Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q13018 (PLA2R_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 113. 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:
Secretory phospholipase A2 receptor

Short name=PLA2-R
Short name=PLA2R
Alternative name(s):
180 kDa secretory phospholipase A2 receptor
C-type lectin domain family 13 member C
M-type receptor

Cleaved into the following chain:

  1. Soluble secretory phospholipase A2 receptor
    Short name=Soluble PLA2-R
    Short name=Soluble PLA2R
Gene names
Name:PLA2R1
Synonyms:CLEC13C
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1463 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Receptor for secretory phospholipase A2 (sPLA2). Acts as a receptor for phosholipase sPLA2-IB/PLA2G1B but not sPLA2-IIA/PLA2G2A. Also able to bind to snake PA2-like toxins. Although its precise function remains unclear, binding of sPLA2 to its receptor participates in both positive and negative regulation of sPLA2 functions as well as clearance of sPLA2. Binding of sPLA2-IB/PLA2G1B induces various effects depending on the cell type, such as activation of the mitogen-activated protein kinase (MAPK) cascade to induce cell proliferation, the production of lipid mediators, selective release of arachidonic acid in bone marrow-derived mast cells. In neutrophils, binding of sPLA2-IB/PLA2G1B can activate p38 MAPK to stimulate elastase release and cell adhesion. May be involved in responses in proinflammatory cytokine productions during endotoxic shock. Also has endocytic properties and rapidly internalizes sPLA2 ligands, which is particularly important for the clearance of extracellular sPLA2s to protect their potent enzymatic activities. The soluble secretory phospholipase A2 receptor form is circulating and acts as a negative regulator of sPLA2 functions by blocking the biological functions of sPLA2-IB/PLA2G1B. Ref.1 Ref.7

Subcellular location

Cell membrane; Single-pass type I membrane protein By similarity.

Soluble secretory phospholipase A2 receptor: Secreted By similarity.

Isoform 2: Secreted Potential.

Tissue specificity

Present in lung macrophage (at protein level). Highly expressed in kidney. Also expressed in pancreas, amnion, choriodecidua and placenta. Isoform 2 is expressed at much lower level. Ref.1 Ref.5 Ref.6 Ref.7

Domain

C-type lectin domains 3-5 mediate the interaction with phospholipase PLA2G1B.

The endocytosis signal probably mediates endocytosis via clathrin-coated pits By similarity.

Post-translational modification

The secretory phospholipase A2 receptor form may be produced by the action of metalloproteinases. It contains all extracellular domains and only lacks transmembrane and cytosolic regions. It is however unclear whether this form is produced by proteolytic cleavage as suggested by some experiments, or by alternative splicing, as in the case of isoform 2 that shares all characteristics of secretory phospholipase A2 receptor form By similarity.

Sequence similarities

Contains 8 C-type lectin domains.

Contains 1 fibronectin type-II domain.

Contains 1 ricin B-type lectin domain.

Ontologies

Keywords
   Biological processEndocytosis
   Cellular componentCell membrane
Membrane
Secreted
   Coding sequence diversityAlternative splicing
Polymorphism
   DomainRepeat
Signal
Transmembrane
Transmembrane helix
   LigandLectin
   Molecular functionReceptor
   PTMDisulfide bond
Glycoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcytokine production

Inferred from mutant phenotype Ref.7. Source: UniProtKB

negative regulation of arachidonic acid secretion

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of phospholipase A2 activity

Inferred from sequence or structural similarity. Source: UniProtKB

oxidative stress-induced premature senescence

Inferred from mutant phenotype PubMed 19197340. Source: UniProtKB

positive regulation of DNA damage response, signal transduction by p53 class mediator

