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Q9Y5Y0 (FLVC1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 97. 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·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Feline leukemia virus subgroup C receptor-related protein 1

Short name=Feline leukemia virus subgroup C receptor
Short name=hFLVCR
Gene names
Name:FLVCR1
Synonyms:FLVCR
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length555 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Isoform 1:Heme transporter that exports cytoplasmic heme. It can also export coproporphyrin and protoporphyrin IX, which are both intermediate products in the heme biosynthetic pathway. Does not export bilirubin. Heme export depends on the presence of HPX and may be required to protect developing erythroid cells from heme toxicity. Heme export also provides protection from heme or ferrous iron toxicities in liver and brain. Causes susceptibility to FeLV-C in vitro. Required during erythtopoiesis to maintain intracellular free heme balance since in proerythroblasts, heme synthesis intensifies and it's accumulation is toxic for cells. Ref.1 Ref.7 Ref.12 Ref.15

Isoform 2:Heme transporter that promotes heme efflux from the mitochondrion to the cytoplasm. Essential for erythroid differentiation. Ref.1 Ref.7 Ref.12 Ref.15

Subunit structure

Interacts with HPX. Ref.12

Subcellular location

Isoform 1: Cell membrane; Multi-pass membrane protein By similarity Ref.8 Ref.15.

Isoform 2: Mitochondrion membrane; Multi-pass membrane protein By similarity Ref.8 Ref.15.

Tissue specificity

Found all hematopoietic tissues including peripheral blood lymphocytes. Some expression is found in pancreas and kidney. Ref.1

Developmental stage

Down-regulated in haemopoietic progenitor cells undergoing differentiation and hemoglobinization. Abundant in fetal liver. Ref.7

Post-translational modification

N-Glycosylated. Ref.8

Involvement in disease

Posterior column ataxia with retinitis pigmentosa (PCARP) [MIM:609033]: A neurodegenerative syndrome beginning in infancy with areflexia and retinitis pigmentosa. Nyctalopia (night blindness) and peripheral visual field loss are usually evident during late childhood or teenage years, with subsequent progressive constriction of the visual fields and loss of central retinal function over time. A sensory ataxia caused by degeneration of the posterior columns of the spinal cord results in a loss of proprioceptive sensation that is clinically evident in the second decade of life and gradually progresses. Scoliosis, camptodactyly, achalasia, gastrointestinal dysmotility, and a sensory peripheral neuropathy are variable features of the disease. Affected individuals have no clinical or radiological evidence of cerebral or cerebellar involvement.
Note: The disease is caused by mutations affecting the gene represented in this entry. Defective neuronal heme transmembrane export due to FLVCR1 mutations may abrogate the neuroprotective effects of neuroglobin and initiate an apoptotic cascade that results in the selective degeneration of photoreceptors in the neurosensory retina and sensory neurons in the posterior spinal cord. Ref.16 Ref.17

Sequence similarities

Belongs to the major facilitator superfamily. Feline leukemia virus subgroup C receptor (TC 2.A.1.28.1) family. [View classification]

Ontologies

Keywords
   Biological processErythrocyte maturation
Transport
   Cellular componentCell membrane
Membrane
Mitochondrion
   Coding sequence diversityAlternative splicing
Polymorphism
   DiseaseDisease mutation
Neurodegeneration
Retinitis pigmentosa
   DomainTransmembrane
Transmembrane helix
   Molecular functionReceptor
   PTMGlycoprotein
Phosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processblood vessel development

