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Q96S37 (S22AC_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 104. 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:
Solute carrier family 22 member 12
Alternative name(s):
Organic anion transporter 4-like protein
Renal-specific transporter
Short name=RST
Urate anion exchanger 1
Gene names
Name:SLC22A12
Synonyms:OATL4, URAT1
ORF Names:UNQ6453/PRO34004
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length553 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Required for efficient urate re-absorption in the kidney. Regulates blood urate levels. Mediates saturable urate uptake by facilitating the exchange of urate against organic anions. Ref.1

Subunit structure

Interacts with PDZK1. Ref.10 Ref.11

Subcellular location

Cell membrane; Multi-pass membrane protein. Note: Detected in the luminal membrane of the epithelium of renal proximal tubules. Ref.1

Tissue specificity

Detected in kidney (at protein level). Detected in fetal and adult kidney. Detected in epithelial cells of proximal tubules in renal cortex. Ref.1 Ref.11

Involvement in disease

Hypouricemia renal 1 (RHUC1) [MIM:220150]: A disorder characterized by impaired uric acid reabsorption at the apical membrane of proximal renal tubule cells, and high urinary urate excretion. Patients often appear asymptomatic, but may be subject to exercise-induced acute renal failure, chronic renal dysfunction and nephrolithiasis.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.1 Ref.9 Ref.12 Ref.13 Ref.14 Ref.15

Sequence similarities

Belongs to the major facilitator (TC 2.A.1) superfamily. Organic cation transporter (TC 2.A.1.19) family. [View classification]

Sequence caution

The sequence BAB68364.1 differs from that shown. Reason: Frameshift at positions 84 and 136.

Alternative products

This entry describes 4 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q96S37-1)

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: Q96S37-2)

The sequence of this isoform differs from the canonical sequence as follows:
     170-277: Missing.
Isoform 3 (identifier: Q96S37-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1-221: Missing.
Isoform 4 (identifier: Q96S37-4)

The sequence of this isoform differs from the canonical sequence as follows:
     187-221: GTAAAFAPAFPVYCLFRFLLAFAVAGVMMNTGTLL → V

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 553553Solute carrier family 22 member 12
PRO_0000307944

Regions

Transmembrane9 – 2921Helical; Potential
Transmembrane146 – 16621Helical; Potential
Transmembrane174 – 19421Helical; Potential
Transmembrane195 – 21521Helical; Potential
Transmembrane232 – 25221Helical; Potential
Transmembrane260 – 28021Helical; Potential
Transmembrane351 – 37121Helical; Potential
Transmembrane378 – 39821Helical; Potential
Transmembrane407 – 42721Helical; Potential
Transmembrane435 – 45521Helical; Potential
Transmembrane466 – 48621Helical; Potential
Transmembrane495 – 51521Helical; Potential

Amino acid modifications

Glycosylation561N-linked (GlcNAc...) Potential
Glycosylation1021N-linked (GlcNAc...) Potential

Natural variations

Alternative sequence1 – 221221Missing in isoform 3.
VSP_054054
Alternative sequence170 – 277108Missing in isoform 2.
VSP_028879
Alternative sequence187 – 22135GTAAA…TGTLL → V in isoform 4.
VSP_054055
Natural variant651G → W.
Corresponds to variant rs12800450 [ dbSNP | Ensembl ].
VAR_036720
Natural variant901R → H in RHUC1; strongly reduced urate transport. Ref.12 Ref.13 Ref.15
VAR_036721
Natural variant921R → C. Ref.16
VAR_036722
Natural variant1381V → M in RHUC1; strongly reduced urate transport. Ref.12
VAR_036723
Natural variant1641G → S in RHUC1; reduced urate transport. Ref.12
VAR_036724
Natural variant2171T → M in RHUC1; strongly reduced urate transport. Ref.1 Ref.12
VAR_036725
Natural variant2261A → V. Ref.13
Corresponds to variant rs145738825 [ dbSNP | Ensembl ].
VAR_036726
Natural variant2841R → G in some gout patients; uncertain pathological significance. Ref.9
VAR_036727
Natural variant2901G → C in some gout patients; uncertain pathological significance. Ref.9
VAR_036728
Natural variant2971Q → E in some gout patients; uncertain pathological significance. Ref.9
VAR_036729
Natural variant2981E → D in RHUC1; strongly reduced urate transport. Ref.1 Ref.9
VAR_036730
Natural variant3051I → S in some gout patients; uncertain pathological significance. Ref.9
VAR_036731
Natural variant3121Q → L. Ref.13
VAR_036732
Natural variant313 – 33321Missing Affects urate transport.
VAR_036733
Natural variant3821Q → L in RHUC1; strongly reduced urate transport. Ref.12 Ref.14
VAR_036734
Natural variant4181L → R in RHUC1; strongly reduced urate transport. Ref.14
VAR_036735
Natural variant4301M → T in RHUC1; reduced urate transport. Ref.12
VAR_036736
Natural variant4771R → H in RHUC1. Ref.13 Ref.15
VAR_036737

