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Q86UX7

- URP2_HUMAN

UniProt

Q86UX7 - URP2_HUMAN

Protein

Fermitin family homolog 3

Gene

FERMT3

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 113 (01 Oct 2014)
      Sequence version 1 (01 Jun 2003)
      Previous versions | rss
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    Functioni

    Plays a central role in cell adhesion in hematopoietic cells. Acts by activating the integrin beta-1-3 (ITGB1, ITGB2 and ITGB3). Required for integrin-mediated platelet adhesion and leukocyte adhesion to endothelial cells. Required for activation of integrin beta-2 (ITGB2) in polymorphonuclear granulocytes (PMNs) By similarity.By similarity
    Isoform 2 may act as a repressor of NF-kappa-B and apoptosis.3 Publications

    GO - Molecular functioni

    1. integrin binding Source: UniProtKB

    GO - Biological processi

    1. integrin activation Source: UniProtKB
    2. integrin-mediated signaling pathway Source: UniProtKB
    3. leukocyte cell-cell adhesion Source: UniProtKB
    4. platelet aggregation Source: UniProtKB
    5. regulation of cell-cell adhesion mediated by integrin Source: UniProtKB
    6. substrate adhesion-dependent cell spreading Source: UniProtKB

    Keywords - Biological processi

    Cell adhesion

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Fermitin family homolog 3
    Alternative name(s):
    Kindlin-3
    MIG2-like protein
    Unc-112-related protein 2
    Gene namesi
    Name:FERMT3
    Synonyms:KIND3, MIG2B, URP2
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 11

    Organism-specific databases

    HGNCiHGNC:23151. FERMT3.

    Subcellular locationi

    Cell projectionpodosome By similarity
    Note: Present in the F-actin surrounding ring structure of podosomes, which are specialized adhesion structures of hematopoietic cells.By similarity

    GO - Cellular componenti

    1. cell junction Source: UniProtKB-KW
    2. cell projection Source: UniProtKB-KW
    3. extracellular vesicular exosome Source: UniProt
    4. membrane Source: UniProtKB
    5. podosome Source: UniProtKB

    Keywords - Cellular componenti

    Cell junction, Cell projection

    Pathology & Biotechi

    Involvement in diseasei

    Leukocyte adhesion deficiency 3 (LAD3) [MIM:612840]: A disorder characterized by recurrent bacterial infections without pus formation, leukocytosis and major bleeding disorders.5 Publications
    Note: The disease is caused by mutations affecting the gene represented in this entry.

    Organism-specific databases

    MIMi612840. phenotype.
    Orphaneti99844. Leukocyte adhesion deficiency type III.
    PharmGKBiPA162388384.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 667667Fermitin family homolog 3PRO_0000219454Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei11 – 111Phosphotyrosine2 Publications
    Modified residuei504 – 5041Phosphotyrosine1 Publication

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiQ86UX7.
    PaxDbiQ86UX7.
    PRIDEiQ86UX7.

    PTM databases

    PhosphoSiteiQ86UX7.

    Miscellaneous databases

    PMAP-CutDBQ86UX7.

    Expressioni

    Tissue specificityi

    Highly expressed in lymph node. Expressed in thymus, spleen and leukocytes. Weakly expressed in placenta, small intestine, stomach, testis and lung. Overexpressed in B-cell malignancies.2 Publications

    Gene expression databases

    ArrayExpressiQ86UX7.
    BgeeiQ86UX7.
    CleanExiHS_FERMT3.
    GenevestigatoriQ86UX7.

    Organism-specific databases

    HPAiHPA053416.

    Interactioni

    Subunit structurei

    Interacts with ITGB1, ITGB2 and ITGB3 (via cytoplasmic tails).By similarity

    Protein-protein interaction databases

    BioGridi123735. 8 interactions.
    IntActiQ86UX7. 6 interactions.
    STRINGi9606.ENSP00000279227.

