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Q13136

- LIPA1_HUMAN

UniProt

Q13136 - LIPA1_HUMAN

Protein

Liprin-alpha-1

Gene

PPFIA1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 127 (01 Oct 2014)
      Sequence version 1 (01 Nov 1996)
      Previous versions | rss
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    Functioni

    May regulate the disassembly of focal adhesions. May localize receptor-like tyrosine phosphatases type 2A at specific sites on the plasma membrane, possibly regulating their interaction with the extracellular environment and their association with substrates.1 Publication

    GO - Molecular functioni

    1. protein binding Source: UniProtKB
    2. signal transducer activity Source: ProtInc

    GO - Biological processi

    1. cell-matrix adhesion Source: ProtInc
    2. negative regulation of establishment of protein localization to plasma membrane Source: MGI
    3. negative regulation of stress fiber assembly Source: MGI
    4. signal transduction Source: ProtInc

    Enzyme and pathway databases

    SignaLinkiQ13136.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Liprin-alpha-1
    Alternative name(s):
    LAR-interacting protein 1
    Short name:
    LIP-1
    Protein tyrosine phosphatase receptor type f polypeptide-interacting protein alpha-1
    Short name:
    PTPRF-interacting protein alpha-1
    Gene namesi
    Name:PPFIA1
    Synonyms:LIP1
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 11

    Organism-specific databases

    HGNCiHGNC:9245. PPFIA1.

    Subcellular locationi

    Cytoplasm 1 Publication
    Note: Colocalizes with PTPRF at the ends of focal adhesions most proximal to the cell nucleus.

    GO - Cellular componenti

    1. cytoplasm Source: HPA
    2. focal adhesion Source: HPA

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA33566.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 12021202Liprin-alpha-1PRO_0000191026Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei230 – 2301Phosphothreonine1 Publication
    Modified residuei239 – 2391Phosphoserine2 Publications
    Modified residuei242 – 2421Phosphoserine3 Publications
    Modified residuei244 – 2441Phosphoserine2 Publications
    Modified residuei448 – 4481Phosphoserine1 Publication
    Modified residuei693 – 6931Phosphoserine1 Publication
    Modified residuei1159 – 11591Phosphothreonine1 Publication

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiQ13136.
    PaxDbiQ13136.
    PRIDEiQ13136.

    PTM databases

    PhosphoSiteiQ13136.

    Miscellaneous databases

    PMAP-CutDBQ13136.

    Expressioni

    Tissue specificityi

    Ubiquitous.2 Publications

    Gene expression databases

    ArrayExpressiQ13136.
    BgeeiQ13136.
    CleanExiHS_PPFIA1.
    GenevestigatoriQ13136.

    Organism-specific databases

    HPAiCAB017032.
    HPA008272.
    HPA042271.

    Interactioni

    Subunit structurei

    Forms homodimers and heterodimers with liprins-alpha and liprins-beta. Interacts with the second PTPase domain of PTPRD, PTPRF and PTPRS. Interacts with GIT1, KIF1A and GRIP1 By similarity.By similarity

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    Gria2P194912EBI-745426,EBI-77718From a different organism.
    Grip1P978794EBI-745426,EBI-936113From a different organism.
    MBIPQ9NS733EBI-745426,EBI-741953
    PPP2R5DQ147382EBI-745426,EBI-396563

    Protein-protein interaction databases

    BioGridi114072. 33 interactions.
    IntActiQ13136. 16 interactions.
    MINTiMINT-1460222.
    STRINGi9606.ENSP00000253925.

    Structurei

    Secondary structure

    1
    1202
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi1198 – 12014

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1N7FX-ray1.80C/D1195-1202[»]
    ProteinModelPortaliQ13136.
    SMRiQ13136. Positions 851-1120.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini878 – 94467SAM 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini963 – 102765SAM 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini1051 – 112070SAM 3PROSITE-ProRule annotationAdd
    BLAST

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili34 – 141108Sequence AnalysisAdd
    BLAST
    Coiled coili176 – 21439Sequence AnalysisAdd
    BLAST
    Coiled coili249 – 521273Sequence AnalysisAdd
    BLAST
    Coiled coili623 – 66947Sequence AnalysisAdd
    BLAST
    Coiled coili847 – 87125Sequence AnalysisAdd
    BLAST
    Coiled coili1021 – 105030Sequence AnalysisAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi17 – 259Poly-Gly

    Domaini

    The N-terminal coiled coil regions mediate homodimerization preferentially and heterodimerization type alpha/alpha. The C-terminal, non-coiled coil regions mediate heterodimerization type alpha/beta and interaction with PTPRD, PTPRF and PTPRS.

