.Show all Align All

Q6PD62-1 [UniParc]FASTA Add to basket

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        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

Computationally mapped potential isoform sequencesⁱ

There are 2 potential isoforms mapped to this entry.BLAST Align Show all Add to basket

Entry	Entry name	Protein names	Gene names	Length	Annotation

H0YCE8	H0YCE8_HUMAN	RNA polymerase-associated protein C... RNA polymerase-associated protein CTR9 homolog	CTR9	300	Annotation score:
A0A2R8Y3S3	A0A2R8Y3S3_HUMAN	RNA polymerase-associated protein C... RNA polymerase-associated protein CTR9 homolog	CTR9	52	Annotation score:

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
The Consensus CDS (CCDS) project More...CCDSⁱ	CCDS7805.1
NCBI Reference Sequences More...RefSeqⁱ	NP_055448.1, NM_014633.4
UniGeneⁱ	Hs.725151

Genome annotation databases

Ensemblⁱ	ENST00000361367; ENSP00000355013; ENSG00000198730
GeneIDⁱ	9646
KEGGⁱ	hsa:9646
UCSC genome browser More...UCSCⁱ	uc001mja.4 human

Similar proteinsⁱ

90% Identity
50% Identity

Protein	Similar proteins		Species	Score	Length	Source
Q6PD62	RNA polymerase-associated protein CTR9 homolog		MOUSE		1173	UniRef90_Q6PD62
RNA polymerase-associated protein CTR9-like protein		wild yak		1185
RNA polymerase-associated protein CTR9 homolog		BALAS		1179
RNA polymerase-associated protein CTR9 homolog		HETGA		1179
RNA polymerase-associated protein CTR9 homolog isoform X2		PHYCD		1178
+231

Protein	Similar proteins		Species	Score	Length	Source
Q6PD62	RNA polymerase-associated protein CTR9 homolog		MOUSE		1173	UniRef50_Q6PD62
RNA polymerase-associated protein CTR9-like protein		wild yak		1185
RNA polymerase-associated protein CTR9 homolog		BALAS		1179
RNA polymerase-associated protein CTR9 homolog		HETGA		1179
RNA polymerase-associated protein CTR9 homolog isoform X2		PHYCD		1178
+232

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
CCDSⁱ	CCDS7805.1
RefSeqⁱ	NP_055448.1, NM_014633.4
UniGeneⁱ	Hs.725151

3D structure databases

Select the link destinations: Protein Data Bank Europe More...PDBeⁱ Protein Data Bank RCSB More...RCSB PDBⁱ Protein Data Bank Japan More...PDBjⁱ Links Updated	PDB entry	Method	Resolution (Å)	Chain	Positions	PDBsum
	5ZYQ	X-ray	2.53	A	1-249	[»]
	6GMH	electron microscopy	3.10	Q	301-1173	[»]
ProteinModelPortalⁱ	Q6PD62
SMRⁱ	Q6PD62
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Protein-protein interaction databases

BioGridⁱ	115004, 110 interactors
CORUMⁱ	Q6PD62
DIPⁱ	DIP-31693N
IntActⁱ	Q6PD62, 92 interactors
MINTⁱ	Q6PD62
STRINGⁱ	9606.ENSP00000355013

PTM databases

iPTMnetⁱ	Q6PD62
PhosphoSitePlusⁱ	Q6PD62

Polymorphism and mutation databases

BioMutaⁱ	CTR9
DMDMⁱ	74758318

Proteomic databases

EPDⁱ	Q6PD62
MaxQBⁱ	Q6PD62
PaxDbⁱ	Q6PD62
PeptideAtlasⁱ	Q6PD62
PRIDEⁱ	Q6PD62
ProteomicsDBⁱ	67068

Protocols and materials databases

Structural Biology Knowledgebase	Search...

Structural Biology Knowledgebase

Search...

Genome annotation databases

Ensemblⁱ	ENST00000361367; ENSP00000355013; ENSG00000198730
GeneIDⁱ	9646
KEGGⁱ	hsa:9646
UCSCⁱ	uc001mja.4 human

Organism-specific databases

CTDⁱ	9646
DisGeNETⁱ	9646
EuPathDBⁱ	HostDB:ENSG00000198730.7
GeneCardsⁱ	CTR9
HGNCⁱ	HGNC:16850 CTR9
HPAⁱ	HPA061027 HPA068122
MIMⁱ	609366 gene
neXtProtⁱ	NX_Q6PD62
OpenTargetsⁱ	ENSG00000198730
PharmGKBⁱ	PA134896774
HUGEⁱ	Search...
GenAtlas: human gene database More...GenAtlasⁱ	Search...