    Structurei

    Secondary structure

    1
    667
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi370 – 3734
    Beta strandi377 – 3804
    Beta strandi385 – 3906
    Turni391 – 3955
    Turni404 – 4063
    Beta strandi408 – 4114
    Helixi415 – 4173
    Beta strandi419 – 4279
    Beta strandi429 – 44113
    Helixi442 – 45615
    Helixi465 – 48016

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2YS3NMR-A349-482[»]
    ProteinModelPortaliQ86UX7.
    SMRiQ86UX7. Positions 7-98, 342-480, 488-639.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ86UX7.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini229 – 558330FERMAdd
    BLAST
    Domaini354 – 457104PHPROSITE-ProRule annotationAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi147 – 1559Poly-Lys

    Domaini

    The FERM domain is not correctly detected by PROSITE or Pfam techniques because it contains the insertion of a PH domain.

    Sequence similaritiesi

    Belongs to the kindlin family.Curated
    Contains 1 FERM domain.Curated
    Contains 1 PH domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiNOG277845.
    HOGENOMiHOG000231715.
    HOVERGENiHBG020688.
    InParanoidiQ86UX7.
    KOiK17084.
    OMAiEMMLFGA.
    OrthoDBiEOG7T7GSC.
    PhylomeDBiQ86UX7.
    TreeFamiTF314677.

    Family and domain databases

    Gene3Di1.20.80.10. 2 hits.
    2.30.29.30. 2 hits.
    InterProiIPR019749. Band_41_domain.
    IPR014352. FERM/acyl-CoA-bd_prot_3-hlx.
    IPR019748. FERM_central.
    IPR001849. PH_domain.
    IPR011993. PH_like_dom.
    [Graphical view]
    PfamiPF00373. FERM_M. 1 hit.
    PF00169. PH. 1 hit.
    [Graphical view]
    SMARTiSM00295. B41. 1 hit.
    SM00233. PH. 1 hit.
    [Graphical view]
    SUPFAMiSSF47031. SSF47031. 2 hits.
    PROSITEiPS00661. FERM_2. 1 hit.
    PS50003. PH_DOMAIN. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q86UX7-1) [UniParc]FASTAAdd to Basket

    Also known as: Long, URP2LF

    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.

    « Hide

    MAGMKTASGD YIDSSWELRV FVGEEDPEAE SVTLRVTGES HIGGVLLKIV    50
    EQINRKQDWS DHAIWWEQKR QWLLQTHWTL DKYGILADAR LFFGPQHRPV 100
    ILRLPNRRAL RLRASFSQPL FQAVAAICRL LSIRHPEELS LLRAPEKKEK 150
    KKKEKEPEEE LYDLSKVVLA GGVAPALFRG MPAHFSDSAQ TEACYHMLSR 200
    PQPPPDPLLL QRLPRPSSLS DKTQLHSRWL DSSRCLMQQG IKAGDALWLR 250
    FKYYSFFDLD PKTDPVRLTQ LYEQARWDLL LEEIDCTEEE MMVFAALQYH 300
    INKLSQSGEV GEPAGTDPGL DDLDVALSNL EVKLEGSAPT DVLDSLTTIP 350
    ELKDHLRIFR IPRRPRKLTL KGYRQHWVVF KETTLSYYKS QDEAPGDPIQ 400
    QLNLKGCEVV PDVNVSGQKF CIKLLVPSPE GMSEIYLRCQ DEQQYARWMA 450
    GCRLASKGRT MADSSYTSEV QAILAFLSLQ RTGSGGPGNH PHGPDASAEG 500
    LNPYGLVAPR FQRKFKAKQL TPRILEAHQN VAQLSLAEAQ LRFIQAWQSL 550
    PDFGISYVMV RFKGSRKDEI LGIANNRLIR IDLAVGDVVK TWRFSNMRQW 600
    NVNWDIRQVA IEFDEHINVA FSCVSASCRI VHEYIGGYIF LSTRERARGE 650
    ELDEDLFLQL TGGHEAF 667
    Length:667
    Mass (Da):75,953
    Last modified:June 1, 2003 - v1
    Checksum:i5ACE15EB689B91B5
    GO
    Isoform 2 (identifier: Q86UX7-2) [UniParc]FASTAAdd to Basket

    Also known as: Short, URP2SF

    The sequence of this isoform differs from the canonical sequence as follows:
         360-363: Missing.