Inferred from electronic annotation. Source: Ensembl

cell death

Inferred from electronic annotation. Source: UniProtKB-KW

cellular iron ion homeostasis

Traceable author statement. Source: Reactome

embryonic digit morphogenesis

Inferred from electronic annotation. Source: Ensembl

embryonic skeletal system morphogenesis

Inferred from electronic annotation. Source: Ensembl

erythrocyte differentiation

Inferred from direct assay Ref.15. Source: MGI

erythrocyte maturation

Inferred from electronic annotation. Source: UniProtKB-KW

head morphogenesis

Inferred from electronic annotation. Source: Ensembl

heme export

Inferred from mutant phenotype Ref.7. Source: UniProtKB

heme transport

Inferred from mutant phenotype Ref.15. Source: MGI

in utero embryonic development

Inferred from electronic annotation. Source: Ensembl

mitochondrial transport

Inferred from direct assay Ref.15. Source: MGI

multicellular organism growth

Inferred from electronic annotation. Source: Ensembl

multicellular organismal development

Traceable author statement PubMed 10648427. Source: ProtInc

regulation of organ growth

Inferred from electronic annotation. Source: Ensembl

spleen development

Inferred from electronic annotation. Source: Ensembl

transmembrane transport

Traceable author statement. Source: Reactome

transport

Traceable author statement PubMed 10648427. Source: ProtInc

   Cellular_componentintegral component of plasma membrane

Traceable author statement PubMed 10648427. Source: ProtInc

mitochondrial membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

mitochondrion

Inferred from direct assay Ref.15. Source: MGI

plasma membrane

Traceable author statement. Source: Reactome

   Molecular_functionheme transporter activity

Inferred from direct assay Ref.12. Source: UniProtKB

transporter activity

Traceable author statement PubMed 10648427. Source: ProtInc

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q9Y5Y0-1)

Also known as: FLVC1a;

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: Q9Y5Y0-2)

Also known as: FLVC1b; mitochondrial;

The sequence of this isoform differs from the canonical sequence as follows:
     1-276: Missing.
Note: Has a probable mitochondrial transit peptide at positions 1-38.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 555555Feline leukemia virus subgroup C receptor-related protein 1
PRO_0000084844

Regions

Topological domain1 – 107107Cytoplasmic Potential
Transmembrane108 – 12821Helical; Potential
Topological domain129 – 14719Extracellular Potential
Transmembrane148 – 16821Helical; Potential
Topological domain169 – 1746Cytoplasmic Potential
Transmembrane175 – 19521Helical; Potential
Topological domain196 – 1994Extracellular Potential
Transmembrane200 – 22021Helical; Potential
Topological domain221 – 24020Cytoplasmic Potential
Transmembrane241 – 26121Helical; Potential
Topological domain262 – 27514Extracellular Potential
Transmembrane276 – 29621Helical; Potential
Topological domain297 – 33135Cytoplasmic Potential
Transmembrane332 – 35221Helical; Potential
Topological domain353 – 37220Extracellular Potential
Transmembrane373 – 39321Helical; Potential
Topological domain394 – 4018Cytoplasmic Potential
Transmembrane402 – 42221Helical; Potential
Topological domain423 – 4242Extracellular Potential
Transmembrane425 – 44521Helical; Potential
Topological domain446 – 45914Cytoplasmic Potential
Transmembrane460 – 48021Helical; Potential
Topological domain481 – 49010Extracellular Potential
Transmembrane491 – 51121Helical; Potential
Topological domain512 – 55544Cytoplasmic Potential

Amino acid modifications

Modified residue561Phosphoserine Ref.11
Glycosylation2651N-linked (GlcNAc...) Potential
Glycosylation2731N-linked (GlcNAc...) Potential

Natural variations

Alternative sequence1 – 276276Missing in isoform 2.
VSP_047866
Natural variant521A → P. Ref.5
Corresponds to variant rs11120047 [ dbSNP | Ensembl ].
VAR_050297
Natural variant1211N → D in PCARP. Ref.16
VAR_065158
Natural variant1921C → R in PCARP. Ref.16
VAR_065159
Natural variant2411A → T in PCARP. Ref.16
VAR_065160
Natural variant4931G → R in PCARP. Ref.17
VAR_065161
Natural variant5441T → M. Ref.5
Corresponds to variant rs3207090 [ dbSNP | Ensembl ].
VAR_050298

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (FLVC1a) [UniParc].

