Q99081 (HTF4_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Transcription factor 12
Short name=TCF-12

Alternative name(s):
Class B basic helix-loop-helix protein 20
Short name=bHLHb20
DNA-binding protein HTF4
E-box-binding protein
Transcription factor HTF-4

Gene names

Name:	TCF12
Synonyms:	BHLHB20, HEB, HTF4

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

General annotation (Comments)

Function	Transcriptional regulator. Involved in the initiation of neuronal differentiation. Activates transcription by binding to the E box (5'-CANNTG-3').
Subunit structure	Efficient DNA binding requires dimerization with another bHLH protein. Forms homo- or heterooligomers with myogenin, E12 and ITF2 proteins. Interacts with PTF1A. Interacts with NEUROD2 By similarity. Interacts with RUNX1T1. Ref.9 Ref.18
Subcellular location	Nucleus.
Tissue specificity	Expressed in several tissues and cell types including skeletal muscle, thymus, and a B-cell line.
Domain	the 9aaTAD motif is a transactivation domain present in a large number of yeast and animal transcription factors. Ref.11
Sequence similarities	Contains 1 bHLH (basic helix-loop-helix) domain.

Ontologies

Keywords
Biological process	Differentiation Neurogenesis Transcription Transcription regulation
Cellular component	Nucleus
Coding sequence diversity	Alternative splicing Polymorphism
Ligand	DNA-binding
Molecular function	Developmental protein
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	immune response Traceable author statement Ref.2. Source: ProtInc muscle organ development Traceable author statement Ref.2. Source: ProtInc positive regulation of neuron differentiation Inferred from electronic annotation. Source: Compara positive regulation of transcription, DNA-dependent Inferred from electronic annotation. Source: Compara regulation of transcription from RNA polymerase II promoter Traceable author statement PubMed 8163514. Source: ProtInc transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	nucleus Inferred from direct assay. Source: LIFEdb transcription factor complex Inferred from electronic annotation. Source: Compara
Molecular_function	E-box binding Inferred from electronic annotation. Source: Compara sequence-specific DNA binding transcription factor activity Inferred from direct assay PubMed 11802795. Source: BHF-UCL
Complete GO annotation...

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q99081-1)

Also known as: a;

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform 2 (identifier: Q99081-2)

Also known as: b;

The sequence of this isoform differs from the canonical sequence as follows:
     1-170: Missing.
     171-193: DSAALDPLQAKKVRKVPPGLPSS → MYCAYPVPGMGSNSLMYYYNGKT

Isoform 3 (identifier: Q99081-3)

Also known as: c;

The sequence of this isoform differs from the canonical sequence as follows:
     396-396: L → LKNRVEQQLHEHLQDAMSFLKDVCE

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 682

682

Transcription factor 12

PRO_0000127228

Regions

Domain

577 – 630

54

bHLH

Region

119 – 140

22

Leucine-zipper

Region

632 – 655

24

Class A specific domain

Motif

19 – 27

9

9aaTAD

Amino acid modifications

Modified residue

67

1

Phosphoserine Ref.15

Modified residue

313

1

Phosphothreonine Ref.14

Modified residue

333

1

Phosphoserine Ref.15

Modified residue

557

1

Phosphothreonine Ref.15

Modified residue

559

1

Phosphoserine Ref.17

Natural variations

Alternative sequence

1 – 170

170

Missing in isoform 2.

VSP_039109

Alternative sequence

171 – 193

23

DSAAL…GLPSS → MYCAYPVPGMGSNSLMYYYN GKT in isoform 2.

VSP_039110

Alternative sequence

396

1

L → LKNRVEQQLHEHLQDAMSFL KDVCE in isoform 3.

VSP_040024

Natural variant

300

1

G → S.
Corresponds to variant rs12442879 [ dbSNP | Ensembl ].

VAR_049543

Experimental info

Sequence conflict

523

1

K → E in CAD89914. Ref.3

Secondary structure

1

.

.

.

.

.

682

Helix Strand Turn

Details...

