Q13769 (THOC5_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
THO complex subunit 5 homolog

Alternative name(s):
Functional spliceosome-associated protein 79
Short name=fSAP79
NF2/meningioma region protein pK1.3
Placental protein 39.2
Short name=PP39.2
hTREX90

Gene names

Name:	THOC5
Synonyms:	C22orf19, KIAA0983

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	683 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Component the THO subcomplex of the TREX complex. The TREX complex specifically associates with spliced mRNA and not with unspliced pre-mRNA. It is recruited to spliced mRNAs by a transcription-independent mechanism. Binds to mRNA upstream of the exon-junction complex (EJC) and is recruited in a splicing- and cap-dependent manner to a region near the 5' end of the mRNA where it functions in mRNA export. The recruitment occurs via an interaction between ALYREF/THOC4 and the cap-binding protein NCBP1. The TREX complex is essential for the export of Kaposi's sarcoma-associated herpesvirus (KSHV) intronless mRNAs and infectious virus production. The recruitment of the TREX complex to the intronless viral mRNA occurs via an interaction beteen KSHV ORF57 protein and ALYREF/THOC4. DDX39B functions as a bridge between ALYREF/THOC4 and the THO complex. THOC5 in conjunction with ALYREF/THOC4 functions in NXF1-NXT1 mediated nuclear export of HSP70 mRNA. Regulates the expression of myeloid transcription factors CEBPA, CEBPB and GAB2 by enhancing the levels of phosphatidylinositol 3,4,5-trisphosphate. May be involved in the differentiation of granulocytes and adipocytes. Essential for hematopoietic primitive cell survival and plays an integral role in monocytic development. Ref.7 Ref.8 Ref.9 Ref.12 Ref.14
Subunit structure	Interacts with phosphorylated CSF1R and THOC1 By similarity. Component of the THO complex, which is composed of THOC1, THOC2, THOC5, THOC6 and THOC7. Together with THOC3, ALYREF/THOC4 and DDX39B, THO forms the transcription/export (TREX) complex. Interacts with ALYREF/THOC4 and THOC7. Interacts (via N-terminus) with the NTF2 domain of NXF1. Forms a complex with CEBPB By similarity. Ref.7 Ref.8 Ref.14 Ref.15
Subcellular location	Nucleus. Cytoplasm By similarity. Note: Shuttles between nucleus and cytoplasm. Ref.14 Ref.15
Tissue specificity	Ubiquitously expressed.
Post-translational modification	Phosphorylated on tyrosine upon binding to activated CSF1R; which causes a dissociation of the two proteins. Phosphorylation on Ser-5 and/or Ser-6 is required for nuclear export. Phosphorylated on Thr-328 in insulin-stimulated adipocytes By similarity. Ref.11
Sequence similarities	Belongs to the THOC5 family.
Sequence caution	The sequence BAA76827.2 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Ontologies