Experimental info

Sequence conflict4511C → Y in AAQ88550. Ref.3
Sequence conflict5381A → T in AK315061. Ref.5

Sequences

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

Last modified December 1, 2001. Version 1.
Checksum: E3F29F38129BAD61

FASTA55359,630
        10         20         30         40         50         60 
MAFSELLDLV GGLGRFQVLQ TMALMVSIMW LCTQSMLENF SAAVPSHRCW APLLDNSTAQ 

        70         80         90        100        110        120 
ASILGSLSPE ALLAISIPPG PNQRPHQCRR FRQPQWQLLD PNATATSWSE ADTEPCVDGW 

       130        140        150        160        170        180 
VYDRSIFTST IVAKWNLVCD SHALKPMAQS IYLAGILVGA AACGPASDRF GRRLVLTWSY 

       190        200        210        220        230        240 
LQMAVMGTAA AFAPAFPVYC LFRFLLAFAV AGVMMNTGTL LMEWTAARAR PLVMTLNSLG 

       250        260        270        280        290        300 
FSFGHGLTAA VAYGVRDWTL LQLVVSVPFF LCFLYSWWLA ESARWLLTTG RLDWGLQELW 

       310        320        330        340        350        360 
RVAAINGKGA VQDTLTPEVL LSAMREELSM GQPPASLGTL LRMPGLRFRT CISTLCWFAF 

       370        380        390        400        410        420 
GFTFFGLALD LQALGSNIFL LQMFIGVVDI PAKMGALLLL SHLGRRPTLA ASLLLAGLCI 

       430        440        450        460        470        480 
LANTLVPHEM GALRSALAVL GLGGVGAAFT CITIYSSELF PTVLRMTAVG LGQMAARGGA 

       490        500        510        520        530        540 
ILGPLVRLLG VHGPWLPLLV YGTVPVLSGL AALLLPETQS LPLPDTIQDV QNQAVKKATH 

       550 
GTLGNSVLKS TQF 

« Hide

Isoform 2 [UniParc].

Checksum: 5385EA4A75ABD7C4
Show »

FASTA44547,648
Isoform 3 [UniParc].

Checksum: 0080739C739B384B
Show »

FASTA33235,570
Isoform 4 [UniParc].

Checksum: A29300D5DC37247A
Show »

