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O60711 (LPXN_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 129. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Leupaxin
Gene names
Name:LPXN
Synonyms:LDLP
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length386 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Transcriptional coactivator for androgen receptor (AR) and serum response factor (SRF). Contributes to the regulation of cell adhesion, spreading and cell migration and acts as a negative regulator in integrin-mediated cell adhesion events. Suppresses the integrin-induced tyrosine phosphorylation of paxillin (PXN). May play a critical role as an adapter protein in the formation of the adhesion zone in osteoclasts. Negatively regulates B-cell antigen receptor (BCR) signaling. Ref.13 Ref.14 Ref.15 Ref.17

Subunit structure

Interacts with PTPN22 By similarity. Interacts with unphosphorylated ITGA4. Interacts with PTK2B/PYK2, PTPN12, AR and SRF. Interacts (via LD motif 3) with LYN and the interaction is induced upon B-cell antigen receptor (BCR) activation. Interacts (via LD motif 3) with PTK2/FAK. Ref.1 Ref.8 Ref.12 Ref.13 Ref.14 Ref.15

Subcellular location

Cytoplasm. Cell junctionfocal adhesion. Nucleus. Cytoplasmperinuclear region By similarity. Cell projectionpodosome. Cell membrane. Note: Shuttles between the cytoplasm and nucleus. Recruited to the cell membrane following B-cell antigen receptor (BCR) cross-linking in B-cells. Enhanced focal adhesion kinase activity (PTK2/FAK) attenuates its nuclear accumulation and limits its ability to enhance serum response factor (SRF)-dependent gene transcription. Targeting to focal adhesions is essential for its tyrosine phosphorylation in response to bombesin. Ref.9 Ref.12 Ref.13 Ref.14 Ref.15 Ref.17

Tissue specificity

Macrophages, monocytes and osteoclasts (at protein level). Strongly expressed in cells and tissues of hematopoietic origin. Highest expression in lymphoid tissues such as spleen, lymph node, thymus and appendix and in the vascular smooth muscle. Lower levels in bone marrow and fetal liver. Also expressed in peripheral blood lymphocytes and a number of hematopoietic cell lines. Very low levels found in epithelial cell lines. Expressed in prostate cancer (PCa) cells and its expression intensity is directly linked to PCa progression. Ref.9 Ref.14 Ref.15

Domain

The LIM domain 3 is critical for focal adhesion targeting and the suppression of paxillin (PXN) tyrosine phosphorylation. The LIM domain 3 alone or both LIM domains 3 and 4 can mediate interaction with AR.

Post-translational modification

Phosphorylated on tyrosine residues. Phosphorylation on Tyr-72 is important for its inhibitory function. Bombesin stimulates phosphorylation on Tyr-22, Tyr-62 and Tyr-72. Ref.13 Ref.17

Sequence similarities

Belongs to the paxillin family.

Contains 4 LIM zinc-binding domains.

Ontologies

Keywords
   Biological processCell adhesion
Transcription
Transcription regulation
   Cellular componentCell junction
Cell membrane
Cell projection
Cytoplasm
Membrane
Nucleus
   Coding sequence diversityAlternative splicing
Polymorphism
   DomainLIM domain
Repeat
   LigandMetal-binding
Zinc
   Molecular functionActivator
   PTMAcetylation
Phosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcell adhesion

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

negative regulation of B cell receptor signaling pathway

Inferred from direct assay Ref.13. Source: UniProtKB

negative regulation of cell adhesion

Inferred from direct assay Ref.17. Source: UniProtKB

protein complex assembly

Traceable author statement Ref.1. Source: ProtInc

regulation of cell adhesion mediated by integrin

Inferred from electronic annotation. Source: Ensembl

regulation of transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

signal transduction

Traceable author statement Ref.1. Source: ProtInc

transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentcell projection

Inferred from electronic annotation. Source: UniProtKB-KW

cytoplasm

Inferred from direct assay Ref.13Ref.15Ref.14. Source: UniProtKB

focal adhesion

Inferred from direct assay Ref.15Ref.14Ref.17. Source: UniProtKB

nucleus

Inferred from direct assay Ref.15Ref.14. Source: UniProtKB

perinuclear region of cytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

plasma membrane

Inferred from direct assay Ref.13. Source: UniProtKB

podosome

Inferred from direct assay Ref.9. Source: UniProtKB

   Molecular_functiontranscription cofactor activity

Inferred from direct assay Ref.15Ref.14. Source: UniProtKB

zinc ion binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Hoxa1P090223EBI-744222,EBI-3957603From a different organism.