Keywords
Biological process	Differentiation Transport mRNA processing mRNA splicing mRNA transport
Cellular component	Cytoplasm Nucleus
Coding sequence diversity	Polymorphism
Ligand	RNA-binding
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	RNA splicing Inferred from electronic annotation. Source: UniProtKB-KW intronless viral mRNA export from host nucleus Inferred from direct assay Ref.12. Source: UniProtKB mRNA processing Inferred from electronic annotation. Source: UniProtKB-KW monocyte differentiation Inferred from direct assay PubMed 19015024. Source: UniProtKB negative regulation of macrophage differentiation Inferred from electronic annotation. Source: Compara primitive hemopoiesis Inferred from sequence or structural similarity. Source: UniProtKB
Cellular_component	THO complex part of transcription export complex Inferred from direct assay Ref.8. Source: UniProtKB cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell intermediate filament cytoskeleton Inferred from direct assay. Source: HPA
Molecular_function	RNA binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 683	683	THO complex subunit 5 homolog		PRO_0000079577
Regions
	Region	1 – 199	199	Interaction with THOC7
	Region	1 – 144	144	Interaction with CSF1R By similarity
	Motif	7 – 10	4	Nuclear localization signal By similarity
Amino acid modifications
	Modified residue	225	1	Phosphotyrosine Ref.11
	Modified residue	307	1	Phosphoserine Ref.10 Ref.13 Ref.16 Ref.17 Ref.19
	Modified residue	312	1	Phosphoserine Ref.10 Ref.13 Ref.16 Ref.17 Ref.19
	Modified residue	314	1	Phosphoserine Ref.10 Ref.13 Ref.16 Ref.17 Ref.19
	Modified residue	328	1	Phosphothreonine Ref.17
Natural variations
	Natural variant	380	1	T → K in a breast cancer sample; somatic mutation. Ref.20		VAR_035692
	Natural variant	475	1	T → S. Corresponds to variant rs8141153 [ dbSNP | Ensembl ].		VAR_037134
	Natural variant	499	1	G → S in a breast cancer sample; somatic mutation. Ref.20		VAR_035693
	Natural variant	525	1	V → I. Ref.1 Ref.2 Ref.3 Ref.5 Corresponds to variant rs737976 [ dbSNP | Ensembl ].		VAR_037135
	Natural variant	579	1	V → I. Ref.1 Ref.3 Ref.5 Corresponds to variant rs1049534 [ dbSNP | Ensembl ].		VAR_021410

Sequences

	Sequence		Length	Mass (Da)
	Q13769 [UniParc]. Last modified September 22, 2009. Version 2. Checksum: 59550FA548835016	FASTA	683	78,508
	10 20 30 40 50 60 MSSESSKKRK PKVIRSDGAP AEGKRNRSDT EQEGKYYSEE AEVDLRDPGR DYELYKYTCQ 70 80 90 100 110 120 ELQRLMAEIQ DLKSRGGKDV AIEIEERRIQ SCVHFMTLKK LNRLAHIRLK KGRDQTHEAK 130 140 150 160 170 180 QKVDAYHLQL QNLLYEVMHL QKEITKCLEF KSKHEEIDLV SLEEFYKEAP PDISKAEVTM 190 200 210 220 230 240 GDPHQQTLAR LDWELEQRKR LAEKYRECLS NKEKILKEIE VKKEYLSSLQ PRLNSIMQAS 250 260 270 280 290 300 LPVQEYLFMP FDQAHKQYET ARHLPPPLYV LFVQATAYGQ ACDKTLSVAI EGSVDEAKAL 310 320 330 340 350 360 FKPPEDSQDD ESDSDAEEEQ TTKRRRPTLG VQLDDKRKEM LKRHPLSVML DLKCKDDSVL 370 380 390 400 410 420 HLTFYYLMNL NIMTVKAKVT TAMELITPIS AGDLLSPDSV LSCLYPGDHG KKTPNPANQY 430 440 450 460 470 480 QFDKVGILTL SDYVLELGHP YLWVQKLGGL HFPKEQPQQT VIADHSLSAS HMETTMKLLK 490 500 510 520 530 540 TRVQSRLALH KQFASLEHGI VPVTSDCQYL FPAKVVSRLV KWVTVAHEDY MELHFTKDIV 550 560 570 580 590 600 DAGLAGDTNL YYMALIERGT AKLQAAVVLN PGYSSIPPVF QLCLNWKGEK TNSNDDNIRA 610 620 630 640 650 660 MEGEVNVCYK ELCGPWPSHQ LLTNQLQRLC VLLDVYLETE SHDDSVEGPK EFPQEKMCLR 670 680 LFRGPSRMKP FKYNHPQGFF SHR