FASTA51956,094

References

« Hide 'large scale' references
[1]"Molecular identification of a renal urate anion exchanger that regulates blood urate levels."
Enomoto A., Kimura H., Chairoungdua A., Shigeta Y., Jutabha P., Cha S.H., Hosoyamada M., Takeda M., Sekine T., Igarashi T., Matsuo H., Kikuchi Y., Oda T., Ichida K., Hosoya T., Shimokata K., Niwa T., Kanai Y., Endou H.
Nature 417:447-452(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, TISSUE SPECIFICITY, SUBCELLULAR LOCATION, VARIANTS RHUC1 MET-217 AND ASP-298, CHARACTERIZATION OF VARIANTS RHUC1 MET-217 AND ASP-298.
Tissue: Kidney.
[2]"Sequencing of human RST gene."
Rowen L., Madan A., Qin S., Baradarani L., Birditt B., Bloom S., Burke J., Dors M., Fleetwood P., Kaur A., Madan A., Nesbitt R., Pate D., Hood L.
Submitted (JUN-2001) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]"The secreted protein discovery initiative (SPDI), a large-scale effort to identify novel human secreted and transmembrane proteins: a bioinformatics assessment."
Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J., Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P., Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E. expand/collapse author list , Heldens S., Huang A., Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D., Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L., Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C., Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J., Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M.
Genome Res. 13:2265-2270(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
[4]"Human organic anion transporter 4 similar gene."
Koyama K.
Submitted (OCT-2000) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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] (ISOFORM 4).
[6]"Human chromosome 11 DNA sequence and analysis including novel gene identification."
Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K., Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F., Bloom T., Bruford E., Chang J.L., Cuomo C.A., Eichler E., FitzGerald M.G. expand/collapse author list , Jaffe D.B., LaButti K., Nicol R., Park H.-S., Seaman C., Sougnez C., Yang X., Zimmer A.R., Zody M.C., Birren B.W., Nusbaum C., Fujiyama A., Hattori M., Rogers J., Lander E.S., Sakaki Y.
Nature 440:497-500(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]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 (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).
Tissue: Colon.
[9]"Molecular analysis of the SLC22A12 (URAT1) gene in patients with primary gout."
Vazquez-Mellado J., Jimenez-Vaca A.L., Cuevas-Covarrubias S., Alvarado-Romano V., Pozo-Molina G., Burgos-Vargas R.
Rheumatology 46:215-219(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 278-318, VARIANT RHUC1 ASP-298, VARIANTS GLY-284; CYS-290; GLU-297 AND SER-305.
[10]"PDZK1: I. a major scaffolder in brush borders of proximal tubular cells."
Gisler S.M., Pribanic S., Bacic D., Forrer P., Gantenbein A., Sabourin L.A., Tsuji A., Zhao Z.-S., Manser E., Biber J., Murer H.
Kidney Int. 64:1733-1745(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH PDZK1.
[11]"The multivalent PDZ domain-containing protein PDZK1 regulates transport activity of renal urate-anion exchanger URAT1 via its C terminus."
Anzai N., Miyazaki H., Noshiro R., Khamdang S., Chairoungdua A., Shin H.J., Enomoto A., Sakamoto S., Hirata T., Tomita K., Kanai Y., Endou H.
J. Biol. Chem. 279:45942-45950(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH PDZK1, TISSUE SPECIFICITY.
[12]"Clinical and molecular analysis of patients with renal hypouricemia in Japan-influence of URAT1 gene on urinary urate excretion."
Ichida K., Hosoyamada M., Hisatome I., Enomoto A., Hikita M., Endou H., Hosoya T.
J. Am. Soc. Nephrol. 15:164-173(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS RHUC1 HIS-90; MET-138; SER-164; MET-217; LEU-382 AND THR-430, CHARACTERIZATION OF VARIANTS RHUC1 HIS-90; MET-138; SER-164; MET-217; LEU-382 AND THR-430.
[13]"A high prevalence of renal hypouricemia caused by inactive SLC22A12 in Japanese."
Iwai N., Mino Y., Hosoyamada M., Tago N., Kokubo Y., Endou H.
Kidney Int. 66:935-944(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS RHUC1 HIS-90 AND HIS-477, VARIANTS VAL-226; LEU-312 AND 313-ASP--PRO-333 DEL, CHARACTERIZATION OF VARIANT 313-ASP--PRO-333 DEL.
[14]"Mutations in human urate transporter 1 gene in presecretory reabsorption defect type of familial renal hypouricemia."
Wakida N., Tuyen D.G., Adachi M., Miyoshi T., Nonoguchi H., Oka T., Ueda O., Tazawa M., Kurihara S., Yoneta Y., Shimada H., Oda T., Kikuchi Y., Matsuo H., Hosoyamada M., Endou H., Otagiri M., Tomita K., Kitamura K.
J. Clin. Endocrinol. Metab. 90:2169-2174(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS RHUC1 LEU-382 AND ARG-418, CHARACTERIZATION OF VARIANTS RHUC1 LEU-382 AND ARG-418.
[15]"Mutational analysis of idiopathic renal hypouricemia in Korea."
Cheong H.I., Kang J.H., Lee J.H., Ha I.S., Kim S., Komoda F., Sekine T., Igarashi T., Choi Y.
Pediatr. Nephrol. 20:886-890(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS RHUC1 HIS-90 AND HIS-477.
[16]"Association of the human urate transporter 1 with reduced renal uric acid excretion and hyperuricemia in a German Caucasian population."
Graessler J., Graessler A., Unger S., Kopprasch S., Tausche A.-K., Kuhlisch E., Schroeder H.-E.
Arthritis Rheum. 54:292-300(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT CYS-92.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB071863 mRNA. Translation: BAB96750.1.
AC044790 Genomic DNA. Translation: AAK68156.1.
AY358183 mRNA. Translation: AAQ88550.1.
AB050269 mRNA. Translation: BAB68364.1. Frameshift.
AK315061 mRNA. No translation available.
AP001092 Genomic DNA. No translation available.
CH471076 Genomic DNA. Translation: EAW74273.1.
CH471076 Genomic DNA. Translation: EAW74274.1.
BC053348 mRNA. Translation: AAH53348.1.
DQ514593 Genomic DNA. Translation: ABF74570.1.
DQ514594 Genomic DNA. Translation: ABF74571.1.
DQ514595 Genomic DNA. Translation: ABF74572.1.
DQ514596 Genomic DNA. Translation: ABF74573.1.
CCDSCCDS60836.1. [Q96S37-2]
CCDS8075.1. [Q96S37-1]
RefSeqNP_001263255.1. NM_001276326.1. [Q96S37-4]
NP_001263256.1. NM_001276327.1. [Q96S37-2]
NP_653186.2. NM_144585.3. [Q96S37-1]
NP_700357.1. NM_153378.2. [Q96S37-3]
UniGeneHs.174424.
Hs.700182.