    Show »
    Length:663
    Mass (Da):75,430
    Checksum:i243CA27636C67079
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti472 – 4721A → P in BAC04220. (PubMed:14702039)Curated
    Sequence conflicti480 – 4801Q → R in BAC04220. (PubMed:14702039)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei360 – 3634Missing in isoform 2. 3 PublicationsVSP_009226

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY093951 mRNA. Translation: AAM19736.1.
    AY093952 mRNA. Translation: AAM19737.1.
    AK093719 mRNA. Translation: BAC04220.1.
    BC004347 mRNA. Translation: AAH04347.2.
    BC013366 mRNA. Translation: AAH13366.1.
    BC015584 mRNA. Translation: AAH15584.1.
    CCDSiCCDS8059.1. [Q86UX7-2]
    CCDS8060.1. [Q86UX7-1]
    RefSeqiNP_113659.3. NM_031471.5. [Q86UX7-2]
    NP_848537.1. NM_178443.2. [Q86UX7-1]
    XP_006718766.1. XM_006718703.1. [Q86UX7-2]
    UniGeneiHs.180535.

    Genome annotation databases

    EnsembliENST00000279227; ENSP00000279227; ENSG00000149781. [Q86UX7-1]
    ENST00000345728; ENSP00000339950; ENSG00000149781. [Q86UX7-2]
    GeneIDi83706.
    KEGGihsa:83706.
    UCSCiuc001nyl.2. human. [Q86UX7-1]
    uc001nym.2. human. [Q86UX7-2]

    Polymorphism databases

    DMDMi41018464.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY093951 mRNA. Translation: AAM19736.1 .
    AY093952 mRNA. Translation: AAM19737.1 .
    AK093719 mRNA. Translation: BAC04220.1 .
    BC004347 mRNA. Translation: AAH04347.2 .
    BC013366 mRNA. Translation: AAH13366.1 .
    BC015584 mRNA. Translation: AAH15584.1 .
    CCDSi CCDS8059.1. [Q86UX7-2 ]
    CCDS8060.1. [Q86UX7-1 ]
    RefSeqi NP_113659.3. NM_031471.5. [Q86UX7-2 ]
    NP_848537.1. NM_178443.2. [Q86UX7-1 ]
    XP_006718766.1. XM_006718703.1. [Q86UX7-2 ]
    UniGenei Hs.180535.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2YS3 NMR - A 349-482 [» ]
    ProteinModelPortali Q86UX7.
    SMRi Q86UX7. Positions 7-98, 342-480, 488-639.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 123735. 8 interactions.
    IntActi Q86UX7. 6 interactions.
    STRINGi 9606.ENSP00000279227.

    PTM databases

    PhosphoSitei Q86UX7.

    Polymorphism databases

    DMDMi 41018464.

    Proteomic databases

    MaxQBi Q86UX7.
    PaxDbi Q86UX7.
    PRIDEi Q86UX7.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000279227 ; ENSP00000279227 ; ENSG00000149781 . [Q86UX7-1 ]
    ENST00000345728 ; ENSP00000339950 ; ENSG00000149781 . [Q86UX7-2 ]
    GeneIDi 83706.
    KEGGi hsa:83706.
    UCSCi uc001nyl.2. human. [Q86UX7-1 ]
    uc001nym.2. human. [Q86UX7-2 ]

    Organism-specific databases

    CTDi 83706.
    GeneCardsi GC11P063975.
    HGNCi HGNC:23151. FERMT3.
    HPAi HPA053416.
    MIMi 607901. gene.
    612840. phenotype.
    neXtProti NX_Q86UX7.
    Orphaneti 99844. Leukocyte adhesion deficiency type III.
    PharmGKBi PA162388384.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG277845.
    HOGENOMi HOG000231715.
    HOVERGENi HBG020688.
    InParanoidi Q86UX7.
    KOi K17084.
    OMAi EMMLFGA.
    OrthoDBi EOG7T7GSC.
    PhylomeDBi Q86UX7.
    TreeFami TF314677.

    Miscellaneous databases

    EvolutionaryTracei Q86UX7.
    GeneWikii FERMT3.
    GenomeRNAii 83706.
    NextBioi 72692.
    PMAP-CutDB Q86UX7.
    PROi Q86UX7.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q86UX7.
    Bgeei Q86UX7.
    CleanExi HS_FERMT3.
    Genevestigatori Q86UX7.

