Q6PD62 (CTR9_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
RNA polymerase-associated protein CTR9 homolog

Alternative name(s):
SH2 domain-binding protein 1

Gene names

Name:	CTR9
Synonyms:	KIAA0155, SH2BP1

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	1173 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	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 By similarity. Ref.5 Ref.6 Ref.12 Ref.13 Ref.15 Ref.16 Ref.19
Subunit structure	Component of the mammalian PAF1 complex, which consists of CDC73, PAF1, LEO1, CTR9, RTF1 and WDR61. Interacts with MLL. Interacts with STAT3 By similarity. Ref.5 Ref.13 Ref.15 Ref.16
Subcellular location	Nucleus speckle By similarity. Note: Found in speckles By similarity.
Tissue specificity	Widely expressed. Ref.1
Sequence similarities	Contains 16 TPR repeats.
Sequence caution	The sequence BAA09925.2 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
Biological process	Transcription Transcription regulation Wnt signaling pathway
Cellular component	Nucleus
Domain	Repeat TPR repeat
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	JAK-STAT cascade Inferred from sequence or structural similarity. Source: UniProtKB Wnt receptor signaling pathway Inferred from electronic annotation. Source: UniProtKB-KW cellular response to lipopolysaccharide Inferred from sequence or structural similarity. Source: UniProtKB endodermal cell fate commitment Inferred from sequence or structural similarity. Source: UniProtKB histone H2B ubiquitination Inferred from direct assay Ref.6. Source: UniProtKB histone H3-K4 trimethylation Inferred from mutant phenotype Ref.5. Source: UniProtKB histone monoubiquitination Inferred from direct assay Ref.6. Source: UniProtKB interleukin-6-mediated signaling pathway Inferred from sequence or structural similarity. Source: UniProtKB negative regulation of myeloid cell differentiation Inferred from direct assay Ref.15. Source: UniProtKB negative regulation of transcription from RNA polymerase II promoter Inferred from sequence or structural similarity. Source: UniProtKB positive regulation of histone H3-K4 methylation Inferred from mutant phenotype Ref.5. Source: UniProtKB positive regulation of histone H3-K79 methylation Inferred from mutant phenotype Ref.5. Source: UniProtKB positive regulation of transcription elongation from RNA polymerase II promoter Inferred from direct assay Ref.16. Source: UniProtKB positive regulation of transcription from RNA polymerase II promoter Inferred from direct assay Ref.16. Source: UniProtKB stem cell maintenance Inferred from direct assay Ref.12. Source: UniProtKB transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	Cdc73/Paf1 complex Inferred from direct assay Ref.6Ref.16. Source: UniProtKB nuclear speck Inferred from electronic annotation. Source: UniProtKB-SubCell transcriptionally active chromatin Inferred from sequence or structural similarity. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
CDC73	Q6P1J9	15	EBI-1019583,EBI-930143
MLL	Q03164	5	EBI-1019583,EBI-591370
PAF1	Q8N7H5	22	EBI-1019583,EBI-2607770
WDR61	Q9GZS3	9	EBI-1019583,EBI-358545

