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Q9HBI1

- PARVB_HUMAN

UniProt

Q9HBI1 - PARVB_HUMAN

Protein

Beta-parvin

Gene

PARVB

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 126 (01 Oct 2014)
      Sequence version 1 (01 Mar 2001)
      Previous versions | rss
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    Functioni

    Adapter protein that plays a role in integrin signaling via ILK and in activation of the GTPases CDC42 and RAC1 by guanine exchange factors, such as ARHGEF6. Is involved in the reorganization of the actin cytoskeleton and formation of lamellipodia. Plays a role in cell adhesion, cell spreading, establishment or maintenance of cell polarity, and cell migration.5 Publications

    GO - Molecular functioni

    1. protein binding Source: IntAct

    GO - Biological processi

    1. actin cytoskeleton reorganization Source: UniProtKB
    2. cell adhesion Source: UniProtKB-KW
    3. cell junction assembly Source: Reactome
    4. cell projection assembly Source: UniProtKB
    5. establishment or maintenance of cell polarity regulating cell shape Source: UniProtKB
    6. lamellipodium assembly Source: UniProtKB

    Keywords - Biological processi

    Cell adhesion

    Keywords - Ligandi

    Actin-binding

    Enzyme and pathway databases

    ReactomeiREACT_20580. Regulation of cytoskeletal remodeling and cell spreading by IPP complex components.
    REACT_20649. Cell-extracellular matrix interactions.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Beta-parvin
    Alternative name(s):
    Affixin
    Gene namesi
    Name:PARVB
    ORF Names:CGI-56
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 22

    Organism-specific databases

    HGNCiHGNC:14653. PARVB.

    Subcellular locationi

    Cell junctionfocal adhesion. Cell membrane; Peripheral membrane protein; Cytoplasmic side. Cytoplasmcytoskeleton. Cell projectionlamellipodium. Cytoplasmmyofibrilsarcomere. CytoplasmmyofibrilsarcomereZ line
    Note: Constituent of focal adhesions. Detected at the tips of the leading edge of cells. Colocalizes with F-actin at the tips of lamellipodia.

    GO - Cellular componenti

    1. cytoskeleton Source: UniProtKB-SubCell
    2. cytosol Source: Reactome
    3. focal adhesion Source: UniProtKB
    4. lamellipodium Source: UniProtKB
    5. plasma membrane Source: UniProtKB-SubCell
    6. Z disc Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cell junction, Cell membrane, Cell projection, Cytoplasm, Cytoskeleton, Membrane

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi256 – 2561V → Q: Abolishes interaction with PXN. 1 Publication
    Mutagenesisi299 – 2991F → D: Abolishes interaction with ILK. Abolishes location at focal adhesion sites. 1 Publication

    Organism-specific databases

    PharmGKBiPA32951.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 364364Beta-parvinPRO_0000121583Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei54 – 541Phosphoserine2 Publications

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiQ9HBI1.
    PaxDbiQ9HBI1.
    PRIDEiQ9HBI1.

    PTM databases

    PhosphoSiteiQ9HBI1.

    Expressioni

    Tissue specificityi

    Expressed predominantly in heart and skeletal muscle.2 Publications

    Gene expression databases

    ArrayExpressiQ9HBI1.
    BgeeiQ9HBI1.
    CleanExiHS_PARVB.
    GenevestigatoriQ9HBI1.

    Interactioni

    Subunit structurei

    Interacts with DYSF. Interacts with ILK, ARHGEF6, PXN (via LD motifs), ACTN2 and actin.7 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    Arhgef6Q8K4I33EBI-1047679,EBI-6272809From a different organism.
    Arhgef7Q9ES2810EBI-1047679,EBI-642580From a different organism.

    Protein-protein interaction databases

    BioGridi118912. 3 interactions.
    IntActiQ9HBI1. 7 interactions.
    MINTiMINT-6178745.