    Family and domain databases

    Gene3Di 1.20.80.10. 2 hits.
    2.30.29.30. 2 hits.
    InterProi IPR019749. Band_41_domain.
    IPR014352. FERM/acyl-CoA-bd_prot_3-hlx.
    IPR019748. FERM_central.
    IPR001849. PH_domain.
    IPR011993. PH_like_dom.
    [Graphical view ]
    Pfami PF00373. FERM_M. 1 hit.
    PF00169. PH. 1 hit.
    [Graphical view ]
    SMARTi SM00295. B41. 1 hit.
    SM00233. PH. 1 hit.
    [Graphical view ]
    SUPFAMi SSF47031. SSF47031. 2 hits.
    PROSITEi PS00661. FERM_2. 1 hit.
    PS50003. PH_DOMAIN. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "URP1: a member of a novel family of PH and FERM domain-containing membrane-associated proteins is significantly over-expressed in lung and colon carcinomas."
      Weinstein E.J., Bourner M., Head R., Zakeri H., Bauer C., Mazzarella R.
      Biochim. Biophys. Acta 1637:207-216(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), TISSUE SPECIFICITY.
    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.
      , 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).
      Tissue: Thymus.
    3. "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).
      Tissue: Lung and Lymph.
    4. "Proteomic analysis of the cell-surface membrane in chronic lymphocytic leukemia: identification of two novel proteins, BCNP1 and MIG2B."
      Boyd R.S., Adam P.J., Patel S., Loader J.A., Berry J., Redpath N.T., Poyser H.R., Fletcher G.C., Burgess N.A., Stamps A.C., Hudson L., Smith P., Griffiths M., Willis T.G., Karran E.L., Oscier D.G., Catovsky D., Terrett J.A., Dyer M.J.S.
      Leukemia 17:1605-1612(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 20-35; 424-438 AND 569-577, IDENTIFICATION BY MASS SPECTROMETRY, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
    5. "URP2SF, a FERM and PH domain containing protein, regulates NF-kappaB and apoptosis."
      Wang L., Deng W., Shi T., Ma D.
      Biochem. Biophys. Res. Commun. 368:899-906(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: POSSIBLE FUNCTION (ISOFORM 2).
    6. Cited for: INVOLVEMENT IN LAD3.
    7. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-11, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Platelet.
    8. "Loss of Kindlin-3 in LAD-III eliminates LFA-1 but not VLA-4 adhesiveness developed under shear flow conditions."
      Manevich-Mendelson E., Feigelson S.W., Pasvolsky R., Aker M., Grabovsky V., Shulman Z., Kilic S.S., Rosenthal-Allieri M.A., Ben-Dor S., Mory A., Bernard A., Moser M., Etzioni A., Alon R.
      Blood 114:2344-2353(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: INVOLVEMENT IN LAD3.
    9. Cited for: INVOLVEMENT IN LAD3, FUNCTION.
    10. "Leukocyte adhesion deficiency-III is caused by mutations in KINDLIN3 affecting integrin activation."
      Svensson L., Howarth K., McDowall A., Patzak I., Evans R., Ussar S., Moser M., Metin A., Fried M., Tomlinson I., Hogg N.
      Nat. Med. 15:306-312(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: INVOLVEMENT IN LAD3, FUNCTION.
    11. "A point mutation in KINDLIN3 ablates activation of three integrin subfamilies in humans."
      Malinin N.L., Zhang L., Choi J., Ciocea A., Razorenova O., Ma Y.-Q., Podrez E.A., Tosi M., Lennon D.P., Caplan A.I., Shurin S.B., Plow E.F., Byzova T.V.
      Nat. Med. 15:313-318(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: INVOLVEMENT IN LAD3, FUNCTION.
    12. "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 TYR-11 AND TYR-504, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    13. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    14. "Solution structure of the PH domain of kindlin-3 from human."
      RIKEN structural genomics initiative (RSGI)
      Submitted (FEB-2009) to the PDB data bank
      Cited for: STRUCTURE BY NMR OF 349-478.

    Entry informationi

    Entry nameiURP2_HUMAN
    AccessioniPrimary (citable) accession number: Q86UX7
    Secondary accession number(s): Q8IUA1, Q8N207, Q9BT48
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 16, 2004
    Last sequence update: June 1, 2003
    Last modified: October 1, 2014
    This is version 113 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (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.

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 11
      Human chromosome 11: entries, gene names and cross-references to MIM
    2. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    3. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    4. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3