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 1173	1173	RNA polymerase-associated protein CTR9 homolog		PRO_0000231588
Regions
	Repeat	41 – 75	35	TPR 1
	Repeat	129 – 162	34	TPR 2
	Repeat	163 – 196	34	TPR 3
	Repeat	198 – 231	34	TPR 4
	Repeat	235 – 268	34	TPR 5
	Repeat	306 – 339	34	TPR 6
	Repeat	341 – 374	34	TPR 7
	Repeat	412 – 444	33	TPR 8
	Repeat	451 – 484	34	TPR 9
	Repeat	497 – 530	34	TPR 10
	Repeat	531 – 564	34	TPR 11
	Repeat	566 – 598	33	TPR 12
	Repeat	613 – 646	34	TPR 13
	Repeat	647 – 680	34	TPR 14
	Repeat	681 – 714	34	TPR 15
	Repeat	717 – 750	34	TPR 16
	Compositional bias	844 – 1011	168	Lys-rich
	Compositional bias	904 – 908	5	Poly-Gly
	Compositional bias	933 – 936	4	Poly-Lys
	Compositional bias	956 – 959	4	Poly-Lys
	Compositional bias	1015 – 1172	158	Ser-rich
Amino acid modifications
	Modified residue	925	1	Phosphothreonine Ref.7 Ref.9 Ref.10 Ref.11 Ref.14 Ref.17 Ref.20
	Modified residue	932	1	Phosphoserine Ref.14
	Modified residue	941	1	Phosphoserine Ref.7 Ref.8 Ref.17 Ref.20
	Modified residue	943	1	Phosphoserine Ref.7 Ref.8 Ref.17 Ref.20
	Modified residue	970	1	Phosphoserine Ref.7 Ref.11 Ref.17 Ref.20
	Modified residue	1020	1	Phosphoserine Ref.8 Ref.20
	Modified residue	1021	1	Phosphoserine Ref.8 Ref.20
	Modified residue	1039	1	Phosphoserine By similarity
	Modified residue	1041	1	Phosphoserine By similarity
	Modified residue	1043	1	Phosphoserine By similarity
	Modified residue	1081	1	Phosphoserine By similarity
	Modified residue	1085	1	Phosphoserine By similarity
	Modified residue	1087	1	Phosphoserine By similarity
	Modified residue	1097	1	Phosphoserine Ref.20
	Modified residue	1102	1	Phosphoserine Ref.20

Sequences

	Sequence		Length	Mass (Da)
	Q6PD62 [UniParc]. Last modified July 5, 2004. Version 1. Checksum: 4B5AC22A5C5573C6	FASTA	1,173	133,502
	10 20 30 40 50 60 MSRGSIEIPL RDTDEVIELD FDQLPEGDEV ISILKQEHTQ LHIWIALALE YYKQGKTEEF 70 80 90 100 110 120 VKLLEAARID GNLDYRDHEK DQMTCLDTLA AYYVQQARKE KNKDNKKDLI TQATLLYTMA 130 140 150 160 170 180 DKIIMYDQNH LLGRACFCLL EGDKMDQADA QFHFVLNQSP NNIPALLGKA CISFNKKDYR 190 200 210 220 230 240 GALAYYKKAL RTNPGCPAEV RLGMGHCFVK LNKLEKARLA FSRALELNSK CVGALVGLAV 250 260 270 280 290 300 LELNNKEADS IKNGVQLLSR AYTIDPSNPM VLNHLANHFF FKKDYSKVQH LALHAFHNTE 310 320 330 340 350 360 VEAMQAESCY QLARSFHVQE DYDQAFQYYY QATQFASSSF VLPFFGLGQM YIYRGDKENA 370 380 390 400 410 420 SQCFEKVLKA YPNNYETMKI LGSLYAASED QEKRDIAKGH LKKVTEQYPD DVEAWIELAQ 430 440 450 460 470 480 ILEQTDIQGA LSAYGTATRI LQEKVQADVP PEILNNVGAL HFRLGNLGEA KKYFLASLDR 490 500 510 520 530 540 AKAEAEHDEH YYNAISVTTS YNLARLYEAM CEFHEAEKLY KNILREHPNY VDCYLRLGAM 550 560 570 580 590 600 ARDKGNFYEA SDWFKEALQI NQDHPDAWSL IGNLHLAKQE WGPGQKKFER ILKQPSTQSD 610 620 630 640 650 660 TYSMLALGNV WLQTLHQPTR DREKEKRHQD RALAIYKQVL RNDAKNLYAA NGIGAVLAHK 670 680 690 700 710 720 GYFREARDVF AQVREATADI SDVWLNLAHI YVEQKQYISA VQMYENCLRK FYKHQNTEVV 730 740 750 760 770 780 LYLARALFKC GKLQECKQTL LKARHVAPSD TVLMFNVALV LQRLATSVLK DEKSNLKEVL 790 800 810 820 830 840 NAVKELELAH RYFSYLSKVG DKMRFDLALA ATEARQCSDL LSQAQYHVAR ARKQDEEERE 850 860 870 880 890 900 LRAKQEQEKE LLRQKLLKEQ EEKRLREKEE QKKLLEQRAQ YVEKTKNILM FTGETEATKE 910 920 930 940 950 960 KKRGGGGGRR SKKGGEFDEF VNDDTDDDLP ISKKKKRRKG SGSEQEGEDE EGGERKKKKR 970 980 990 1000 1010 1020 RRHPKGEEGS DDDETENGPK PKKRRPPKAE KKKAPKPERL PPSMKGKIKS KAIISSSDDS 1030 1040 1050 1060 1070 1080 SDEDKLKIAD EGHPRNSNSN SDSDEDEQRK KCASSESDSD ENQNKSGSEA GSPRRPRRQR 1090 1100 1110 1120 1130 1140 SDQDSDSDQP SRKRRPSGSE QSDNESVQSG RSHSGVSEND SRPASPSAES DHESERGSDN 1150 1160 1170 EGSGQGSGNE SEPEGSNNEA SDRGSEHGSD DSD