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Cloning of a novel, anonymous gene from a megabase-range YAC and cosmid contig in the neurofibromatosis type 2/meningioma region on human chromosome 22q12." Xie Y.G., Han F.Y., Peyrard M., Ruttledge M.H., Fransson I., deJong P., Collins J., Dunham I., Nordenskjold M., Dumanski J.P. Hum. Mol. Genet. 2:1361-1368(1993) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS ILE-525 AND ILE-579. Tissue: Fetus.
[2]	"Prediction of the coding sequences of unidentified human genes. XIII. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro." Nagase T., Ishikawa K., Suyama M., Kikuno R., Hirosawa M., Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O. DNA Res. 6:63-70(1999) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT ILE-525. Tissue: Brain.
[3]	"A genome annotation-driven approach to cloning the human ORFeome." Collins J.E., Wright C.L., Edwards C.A., Davis M.P., Grinham J.A., Cole C.G., Goward M.E., Aguado B., Mallya M., Mokrab Y., Huckle E.J., Beare D.M., Dunham I. Genome Biol. 5:R84.1-R84.11(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANTS ILE-525 AND ILE-579.
[4]	"The DNA sequence of human chromosome 22." Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M., Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C., Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E., Bridgeman A.M. , Buck D., Burgess J., Burrill W.D., Burton J., Carder C., Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G., Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V., Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M., Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A., Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C., Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E., Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F., Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M., Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A., Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D., Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y., Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S., Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E., Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L., Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L., Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N., Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A., Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L., Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P., Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P., Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q., Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J., Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J., Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D., Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T., Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P., Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K., Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R., Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L., McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J., Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E., Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P., Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y., Wright H. Nature 402:489-495(1999) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]	"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], VARIANTS ILE-525 AND ILE-579. Tissue: Colon.
[6]	"Differential expression of placental genes." Page N.M., Butlin D.J., Manyonda I., Bicknell A.B., Lowry P.J. Submitted (MAY-1998) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 548-650. Tissue: Placenta.
[7]	"Linking transcriptional elongation and messenger RNA export to metastatic breast cancers." Guo S., Hakimi M.A., Baillat D., Chen X., Farber M.J., Klein-Szanto A.J., Cooch N.S., Godwin A.K., Shiekhattar R. Cancer Res. 65:3011-3016(2005) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION IN THE TREX COMPLEX, FUNCTION OF THE TREX COMPLEX, MASS SPECTROMETRY.
[8]	"Recruitment of the human TREX complex to mRNA during splicing." Masuda S., Das R., Cheng H., Hurt E., Dorman N., Reed R. Genes Dev. 19:1512-1517(2005) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION IN THE THO AND TREX COMPLEX, FUNCTION OF THE TREX COMPLEX, MASS SPECTROMETRY.
[9]	"Human mRNA export machinery recruited to the 5' end of mRNA." Cheng H., Dufu K., Lee C.-S., Hsu J.L., Dias A., Reed R. Cell 127:1389-1400(2006) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION OF THE TREX COMPLEX.