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: O60711-1)

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: O60711-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-4: MEEL → MSTLLISSS
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 386386Leupaxin
PRO_0000075836

Regions

Domain150 – 20859LIM zinc-binding 1
Domain209 – 26759LIM zinc-binding 2
Domain268 – 32659LIM zinc-binding 3
Domain327 – 38660LIM zinc-binding 4
Motif3 – 1513LD motif 1
Motif70 – 8213LD motif 2
Motif92 – 10312LD motif 3

Amino acid modifications

Modified residue11N-acetylmethionine Ref.19
Modified residue191Phosphoserine Ref.10
Modified residue221Phosphotyrosine Ref.17
Modified residue541Phosphoserine By similarity
Modified residue621Phosphotyrosine Ref.17
Modified residue721Phosphotyrosine; by LYN Ref.13 Ref.17

Natural variations

Alternative sequence1 – 44MEEL → MSTLLISSS in isoform 2.
VSP_042655
Natural variant1481P → T.
Corresponds to variant rs12271558 [ dbSNP | Ensembl ].
VAR_050152

Experimental info

Sequence conflict21E → D in CAG38768. Ref.3
Sequence conflict141S → T in BAD96885. Ref.4
Sequence conflict1001L → M in CAG38768. Ref.3

Secondary structure

............... 386
Helix Strand Turn

Details...

Sequences

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

Last modified August 1, 1998. Version 1.
Checksum: C8D2BE61FAB11F3A

FASTA38643,332
        10         20         30         40         50         60 
MEELDALLEE LERSTLQDSD EYSNPAPLPL DQHSRKETNL DETSEILSIQ DNTSPLPAQL 

        70         80         90        100        110        120 
VYTTNIQELN VYSEAQEPKE SPPPSKTSAA AQLDELMAHL TEMQAKVAVR ADAGKKHLPD 

       130        140        150        160        170        180 
KQDHKASLDS MLGGLEQELQ DLGIATVPKG HCASCQKPIA GKVIHALGQS WHPEHFVCTH 

       190        200        210        220        230        240 
CKEEIGSSPF FERSGLAYCP NDYHQLFSPR CAYCAAPILD KVLTAMNQTW HPEHFFCSHC 

       250        260        270        280        290        300 
GEVFGAEGFH EKDKKPYCRK DFLAMFSPKC GGCNRPVLEN YLSAMDTVWH PECFVCGDCF 

       310        320        330        340        350        360 
TSFSTGSFFE LDGRPFCELH YHHRRGTLCH GCGQPITGRC ISAMGYKFHP EHFVCAFCLT 

       370        380 
QLSKGIFREQ NDKTYCQPCF NKLFPL 

« Hide

Isoform 2 [UniParc].

Checksum: A8F1FFD11D4DB7BD
Show »