    Sequence similaritiesi

    Belongs to the liprin family. Liprin-alpha subfamily.Curated
    Contains 3 SAM (sterile alpha motif) domains.PROSITE-ProRule annotation

    Keywords - Domaini

    Coiled coil, Repeat

    Phylogenomic databases

    eggNOGiNOG322697.
    HOGENOMiHOG000017513.
    HOVERGENiHBG052330.
    InParanoidiQ13136.
    OMAiSVPDFRF.
    OrthoDBiEOG7T7GS7.
    PhylomeDBiQ13136.
    TreeFamiTF314207.

    Family and domain databases

    Gene3Di1.10.150.50. 2 hits.
    InterProiIPR029515. Liprin.
    IPR001660. SAM.
    IPR013761. SAM/pointed.
    IPR011510. SAM_2.
    IPR021129. SAM_type1.
    [Graphical view]
    PANTHERiPTHR12587. PTHR12587. 1 hit.
    PfamiPF00536. SAM_1. 2 hits.
    PF07647. SAM_2. 1 hit.
    [Graphical view]
    SMARTiSM00454. SAM. 3 hits.
    [Graphical view]
    SUPFAMiSSF47769. SSF47769. 3 hits.
    PROSITEiPS50105. SAM_DOMAIN. 3 hits.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q13136-1) [UniParc]FASTAAdd to Basket

    Also known as: LAR-interacting protein 1b, LIP.1b, b

    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

    MMCEVMPTIS EAEGPPGGGG GHGSGSPSQP DADSHFEQLM VSMLEERDRL     50
    LDTLRETQET LALTQGKLHE VGHERDSLQR QLNTALPQEF AALTKELNVC 100
    REQLLEREEE IAELKAERNN TRLLLEHLEC LVSRHERSLR MTVVKRQAQS 150
    PAGVSSEVEV LKALKSLFEH HKALDEKVRE RLRVALERCS LLEEELGATH 200
    KELMILKEQN NQKKTLTDGV LDINHEQENT PSTSGKRSSD GSLSHEEDLA 250
    KVIELQEIIS KQSREQSQMK ERLASLSSHV TELEEDLDTA RKDLIKSEEM 300
    NTKLQRDVRE AMAQKEDMEE RITTLEKRYL AAQREATSVH DLNDKLENEI 350
    ANKDSMHRQT EDKNRQLQER LELAEQKLQQ TLRKAETLPE VEAELAQRVA 400
    ALSKAEERHG NIEERLRQME AQLEEKNQEL QRARQREKMN EEHNKRLSDT 450
    VDKLLSESNE RLQLHLKERM AALEDKNSLL REVESAKKQL EETQHDKDQL 500
    VLNIEALRAE LDHMRLRGAS LHHGRPHLGS VPDFRFPMAD GHTDSYSTSA 550
    VLRRPQKGRL AALRDEPSKV QTLNEQDWER AQQASVLANV AQAFESDADV 600
    SDGEDDRDTL LSSVDLLSPS GQADAHTLAM MLQEQLDAIN KEIRLIQEEK 650
    ENTEQRAEEI ESRVGSGSLD NLGRFRSMSS IPPYPASSLA SSSPPGSGRS 700
    TPRRIPHSPA REVDRLGVMT LLPPSREEVR DDKTTIKCET SPPSSPRALR 750
    LDRLHKGALH TVSHEDIRDI RNSTGSQDGP VSNPSSSNSS QDSLHKAPKK 800
    KGIKSSIGRL FGKKEKGRPG QTGKEALGQA GVSETDNSSQ DALGLSKLGG 850
    QAEKNRKLQK KHELLEEARR QGLPFAQWDG PTVVVWLELW VGMPAWYVAA 900
    CRANVKSGAI MSALSDTEIQ REIGISNPLH RLKLRLAIQE IMSLTSPSAP 950
    PTSRTTLAYG DMNHEWIGNE WLPSLGLPQY RSYFMECLVD ARMLDHLTKK 1000
    DLRGQLKMVD SFHRNSFQCG IMCLRRLNYD RKELERKREE SQSEIKDVLV 1050
    WSNDRVIRWI LSIGLKEYAN NLIESGVHGA LLALDETFDF SALALLLQIP 1100
    TQNTQARAVL EREFNNLLVM GTDRRFDEDD DKSFRRAPSW RKKFRPKDIR 1150
    GLAAGSAETL PANFRVTSSM SSPSMQPKKM QMDGNVSGTQ RLDSATVRTY 1200
    SC 1202
    Length:1,202
    Mass (Da):135,779
    Last modified:November 1, 1996 - v1
    Checksum:iC8CF7C20B298BFB1
    GO
    Isoform 2 (identifier: Q13136-2) [UniParc]FASTAAdd to Basket

