Skip Header

Contribute Send feedback
Read comments (0) or add your own

Reviewed, UniProtKB/Swiss-Prot O76082 (S22A5_HUMAN)

Last modified February 9, 2010. Version 92. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Alternative products · Sequence annotation (Features) · Sequences · References · Web resources · Cross-references · Entry information · Relevant documents

Hide | Top

Names and origin

Protein namesRecommended name:
    Solute carrier family 22 member 5
Alternative name(s):
    Organic cation/carnitine transporter 2
    High-affinity sodium-dependent carnitine cotransporter
Gene names
Name: SLC22A5
Synonyms: OCTN2
OrganismHomo sapiens (Human) [Complete proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Hide | Top

Protein attributes

Sequence length557 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level.

Hide | Top

General annotation (Comments)

Function

Sodium-ion dependent, high affinity carnitine transporter. Involved in the active cellular uptake of carnitine. Transports one sodium ion with one molecule of carnitine. Also transports organic cations such as tetraethylammonium (TEA) without the involvement of sodium. Also Relative uptake activity ratio of carnitine to TEA is 11.3.

Subunit structure

Interacts with PDZK1 By similarity.

Subcellular location

Membrane; Multi-pass membrane protein Ref.16.

Tissue specificity

Strongly expressed in kidney, skeletal muscle, heart and placenta. Highly expressed in intestinal cell types affected by Crohn disease, including epithelial cells. Expressed in CD68 macrophage and CD43 T-cells but not in CD20 B-cells.

Involvement in disease

Defects in SLC22A5 are the cause of systemic primary carnitine deficiency (CDSP) [MIM:212140]. CDSP is an autosomal recessive disorder of fatty acid oxidation caused by defective carnitine transport. Present early in life with hypoketotic hypoglycemia and acute metabolic decompensation, or later in life with skeletal myopathy or cardiomyopathy. Ref.16 Ref.10 Ref.11 Ref.12 Ref.13 Ref.14 Ref.15

Defects in SLC22A5 may be a cause of susceptibility to Crohn disease (CD) [MIM:266600]. CD is a form of remitting inflammatory bowel disease (IBD). CD may involve any part of the gastrointestinal tract, but most frequently the terminal ileum and colon. Bowel inflammation is transmural and discontinuous. CD is commonly classified as an autoimmune disease. Ref.16 Ref.10 Ref.11 Ref.12 Ref.13 Ref.14 Ref.15 Ref.17

Miscellaneous

Inhibited by emetine, quinidine and verapamil. The IC50 of emetine is 4.2 µM. Not inhibited by valproic acid.

Sequence similarities

Belongs to the major facilitator superfamily. Organic cation transporter family.

Hide | Top

Ontologies

Keywords
   Biological processIon transport
Sodium transport
Symport
Transport
   Cellular componentMembrane
   Coding sequence diversityAlternative splicing
Polymorphism
   DiseaseDisease mutation
   DomainTransmembrane
   LigandATP-binding
Nucleotide-binding
Sodium
   PTMGlycoprotein
Phosphoprotein
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processcarnitine transport Ref.2 Ref.3

Inferred from direct assay. Source: UniProtKB

drug transport

Inferred by curator. Source: UniProtKB

positive regulation of intestinal epithelial structure maintenance

Inferred from mutant phenotype. Source: UniProtKB

quorum sensing during interaction with host

Inferred from mutant phenotype. Source: UniProtKB

sodium ion transport

Inferred from electronic annotation. Source: UniProtKB-KW

sodium-dependent organic cation transport Ref.2

Inferred from direct assay. Source: UniProtKB

transmembrane transport

Inferred from electronic annotation. Source: InterPro

   Cellular componentapical plasma membrane

Inferred from direct assay. Source: UniProtKB

brush border membrane

Inferred from direct assay. Source: UniProtKB

integral to membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

PDZ domain binding

Inferred from physical interaction. Source: UniProtKB

carnitine transporter activity Ref.2 Ref.3

Inferred from direct assay. Source: UniProtKB

drug transporter activity

Inferred by curator. Source: UniProtKB

sodium ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

symporter activity

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Hide | Top

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: O76082-1)

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: O76082-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-336: Missing.
     337-351: TWNIRMVTIMSIMLW → MWILLFQLSSALCFR
Note: No experimental confirmation available.