    Structurei

    Secondary structure

    1
    364
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi243 – 2464
    Helixi250 – 2523
    Helixi254 – 26815
    Helixi269 – 2713
    Turni278 – 2847
    Helixi286 – 29510
    Helixi302 – 3043
    Helixi312 – 32817
    Helixi338 – 3425
    Helixi346 – 36015

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    4EDLX-ray2.10A/B/C/D/E/F235-364[»]
    4EDMX-ray2.00A/B235-364[»]
    4EDNX-ray2.90A/B/C/D/E/F/G/H/I/J235-364[»]
    ProteinModelPortaliQ9HBI1.
    SMRiQ9HBI1. Positions 90-196, 235-364.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini87 – 194108CH 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini254 – 361108CH 2PROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

    Belongs to the parvin family.Curated
    Contains 2 CH (calponin-homology) domains.PROSITE-ProRule annotation

    Keywords - Domaini

    Repeat

    Phylogenomic databases

    eggNOGiNOG303418.
    HOVERGENiHBG053517.
    KOiK06275.
    OMAiPMQQHPM.
    OrthoDBiEOG70KGPW.
    PhylomeDBiQ9HBI1.
    TreeFamiTF314025.

    Family and domain databases

    Gene3Di1.10.418.10. 2 hits.
    InterProiIPR001715. CH-domain.
    IPR028433. Parvin.
    [Graphical view]
    PANTHERiPTHR12114. PTHR12114. 1 hit.
    PfamiPF00307. CH. 2 hits.
    [Graphical view]
    SMARTiSM00033. CH. 2 hits.
    [Graphical view]
    SUPFAMiSSF47576. SSF47576. 2 hits.
    PROSITEiPS50021. CH. 2 hits.
    [Graphical view]

    Sequences (3)i

    Sequence statusi: Complete.

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q9HBI1-1) [UniParc]FASTAAdd to Basket

    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

    MSSAPRSPTP RPRRMKKDES FLGKLGGTLA RKRRAREVSD LQEEGKNAIN    50
    SPMSPALVDV HPEDTQLEEN EERTMIDPTS KEDPKFKELV KVLLDWINDV 100
    LVEERIIVKQ LEEDLYDGQV LQKLLEKLAG CKLNVAEVTQ SEIGQKQKLQ 150
    TVLEAVHDLL RPRGWALRWS VDSIHGKNLV AILHLLVSLA MHFRAPIRLP 200
    EHVTVQVVVV RKREGLLHSS HISEELTTTT EMMMGRFERD AFDTLFDHAP 250
    DKLSVVKKSL ITFVNKHLNK LNLEVTELET QFADGVYLVL LMGLLEDYFV 300
    PLHHFYLTPE SFDQKVHNVS FAFELMLDGG LKKPKARPED VVNLDLKSTL 350
    RVLYNLFTKY KNVE 364
    Length:364
    Mass (Da):41,714
    Last modified:March 1, 2001 - v1
    Checksum:i4BA4B50C83083DC7
    GO
    Isoform 2 (identifier: Q9HBI1-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-37: MSSAPRSPTP...TLARKRRARE → MHHVFKDHQR...VETSEYAQGG

    Show »
    Length:397
    Mass (Da):45,183
    Checksum:iBA4335437824E465
    GO
    Isoform 3 (identifier: Q9HBI1-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-38: MSSAPRSPTPRPRRMKKDESFLGKLGGTLARKRRAREV → M

    Note: No experimental confirmation available.

    Show »
    Length:327
    Mass (Da):37,538
    Checksum:iBD4A2F8D5ECD7768
    GO

    Sequence cautioni

    The sequence AAD34051.1 differs from that shown. Reason: Frameshift at positions 4, 14, 48, 58, 155, 162, 171, 327, 331 and 344.
    The sequence BG743702 differs from that shown. Reason: Frameshift at positions 136, 232 and 237.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti27 – 271G → V in AAD34051. (PubMed:10810093)Curated
    Sequence conflicti59 – 591D → M in AAD34051. (PubMed:10810093)Curated
    Sequence conflicti349 – 3491T → P in AAD34051. (PubMed:10810093)Curated
    Isoform 2 (identifier: Q9HBI1-2)
    Sequence conflicti4 – 41V → G in BG743702. (PubMed:15489334)Curated
    Sequence conflicti21 – 211N → K in AAL08219. 1 PublicationCurated
    Sequence conflicti37 – 371W → R in AAL08219. 1 PublicationCurated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti52 – 521P → R.
    Corresponds to variant rs34476853 [ dbSNP | Ensembl ].
    VAR_034369
    Natural varianti58 – 581V → A.4 Publications
    Corresponds to variant rs1983609 [ dbSNP | Ensembl ].
    VAR_017242

