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Q9Y613

- FHOD1_HUMAN

UniProt

Q9Y613 - FHOD1_HUMAN

Protein

FH1/FH2 domain-containing protein 1

Gene

FHOD1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 129 (01 Oct 2014)
      Sequence version 3 (23 Jan 2007)
      Previous versions | rss
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    Functioni

    Required for the assembly of F-actin structures, such as stress fibers. Depends on the Rho-ROCK cascade for its activity. Contributes to the coordination of microtubules with actin fibers and plays a role in cell elongation. Acts synergistically with ROCK1 to promote SRC-dependent non-apoptotic plasma membrane blebbing.3 Publications

    GO - Molecular functioni

    1. identical protein binding Source: IntAct
    2. protein binding Source: BHF-UCL

    GO - Biological processi

    1. positive regulation of stress fiber assembly Source: BHF-UCL
    2. positive regulation of transcription from RNA polymerase II promoter Source: BHF-UCL

    Keywords - Ligandi

    Actin-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    FH1/FH2 domain-containing protein 1
    Alternative name(s):
    Formin homolog overexpressed in spleen 1
    Short name:
    FHOS
    Formin homology 2 domain-containing protein 1
    Gene namesi
    Name:FHOD1
    Synonyms:FHOS, FHOS1
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 16

    Organism-specific databases

    HGNCiHGNC:17905. FHOD1.

    Subcellular locationi

    Cytoplasm. Cytoplasmcytoskeleton. Cell projectionbleb
    Note: Predominantly cytoplasmic.

    GO - Cellular componenti

    1. bleb Source: UniProtKB-SubCell
    2. cytoplasm Source: HPA
    3. cytoskeleton Source: UniProtKB-SubCell
    4. membrane Source: UniProtKB
    5. nucleus Source: BHF-UCL

    Keywords - Cellular componenti

    Cell projection, Cytoplasm, Cytoskeleton

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA28143.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 11641163FH1/FH2 domain-containing protein 1PRO_0000194905Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei367 – 3671Phosphoserine3 Publications
    Modified residuei486 – 4861Phosphoserine2 Publications
    Modified residuei495 – 4951Phosphothreonine2 Publications
    Modified residuei498 – 4981Phosphoserine3 Publications
    Modified residuei523 – 5231Phosphoserine4 Publications
    Modified residuei573 – 5731Phosphoserine2 Publications
    Modified residuei690 – 6901Phosphothreonine2 Publications

    Post-translational modificationi

    Phosphorylated by ROCK1.5 Publications

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiQ9Y613.
    PaxDbiQ9Y613.
    PeptideAtlasiQ9Y613.
    PRIDEiQ9Y613.

    PTM databases

    PhosphoSiteiQ9Y613.

    Expressioni

    Tissue specificityi

    Ubiquitous. Highly expressed in spleen.

    Gene expression databases

    ArrayExpressiQ9Y613.
    BgeeiQ9Y613.
    CleanExiHS_FHOD1.
    GenevestigatoriQ9Y613.

    Organism-specific databases

    HPAiHPA024468.

    Interactioni

    Subunit structurei

    Self-associates via the FH2 domain. Binds to F-actin via its N-terminus. Binds to the cytoplasmic domain of CD21 via its C-terminus. Interacts with ROCK1 in a Src-dependent manner.3 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    itself8EBI-348433,EBI-348433

    Protein-protein interaction databases

    BioGridi118877. 21 interactions.
    DIPiDIP-31134N.
    IntActiQ9Y613. 13 interactions.
    MINTiMINT-1033686.
    STRINGi9606.ENSP00000258201.

    Structurei

    Secondary structure

    1
    1164
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi15 – 228
    Beta strandi36 – 394
    Beta strandi42 – 465
    Helixi51 – 533
    Helixi55 – 617
    Beta strandi68 – 758
    Turni76 – 783
    Turni88 – 936
    Helixi98 – 1003
    Helixi102 – 1043
    Beta strandi109 – 1146
    Helixi116 – 12914
    Helixi132 – 14716
    Helixi152 – 1587
    Helixi161 – 1699
    Helixi174 – 18714
    Helixi191 – 1999
    Helixi201 – 2099
    Helixi210 – 2123
    Helixi216 – 23217
    Helixi234 – 2363
    Helixi237 – 25115
    Helixi257 – 2637
    Turni264 – 2674
    Helixi271 – 28717
    Helixi291 – 30313
    Helixi306 – 3149
    Helixi321 – 33818

