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Q9Y2N7 (HIF3A_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 115. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Hypoxia-inducible factor 3-alpha

Short name=HIF-3-alpha
Short name=HIF3-alpha
Alternative name(s):
Basic-helix-loop-helix-PAS protein MOP7
Class E basic helix-loop-helix protein 17
Short name=bHLHe17
HIF3-alpha-1
Inhibitory PAS domain protein
Short name=IPAS
Member of PAS protein 7
PAS domain-containing protein 7
Gene names
Name:HIF3A
Synonyms:BHLHE17, MOP7, PASD7
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length669 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Involved in adaptive response to hypoxia. Suppresses hypoxia-inducible expression of HIF1A and EPAS1. Binds to core DNA sequence 5'-TACGTG-3' within the hypoxia response element (HRE) of target gene promoters. The complex HIF3A-ARNT activates the transcription of reporter genes driven by HRE. Isoform 4 has a dominant-negative function of inactivating HIF1A-mediated transcription. Isoform 4 attenuates the binding of HIF1A to hypoxia-responsive elements (HRE), thus inhibiting HRE-driven transcription. Hypoxia induces down-regulation of isoform 4, leading to activation of HIF1A in hypoxia. Conversely, upon restoring normoxia, the expression of isoform 4 increases and thereby secure an inhibition of HIF1A activity. Isoform 4 may be a negative regulator of hypoxia-inducible gene expression in the kidney and may be involved in renal tumorigenesis. Functions as an inhibitor of angiogenesis in the cornea By similarity. Ref.1

Subunit structure

Heterodimerizes with ARNT. Interacts via the oxygen-dependent degradation domain (ODD) with the beta domain of VHL. Ref.3 Ref.9

Subcellular location

Nucleus. Cytoplasm. Note: In the nuclei of all periportal and perivenous hepatocytes. In the distal perivenous zone, detected in the cytoplasm of the hepatocytes By similarity.

Tissue specificity

Expressed in kidney. Expressed abundantly in lung epithelial cells. Expression is regulated in an oxygen-dependent manner. Ref.1

Induction

Strongly induced by hypoxia (1% O2), both at the level of protein and mRNA due to an increase in protein stability and transcriptional activation. Ref.10

Post-translational modification

In normoxia, hydroxylated on Pro-492 in the oxygen-dependent degradation domain (ODD) by PHD. The hydroxylated proline promotes interaction with VHL, initiating rapid ubiquitination and subsequent proteasomal degradation.

Sequence similarities

Contains 1 bHLH (basic helix-loop-helix) domain.

Contains 2 PAS (PER-ARNT-SIM) domains.

Alternative products

This entry describes 7 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q9Y2N7-1)

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: Q9Y2N7-2)

Also known as: HIF-3alpha1;

The sequence of this isoform differs from the canonical sequence as follows:
     1-8: MALGLQRA → MDWQDH
Isoform 3 (identifier: Q9Y2N7-3)

Also known as: HIF-3alpha2;

The sequence of this isoform differs from the canonical sequence as follows:
     611-669: SFLLTGGPAP...QPRAGSAQAD → VCWGINGILWPSLPSWLKPTVL
Isoform 4 (identifier: Q9Y2N7-4)

Also known as: HIF-3alpha4;

The sequence of this isoform differs from the canonical sequence as follows:
     293-363: LLSKGQAVTG...EQTEQHSRRP → CMYPISPGAK...FSPHLPPWWP
     364-669: Missing.
Isoform 5 (identifier: Q9Y2N7-5)

Also known as: HIF-3alpha3;

The sequence of this isoform differs from the canonical sequence as follows:
     1-56: Missing.
     627-669: STPLLNLNEP...QPRAGSAQAD → TELTQFLLSV...APSPLGWFAI
Isoform 6 (identifier: Q9Y2N7-6)

Also known as: HIF-3alpha6;

The sequence of this isoform differs from the canonical sequence as follows:
     1-86: Missing.
     87-137: ACYLKALEGF...SIFDFIHPCD → MRPAAGAARR...ATCACTASAP
     234-323: PPLGRGAFLS...LWTQTQATVV → GFVMVLTAEG...FSPHLPPWWP
     324-669: Missing.
Isoform 7 (identifier: Q9Y2N7-7)

The sequence of this isoform differs from the canonical sequence as follows:
     1-120: MALGLQRARS...ENVSKHLGLS → MRPAAGAARR...ATCACTASAP
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 669669Hypoxia-inducible factor 3-alpha
PRO_0000284414