Hide | Top

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 557557Solute carrier family 22 member 5
PRO_0000220500

Regions

Topological domain1 – 2020Cytoplasmic Potential
Transmembrane21 – 41211 Potential
Topological domain42 – 142101Extracellular Potential
Transmembrane143 – 163212 Potential
Topological domain164 – 1729Cytoplasmic Potential
Transmembrane173 – 193213 Potential
Topological domain194 – 1974Extracellular Potential
Transmembrane198 – 218214 Potential
Topological domain219 – 23214Cytoplasmic Potential
Transmembrane233 – 253215 Potential
Topological domain254 – 2574Extracellular Potential
Transmembrane258 – 278216 Potential
Topological domain279 – 34163Cytoplasmic Potential
Transmembrane342 – 362217 Potential
Topological domain363 – 37311Extracellular Potential
Transmembrane374 – 394218 Potential
Topological domain395 – 40612Cytoplasmic Potential
Transmembrane407 – 427219 Potential
Topological domain428 – 4303Extracellular Potential
Transmembrane431 – 4512110 Potential
Topological domain452 – 46211Cytoplasmic Potential
Transmembrane463 – 4832111 Potential
Topological domain484 – 4885Extracellular Potential
Transmembrane489 – 5092112 Potential
Nucleotide binding218 – 2258ATP Potential

Amino acid modifications

Modified residue4861Phosphotyrosine Ref.9
Glycosylation571N-linked (GlcNAc...) Ref.8
Glycosylation641N-linked (GlcNAc...) Potential
Glycosylation911N-linked (GlcNAc...) Ref.8

Natural variations

Alternative sequence1 – 336336Missing in isoform 2.
VSP_011120
Alternative sequence337 – 35115TWNIR…SIMLW → MWILLFQLSSALCFR in isoform 2.
VSP_011121
Natural variant171F → L
VAR_020347
Natural variant1441L → F: dbSNP rs10040427. Ref.18
VAR_020348
Natural variant1691R → Q in CDSP. Ref.10
VAR_009252
Natural variant1791M → L in CDSP. Ref.13
VAR_022564
Natural variant2111Y → C in CDSP. Ref.11
VAR_009253
Natural variant2831W → C in CDSP; reduces L-carnitine uptake. Ref.13
VAR_022565
Natural variant2831W → R in CDSP. Ref.15
VAR_009254
Natural variant4461V → F in CDSP. Ref.15
VAR_009255
Natural variant4491Y → D: dbSNP rs11568514. Ref.18
VAR_029315
Natural variant4521E → K in CDSP. Ref.16
VAR_009256
Natural variant4671S → C in CDSP; reduces L-carnitine uptake. Ref.13
VAR_022566
Natural variant4781P → L in CDSP; loss of carnitine transport but stimulated organic cation transport. Ref.12 Ref.14
VAR_009257
Natural variant4811V → F
VAR_020349
Natural variant4811V → I
VAR_036816
Natural variant5081F → L
VAR_029316
Natural variant5301M → V
VAR_029317
Natural variant5491P → S: dbSNP rs11568525. Ref.18
VAR_020350

Experimental info

Mutagenesis3521M → R: Loss of both carnitine and organic cation transport functionalities.
Sequence conflict1141L → P in AAH12325. Ref.6

Hide | Top

Sequences

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

Last modified November 1, 1998. Version 1.
Checksum: 928B1F6EFF63C48D

FASTA55762,752
        10         20         30         40         50         60 
MRDYDEVTAF LGEWGPFQRL IFFLLSASII PNGFTGLSSV FLIATPEHRC RVPDAANLSS 

        70         80         90        100        110        120 
AWRNHTVPLR LRDGREVPHS CRRYRLATIA NFSALGLEPG RDVDLGQLEQ ESCLDGWEFS 

       130        140        150        160        170        180 
QDVYLSTIVT EWNLVCEDDW KAPLTISLFF VGVLLGSFIS GQLSDRFGRK NVLFVTMGMQ 

       190        200        210        220        230        240 
TGFSFLQIFS KNFEMFVVLF VLVGMGQISN YVAAFVLGTE ILGKSVRIIF STLGVCIFYA 

       250        260        270        280        290        300 
FGYMVLPLFA YFIRDWRMLL VALTMPGVLC VALWWFIPES PRWLISQGRF EEAEVIIRKA 

       310        320        330        340        350        360 
AKANGIVVPS TIFDPSELQD LSSKKQQSHN ILDLLRTWNI RMVTIMSIML WMTISVGYFG 

       370        380        390        400        410        420 
LSLDTPNLHG DIFVNCFLSA MVEVPAYVLA WLLLQYLPRR YSMATALFLG GSVLLFMQLV 

       430        440        450        460        470        480 
PPDLYYLATV LVMVGKFGVT AAFSMVYVYT AELYPTVVRN MGVGVSSTAS RLGSILSPYF 

       490        500        510        520        530        540 
VYLGAYDRFL PYILMGSLTI LTAILTLFLP ESFGTPLPDT IDQMLRVKGM KHRKTPSHTR 

       550 
MLKDGQERPT ILKSTAF

« Hide

Isoform 2.