Helix

15 – 18

4

Turn

24 – 26

3

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 (a) [UniParc]. Last modified October 1, 1996. Version 1. Checksum: 9736113D9361D3F5	FASTA	682	72,965
	10 20 30 40 50 60 MNPQQQRMAA IGTDKELSDL LDFSAMFSPP VNSGKTRPTT LGSSQFSGSG IDERGGTTSW 70 80 90 100 110 120 GTSGQPSPSY DSSRGFTDSP HYSDHLNDSR LGAHEGLSPT PFMNSNLMGK TSERGSFSLY 130 140 150 160 170 180 SRDTGLPGCQ SSLLRQDLGL GSPAQLSSSG KPGTAYYSFS ATSSRRRPLH DSAALDPLQA 190 200 210 220 230 240 KKVRKVPPGL PSSVYAPSPN SDDFNRESPS YPSPKPPTSM FASTFFMQDG THNSSDLWSS 250 260 270 280 290 300 SNGMSQPGFG GILGTSTSHM SQSSSYGNLH SHDRLSYPPH SVSPTDINTS LPPMSSFHRG 310 320 330 340 350 360 STSSSPYVAA SHTPPINGSD SILGTRGNAA GSSQTGDALG KALASIYSPD HTSSSFPSNP 370 380 390 400 410 420 STPVGSPSPL TGTSQWPRPG GQAPSSPSYE NSLHSLQSRM EDRLDRLDDA IHVLRNHAVG 430 440 450 460 470 480 PSTSLPAGHS DIHSLLGPSH NAPIGSLNSN YGGSSLVASS RSASMVGTHR EDSVSLNGNH 490 500 510 520 530 540 SVLSSTVTTS STDLNHKTQE NYRGGLQSQS GTVVTTEIKT ENKEKDENLH EPPSSDDMKS 550 560 570 580 590 600 DDESSQKDIK VSSRGRTSST NEDEDLNPEQ KIEREKERRM ANNARERLRV RDINEAFKEL 610 620 630 640 650 660 GRMCQLHLKS EKPQTKLLIL HQAVAVILSL EQQVRERNLN PKAACLKRRE EEKVSAVSAE 670 680 PPTTLPGTHP GLSETTNPMG HM
	Isoform 2 (b) [UniParc]. Checksum: 98AF7F83F8A2AEF4	FASTA	512	55,142
	10 20 30 40 50 60 MYCAYPVPGM GSNSLMYYYN GKTVYAPSPN SDDFNRESPS YPSPKPPTSM FASTFFMQDG 70 80 90 100 110 120 THNSSDLWSS SNGMSQPGFG GILGTSTSHM SQSSSYGNLH SHDRLSYPPH SVSPTDINTS 130 140 150 160 170 180 LPPMSSFHRG STSSSPYVAA SHTPPINGSD SILGTRGNAA GSSQTGDALG KALASIYSPD 190 200 210 220 230 240 HTSSSFPSNP STPVGSPSPL TGTSQWPRPG GQAPSSPSYE NSLHSLQSRM EDRLDRLDDA 250 260 270 280 290 300 IHVLRNHAVG PSTSLPAGHS DIHSLLGPSH NAPIGSLNSN YGGSSLVASS RSASMVGTHR 310 320 330 340 350 360 EDSVSLNGNH SVLSSTVTTS STDLNHKTQE NYRGGLQSQS GTVVTTEIKT ENKEKDENLH 370 380 390 400 410 420 EPPSSDDMKS DDESSQKDIK VSSRGRTSST NEDEDLNPEQ KIEREKERRM ANNARERLRV 430 440 450 460 470 480 RDINEAFKEL GRMCQLHLKS EKPQTKLLIL HQAVAVILSL EQQVRERNLN PKAACLKRRE 490 500 510 EEKVSAVSAE PPTTLPGTHP GLSETTNPMG HM
	Isoform 3 (c) [UniParc]. Checksum: 75B7B4173C9B660D	FASTA	706	75,845
	10 20 30 40 50 60 MNPQQQRMAA IGTDKELSDL LDFSAMFSPP VNSGKTRPTT LGSSQFSGSG IDERGGTTSW 70 80 90 100 110 120 GTSGQPSPSY DSSRGFTDSP HYSDHLNDSR LGAHEGLSPT PFMNSNLMGK TSERGSFSLY 130 140 150 160 170 180 SRDTGLPGCQ SSLLRQDLGL GSPAQLSSSG KPGTAYYSFS ATSSRRRPLH DSAALDPLQA 190 200 210 220 230 240 KKVRKVPPGL PSSVYAPSPN SDDFNRESPS YPSPKPPTSM FASTFFMQDG THNSSDLWSS 250 260 270 280 290 300 SNGMSQPGFG GILGTSTSHM SQSSSYGNLH SHDRLSYPPH SVSPTDINTS LPPMSSFHRG 310 320 330 340 350 360 STSSSPYVAA SHTPPINGSD SILGTRGNAA GSSQTGDALG KALASIYSPD HTSSSFPSNP 370 380 390 400 410 420 STPVGSPSPL TGTSQWPRPG GQAPSSPSYE NSLHSLKNRV EQQLHEHLQD AMSFLKDVCE 430 440 450 460 470 480 QSRMEDRLDR LDDAIHVLRN HAVGPSTSLP AGHSDIHSLL GPSHNAPIGS LNSNYGGSSL 490 500 510 520 530 540 VASSRSASMV GTHREDSVSL NGNHSVLSST VTTSSTDLNH KTQENYRGGL QSQSGTVVTT 550 560 570 580 590 600 EIKTENKEKD ENLHEPPSSD DMKSDDESSQ KDIKVSSRGR TSSTNEDEDL NPEQKIEREK 610 620 630 640 650 660 ERRMANNARE RLRVRDINEA FKELGRMCQL HLKSEKPQTK LLILHQAVAV ILSLEQQVRE 670 680 690 700 RNLNPKAACL KRREEEKVSA VSAEPPTTLP GTHPGLSETT NPMGHM