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3DADX-ray2.30A/B1-339[»]
    DisProtiDP00448.
    ProteinModelPortaliQ9Y613.
    SMRiQ9Y613. Positions 14-339, 651-1013.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ9Y613.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini53 – 458406GBD/FH3PROSITE-ProRule annotationAdd
    BLAST
    Domaini487 – 615129FH1Add
    BLAST
    Domaini616 – 1013398FH2PROSITE-ProRule annotationAdd
    BLAST
    Domaini1053 – 113381DADAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni612 – 807196Interaction with ROCK1Add
    BLAST

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili884 – 92138Sequence AnalysisAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi583 – 59311Poly-ProAdd
    BLAST
    Compositional biasi597 – 6059Poly-Pro
    Compositional biasi996 – 10016Poly-Gln

    Domaini

    The DAD domain regulates activation via by an autoinhibitory interaction with the GBD/FH3 domain. This autoinhibition is released upon competitive binding of an activated GTPase. The release of DAD allows the FH2 domain to then nucleate and elongate nonbranched actin filaments.1 Publication

    Sequence similaritiesi

    Belongs to the formin homology family.Curated
    Contains 1 FH2 (formin homology 2) domain.PROSITE-ProRule annotation
    Contains 1 GBD/FH3 (Rho GTPase-binding/formin homology 3) domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Coiled coil

    Phylogenomic databases

    eggNOGiNOG246341.
    HOGENOMiHOG000015130.
    HOVERGENiHBG051615.
    InParanoidiQ9Y613.
    OMAiPKLCIGD.
    OrthoDBiEOG71G9T2.
    PhylomeDBiQ9Y613.
    TreeFamiTF316268.