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Prediction of the coding sequences of unidentified human genes. IV. The coding sequences of 40 new genes (KIAA0121-KIAA0160) deduced by analysis of cDNA clones from human cell line KG-1." Nagase T., Seki N., Tanaka A., Ishikawa K., Nomura N. DNA Res. 2:167-174(1995) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], TISSUE SPECIFICITY. Tissue: Bone marrow.
[2]	Ohara O., Nagase T., Kikuno R., Nomura N. Submitted (AUG-1995) to the EMBL/GenBank/DDBJ databases Cited for: SEQUENCE REVISION.
[3]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Uterus.
[5]	"The human PAF complex coordinates transcription with events downstream of RNA synthesis." Zhu B., Mandal S.S., Pham A.D., Zheng Y., Erdjument-Bromage H., Batra S.K., Tempst P., Reinberg D. Genes Dev. 19:1668-1673(2005) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, IDENTIFICATION IN THE PAF1 COMPLEX.
[6]	"Monoubiquitination of human histone H2B: the factors involved and their roles in HOX gene regulation." Zhu B., Zheng Y., Pham A.-D., Mandal S.S., Erdjument-Bromage H., Tempst P., Reinberg D. Mol. Cell 20:601-611(2005) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[7]	"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks." Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M. Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-925; SER-941; SER-943 AND SER-970, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[8]	"A probability-based approach for high-throughput protein phosphorylation analysis and site localization." Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P. Nat. Biotechnol. 24:1285-1292(2006) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-941; SER-943; SER-1020 AND SER-1021, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[9]	"Phosphorylation analysis of primary human T lymphocytes using sequential IMAC and titanium oxide enrichment." Carrascal M., Ovelleiro D., Casas V., Gay M., Abian J. J. Proteome Res. 7:5167-5176(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-925, MASS SPECTROMETRY. Tissue: T-cell.
[10]	"Kinase-selective enrichment enables quantitative phosphoproteomics of the 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) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-925, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[11]	"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) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-925 AND SER-970, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[12]	"A genome-scale RNAi screen for Oct4 modulators defines a role of the Paf1 complex for embryonic stem cell identity." Ding L., Paszkowski-Rogacz M., Nitzsche A., Slabicki M.M., Heninger A.K., de Vries I., Kittler R., Junqueira M., Shevchenko A., Schulz H., Hubner N., Doss M.X., Sachinidis A., Hescheler J., Iacone R., Anastassiadis K., Stewart A.F., Pisabarro M.T. , Caldarelli A., Poser I., Theis M., Buchholz F. Cell Stem Cell 4:403-415(2009) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[13]	"DSIF, the Paf1 complex, and Tat-SF1 have nonredundant, cooperative roles in RNA polymerase II elongation." Chen Y., Yamaguchi Y., Tsugeno Y., Yamamoto J., Yamada T., Nakamura M., Hisatake K., Handa H. Genes Dev. 23:2765-2777(2009) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION IN THE PAF1 COMPLEX, FUNCTION OF THE PAF1 COMPLEX.