Last modified November 1, 1999. Version 1.
Checksum: D0EBA9886CC8E747

FASTA55559,863
        10         20         30         40         50         60 
MARPDDEEGA AVAPGHPLAK GYLPLPRGAP VGKESVELQN GPKAGTFPVN GAPRDSLAAA 

        70         80         90        100        110        120 
SGVLGGPQTP LAPEEETQAR LLPAGAGAET PGAESSPLPL TALSPRRFVV LLIFSLYSLV 

       130        140        150        160        170        180 
NAFQWIQYSI ISNVFEGFYG VTLLHIDWLS MVYMLAYVPL IFPATWLLDT RGLRLTALLG 

       190        200        210        220        230        240 
SGLNCLGAWI KCGSVQQHLF WVTMLGQCLC SVAQVFILGL PSRIASVWFG PKEVSTACAT 

       250        260        270        280        290        300 
AVLGNQLGTA VGFLLPPVLV PNTQNDTNLL ACNISTMFYG TSAVATLLFI LTAIAFKEKP 

       310        320        330        340        350        360 
RYPPSQAQAA LQDSPPEEYS YKKSIRNLFK NIPFVLLLIT YGIMTGAFYS VSTLLNQMIL 

       370        380        390        400        410        420 
TYYEGEEVNA GRIGLTLVVA GMVGSILCGL WLDYTKTYKQ TTLIVYILSF IGMVIFTFTL 

       430        440        450        460        470        480 
DLRYIIIVFV TGGVLGFFMT GYLPLGFEFA VEITYPESEG TSSGLLNASA QIFGILFTLA 

       490        500        510        520        530        540 
QGKLTSDYGP KAGNIFLCVW MFIGIILTAL IKSDLRRHNI NIGITNVDVK AIPADSPTDQ 

       550 
EPKTVMLSKQ SESAI 

« Hide

Isoform 2 (FLVC1b) (mitochondrial) [UniParc].

Checksum: FA59C9CBEE5CE3CA
Show »

FASTA27930,744

References

« Hide 'large scale' references
[1]"A putative cell surface receptor for anemia-inducing feline leukemia virus subgroup C is a member of a transporter superfamily."
Tailor C.S., Willett B.J., Kabat D.
J. Virol. 73:6500-6505(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, CHARACTERIZATION OF FELV-C RECEPTOR FUNCTION.
Tissue: Lymphocyte.
[2]"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] (ISOFORM 2).
[3]NHLBI resequencing and genotyping service (RS&G)
Submitted (APR-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[4]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. 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 (SEP-2005) to the EMBL/GenBank/DDBJ databases
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] (ISOFORM 2), VARIANTS PRO-52 AND MET-544.
Tissue: Duodenum.
[6]"Genomic structure and evolutionary context of the human feline leukemia virus subgroup C receptor (hFLVCR) gene: evidence for block duplications and de novo gene formation within duplicons of the hFLVCR locus."
Lipovich L., Hughes A.L., King M.-C., Abkowitz J.L., Quigley J.G.
Gene 286:203-213(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: GENE STRUCTURE.
[7]"Identification of a human heme exporter that is essential for erythropoiesis."
Quigley J.G., Yang Z., Worthington M.T., Phillips J.D., Sabo K.M., Sabath D.E., Berg C.L., Sassa S., Wood B.L., Abkowitz J.L.
Cell 118:757-766(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, DEVELOPMENTAL STAGE.
[8]"Comprehensive mapping of receptor-functioning domains in feline leukemia virus subgroup C receptor FLVCR1."
Brown J.K., Fung C., Tailor C.S.
J. Virol. 80:1742-1751(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, TOPOLOGY, GLYCOSYLATION.
[9]"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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[10]"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[11]"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-56, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[12]"Kinetics and specificity of feline leukemia virus subgroup C receptor (FLVCR) export function and its dependence on hemopexin."
Yang Z., Philips J.D., Doty R.T., Giraudi P., Ostrow J.D., Tiribelli C., Smith A., Abkowitz J.L.
J. Biol. Chem. 285:28874-28882(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH HPX.
[13]"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.
[14]"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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[15]"The mitochondrial heme exporter FLVCR1b mediates erythroid differentiation."
Chiabrando D., Marro S., Mercurio S., Giorgi C., Petrillo S., Vinchi F., Fiorito V., Fagoonee S., Camporeale A., Turco E., Merlo G.R., Silengo L., Altruda F., Pinton P., Tolosano E.
J. Clin. Invest. 122:4569-4579(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ALTERNATIVE SPLICING (ISOFORM 2), FUNCTION (ISOFORM 2), SUBCELLULAR LOCATION (ISOFORM 2).
[16]"Mutations in FLVCR1 cause posterior column ataxia and retinitis pigmentosa."
Rajadhyaksha A.M., Elemento O., Puffenberger E.G., Schierberl K.C., Xiang J.Z., Putorti M.L., Berciano J., Poulin C., Brais B., Michaelides M., Weleber R.G., Higgins J.J.
Am. J. Hum. Genet. 87:643-654(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS PCARP ASP-121; ARG-192 AND THR-241.
[17]"Posterior column ataxia with retinitis pigmentosa in a Japanese family with a novel mutation in FLVCR1."
Ishiura H., Fukuda Y., Mitsui J., Nakahara Y., Ahsan B., Takahashi Y., Ichikawa Y., Goto J., Sakai T., Tsuji S.
Neurogenetics 12:117-121(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT PCARP ARG-493.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF118637 mRNA. Translation: AAD45243.1.
AK001419 mRNA. Translation: BAA91679.1.
DQ496107 Genomic DNA. Translation: ABF47096.1.
CH471100 Genomic DNA. Translation: EAW93374.1.
BC048312 mRNA. Translation: AAH48312.1.
RefSeqNP_054772.1. NM_014053.3.
UniGeneHs.7055.