Checksum: B66DFBC13A50BDAF
Show »

FASTA22124,688

Hide | Top

References

« Hide 'large scale' references
[1]"cDNA sequence, transport function, and genomic organization of human OCTN2, a new member of the organic cation transporter family."
Wu X., Prasad P.D., Leibach F.H., Ganapathy V.
Biochem. Biophys. Res. Commun. 246:589-595(1998) [PubMed: 9618255] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[2]"Molecular and functional identification of sodium ion-dependent, high affinity human carnitine transporter OCTN2."
Tamai I., Ohashi R., Nezu J., Yabuuchi H., Oku A., Shimane M., Sai Y., Tsuji A.
J. Biol. Chem. 273:20378-20382(1998) [PubMed: 9685390] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Tissue: Kidney.
[3]"Primary systemic carnitine deficiency is caused by mutations in a gene encoding sodium ion-dependent carnitine transporter."
Nezu J., Tamai I., Oku A., Ohashi R., Yabuuchi H., Hashimoto N., Nikaido H., Sai Y., Koizumi A., Shoji Y., Takada G., Matsuishi T., Yashino M., Kato H., Ohura T., Tsujimoto G., Hayakawa J., Shimane M., Tsuji A.
Nat. Genet. 21:91-94(1999) [PubMed: 9916797] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1).
[4]"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: 14702039] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
Tissue: Trachea.
[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. 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].
[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: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Tissue: Lung.
[7]"Functional characteristics and tissue distribution pattern of organic cation transporter 2 (OCTN2), an organic cation/carnitine transporter."
Wu X., Huang W., Prasad P.D., Seth P., Rajan D.P., Leibach F.H., Chen J., Conway S.J., Ganapathy V.
J. Pharmacol. Exp. Ther. 290:1482-1492(1999) [PubMed: 10454528] [Abstract]
Cited for: CHARACTERIZATION.
[8]"Mass-spectrometric identification and relative quantification of N-linked cell surface glycoproteins."
Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M., Schiess R., Aebersold R., Watts J.D.
Nat. Biotechnol. 27:378-386(2009) [PubMed: 19349973] [Abstract]
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-57 AND ASN-91, MASS SPECTROMETRY.
[9]"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: 19690332] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-486, MASS SPECTROMETRY.
Tissue: T-cell.
[10]"Carnitine transporter OCTN2 mutations in systemic primary carnitine deficiency: a novel Arg169Gln mutation and a recurrent Arg282ter mutation associated with an unconventional splicing abnormality."
Burwinkel B., Kreuder J., Schweitzer S., Vorgerd M., Gempel K., Gerbitz K.-D., Kilimann M.W.
Biochem. Biophys. Res. Commun. 261:484-487(1999) [PubMed: 10425211] [Abstract]
Cited for: VARIANT CDSP GLN-169.
[11]"Identification of two novel mutations in OCTN2 of three patients with systemic carnitine deficiency."
Vaz F.M., Scholte H.R., Ruiter J., Hussaarts-Odijk L.M., Rodrigues Pereira R., Schweitzer S., de Klerk J.B.C., Waterham H.R., Wanders R.J.A.
Hum. Genet. 105:157-161(1999) [PubMed: 10480371] [Abstract]
Cited for: VARIANT CDSP CYS-211.
[12]"Mutations of OCTN2, an organic cation/carnitine transporter, lead to deficient cellular carnitine uptake in primary carnitine deficiency."
Tang N.L., Ganapathy V., Wu X., Hui J., Seth P., Yuen P.M., Wanders R.J., Fok T.F., Hjelm N.M.
Hum. Mol. Genet. 8:655-660(1999) [PubMed: 10072434] [Abstract]
Cited for: VARIANT CDSP LEU-478.
[13]"Genetic epidemiology of the carnitine transporter OCTN2 gene in a Japanese population and phenotypic characterization in Japanese pedigrees with primary systemic carnitine deficiency."
Koizumi A., Nozaki J., Ohura T., Kayo T., Wada Y., Nezu J., Ohashi R., Tamai I., Shoji Y., Takada G., Kibira S., Matsuishi T., Tsuji A.
Hum. Mol. Genet. 8:2247-2254(1999) [PubMed: 10545605] [Abstract]
Cited for: VARIANTS CDSP LEU-179; CYS-283 AND CYS-467, CHARACTERIZATION OF VARIANTS CDSP LEU-179; CYS-283 AND CYS-467.
[14]"Mutations in novel organic cation transporter (OCTN2), an organic cation/carnitine transporter, with differential effects on the organic cation transport function and the carnitine transport function."
Seth P., Wu X., Huang W., Leibach F.H., Ganapathy V.
J. Biol. Chem. 274:33388-33392(1999) [PubMed: 10559218] [Abstract]
Cited for: CHARACTERIZATION OF VARIANT CDSP LEU-478, MUTAGENESIS.
[15]"Two novel missense mutations of the OCTN2 gene (W283R and V446F) in a patient with primary systemic carnitine deficiency."
Mayatepek E., Nezu J., Tamai I., Oku A., Katsura M., Shimane M., Tsuji A.
Hum. Mutat. 15:118-118(2000) [PubMed: 10612840] [Abstract]
Cited for: VARIANTS CDSP ARG-283 AND PHE-446.
[16]"A missense mutation in the OCTN2 gene associated with residual carnitine transport activity."
Wang Y., Kelly M.A., Cowan T.M., Longo N.
Hum. Mutat. 15:238-245(2000) [PubMed: 10679939] [Abstract]
Cited for: SUBCELLULAR LOCATION, VARIANT CDSP LYS-452.
[17]"Functional variants of OCTN cation transporter genes are associated with Crohn disease."
Peltekova V.D., Wintle R.F., Rubin L.A., Amos C.I., Huang Q., Gu X., Newman B., Van Oene M., Cescon D., Greenberg G., Griffiths A.M., St George-Hyslop P.H., Siminovitch K.A.
Nat. Genet. 36:471-475(2004) [PubMed: 15107849] [Abstract]
Cited for: INVOLVEMENT IN CD.
[18]"Functional genetic diversity in the high-affinity carnitine transporter OCTN2 (SLC22A5)."
Urban T.J., Gallagher R.C., Brown C., Castro R.A., Lagpacan L.L., Brett C.M., Taylor T.R., Carlson E.J., Ferrin T.E., Burchard E.G., Packman S., Giacomini K.M.
Mol. Pharmacol. 70:1602-1611(2006) [PubMed: 16931768] [Abstract]
Cited for: VARIANTS LEU-17; PHE-144; ASP-449; ILE-481; PHE-481; LEU-508; VAL-530 AND SER-549.
+Additional computationally mapped references.