[14]	"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals 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) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-925 AND SER-932, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[15]	"The PAF complex synergizes with MLL fusion proteins at HOX loci to promote leukemogenesis." Muntean A.G., Tan J., Sitwala K., Huang Y., Bronstein J., Connelly J.A., Basrur V., Elenitoba-Johnson K.S., Hess J.L. Cancer Cell 17:609-621(2010) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION OF THE PAF1 COMPLEX, INTERACTION WITH MLL.
[16]	"The human PAF1 complex acts in chromatin transcription elongation both independently and cooperatively with SII/TFIIS." Kim J., Guermah M., Roeder R.G. Cell 140:491-503(2010) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION IN THE PAF1 COMPLEX, COMPOSITION OF THE PAF1 COMPLEX, FUNCTION OF THE PAF1 COMPLEX.
[17]	"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis." Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M. Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-925; SER-941; SER-943 AND SER-970, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[18]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[19]	"Transcriptional activators enhance polyadenylation of mRNA precursors." Nagaike T., Logan C., Hotta I., Rozenblatt-Rosen O., Meyerson M., Manley J.L. Mol. Cell 41:409-418(2011) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, FUNCTION OF THE PAF1 COMPLEX.
[20]	"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation." Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B. Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-925; SER-941; SER-943; SER-970; SER-1020; SER-1021; SER-1097 AND SER-1102, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	D63875 mRNA. Translation: BAA09925.2. Different initiation. CH471064 Genomic DNA. Translation: EAW68557.1. CH471064 Genomic DNA. Translation: EAW68558.1. BC058914 mRNA. Translation: AAH58914.1.
IPI	IPI00477468.
RefSeq	NP_055448.1. NM_014633.3.
UniGene	Hs.725151.
3D structure databases
ProteinModelPortal	Q6PD62.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-31693N.
IntAct	Q6PD62. 28 interactions.
MINT	MINT-1182366.
STRING	9606.ENSP00000355013.
PTM databases
PhosphoSite	Q6PD62.
Polymorphism databases
DMDM	74758318.
Proteomic databases
PaxDb	Q6PD62.
PRIDE	Q6PD62.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000361367; ENSP00000355013; ENSG00000198730.
GeneID	9646.
KEGG	hsa:9646.
UCSC	uc001mja.3. human.
Organism-specific databases
CTD	9646.
GeneCards	GC11P010772.
HGNC	HGNC:16850. CTR9.
MIM	609366. gene.
neXtProt	NX_Q6PD62.
PharmGKB	PA134896774.
HUGE	Search...
GenAtlas	Search...
Phylogenomic databases
eggNOG	COG0457.
HOGENOM	HOG000246926.
HOVERGEN	HBG081372.
InParanoid	Q6PD62.
KO	K15176.
OMA	TQNDTYS.
OrthoDB	EOG4NKBTV.
Gene expression databases
ArrayExpress	Q6PD62.
Bgee	Q6PD62.
CleanEx	HS_CTR9.
Genevestigator	Q6PD62.
GermOnline	ENSG00000198730. Homo sapiens.
Family and domain databases
Gene3D	1.25.40.10. 5 hits.
InterPro	IPR001440. TPR-1. IPR013026. TPR-contain_dom. IPR011990. TPR-like_helical. IPR013105. TPR_2. IPR019734. TPR_repeat. [Graphical view]
Pfam	PF00515. TPR_1. 7 hits. PF07719. TPR_2. 1 hit. [Graphical view]
SMART	SM00028. TPR. 9 hits. [Graphical view]
PROSITE	PS50005. TPR. 10 hits. PS50293. TPR_REGION. 1 hit. [Graphical view]
ProtoNet	Search...
Other
ChiTaRS	CTR9. human.
GenomeRNAi	9646.
NextBio	36207.
PMAP-CutDB	Q6PD62.
SOURCE	Search...

Entry information

Entry name

CTR9_HUMAN

Accession

Primary (citable) accession number: Q6PD62
Secondary accession number(s): D3DQV8, Q15015

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 4, 2006
Last sequence update:	July 5, 2004
Last modified:	May 1, 2013
This is version 94 of the entry and version 1 of the sequence. [Complete history]

Entry status

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.