    Also known as: LAR-interacting protein 1a, LIP.1a, a

    The sequence of this isoform differs from the canonical sequence as follows:
         1185-1202: NVSGTQRLDSATVRTYSC → M

    Note: Due to intron retention. No experimental confirmation available.

    Show »
    Length:1,185
    Mass (Da):133,970
    Checksum:i00E9FA5C94C8217C
    GO

    Sequence cautioni

    The sequence BAA08353.1 differs from that shown. Reason: Frameshift at positions 1033, 1041, 1045, 1067 and 1113.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti492 – 4921E → G in AAH34046. (PubMed:15489334)Curated
    Sequence conflicti555 – 5551P → T in AAH34046. (PubMed:15489334)Curated
    Sequence conflicti672 – 6743LGR → EFG in BAA08353. 1 PublicationCurated
    Sequence conflicti800 – 8012KK → EE in BAA08353. 1 PublicationCurated
    Sequence conflicti866 – 8661E → G in AAH34046. (PubMed:15489334)Curated
    Sequence conflicti994 – 9941L → Q in BAA08353. 1 PublicationCurated
    Sequence conflicti1023 – 10231C → S in BAA08353. 1 PublicationCurated
    Sequence conflicti1044 – 10441E → EVRV in BAA08353. 1 PublicationCurated
    Sequence conflicti1121 – 11233GTD → PEF in BAA08353. 1 PublicationCurated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti71 – 711V → I.
    Corresponds to variant rs546502 [ dbSNP | Ensembl ].
    VAR_017756
    Natural varianti1072 – 10721L → F.
    Corresponds to variant rs11236045 [ dbSNP | Ensembl ].
    VAR_049998

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1185 – 120218NVSGT…RTYSC → M in isoform 2. 1 PublicationVSP_009391Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U22815 mRNA. Translation: AAC50172.1.
    U22816 mRNA. Translation: AAC50173.1.
    AP002336 Genomic DNA. No translation available.
    BC034046 mRNA. Translation: AAH34046.1.
    D49354 mRNA. Translation: BAA08353.1. Frameshift.
    CCDSiCCDS31627.1. [Q13136-1]
    CCDS31628.1. [Q13136-2]
    PIRiS55553.
    RefSeqiNP_003617.1. NM_003626.3. [Q13136-1]
    NP_803172.1. NM_177423.2. [Q13136-2]
    UniGeneiHs.530749.
    Hs.708791.

    Genome annotation databases

    EnsembliENST00000253925; ENSP00000253925; ENSG00000131626. [Q13136-1]
    ENST00000389547; ENSP00000374198; ENSG00000131626. [Q13136-2]
    GeneIDi8500.
    KEGGihsa:8500.
    UCSCiuc001opn.2. human. [Q13136-2]
    uc001opo.3. human. [Q13136-1]

    Polymorphism databases

    DMDMi42558969.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U22815 mRNA. Translation: AAC50172.1 .
    U22816 mRNA. Translation: AAC50173.1 .
    AP002336 Genomic DNA. No translation available.
    BC034046 mRNA. Translation: AAH34046.1 .
    D49354 mRNA. Translation: BAA08353.1 . Frameshift.
    CCDSi CCDS31627.1. [Q13136-1 ]
    CCDS31628.1. [Q13136-2 ]
    PIRi S55553.
    RefSeqi NP_003617.1. NM_003626.3. [Q13136-1 ]
    NP_803172.1. NM_177423.2. [Q13136-2 ]
    UniGenei Hs.530749.
    Hs.708791.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1N7F X-ray 1.80 C/D 1195-1202 [» ]
    ProteinModelPortali Q13136.
    SMRi Q13136. Positions 851-1120.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 114072. 33 interactions.
    IntActi Q13136. 16 interactions.
    MINTi MINT-1460222.
    STRINGi 9606.ENSP00000253925.

    PTM databases

    PhosphoSitei Q13136.

    Polymorphism databases

    DMDMi 42558969.