Inferred from mutant phenotype PubMed 19197340. Source: UniProtKB

positive regulation of arachidonic acid secretion

Inferred from sequence or structural similarity. Source: UniProtKB

reactive oxygen species metabolic process

Inferred from direct assay PubMed 19197340. Source: UniProtKB

receptor-mediated endocytosis

Inferred from direct assay Ref.1. Source: UniProtKB

replicative senescence

Inferred from mutant phenotype PubMed 19197340. Source: UniProtKB

   Cellular_componentcell surface

Inferred from direct assay Ref.7. Source: UniProtKB

extracellular region

Inferred from sequence or structural similarity. Source: UniProtKB

integral component of membrane

Inferred from electronic annotation. Source: UniProtKB-KW

integral component of plasma membrane

Non-traceable author statement Ref.1. Source: UniProtKB

plasma membrane

Inferred from direct assay PubMed 12225974. Source: UniProtKB

receptor complex

Inferred from direct assay PubMed 23382219. Source: MGI

   Molecular_functioncarbohydrate binding

Inferred from electronic annotation. Source: InterPro

phospholipase binding

Inferred from physical interaction Ref.1. Source: UniProtKB

receptor activity

Inferred from direct assay Ref.1. Source: UniProtKB

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q13018-1)

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: Q13018-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1323-1324: NE → SK
     1325-1463: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2020 By similarity
Chain21 – 14631443Secretory phospholipase A2 receptor
PRO_5000144349
Chain21 – ?Soluble secretory phospholipase A2 receptor By similarityPRO_0000311250

Regions

Topological domain21 – 13971377Extracellular Potential
Transmembrane1398 – 141821Helical; Potential
Topological domain1419 – 146345Cytoplasmic Potential
Domain38 – 161124Ricin B-type lectin
Domain173 – 22149Fibronectin type-II
Domain238 – 355118C-type lectin 1
Domain385 – 502118C-type lectin 2
Domain522 – 643122C-type lectin 3
Domain673 – 797125C-type lectin 4
Domain819 – 938120C-type lectin 5
Domain965 – 1096132C-type lectin 6
Domain1121 – 1232112C-type lectin 7
Domain1257 – 1378122C-type lectin 8
Motif1436 – 14427Endocytosis signal

Amino acid modifications

Glycosylation931N-linked (GlcNAc...) Potential
Glycosylation4541N-linked (GlcNAc...) Potential
Disulfide bond51 ↔ 64 By similarity
Disulfide bond89 ↔ 106 By similarity
Disulfide bond178 ↔ 204 By similarity
Disulfide bond192 ↔ 219 By similarity
Disulfide bond260 ↔ 354 By similarity
Disulfide bond330 ↔ 346 By similarity
Disulfide bond406 ↔ 501 By similarity
Disulfide bond478 ↔ 493 By similarity
Disulfide bond617 ↔ 634 By similarity
Disulfide bond699 ↔ 796 By similarity
Disulfide bond774 ↔ 788 By similarity
Disulfide bond840 ↔ 937 By similarity
Disulfide bond914 ↔ 929 By similarity
Disulfide bond1067 ↔ 1087 By similarity
Disulfide bond1209 ↔ 1223 By similarity
Disulfide bond1280 ↔ 1377 By similarity
Disulfide bond1354 ↔ 1369 By similarity

Natural variations

Alternative sequence1323 – 13242NE → SK in isoform 2.
VSP_029493
Alternative sequence1325 – 1463139Missing in isoform 2.
VSP_029494
Natural variant1421R → Q.
Corresponds to variant rs12327936 [ dbSNP | Ensembl ].
VAR_037203
Natural variant1771P → S.
Corresponds to variant rs13394676 [ dbSNP | Ensembl ].
VAR_037204
Natural variant2791I → V.
Corresponds to variant rs965290 [ dbSNP | Ensembl ].
VAR_037205
Natural variant2921M → V. Ref.1
Corresponds to variant rs3749117 [ dbSNP | Ensembl ].
VAR_037206
Natural variant3001H → D. Ref.1
Corresponds to variant rs35771982 [ dbSNP | Ensembl ].
VAR_037207
Natural variant3701A → E.
Corresponds to variant rs34916310 [ dbSNP | Ensembl ].
VAR_061354
Natural variant4041R → H.
Corresponds to variant rs33985939 [ dbSNP | Ensembl ].
VAR_037208
Natural variant11061G → S.
Corresponds to variant rs3828323 [ dbSNP | Ensembl ].
VAR_037209