[10]	"ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage." Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J. Science 316:1160-1166(2007) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-307; SER-312 AND SER-314, MASS SPECTROMETRY. Tissue: Embryonic kidney.
[11]	"THOC5 spliceosome protein: a target for leukaemogenic tyrosine kinases that affects inositol lipid turnover." Pierce A., Carney L., Hamza H.G., Griffiths J.R., Zhang L., Whetton B.A., Gonzalez Sanchez M.B., Tamura T., Sternberg D., Whetton A.D. Br. J. Haematol. 141:641-650(2008) [PubMed] [Europe PMC] [Abstract] Cited for: MASS SPECTROMETRY, PHOSPHORYLATION AT TYR-225.
[12]	"Recruitment of the complete hTREX complex is required for Kaposi's sarcoma-associated herpesvirus intronless mRNA nuclear export and virus replication." Boyne J.R., Colgan K.J., Whitehouse A. PLoS Pathog. 4:E1000194-E1000194(2008) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION OF THE TREX COMPLEX.
[13]	"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 SER-307; SER-312 AND SER-314, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[14]	"Adaptor Aly and co-adaptor Thoc5 function in the Tap-p15-mediated nuclear export of HSP70 mRNA." Katahira J., Inoue H., Hurt E., Yoneda Y. EMBO J. 28:556-567(2009) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH ALYREF/THOC4 AND NXF1.
[15]	"Nuclear localization of the pre-mRNA associating protein THOC7 depends upon its direct interaction with Fms tyrosine kinase interacting protein (FMIP)." El Bounkari O., Guria A., Klebba-Faerber S., Claussen M., Pieler T., Griffiths J.R., Whetton A.D., Koch A., Tamura T. FEBS Lett. 583:13-18(2009) [PubMed] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION, INTERACTION WITH THOC7.
[16]	"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 SER-307; SER-312 AND SER-314, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[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 SER-307; SER-312; SER-314 AND THR-328, 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]	"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 SER-307; SER-312 AND SER-314, MASS SPECTROMETRY.
[20]	"The consensus coding sequences of human breast and colorectal cancers." Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V. , Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., Velculescu V.E. Science 314:268-274(2006) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS [LARGE SCALE ANALYSIS] LYS-380 AND SER-499.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	L18972 Genomic DNA. Translation: AAC26837.1. AB023200 mRNA. Translation: BAA76827.2. Different initiation. CR456542 mRNA. Translation: CAG30428.1. AC005529 Genomic DNA. No translation available. BC003615 mRNA. Translation: AAH03615.1. AJ006069 mRNA. Translation: CAA06841.1.
IPI	IPI00299417.
PIR	I39463.
RefSeq	NP_001002877.1. NM_001002877.1. NP_001002878.1. NM_001002878.1. NP_001002879.1. NM_001002879.1. NP_003669.4. NM_003678.4.
UniGene	Hs.75361.
3D structure databases
ProteinModelPortal	Q13769.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q13769. 1 interaction.
MINT	MINT-4532759.
STRING	9606.ENSP00000380969.
PTM databases
PhosphoSite	Q13769.
Polymorphism databases
DMDM	259016156.
Proteomic databases
PaxDb	Q13769.
PRIDE	Q13769.
Protocols and materials databases
DNASU	8563.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000397871; ENSP00000380969; ENSG00000100296. ENST00000397872; ENSP00000380970; ENSG00000100296. ENST00000397873; ENSP00000380971; ENSG00000100296. ENST00000490103; ENSP00000420306; ENSG00000100296.
GeneID	8563.
KEGG	hsa:8563.
UCSC	uc003afq.3. human.
Organism-specific databases
CTD	8563.
GeneCards	GC22M029901.
HGNC	HGNC:19074. THOC5.
HPA	HPA029812.
MIM	612733. gene.
neXtProt	NX_Q13769.
PharmGKB	PA38188.
HUGE	Search...
GenAtlas	Search...
Phylogenomic databases
eggNOG	NOG266546.
HOGENOM	HOG000007514.
HOVERGEN	HBG051271.
InParanoid	Q13769.
KO	K13174.
OMA	ATELITP.
OrthoDB	EOG447FST.
PhylomeDB	Q13769.
Gene expression databases
ArrayExpress	Q13769.
Bgee	Q13769.
CleanEx	HS_THOC5.
Genevestigator	Q13769.
GermOnline	ENSG00000100296. Homo sapiens.
Family and domain databases
InterPro	IPR019163. THO_Thoc5. [Graphical view]
Pfam	PF09766. FimP. 1 hit. [Graphical view]
ProtoNet	Search...
Other
GenomeRNAi	8563.
NextBio	32099.
SOURCE	Search...

Entry information

Entry name

THOC5_HUMAN

Accession

Primary (citable) accession number: Q13769
Secondary accession number(s): O60839, Q9UPZ5

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 2, 2002
Last sequence update:	September 22, 2009
Last modified:	April 3, 2013
This is version 105 of the entry and version 2 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.