    Family and domain databases

    InterProiIPR016024. ARM-type_fold.
    IPR015425. FH2_Formin.
    IPR027647. FHDC1.
    IPR014768. GTPase-bd/formin_homology_3.
    [Graphical view]
    PANTHERiPTHR23213:SF189. PTHR23213:SF189. 1 hit.
    PfamiPF02181. FH2. 1 hit.
    [Graphical view]
    SMARTiSM00498. FH2. 1 hit.
    [Graphical view]
    SUPFAMiSSF48371. SSF48371. 1 hit.
    PROSITEiPS51444. FH2. 1 hit.
    PS51232. GBD_FH3. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    Q9Y613-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAGGEDRGDG EPVSVVTVRV QYLEDTDPFA CANFPEPRRA PTCSLDGALP     50
    LGAQIPAVHR LLGAPLKLED CALQVSPSGY YLDTELSLEE QREMLEGFYE 100
    EISKGRKPTL ILRTQLSVRV NAILEKLYSS SGPELRRSLF SLKQIFQEDK 150
    DLVPEFVHSE GLSCLIRVGA AADHNYQSYI LRALGQLMLF VDGMLGVVAH 200
    SDTIQWLYTL CASLSRLVVK TALKLLLVFV EYSENNAPLF IRAVNSVAST 250
    TGAPPWANLV SILEEKNGAD PELLVYTVTL INKTLAALPD QDSFYDVTDA 300
    LEQQGMEALV QRHLGTAGTD VDLRTQLVLY ENALKLEDGD IEEAPGAGGR 350
    RERRKPSSEE GKRSRRSLEG GGCPARAPEP GPTGPASPVG PTSSTGPALL 400
    TGPASSPVGP PSGLQASVNL FPTISVAPSA DTSSERSIYK ARFLENVAAA 450
    ETEKQVALAQ GRAETLAGAM PNEAGGHPDA RQLWDSPETA PAARTPQSPA 500
    PCVLLRAQRS LAPEPKEPLI PASPKAEPIW ELPTRAPRLS IGDLDFSDLG 550
    EDEDQDMLNV ESVEAGKDIP APSPPLPLLS GVPPPPPLPP PPPIKGPFPP 600
    PPPLPLAAPL PHSVPDSSAL PTKRKTVKLF WRELKLAGGH GVSASRFGPC 650
    ATLWASLDPV SVDTARLEHL FESRAKEVLP SKKAGEGRRT MTTVLDPKRS 700
    NAINIGLTTL PPVHVIKAAL LNFDEFAVSK DGIEKLLTMM PTEEERQKIE 750
    EAQLANPDIP LGPAENFLMT LASIGGLAAR LQLWAFKLDY DSMEREIAEP 800
    LFDLKVGMEQ LVQNATFRCI LATLLAVGNF LNGSQSSGFE LSYLEKVSEV 850
    KDTVRRQSLL HHLCSLVLQT RPESSDLYSE IPALTRCAKV DFEQLTENLG 900
    QLERRSRAAE ESLRSLAKHE LAPALRARLT HFLDQCARRV AMLRIVHRRV 950
    CNRFHAFLLY LGYTPQAARE VRIMQFCHTL REFALEYRTC RERVLQQQQK 1000
    QATYRERNKT RGRMITETEK FSGVAGEAPS NPSVPVAVSS GPGRGDADSH 1050
    ASMKSLLTSR PEDTTHNRRS RGMVQSSSPI MPTVGPSTAS PEEPPGSSLP 1100
    SDTSDEIMDL LVQSVTKSSP RALAARERKR SRGNRKSLRR TLKSGLGDDL 1150
    VQALGLSKGP GLEV 1164
    Length:1,164
    Mass (Da):126,551
    Last modified:January 23, 2007 - v3
    Checksum:iE6C7AE1FB8DC3FC7
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti249 – 2491S → T in AAD39906. (PubMed:10352228)Curated
    Sequence conflicti249 – 2491S → T in AAO38757. (PubMed:15138285)Curated
    Sequence conflicti264 – 2641E → D in AAO38757. (PubMed:15138285)Curated
    Sequence conflicti277 – 2771T → M in BAD06250. (PubMed:14576350)Curated
    Sequence conflicti307 – 3082EA → DT in AAD39906. (PubMed:10352228)Curated
    Sequence conflicti307 – 3082EA → DT in AAO38757. (PubMed:15138285)Curated
    Sequence conflicti359 – 3591E → D in AAO38757. (PubMed:15138285)Curated
    Sequence conflicti387 – 3871S → T in AAO38757. (PubMed:15138285)Curated
    Sequence conflicti533 – 5331P → L in BAD92821. 1 PublicationCurated
    Sequence conflicti633 – 6342EL → DV in AAD39906. (PubMed:10352228)Curated
    Sequence conflicti689 – 6891R → Q in AAO38757. (PubMed:15138285)Curated
    Sequence conflicti700 – 7001S → T in AAD39906. (PubMed:10352228)Curated
    Sequence conflicti745 – 7451E → G in AAO38757. (PubMed:15138285)Curated
    Sequence conflicti751 – 7511E → G in AAD39906. (PubMed:10352228)Curated
    Sequence conflicti849 – 8491E → D in AAD39906. (PubMed:10352228)Curated
    Sequence conflicti1061 – 10611P → L in AAD39906. (PubMed:10352228)Curated
    Sequence conflicti1061 – 10611P → L in AAO38757. (PubMed:15138285)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF113615 mRNA. Translation: AAD39906.1.
    AB041046 mRNA. Translation: BAD06250.1.
    AY192154 mRNA. Translation: AAO38757.1.
    BC033084 mRNA. Translation: AAH33084.1.
    AB209584 mRNA. Translation: BAD92821.1.
    CCDSiCCDS10834.1.
    RefSeqiNP_037373.2. NM_013241.2.
    UniGeneiHs.95231.

    Genome annotation databases

    EnsembliENST00000258201; ENSP00000258201; ENSG00000135723.
    GeneIDi29109.
    KEGGihsa:29109.
    UCSCiuc002esl.3. human.

    Polymorphism databases

    DMDMi62512187.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF113615 mRNA. Translation: AAD39906.1 .
    AB041046 mRNA. Translation: BAD06250.1 .
    AY192154 mRNA. Translation: AAO38757.1 .
    BC033084 mRNA. Translation: AAH33084.1 .
    AB209584 mRNA. Translation: BAD92821.1 .
    CCDSi CCDS10834.1.
    RefSeqi NP_037373.2. NM_013241.2.
    UniGenei Hs.95231.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3DAD X-ray 2.30 A/B 1-339 [» ]
    DisProti DP00448.
    ProteinModelPortali Q9Y613.
    SMRi Q9Y613. Positions 14-339, 651-1013.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 118877. 21 interactions.
    DIPi DIP-31134N.
    IntActi Q9Y613. 13 interactions.
    MINTi MINT-1033686.
    STRINGi 9606.ENSP00000258201.

    PTM databases

    PhosphoSitei Q9Y613.

    Polymorphism databases

    DMDMi 62512187.

    Proteomic databases

    MaxQBi Q9Y613.
    PaxDbi Q9Y613.
    PeptideAtlasi Q9Y613.
    PRIDEi Q9Y613.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000258201 ; ENSP00000258201 ; ENSG00000135723 .
    GeneIDi 29109.
    KEGGi hsa:29109.
    UCSCi uc002esl.3. human.