Experimental info

Sequence conflict15 – 173APR → GAA in AAA70110. Ref.1
Sequence conflict15 – 173APR → GAA in AAC50163. Ref.1
Sequence conflict62 – 643ENC → GRTGS in AAA70110. Ref.1
Sequence conflict62 – 643ENC → GRTGS in AAC50163. Ref.1
Sequence conflict521 – 5233RHG → ETC in AAA70110. Ref.1
Sequence conflict521 – 5233RHG → ETC in AAC50163. Ref.1
Sequence conflict7241S → P in AAA70110. Ref.1
Sequence conflict7241S → P in AAC50163. Ref.1
Sequence conflict7791A → P in AAA70110. Ref.1
Sequence conflict7791A → P in AAC50163. Ref.1
Sequence conflict12241E → D in AAA70110. Ref.1
Sequence conflict12241E → D in AAC50163. Ref.1
Sequence conflict12631S → K in AAA70110. Ref.1

Sequences

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

Last modified November 13, 2007. Version 2.
Checksum: 4E65EA5AC5D597E2

FASTA1,463168,600
        10         20         30         40         50         60 
MLLSPSLLLL LLLGAPRGCA EGVAAALTPE RLLEWQDKGI FVIQSESLKK CIQAGKSVLT 

        70         80         90        100        110        120 
LENCKQANKH MLWKWVSNHG LFNIGGSGCL GLNFSAPEQP LSLYECDSTL VSLRWRCNRK 

       130        140        150        160        170        180 
MITGPLQYSV QVAHDNTVVA SRKYIHKWIS YGSGGGDICE YLHKDLHTIK GNTHGMPCMF 

       190        200        210        220        230        240 
PFQYNHQWHH ECTREGREDD LLWCATTSRY ERDEKWGFCP DPTSAEVGCD TIWEKDLNSH 

       250        260        270        280        290        300 
ICYQFNLLSS LSWSEAHSSC QMQGGTLLSI TDETEENFIR EHMSSKTVEV WMGLNQLDEH 

       310        320        330        340        350        360 
AGWQWSDGTP LNYLNWSPEV NFEPFVEDHC GTFSSFMPSA WRSRDCESTL PYICKKYLNH 

       370        380        390        400        410        420 
IDHEIVEKDA WKYYATHCEP GWNPYNRNCY KLQKEEKTWH EALRSCQADN SALIDITSLA 

       430        440        450        460        470        480 
EVEFLVTLLG DENASETWIG LSSNKIPVSF EWSNDSSVIF TNWHTLEPHI FPNRSQLCVS 

       490        500        510        520        530        540 
AEQSEGHWKV KNCEERLFYI CKKAGHVLSD AESGCQEGWE RHGGFCYKID TVLRSFDQAS 

       550        560        570        580        590        600 
SGYYCPPALV TITNRFEQAF ITSLISSVVK MKDSYFWIAL QDQNDTGEYT WKPVGQKPEP 

       610        620        630        640        650        660 
VQYTHWNTHQ PRYSGGCVAM RGRHPLGRWE VKHCRHFKAM SLCKQPVENQ EKAEYEERWP 

       670        680        690        700        710        720 
FHPCYLDWES EPGLASCFKV FHSEKVLMKR TWREAEAFCE EFGAHLASFA HIEEENFVNE 

       730        740        750        760        770        780 
LLHSKFNWTE ERQFWIGFNK RNPLNAGSWE WSDRTPVVSS FLDNTYFGED ARNCAVYKAN 