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The nucleotide sequence of the human transcription factor HTF4a cDNA." Zhang Y., Bina M. DNA Seq. 2:397-403(1992) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[2]	"HEB, a helix-loop-helix protein related to E2A and ITF2 that can modulate the DNA-binding ability of myogenic regulatory factors." Hu J.S., Olson E.N., Kingston R.E. Mol. Cell. Biol. 12:1031-1042(1992) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). Tissue: Skeletal muscle.
[3]	"The full-ORF clone resource of the German cDNA consortium." Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I. BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2). Tissue: Endometrium and Skeletal muscle.
[4]	"Analysis of the DNA sequence and duplication history of human chromosome 15." Zody M.C., Garber M., Sharpe T., Young S.K., Rowen L., O'Neill K., Whittaker C.A., Kamal M., Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Kodira C.D., Madan A., Qin S., Yang X., Abbasi N., Abouelleil A. , Arachchi H.M., Baradarani L., Birditt B., Bloom S., Bloom T., Borowsky M.L., Burke J., Butler J., Cook A., DeArellano K., DeCaprio D., Dorris L. III, Dors M., Eichler E.E., Engels R., Fahey J., Fleetwood P., Friedman C., Gearin G., Hall J.L., Hensley G., Johnson E., Jones C., Kamat A., Kaur A., Locke D.P., Madan A., Munson G., Jaffe D.B., Lui A., Macdonald P., Mauceli E., Naylor J.W., Nesbitt R., Nicol R., O'Leary S.B., Ratcliffe A., Rounsley S., She X., Sneddon K.M.B., Stewart S., Sougnez C., Stone S.M., Topham K., Vincent D., Wang S., Zimmer A.R., Birren B.W., Hood L., Lander E.S., Nusbaum C. Nature 440:671-675(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]	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 (JUL-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]	"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] (ISOFORM 3). Tissue: Brain.
[7]	"HTF4: a new human helix-loop-helix protein." Zhang Y., Babin J., Feldhaus A.L., Singh H., Sharp P.A., Bina M. Nucleic Acids Res. 19:4555-4555(1991) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 352-682.
[8]	"Genomic organization of human TCF12 gene and spliced mRNA variants producing isoforms of transcription factor HTF4." Gan T.I., Rowen L., Nesbitt R., Roe B.A., Wu H., Hu P., Yao Z., Kim U.J., O'Sickey T., Bina M. Cytogenet. Genome Res. 98:245-248(2002) [PubMed] [Europe PMC] [Abstract] Cited for: GENE ORGANIZATION, ALTERNATIVE SPLICING.
[9]	"The tetramer structure of the Nervy homology two domain, NHR2, is critical for AML1/ETO's activity." Liu Y., Cheney M.D., Gaudet J.J., Chruszcz M., Lukasik S.M., Sugiyama D., Lary J., Cole J., Dauter Z., Minor W., Speck N.A., Bushweller J.H. Cancer Cell 9:249-260(2006) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH RUNX1T1.
[10]	"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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Tissue: Cervix carcinoma.
[11]	"Nine-amino-acid transactivation domain: establishment and prediction utilities." Piskacek S., Gregor M., Nemethova M., Grabner M., Kovarik P., Piskacek M. Genomics 89:756-768(2007) [PubMed] [Europe PMC] [Abstract] Cited for: DOMAIN.
[12]	"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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Tissue: Embryonic kidney.
[13]	"Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis." Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III J. Proteome Res. 7:1346-1351(2008) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Tissue: Cervix carcinoma.
[14]	"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-313, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[15]	"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-67; SER-333 AND THR-557, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[16]	"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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Tissue: Cervix carcinoma.
[17]	"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-559, MASS SPECTROMETRY.
[18]	"Structure of the AML1-ETO eTAFH domain-HEB peptide complex and its contribution to AML1-ETO activity." Park S., Chen W., Cierpicki T., Tonelli M., Cai X., Speck N.A., Bushweller J.H. Blood 113:3558-3567(2009) [PubMed] [Europe PMC] [Abstract] Cited for: STRUCTURE BY NMR OF 11-28 IN COMPLEX WITH RUNX1T1, SUBUNIT.
+	Additional computationally mapped references.