    Proteomic databases

    MaxQBi Q13136.
    PaxDbi Q13136.
    PRIDEi Q13136.

    Protocols and materials databases

    DNASUi 8500.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000253925 ; ENSP00000253925 ; ENSG00000131626 . [Q13136-1 ]
    ENST00000389547 ; ENSP00000374198 ; ENSG00000131626 . [Q13136-2 ]
    GeneIDi 8500.
    KEGGi hsa:8500.
    UCSCi uc001opn.2. human. [Q13136-2 ]
    uc001opo.3. human. [Q13136-1 ]

    Organism-specific databases

    CTDi 8500.
    GeneCardsi GC11P070116.
    HGNCi HGNC:9245. PPFIA1.
    HPAi CAB017032.
    HPA008272.
    HPA042271.
    MIMi 611054. gene.
    neXtProti NX_Q13136.
    PharmGKBi PA33566.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG322697.
    HOGENOMi HOG000017513.
    HOVERGENi HBG052330.
    InParanoidi Q13136.
    OMAi SVPDFRF.
    OrthoDBi EOG7T7GS7.
    PhylomeDBi Q13136.
    TreeFami TF314207.

    Enzyme and pathway databases

    SignaLinki Q13136.

    Miscellaneous databases

    GeneWikii Liprin-alpha-1.
    GenomeRNAii 8500.
    NextBioi 31805.
    PMAP-CutDB Q13136.
    PROi Q13136.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q13136.
    Bgeei Q13136.
    CleanExi HS_PPFIA1.
    Genevestigatori Q13136.

    Family and domain databases

    Gene3Di 1.10.150.50. 2 hits.
    InterProi IPR029515. Liprin.
    IPR001660. SAM.
    IPR013761. SAM/pointed.
    IPR011510. SAM_2.
    IPR021129. SAM_type1.
    [Graphical view ]
    PANTHERi PTHR12587. PTHR12587. 1 hit.
    Pfami PF00536. SAM_1. 2 hits.
    PF07647. SAM_2. 1 hit.
    [Graphical view ]
    SMARTi SM00454. SAM. 3 hits.
    [Graphical view ]
    SUPFAMi SSF47769. SSF47769. 3 hits.
    PROSITEi PS50105. SAM_DOMAIN. 3 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "The LAR transmembrane protein tyrosine phosphatase and a coiled-coil LAR-interacting protein co-localize at focal adhesions."
      Serra-Pages C., Kedersha N.L., Fazikas L., Medley Q.G., Debant A., Streuli M.
      EMBO J. 14:2827-2838(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), TISSUE SPECIFICITY, FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH PTPRF.
    2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    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 1).
      Tissue: Brain.
    4. "Molecular cloning of a cDNA encoding enhancer protein in hsp70 gene."
      Taira T., Iguchi-Ariga S.M., Ariga H.
      Submitted (FEB-1995) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 672-1123.
    5. "The LAR/PTP delta/PTP sigma subfamily of transmembrane protein-tyrosine-phosphatases: multiple human LAR, PTP delta, and PTP sigma isoforms are expressed in a tissue-specific manner and associate with the LAR-interacting protein LIP.1."
      Pulido R., Serra-Pages C., Tang M., Streuli M.
      Proc. Natl. Acad. Sci. U.S.A. 92:11686-11690(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH PTPRD; PTPRF AND PTPRS.
    6. "Liprins, a family of LAR transmembrane protein-tyrosine phosphatase-interacting proteins."
      Serra-Pages C., Medley Q.G., Tang M., Hart A., Streuli M.
      J. Biol. Chem. 273:15611-15620(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: TISSUE SPECIFICITY, INTERACTION WITH PTPRD; PTPRF AND PTPRS.
    7. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
      Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
      Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    8. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Embryonic kidney.
    9. "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis."
      Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III
      J. Proteome Res. 7:1346-1351(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    10. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-230; SER-242 AND SER-244, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    11. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
      Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
      Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    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 SER-239; SER-242; SER-693 AND THR-1159, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    13. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    14. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
      Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
      Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-239; SER-242; SER-244 AND SER-448, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiLIPA1_HUMAN
    AccessioniPrimary (citable) accession number: Q13136
    Secondary accession number(s): A6NLE3
    , Q13135, Q14567, Q8N4I2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 16, 2004
    Last sequence update: November 1, 1996
    Last modified: October 1, 2014
    This is version 127 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, Reference proteome

    Documents

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

    External Data

    Dasty 3