FASTA39143,750

References

« Hide 'large scale' references
[1]"Leupaxin is a novel LIM domain protein that forms a complex with PYK2."
Lipsky B.P., Beals C.R., Staunton D.E.
J. Biol. Chem. 273:11709-11713(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), INTERACTION WITH PTK2B/PYK2, CHARACTERIZATION.
Tissue: Spleen.
[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] (ISOFORMS 1 AND 2).
Tissue: Small intestine and Spleen.
[3]"Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
[4]Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.
Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Tissue: Lung.
[5]"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].
[6]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].
[7]"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: B-cell.
[8]"Binding of paxillin to alpha4 integrins modifies integrin-dependent biological responses."
Liu S., Thomas S.M., Woodside D.G., Rose D.M., Kiosses W.B., Pfaff M., Ginsberg M.H.
Nature 402:676-681(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH ITGA4.
[9]"Leupaxin is a critical adaptor protein in the adhesion zone of the osteoclast."
Gupta A., Lee B.S., Khadeer M.A., Tang Z., Chellaiah M., Abu-Amer Y., Goldknopf J., Hruska K.A.
J. Bone Miner. Res. 18:669-685(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
[10]"Robust phosphoproteomic profiling of tyrosine phosphorylation sites from human T cells using immobilized metal affinity chromatography and tandem mass spectrometry."
Brill L.M., Salomon A.R., Ficarro S.B., Mukherji M., Stettler-Gill M., Peters E.C.
Anal. Chem. 76:2763-2772(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-19, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[11]"Immunoaffinity profiling of tyrosine phosphorylation in cancer cells."
Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H., Zha X.-M., Polakiewicz R.D., Comb M.J.
Nat. Biotechnol. 23:94-101(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[12]"Interaction of Pyk2 and PTP-PEST with leupaxin in prostate cancer cells."
Sahu S.N., Nunez S., Bai G., Gupta A.
Am. J. Physiol. 292:C2288-C2296(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH PTK2B/PYK2 AND PTPN12, SUBCELLULAR LOCATION.
[13]"Leupaxin negatively regulates B cell receptor signaling."
Chew V., Lam K.P.
J. Biol. Chem. 282:27181-27191(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, PHOSPHORYLATION AT TYR-72 BY LYN, INTERACTION WITH LYN.
[14]"The LIM protein leupaxin is enriched in smooth muscle and functions as an serum response factor cofactor to induce smooth muscle cell gene transcription."
Sundberg-Smith L.J., DiMichele L.A., Sayers R.L., Mack C.P., Taylor J.M.
Circ. Res. 102:1502-1511(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, INTERACTION WITH PTK2/FAK AND SRF.
[15]"Leupaxin, a novel coactivator of the androgen receptor, is expressed in prostate cancer and plays a role in adhesion and invasion of prostate carcinoma cells."
Kaulfuss S., Grzmil M., Hemmerlein B., Thelen P., Schweyer S., Neesen J., Bubendorf L., Glass A.G., Jarry H., Auber B., Burfeind P.
Mol. Endocrinol. 22:1606-1621(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, INTERACTION WITH AR.
[16]"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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[17]"Leupaxin is similar to paxillin in focal adhesion targeting and tyrosine phosphorylation but has distinct roles in cell adhesion and spreading."
Chen P.W., Kroog G.S.
Cell Adh. Migr. 4:527-540(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, PHOSPHORYLATION AT TYR-22; TYR-62 AND TYR-72.
[18]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[19]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[20]"Solution structure of the LIM domain of human leupaxin."
RIKEN structural genomics initiative (RSGI)
Submitted (JAN-2006) to the PDB data bank
Cited for: STRUCTURE BY NMR OF 260-326.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF062075 mRNA. Translation: AAC16014.1.
AK300955 mRNA. Translation: BAG62583.1.
AK313306 mRNA. Translation: BAG36111.1.
CR536531 mRNA. Translation: CAG38768.1.
AK223165 mRNA. Translation: BAD96885.1.
AP001350 Genomic DNA. No translation available.
AP003557 Genomic DNA. No translation available.
CH471076 Genomic DNA. Translation: EAW73808.1.
BC019035 mRNA. Translation: AAH19035.1.
RefSeqNP_001137467.1. NM_001143995.1.
NP_004802.1. NM_004811.2.
UniGeneHs.125474.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1X3HNMR-A260-326[»]
ProteinModelPortalO60711.
SMRO60711. Positions 152-384.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid114801. 15 interactions.
IntActO60711. 25 interactions.
MINTMINT-1449182.
STRING9606.ENSP00000263845.

PTM databases

PhosphoSiteO60711.

Proteomic databases

PaxDbO60711.
PeptideAtlasO60711.
PRIDEO60711.

Protocols and materials databases

DNASU9404.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000395074; ENSP00000378512; ENSG00000110031. [O60711-1]
ENST00000528954; ENSP00000431284; ENSG00000110031. [O60711-2]
GeneID9404.
KEGGhsa:9404.
UCSCuc001nmw.3. human. [O60711-1]
uc010rkj.2. human. [O60711-2]

Organism-specific databases

CTD9404.
GeneCardsGC11M058294.
HGNCHGNC:14061. LPXN.
HPACAB046478.
HPA043741.
MIM605390. gene.
neXtProtNX_O60711.
PharmGKBPA30441.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG267887.
HOGENOMHOG000018764.
HOVERGENHBG001512.
InParanoidO60711.
OMACGEVFGA.
PhylomeDBO60711.
TreeFamTF314113.

Enzyme and pathway databases

SignaLinkO60711.

Gene expression databases

ArrayExpressO60711.
BgeeO60711.
CleanExHS_LPXN.
GenevestigatorO60711.

Family and domain databases

Gene3D2.10.110.10. 4 hits.
InterProIPR017305. Tgfb1i1/Leupaxin.
IPR001781. Znf_LIM.
[Graphical view]
PfamPF00412. LIM. 4 hits.
[Graphical view]
PIRSFPIRSF037881. Leupaxin. 1 hit.
SMARTSM00132. LIM. 4 hits.
[Graphical view]
PROSITEPS00478. LIM_DOMAIN_1. 4 hits.
PS50023. LIM_DOMAIN_2. 4 hits.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceO60711.
GeneWikiLPXN.
GenomeRNAi9404.
NextBio35232.
PROO60711.
SOURCESearch...

Entry information

Entry nameLPXN_HUMAN
AccessionPrimary (citable) accession number: O60711
Secondary accession number(s): B2R8B4 expand/collapse secondary AC list , B4DV71, Q53FW6, Q6FI07
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: August 1, 1998
Last modified: April 16, 2014
This is version 129 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

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