Regions

Domain14 – 6754bHLH
Domain82 – 15473PAS 1
Domain227 – 29771PAS 2
Region452 – 581130ODD
Region454 – 50653NTAD
Motif414 – 4185LRRLL
Motif490 – 4978LAPYISMD

Amino acid modifications

Modified residue49214-hydroxyproline Ref.9
Cross-link467Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.9
Cross-link570Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.9

Natural variations

Alternative sequence1 – 120120MALGL…HLGLS → MRPAAGAARRPRCCTSWLTR CPSPAASAPTWTRPLSCASP SATCACTASAP in isoform 7.
VSP_043429
Alternative sequence1 – 8686Missing in isoform 6.
VSP_024518
Alternative sequence1 – 5656Missing in isoform 5.
VSP_024519
Alternative sequence1 – 88MALGLQRA → MDWQDH in isoform 2.
VSP_024520
Alternative sequence87 – 13751ACYLK…IHPCD → MRPAAGAARRPRCCTSWLTR CPSPAASAPTWTRPLSCASP SATCACTASAP in isoform 6.
VSP_024521
Alternative sequence234 – 32390PPLGR…QATVV → GFVMVLTAEGDMAYLSENVS NHLGLSQLELIGHSIFDFIH PCDQEELQDALTPHLNTSSL LPKPQGTVSFLAPSYPVPRS FSPHLPPWWP in isoform 6.
VSP_024522
Alternative sequence293 – 36371LLSKG…HSRRP → CMYPISPGAKPAATWPPADT RTPQLPIPQDALPPHLNTSS LLPKPQGTVSFLAPSYPVPR SFSPHLPPWWP in isoform 4.
VSP_024523
Alternative sequence324 – 669346Missing in isoform 6.
VSP_024524
Alternative sequence364 – 669306Missing in isoform 4.
VSP_024525
Alternative sequence611 – 66959SFLLT…SAQAD → VCWGINGILWPSLPSWLKPT VL in isoform 3.
VSP_024526
Alternative sequence627 – 66943STPLL…SAQAD → TELTQFLLSVLSFPILDPYP LGCAAPGLHASPFSLPTISV PQNPLHSPPQPSRHALTLTL PHMFGAPGAPSPLGWFAI in isoform 5.
VSP_024527
Natural variant3431Q → R. Ref.8
Corresponds to variant rs3764609 [ dbSNP | Ensembl ].
VAR_031731
Natural variant4631F → L.
Corresponds to variant rs7253301 [ dbSNP | Ensembl ].
VAR_031732

Experimental info

Mutagenesis4671K → R: No loss of ubiquitination. Reduced ubiquitination; when associated with R-570. Ref.9
Mutagenesis4921P → A: Reduced ubiquitination. Ref.9
Mutagenesis5701K → R: No loss of ubiquitination. Reduced ubiquitination; when associated with R-467. Ref.9
Sequence conflict2021A → V in BAB55324. Ref.5
Sequence conflict4971D → G in BAB55324. Ref.5

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified April 17, 2007. Version 2.
Checksum: 81C4C84517000DE2

FASTA66972,433
        10         20         30         40         50         60 
MALGLQRARS TTELRKEKSR DAARSRRSQE TEVLYQLAHT LPFARGVSAH LDKASIMRLT 

        70         80         90        100        110        120 
ISYLRMHRLC AAGEWNQVGA GGEPLDACYL KALEGFVMVL TAEGDMAYLS ENVSKHLGLS 

       130        140        150        160        170        180 
QLELIGHSIF DFIHPCDQEE LQDALTPQQT LSRRKVEAPT ERCFSLRMKS TLTSRGRTLN 

       190        200        210        220        230        240 
LKAATWKVLN CSGHMRAYKP PAQTSPAGSP DSEPPLQCLV LICEAIPHPG SLEPPLGRGA 

       250        260        270        280        290        300 
FLSRHSLDMK FTYCDDRIAE VAGYSPDDLI GCSAYEYIHA LDSDAVSKSI HTLLSKGQAV 

       310        320        330        340        350        360 
TGQYRFLARS GGYLWTQTQA TVVSGGRGPQ SESIVCVHFL ISQVEETGVV LSLEQTEQHS 

       370        380        390        400        410        420 
RRPIQRGAPS QKDTPNPGDS LDTPGPRILA FLHPPSLSEA ALAADPRRFC SPDLRRLLGP 