Hide | Top

Web resources

GeneReviews

Hide | Top

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AF057164 mRNA. Translation: AAC24828.1.
AB015050 mRNA. Translation: BAA29023.1.
AB016625 Genomic DNA. Translation: BAA36712.1.
AK128610 mRNA. Translation: BAC87527.1.
AK313230 mRNA. Translation: BAG36041.1.
CH471062 Genomic DNA. Translation: EAW62337.1.
BC012325 mRNA. Translation: AAH12325.1.
IPIIPI00435872.
IPI00435873.
PIRJW0089.
RefSeqNP_003051.1.
UniGeneHs.443572

3D structure databases

SMRO76082. Positions 125-282, 142-508.
ModBaseSearch...

Protein-protein interaction databases

STRINGO76082.

Protein family/group databases

TCDB2.A.1.19.3. major facilitator superfamily (MFS).

Proteomic databases

PRIDEO76082.

Genome annotation databases

EnsemblENST00000245407; ENSP00000245407; ENSG00000197375; Homo sapiens. [Genome view]
GeneID6584.
KEGGhsa:6584.
UCSCuc003kww.2. human.

Organism-specific databases

CTD6584.
GeneCardsGC05P131733.
H-InvDBHIX0005155.
HGNCHGNC:10969. SLC22A5.
MIM212140. phenotype.
266600. phenotype.
603377. gene.
Orphanet158. Carnitine uptake deficiency.
PharmGKBPA333.
GenAtlasSearch...

Phylogenomic databases

eggNOGprNOG18524.
HOVERGENO76082.
InParanoidO76082.
PhylomeDBO76082.

Gene expression databases

ArrayExpressO76082.
BgeeO76082.
CleanExHS_SLC22A5.
GenevestigatorO76082.
GermOnlineENSG00000197375. Homo sapiens.

Family and domain databases

InterProIPR016196. MFS_general_subst_transpt.
IPR004749. Orgcat_transp.
IPR005829. Sugar_transporter_CS.
[Graphical view]
TIGRFAMsTIGR00898. 2A0119. 1 hit.
PROSITEPS50850. MFS. 1 hit.
PS00216. SUGAR_TRANSPORT_1. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

DrugBankDB00583. L-Carnitine.
NextBio25621.
SOURCESearch...

Hide | Top

Entry information

Entry nameS22A5_HUMAN
AccessionPrimary (citable) accession number: O76082
Secondary accession number(s): B2R844, Q6ZQZ8, Q96EH6
Entry history
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: November 1, 1998
Last modified: February 9, 2010
This is version 92 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)
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.

Hide | Top

Relevant documents

Human chromosome 5

Human chromosome 5: entries, gene names and cross-references to MIM

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

MIM cross-references

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

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Alternative products · Sequence annotation (Features) · Sequences · References · Web resources · Cross-references · Entry information · Relevant documents