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 3838MSSAP…RAREV → M in isoform 3. 1 PublicationVSP_045555Add
    BLAST
    Alternative sequencei1 – 3737MSSAP…RRARE → MHHVFKDHQRGEKRGFLSPE NKNCRRLELRRGCSCSWGLC SQALMASLAGSLLPGSDRSG VETSEYAQGG in isoform 2. 2 PublicationsVSP_041336Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF303887 mRNA. Translation: AAL08219.1.
    AB048276 mRNA. Translation: BAB62077.1.
    AF237769 mRNA. Translation: AAG27171.1.
    AF151814 mRNA. Translation: AAD34051.1. Frameshift.
    AK313957 mRNA. Translation: BAG36673.1.
    AL031595, AL033543, Z82178 Genomic DNA. Translation: CAI22312.1.
    AL033543, AL031595, Z82178 Genomic DNA. Translation: CAI17969.1.
    Z82178, AL031595, AL033543 Genomic DNA. Translation: CAI18767.1.
    AL033543, AL031595, Z82174 Genomic DNA. Translation: CAQ06491.1.
    AL033543, AL031595, AL035398 Genomic DNA. Translation: CAQ06493.1.
    AL031595, AL033543, Z82174 Genomic DNA. Translation: CAQ08141.1.
    AL031595, AL033543, AL035398 Genomic DNA. Translation: CAQ08144.1.
    Z82174, AL031595, AL033543 Genomic DNA. Translation: CAQ08662.1.
    AL035398, AL031595, AL033543 Genomic DNA. Translation: CAQ09485.1.
    CH471138 Genomic DNA. Translation: EAW73328.1.
    BC039811 mRNA. No translation available.
    BC046103 mRNA. Translation: AAH46103.2.
    BG743702 mRNA. No translation available.
    AL159142 mRNA. Translation: CAB76900.1.
    CCDSiCCDS14056.1. [Q9HBI1-1]
    CCDS46724.1. [Q9HBI1-2]
    CCDS58808.1. [Q9HBI1-3]
    RefSeqiNP_001003828.1. NM_001003828.2. [Q9HBI1-2]
    NP_001230314.1. NM_001243385.1. [Q9HBI1-3]
    NP_001230315.1. NM_001243386.1.
    NP_037459.2. NM_013327.4. [Q9HBI1-1]
    XP_005261650.1. XM_005261593.1. [Q9HBI1-3]
    XP_005261651.1. XM_005261594.1. [Q9HBI1-3]
    XP_005261652.1. XM_005261595.1. [Q9HBI1-3]
    XP_006724299.1. XM_006724236.1. [Q9HBI1-3]
    UniGeneiHs.475074.

    Genome annotation databases

    EnsembliENST00000338758; ENSP00000342492; ENSG00000188677. [Q9HBI1-1]
    ENST00000404989; ENSP00000384353; ENSG00000188677. [Q9HBI1-3]
    ENST00000406477; ENSP00000384515; ENSG00000188677. [Q9HBI1-2]
    GeneIDi29780.
    KEGGihsa:29780.
    UCSCiuc003bem.3. human. [Q9HBI1-2]
    uc003ben.3. human. [Q9HBI1-1]
    uc003beo.3. human.

    Polymorphism databases

    DMDMi20139178.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Web resourcesi