       430        440        450        460        470        480 
ILDGASVAAT PSTPLATRHP QSPLSADLPD ELPVGTENVH RLFTSGKDTE AVETDLDIAQ 

       490        500        510        520        530        540 
DADALDLEML APYISMDDDF QLNASEQLPR AYHRPLGAVP RPRARSFHGL SPPALEPSLL 

       550        560        570        580        590        600 
PRWGSDPRLS CSSPSRGDPS ASSPMAGARK RTLAQSSEDE DEGVELLGVR PPKRSPSPEH 

       610        620        630        640        650        660 
ENFLLFPLSL SFLLTGGPAP GSLQDPSTPL LNLNEPLGLG PSLLSPYSDE DTTQPGGPFQ 


PRAGSAQAD 

« Hide

Isoform 2 (HIF-3alpha1) [UniParc].

Checksum: 67B8794FF9DCCF4B
Show »

FASTA66772,405
Isoform 3 (HIF-3alpha2) [UniParc].

Checksum: 9665B0AF3998F8EF
Show »

FASTA63268,964
Isoform 4 (HIF-3alpha4) [UniParc].

Checksum: 66CE5B85A2C50A15
Show »

FASTA36339,962
Isoform 5 (HIF-3alpha3) [UniParc].

Checksum: F41051A16B629167
Show »

FASTA64869,967
Isoform 6 (HIF-3alpha6) [UniParc].

Checksum: A78EC74708561F68
Show »

FASTA23725,710
Isoform 7 [UniParc].

Checksum: 822B55E0513AF129
Show »

FASTA60064,359

References

« Hide 'large scale' references
[1]"Expression and characterization of hypoxia-inducible factor (HIF)-3alpha in human kidney: suppression of HIF-mediated gene expression by HIF-3alpha."
Hara S., Hamada J., Kobayashi C., Kondo Y., Imura N.
Biochem. Biophys. Res. Commun. 287:808-813(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION, TISSUE SPECIFICITY.
Tissue: Kidney.
[2]"Cloning and characterization of human inhibitory PAS domain protein."
Cheng J.Q.
Submitted (DEC-2001) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
[3]"Human HIF-3alpha4 is a dominant-negative regulator of HIF-1 and is down-regulated in renal cell carcinoma."
Maynard M.A., Evans A.J., Hosomi T., Hara S., Jewett M.A., Ohh M.
FASEB J. 19:1396-1406(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4), INTERACTION WITH HIF1A AND ARNT.
Tissue: Cerebellum.
[4]"HIF-3alpha2, one of splicing variants of human hypoxia-inducible factor-3alpha, functions as an inhibitor of hypoxia-induced gene expression and tumor growth."
Hara S., Hosomi T., Mita M., Sakaue M., Kondo Y.
Submitted (FEB-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
Tissue: Kidney.
[5]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 3; 5 AND 7).
Tissue: Embryo, Heart and Ovary.
[6]"The DNA sequence and biology of human chromosome 19."
Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S., Carrano A.V. expand/collapse author list , Caoile C., Chan Y.M., Christensen M., Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E., Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M., Rubin E.M., Lucas S.M.
Nature 428:529-535(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]Mural R.J., Istrail S., Sutton 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. expand/collapse author list , 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].
[8]"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 1), VARIANT ARG-343.
Tissue: Pancreas.
[9]"Multiple splice variants of the human HIF-3 alpha locus are targets of the von Hippel-Lindau E3 ubiquitin ligase complex."
Maynard M.A., Qi H., Chung J., Lee E.H., Kondo Y., Hara S., Conaway R.C., Conaway J.W., Ohh M.
J. Biol. Chem. 278:11032-11040(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: ALTERNATIVE SPLICING, INTERACTION WITH VHL, UBIQUITINATION AT LYS-467 AND LYS-570, HYDROXYLATION AT PRO-492, MUTAGENESIS OF LYS-467; PRO-492 AND LYS-570.
[10]"Hypoxia upregulates hypoxia inducible factor (HIF)-3alpha expression in lung epithelial cells: characterization and comparison with HIF-1alpha."
Li Q.F., Wang X.R., Yang Y.W., Lin H.
Cell Res. 16:548-558(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: INDUCTION.
+Additional computationally mapped references.