3D structure databases

ProteinModelPortalQ96S37.
SMRQ96S37. Positions 150-287.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid125471. 1 interaction.
STRING9606.ENSP00000366797.

Chemistry

BindingDBQ96S37.
ChEMBLCHEMBL6120.

Protein family/group databases

TCDB2.A.1.19.11. the major facilitator superfamily (mfs).

PTM databases

PhosphoSiteQ96S37.

Polymorphism databases

DMDM74732700.

Proteomic databases

PaxDbQ96S37.
PRIDEQ96S37.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000377567; ENSP00000366790; ENSG00000197891. [Q96S37-2]
ENST00000377572; ENSP00000366795; ENSG00000197891. [Q96S37-2]
ENST00000377574; ENSP00000366797; ENSG00000197891. [Q96S37-1]
ENST00000473690; ENSP00000438437; ENSG00000197891.
GeneID116085.
KEGGhsa:116085.
UCSCuc001oal.2. human. [Q96S37-1]
uc001oan.2. human. [Q96S37-2]

Organism-specific databases

CTD116085.
GeneCardsGC11P064359.
HGNCHGNC:17989. SLC22A12.
HPAHPA024575.
MIM220150. phenotype.
607096. gene.
neXtProtNX_Q96S37.
Orphanet94088. Hereditary renal hypouricemia.
PharmGKBPA38478.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG238692.
HOVERGENHBG108433.
InParanoidQ96S37.
KOK08208.
OMAPIMWLTT.
OrthoDBEOG7NW68T.
PhylomeDBQ96S37.
TreeFamTF315847.

Enzyme and pathway databases

ReactomeREACT_15518. Transmembrane transport of small molecules.

Gene expression databases

ArrayExpressQ96S37.
BgeeQ96S37.
CleanExHS_SLC22A12.
GenevestigatorQ96S37.

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

ChiTaRSSLC22A12. human.
GeneWikiSLC22A12.
GenomeRNAi116085.
NextBio79751.
PROQ96S37.
SOURCESearch...

Entry information

Entry nameS22AC_HUMAN
AccessionPrimary (citable) accession number: Q96S37
Secondary accession number(s): B7WPG1 expand/collapse secondary AC list , G3XAN7, Q19PF7, Q19PF8, Q19PF9, Q19PG0, Q6UXW3, Q96DT2
Entry history
Integrated into UniProtKB/Swiss-Prot: October 23, 2007
Last sequence update: December 1, 2001
Last modified: July 9, 2014
This is version 104 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 11

Human chromosome 11: entries, gene names and cross-references to MIM