Phylogenomic databases

eggNOGⁱ	KOG2002 Eukaryota COG0457 LUCA
GeneTreeⁱ	ENSGT00390000005097
HOGENOMⁱ	HOG000246926
HOVERGENⁱ	HBG081372
InParanoidⁱ	Q6PD62
KOⁱ	K15176
OMAⁱ	MLAAHYV
OrthoDBⁱ	EOG091G01GC
PhylomeDBⁱ	Q6PD62
TreeFamⁱ	TF314342

Enzyme and pathway databases

Reactomeⁱ	R-HSA-112382 Formation of RNA Pol II elongation complex R-HSA-674695 RNA Polymerase II Pre-transcription Events R-HSA-75955 RNA Polymerase II Transcription Elongation R-HSA-8866654 E3 ubiquitin ligases ubiquitinate target proteins

Reactomeⁱ

Miscellaneous databases

ChiTaRSⁱ	CTR9 human
GeneWikiⁱ	CTR9
GenomeRNAiⁱ	9646
PMAP-CutDBⁱ	Q6PD62
Protein Ontology More...PROⁱ	PR:Q6PD62
SOURCEⁱ	Search...

Gene expression databases

Bgeeⁱ	ENSG00000198730 Expressed in 242 organ(s), highest expression level in caput epididymis
CleanExⁱ	HS_CTR9
ExpressionAtlasⁱ	Q6PD62 baseline and differential
Genevisibleⁱ	Q6PD62 HS

Family and domain databases

Gene3Dⁱ	1.25.40.10, 3 hits
InterProⁱ	View protein in InterPro IPR031101 Ctr9 IPR013026 TPR-contain_dom IPR011990 TPR-like_helical_dom_sf IPR019734 TPR_repeat
PANTHERⁱ	PTHR14027 PTHR14027, 1 hit
Pfamⁱ	View protein in Pfam PF13181 TPR_8, 4 hits
SMARTⁱ	View protein in SMART SM00028 TPR, 10 hits
SUPFAMⁱ	SSF48452 SSF48452, 3 hits
PROSITEⁱ	View protein in PROSITE PS50005 TPR, 10 hits PS50293 TPR_REGION, 1 hit
ProtoNetⁱ	Search...

Entry informationⁱ

Entry nameⁱ	CTR9_HUMAN
Accessionⁱ	Q6PD62Primary (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 7, 2018
	This is version 147 of the entry and version 1 of the sequence. See complete history.
Entry statusⁱ	Reviewed (UniProtKB/Swiss-Prot)
Annotation program	Chordata Protein Annotation Program
Disclaimer	Any 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

3D-structure, Complete proteome, Reference proteome

Documents

MIM cross-references
Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
PDB cross-references
Index of Protein Data Bank (PDB) cross-references
Human chromosome 11
Human chromosome 11: entries, gene names and cross-references to MIM

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UniProtKB - Q6PD62 (CTR9_HUMAN)

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RNA polymerase-associated protein CTR9 homolog

CTR9

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<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

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GO - Biological processi

Enzyme and pathway databases

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Gene expression databases

Organism-specific databases

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Secondary structure

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<p>This subsection of the ‘Sequence’ section reports difference(s) between the protein sequence shown in the UniProtKB entry and other available protein sequences derived from the same gene.<p><a href='/help/sequence_caution' target='_top'>More...</a></p>Sequence cautioni

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Genome annotation databases

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Functionⁱ

GO - Molecular functionⁱ

GO - Biological processⁱ

Names & Taxonomyⁱ

Subcellular locationⁱ

Keywords - Cellular componentⁱ

Pathology & Biotechⁱ

PTM / Processingⁱ

Keywords - PTMⁱ

Expressionⁱ

Interactionⁱ

GO - Molecular functionⁱ

Structureⁱ

Family & Domainsⁱ

Keywords - Domainⁱ

Sequence cautionⁱ

Cross-referencesⁱ

Entry informationⁱ

Miscellaneousⁱ

Keywords - Technical termⁱ