    Organism-specific databases

    CTDi 29109.
    GeneCardsi GC16M067263.
    HGNCi HGNC:17905. FHOD1.
    HPAi HPA024468.
    MIMi 606881. gene.
    neXtProti NX_Q9Y613.
    PharmGKBi PA28143.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG246341.
    HOGENOMi HOG000015130.
    HOVERGENi HBG051615.
    InParanoidi Q9Y613.
    OMAi PKLCIGD.
    OrthoDBi EOG71G9T2.
    PhylomeDBi Q9Y613.
    TreeFami TF316268.

    Miscellaneous databases

    EvolutionaryTracei Q9Y613.
    GeneWikii FHOD1.
    GenomeRNAii 29109.
    NextBioi 52175.
    PROi Q9Y613.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9Y613.
    Bgeei Q9Y613.
    CleanExi HS_FHOD1.
    Genevestigatori Q9Y613.

    Family and domain databases

    InterProi IPR016024. ARM-type_fold.
    IPR015425. FH2_Formin.
    IPR027647. FHDC1.
    IPR014768. GTPase-bd/formin_homology_3.
    [Graphical view ]
    PANTHERi PTHR23213:SF189. PTHR23213:SF189. 1 hit.
    Pfami PF02181. FH2. 1 hit.
    [Graphical view ]
    SMARTi SM00498. FH2. 1 hit.
    [Graphical view ]
    SUPFAMi SSF48371. SSF48371. 1 hit.
    PROSITEi PS51444. FH2. 1 hit.
    PS51232. GBD_FH3. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Identification and characterization of a protein containing formin homology (FH1/FH2) domains."
      Westendorf J.J., Mernaugh R., Hiebert S.W.
      Gene 232:173-182(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    2. "Fhos, a mammalian formin, directly binds to F-actin via a region N-terminal to the FH1 domain and forms a homotypic complex via the FH2 domain to promote actin fiber formation."
      Takeya R., Sumimoto H.
      J. Cell Sci. 116:4567-4575(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBUNIT.
    3. "EBV attachment stimulates FHOS/FHOD1 redistribution and co-aggregation with CD21: formin interactions with the cytoplasmic domain of human CD21."
      Gill M.B., Roecklein-Canfield J., Sage D.R., Zambela-Soediono M., Longtine N., Uknis M., Fingeroth J.D.
      J. Cell Sci. 117:2709-2720(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], SUBUNIT.
    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].
      Tissue: Prostate.
    5. "Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides."
      Gevaert K., Goethals M., Martens L., Van Damme J., Staes A., Thomas G.R., Vandekerckhove J.
      Nat. Biotechnol. 21:566-569(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 2-19.
      Tissue: Platelet.
    6. Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S., Ohara O., Nagase T., Kikuno R.F.
      Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 148-1164.
      Tissue: Spleen.
    7. "FHOD1 coordinates actin filament and microtubule alignment to mediate cell elongation."
      Gasteier J.E., Schroeder S., Muranyi W., Madrid R., Benichou S., Fackler O.T.
      Exp. Cell Res. 306:192-202(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, AUTOINHIBITION, SUBCELLULAR LOCATION.
    8. "Biochemical characterization of the diaphanous autoregulatory interaction in the formin homology protein FHOD1."
      Schonichen A., Alexander M., Gasteier J.E., Cuesta F.E., Fackler O.T., Geyer M.
      J. Biol. Chem. 281:5084-5093(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: DOMAIN DAD, AUTOINHIBITION.
    9. "The diaphanous-related formin FHOD1 associates with ROCK1 and promotes Src-dependent plasma membrane blebbing."
      Hannemann S., Madrid R., Stastna J., Kitzing T., Gasteier J., Schoenichen A., Bouchet J., Jimenez A., Geyer M., Grosse R., Benichou S., Fackler O.T.
      J. Biol. Chem. 283:27891-27903(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH ROCK1, PHOSPHORYLATION.
    10. "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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-498, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    11. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-367; THR-495; SER-498 AND SER-523, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Platelet.
    12. "Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
      Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
      Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-367; SER-486; SER-523 AND SER-573, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    13. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-523 AND THR-690, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    14. "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].
    15. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiFHOD1_HUMAN
    AccessioniPrimary (citable) accession number: Q9Y613
    Secondary accession number(s): Q59F76
    , Q6Y1F2, Q76MS8, Q8N521
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 21, 2001
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 129 of the entry and version 3 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 16
      Human chromosome 16: 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