Web resources

Wikipedia

Hypoxia inducible factor entry

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB054067 mRNA. Translation: BAB69689.1.
AF463492 mRNA. Translation: AAL69947.1.
AB118749 mRNA. Translation: BAD93355.1.
AB295039 mRNA. Translation: BAG07185.1.
AK021653 mRNA. Translation: BAB13865.1.
AK024095 mRNA. Translation: BAB14824.1.
AK027725 mRNA. Translation: BAB55324.1.
AK297828 mRNA. Translation: BAG60164.1.
AC007193 Genomic DNA. Translation: AAD22668.1.
CH471126 Genomic DNA. Translation: EAW57410.1.
BC080551 mRNA. Translation: AAH80551.1.
CCDSCCDS12681.2. [Q9Y2N7-1]
CCDS12682.1. [Q9Y2N7-2]
CCDS42580.2. [Q9Y2N7-7]
PIRJC7771.
RefSeqNP_071907.4. NM_022462.4. [Q9Y2N7-7]
NP_690007.1. NM_152794.3. [Q9Y2N7-2]
NP_690008.2. NM_152795.3. [Q9Y2N7-1]
XP_005259211.1. XM_005259154.2. [Q9Y2N7-7]
XP_006723388.1. XM_006723325.1. [Q9Y2N7-7]
UniGeneHs.420830.

3D structure databases

ProteinModelPortalQ9Y2N7.
SMRQ9Y2N7. Positions 11-342.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid122143. 4 interactions.
STRING9606.ENSP00000366898.

PTM databases

PhosphoSiteQ9Y2N7.

Polymorphism databases

DMDM145558932.

Proteomic databases

PaxDbQ9Y2N7.
PRIDEQ9Y2N7.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000244303; ENSP00000244303; ENSG00000124440. [Q9Y2N7-7]
ENST00000300862; ENSP00000300862; ENSG00000124440. [Q9Y2N7-2]
ENST00000377670; ENSP00000366898; ENSG00000124440. [Q9Y2N7-1]
GeneID64344.
KEGGhsa:64344.
UCSCuc002peg.4. human. [Q9Y2N7-3]
uc002peh.3. human. [Q9Y2N7-1]
uc002pel.3. human. [Q9Y2N7-2]
uc010xxy.2. human. [Q9Y2N7-7]

Organism-specific databases

CTD64344.
GeneCardsGC19P046800.
HGNCHGNC:15825. HIF3A.
HPAHPA041141.
MIM609976. gene.
neXtProtNX_Q9Y2N7.
PharmGKBPA29285.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG288942.
HOGENOMHOG000234306.
HOVERGENHBG060456.
InParanoidQ9Y2N7.
KOK09096.
OMAAVGQSIH.
OrthoDBEOG7JDQX8.
PhylomeDBQ9Y2N7.
TreeFamTF317772.

Enzyme and pathway databases

ReactomeREACT_120956. Cellular responses to stress.

Gene expression databases

ArrayExpressQ9Y2N7.
BgeeQ9Y2N7.
CleanExHS_HIF3A.
GenevestigatorQ9Y2N7.

Family and domain databases

InterProIPR011598. bHLH_dom.
IPR021537. HIF_alpha_subunit.
IPR001610. PAC.
IPR000014. PAS.
IPR013767. PAS_fold.
[Graphical view]
PfamPF11413. HIF-1. 1 hit.
PF00989. PAS. 1 hit.
[Graphical view]
SMARTSM00353. HLH. 1 hit.
SM00086. PAC. 1 hit.
SM00091. PAS. 2 hits.
[Graphical view]
SUPFAMSSF47459. SSF47459. 1 hit.
SSF55785. SSF55785. 2 hits.
TIGRFAMsTIGR00229. sensory_box. 1 hit.
PROSITEPS50888. BHLH. 1 hit.
PS50112. PAS. 2 hits.
[Graphical view]
ProtoNetSearch...

Other

GenomeRNAi64344.
NextBio66283.
PROQ9Y2N7.
SOURCESearch...

Entry information

Entry nameHIF3A_HUMAN
AccessionPrimary (citable) accession number: Q9Y2N7
Secondary accession number(s): B0M185 expand/collapse secondary AC list , B4DNA2, Q58A43, Q66K72, Q8WXA1, Q96K34, Q9H7Z9, Q9HAI2
Entry history
Integrated into UniProtKB/Swiss-Prot: April 17, 2007
Last sequence update: April 17, 2007
Last modified: July 9, 2014
This is version 115 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 19

Human chromosome 19: entries, gene names and cross-references to MIM