Web resources

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

M83233 mRNA. Translation: AAB62389.1.
M80627 mRNA. Translation: AAA58632.1.
AL831981 mRNA. Translation: CAD89914.1.
BX537967 mRNA. Translation: CAD97931.1.
AC010999 Genomic DNA. No translation available.
AC016525 Genomic DNA. No translation available.
AC090511 Genomic DNA. No translation available.
AC090532 Genomic DNA. No translation available.
CH471082 Genomic DNA. Translation: EAW77512.1.
BC050556 mRNA. Translation: AAH50556.1.
M65209 mRNA. Translation: AAC37571.1.
BK001049 mRNA. Translation: DAA01129.1.

IPI

IPI00012966.
IPI00384333.
IPI00384979.

PIR

A42121.

RefSeq

NP_003196.1. NM_003205.3.
NP_996919.1. NM_207036.1.
NP_996920.1. NM_207037.1.
NP_996921.1. NM_207038.1.
NP_996923.1. NM_207040.1.

UniGene

Hs.511504.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2KNH	NMR	-	B	11-28	[»]

ProteinModelPortal

Q99081.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-29403N.

IntAct

Q99081. 10 interactions.

MINT

MINT-1425247.

STRING

9606.ENSP00000331057.

Polymorphism databases

DMDM

1708332.

Proteomic databases

PaxDb

Q99081.

PRIDE

Q99081.

Protocols and materials databases

DNASU

6938.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000267811; ENSP00000267811; ENSG00000140262.
ENST00000333725; ENSP00000331057; ENSG00000140262.
ENST00000343827; ENSP00000342459; ENSG00000140262.
ENST00000438423; ENSP00000388940; ENSG00000140262.
ENST00000557843; ENSP00000453737; ENSG00000140262.

GeneID

6938.

KEGG

hsa:6938.

UCSC

uc002aea.3. human.
uc002aec.3. human.
uc002aee.3. human.

Organism-specific databases

CTD

6938.

GeneCards

GC15P057210.

HGNC

HGNC:11623. TCF12.

HPA

CAB004432.
HPA002103.

MIM

600480. gene.

neXtProt

NX_Q99081.

PharmGKB

PA36381.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG282899.

HOGENOM

HOG000234180.

HOVERGEN

HBG003854.

KO

K15603.

OMA

TSSTNED.

OrthoDB

EOG4K3KVX.

Enzyme and pathway databases

Reactome

REACT_111045. Developmental Biology.

Gene expression databases

ArrayExpress

Q99081.

Bgee

Q99081.

CleanEx

HS_TCF12.

Genevestigator

Q99081.

GermOnline

ENSG00000140262. Homo sapiens.

Family and domain databases

Gene3D

4.10.280.10. 1 hit.

InterPro

IPR011598. bHLH_dom.
[Graphical view]

Pfam

PF00010. HLH. 1 hit.
[Graphical view]

SMART

SM00353. HLH. 1 hit.
[Graphical view]

SUPFAM

SSF47459. HLH_basic. 1 hit.

PROSITE

PS50888. BHLH. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

ChiTaRS

TCF12. human.

EvolutionaryTrace

Q99081.

GenomeRNAi

6938.

NextBio

27145.

SOURCE

Search...

Entry information

Entry name

HTF4_HUMAN

Accession

Primary (citable) accession number: Q99081
Secondary accession number(s): Q7Z3D9, Q86TC1, Q86VM2

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1996
Last sequence update:	October 1, 1996
Last modified:	May 1, 2013
This is version 119 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.