       790        800        810        820        830        840 
KTLLPLHCGS KREWICKIPR DVKPKIPFWY QYDVPWLFYQ DAEYLFHTFA SEWLNFEFVC 

       850        860        870        880        890        900 
SWLHSDLLTI HSAHEQEFIH SKIKALSKYG ASWWIGLQEE RANDEFRWRD GTPVIYQNWD 

       910        920        930        940        950        960 
TGRERTVNNQ SQRCGFISSI TGLWGSEECS VSMPSICKRK KVWLIEKKKD TPKQHGTCPK 

       970        980        990       1000       1010       1020 
GWLYFNYKCL LLNIPKDPSS WKNWTHAQHF CAEEGGTLVA IESEVEQAFI TMNLFGQTTS 

      1030       1040       1050       1060       1070       1080 
VWIGLQNDDY ETWLNGKPVV YSNWSPFDII NIPSHNTTEV QKHIPLCALL SSNPNFHFTG 

      1090       1100       1110       1120       1130       1140 
KWYFEDCGKE GYGFVCEKMQ DTSGHGVNTS DMYPMPNTLE YGNRTYKIIN ANMTWYAAIK 

      1150       1160       1170       1180       1190       1200 
TCLMHKAQLV SITDQYHQSF LTVVLNRLGY AHWIGLFTTD NGLNFDWSDG TKSSFTFWKD 

      1210       1220       1230       1240       1250       1260 
EESSLLGDCV FADSNGRWHS TACESFLQGA ICHVPPETRQ SEHPELCSET SIPWIKFKSN 

      1270       1280       1290       1300       1310       1320 
CYSFSTVLDS MSFEAAHEFC KKEGSNLLTI KDEAENAFLL EELFAFGSSV QMVWLNAQFD 

      1330       1340       1350       1360       1370       1380 
GNNETIKWFD GTPTDQSNWG IRKPDTDYFK PHHCVALRIP EGLWQLSPCQ EKKGFICKME 

      1390       1400       1410       1420       1430       1440 
ADIHTAEALP EKGPSHSIIP LAVVLTLIVI VAICTLSFCI YKHNGGFFRR LAGFRNPYYP 

      1450       1460 
ATNFSTVYLE ENILISDLEK SDQ 

« Hide

Isoform 2 [UniParc].

Checksum: E00D5FDFF05DC9FC
Show »

FASTA1,324152,805

References

« Hide 'large scale' references
[1]"The human 180-kDa receptor for secretory phospholipases A2. Molecular cloning, identification of a secreted soluble form, expression, and chromosomal localization."
Ancian P., Lambeau G., Mattei M.-G., Lazdunski M.
J. Biol. Chem. 270:8963-8970(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), FUNCTION, TISSUE SPECIFICITY, VARIANTS VAL-292 AND ASP-300.
Tissue: Kidney.
[2]"Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H. expand/collapse author list , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]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].
[4]"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: Brain.
[5]"Structural comparison of phospholipase-A2-binding regions in phospholipase-A2 receptors from various mammals."
Higashino K., Ishizaki J., Kishino J., Ohara O., Arita H.
Eur. J. Biochem. 225:375-382(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 532-942, TISSUE SPECIFICITY.
Tissue: Placenta.
[6]"Distribution of the phospholipase A2 receptor messenger RNA in human gestational tissues."
Moses E.K., Freed K.A., Brennecke S.P., Rice G.E.
Placenta 19:35-40(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: TISSUE SPECIFICITY.
[7]"Activation of cytokine production by secreted phospholipase A2 in human lung macrophages expressing the M-type receptor."
Granata F., Petraroli A., Boilard E., Bezzine S., Bollinger J., Del Vecchio L., Gelb M.H., Lambeau G., Marone G., Triggiani M.
J. Immunol. 174:464-474(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, TISSUE SPECIFICITY.
+Additional computationally mapped references.