3D structure databases

ProteinModelPortalQ9Y5Y0.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid118803. 1 interaction.
STRING9606.ENSP00000355938.

Protein family/group databases

TCDB2.A.1.28.1. the major facilitator superfamily (mfs).

PTM databases

PhosphoSiteQ9Y5Y0.

Polymorphism databases

DMDM46396053.

Proteomic databases

PaxDbQ9Y5Y0.
PRIDEQ9Y5Y0.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000366971; ENSP00000355938; ENSG00000162769. [Q9Y5Y0-1]
GeneID28982.
KEGGhsa:28982.
UCSCuc001hjt.3. human. [Q9Y5Y0-1]

Organism-specific databases

CTD28982.
GeneCardsGC01P213031.
HGNCHGNC:24682. FLVCR1.
HPAHPA046646.
MIM609033. phenotype.
609144. gene.
neXtProtNX_Q9Y5Y0.
Orphanet88628. Posterior column ataxia - retinitis pigmentosa.
PharmGKBPA162388695.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG297699.
HOGENOMHOG000019717.
HOVERGENHBG051631.
InParanoidQ9Y5Y0.
KOK08220.
OMAFKEKPQY.
OrthoDBEOG7KQ21D.
PhylomeDBQ9Y5Y0.
TreeFamTF314292.

Enzyme and pathway databases

ReactomeREACT_15518. Transmembrane transport of small molecules.

Gene expression databases

BgeeQ9Y5Y0.
CleanExHS_FLVCR1.
GenevestigatorQ9Y5Y0.

Family and domain databases

InterProIPR011701. MFS.
IPR020846. MFS_dom.
IPR016196. MFS_dom_general_subst_transpt.
[Graphical view]
PfamPF07690. MFS_1. 1 hit.
[Graphical view]
SUPFAMSSF103473. SSF103473. 1 hit.
PROSITEPS50850. MFS. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GeneWikiFLVCR1.
GenomeRNAi28982.
NextBio51873.
PROQ9Y5Y0.
SOURCESearch...

Entry information

Entry nameFLVC1_HUMAN
AccessionPrimary (citable) accession number: Q9Y5Y0
Secondary accession number(s): Q1HE16, Q86XY9, Q9NVR9
Entry history
Integrated into UniProtKB/Swiss-Prot: April 13, 2004
Last sequence update: November 1, 1999
Last modified: April 16, 2014
This is version 97 of the entry and version 1 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 1

Human chromosome 1: entries, gene names and cross-references to MIM