Web resources

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U17033 mRNA. Translation: AAA70110.1.
U17034 mRNA. Translation: AAC50163.1.
AC080166 Genomic DNA. Translation: AAY24052.1.
AC093873 Genomic DNA. Translation: AAY24190.1.
CH471058 Genomic DNA. Translation: EAX11392.1.
CH471058 Genomic DNA. Translation: EAX11393.1.
BC140823 mRNA. Translation: AAI40824.1.
D30780 mRNA. Translation: BAA06444.1.
CCDSCCDS33309.1. [Q13018-1]
CCDS42767.1. [Q13018-2]
PIRA56395.
B56395.
RefSeqNP_001007268.1. NM_001007267.2. [Q13018-2]
NP_001182570.1. NM_001195641.1.
NP_031392.3. NM_007366.4. [Q13018-1]
XP_005246449.1. XM_005246392.1. [Q13018-1]
UniGeneHs.410477.

3D structure databases

ProteinModelPortalQ13018.
SMRQ13018. Positions 132-223, 229-355, 377-502, 664-805, 816-939, 957-1101, 1119-1232, 1254-1382.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING9606.ENSP00000283243.

Protein family/group databases

MEROPSS63.015.

Polymorphism databases

DMDM160419241.

Proteomic databases

PaxDbQ13018.
PRIDEQ13018.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000283243; ENSP00000283243; ENSG00000153246. [Q13018-1]
ENST00000392771; ENSP00000376524; ENSG00000153246. [Q13018-2]
GeneID22925.
KEGGhsa:22925.
UCSCuc002ube.2. human. [Q13018-1]
uc002ubf.3. human. [Q13018-2]

Organism-specific databases

CTD22925.
GeneCardsGC02M160788.
H-InvDBHIX0024010.
HGNCHGNC:9042. PLA2R1.
HPAHPA012657.
MIM604939. gene.
neXtProtNX_Q13018.
PharmGKBPA33369.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG288621.
HOVERGENHBG108261.
InParanoidQ13018.
KOK06560.
OMAWCATTSR.
OrthoDBEOG7FFMQR.
PhylomeDBQ13018.
TreeFamTF316663.

Gene expression databases

BgeeQ13018.
CleanExHS_PLA2R1.
GenevestigatorQ13018.

Family and domain databases

Gene3D2.10.10.10. 1 hit.
3.10.100.10. 8 hits.
InterProIPR001304. C-type_lectin.
IPR016186. C-type_lectin-like.
IPR018378. C-type_lectin_CS.
IPR016187. C-type_lectin_fold.
IPR000562. FN_type2_col-bd.
IPR000772. Ricin_B_lectin.
[Graphical view]
PfamPF00040. fn2. 1 hit.
PF00059. Lectin_C. 8 hits.
[Graphical view]
SMARTSM00034. CLECT. 8 hits.
SM00059. FN2. 1 hit.
SM00458. RICIN. 1 hit.
[Graphical view]
SUPFAMSSF50370. SSF50370. 1 hit.
SSF56436. SSF56436. 8 hits.
PROSITEPS00615. C_TYPE_LECTIN_1. 3 hits.
PS50041. C_TYPE_LECTIN_2. 8 hits.
PS00023. FN2_1. 1 hit.
PS51092. FN2_2. 1 hit.
PS50231. RICIN_B_LECTIN. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSPLA2R1. human.
GenomeRNAi22925.
NextBio43633.
PROQ13018.
SOURCESearch...

Entry information

Entry namePLA2R_HUMAN
AccessionPrimary (citable) accession number: Q13018
Secondary accession number(s): B2RTU9 expand/collapse secondary AC list , D3DPB1, Q13019, Q15095, Q53R45, Q53RR7
Entry history
Integrated into UniProtKB/Swiss-Prot: November 13, 2007
Last sequence update: November 13, 2007
Last modified: July 9, 2014
This is version 113 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 2

Human chromosome 2: entries, gene names and cross-references to MIM