    Atlas of Genetics and Cytogenetics in Oncology and Haematology

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF303887 mRNA. Translation: AAL08219.1 .
    AB048276 mRNA. Translation: BAB62077.1 .
    AF237769 mRNA. Translation: AAG27171.1 .
    AF151814 mRNA. Translation: AAD34051.1 . Frameshift.
    AK313957 mRNA. Translation: BAG36673.1 .
    AL031595 , AL033543 , Z82178 Genomic DNA. Translation: CAI22312.1 .
    AL033543 , AL031595 , Z82178 Genomic DNA. Translation: CAI17969.1 .
    Z82178 , AL031595 , AL033543 Genomic DNA. Translation: CAI18767.1 .
    AL033543 , AL031595 , Z82174 Genomic DNA. Translation: CAQ06491.1 .
    AL033543 , AL031595 , AL035398 Genomic DNA. Translation: CAQ06493.1 .
    AL031595 , AL033543 , Z82174 Genomic DNA. Translation: CAQ08141.1 .
    AL031595 , AL033543 , AL035398 Genomic DNA. Translation: CAQ08144.1 .
    Z82174 , AL031595 , AL033543 Genomic DNA. Translation: CAQ08662.1 .
    AL035398 , AL031595 , AL033543 Genomic DNA. Translation: CAQ09485.1 .
    CH471138 Genomic DNA. Translation: EAW73328.1 .
    BC039811 mRNA. No translation available.
    BC046103 mRNA. Translation: AAH46103.2 .
    BG743702 mRNA. No translation available.
    AL159142 mRNA. Translation: CAB76900.1 .
    CCDSi CCDS14056.1. [Q9HBI1-1 ]
    CCDS46724.1. [Q9HBI1-2 ]
    CCDS58808.1. [Q9HBI1-3 ]
    RefSeqi NP_001003828.1. NM_001003828.2. [Q9HBI1-2 ]
    NP_001230314.1. NM_001243385.1. [Q9HBI1-3 ]
    NP_001230315.1. NM_001243386.1.
    NP_037459.2. NM_013327.4. [Q9HBI1-1 ]
    XP_005261650.1. XM_005261593.1. [Q9HBI1-3 ]
    XP_005261651.1. XM_005261594.1. [Q9HBI1-3 ]
    XP_005261652.1. XM_005261595.1. [Q9HBI1-3 ]
    XP_006724299.1. XM_006724236.1. [Q9HBI1-3 ]
    UniGenei Hs.475074.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    4EDL X-ray 2.10 A/B/C/D/E/F 235-364 [» ]
    4EDM X-ray 2.00 A/B 235-364 [» ]
    4EDN X-ray 2.90 A/B/C/D/E/F/G/H/I/J 235-364 [» ]
    ProteinModelPortali Q9HBI1.
    SMRi Q9HBI1. Positions 90-196, 235-364.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 118912. 3 interactions.
    IntActi Q9HBI1. 7 interactions.
    MINTi MINT-6178745.

    PTM databases

    PhosphoSitei Q9HBI1.

    Polymorphism databases

    DMDMi 20139178.

    Proteomic databases

    MaxQBi Q9HBI1.
    PaxDbi Q9HBI1.
    PRIDEi Q9HBI1.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000338758 ; ENSP00000342492 ; ENSG00000188677 . [Q9HBI1-1 ]
    ENST00000404989 ; ENSP00000384353 ; ENSG00000188677 . [Q9HBI1-3 ]
    ENST00000406477 ; ENSP00000384515 ; ENSG00000188677 . [Q9HBI1-2 ]
    GeneIDi 29780.
    KEGGi hsa:29780.
    UCSCi uc003bem.3. human. [Q9HBI1-2 ]
    uc003ben.3. human. [Q9HBI1-1 ]
    uc003beo.3. human.

    Organism-specific databases

    CTDi 29780.
    GeneCardsi GC22P044395.
    HGNCi HGNC:14653. PARVB.
    MIMi 608121. gene.
    neXtProti NX_Q9HBI1.
    PharmGKBi PA32951.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG303418.
    HOVERGENi HBG053517.
    KOi K06275.
    OMAi PMQQHPM.
    OrthoDBi EOG70KGPW.
    PhylomeDBi Q9HBI1.
    TreeFami TF314025.

    Enzyme and pathway databases

    Reactomei REACT_20580. Regulation of cytoskeletal remodeling and cell spreading by IPP complex components.
    REACT_20649. Cell-extracellular matrix interactions.

    Miscellaneous databases

    GeneWikii PARVB.
    GenomeRNAii 29780.
    NextBioi 52306.
    PROi Q9HBI1.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9HBI1.
    Bgeei Q9HBI1.
    CleanExi HS_PARVB.
    Genevestigatori Q9HBI1.

    Family and domain databases

    Gene3Di 1.10.418.10. 2 hits.
    InterProi IPR001715. CH-domain.
    IPR028433. Parvin.
    [Graphical view ]
    PANTHERi PTHR12114. PTHR12114. 1 hit.
    Pfami PF00307. CH. 2 hits.
    [Graphical view ]
    SMARTi SM00033. CH. 2 hits.
    [Graphical view ]
    SUPFAMi SSF47576. SSF47576. 2 hits.
    PROSITEi PS50021. CH. 2 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "CLINT, Calponin homology domain protein binding to integrin-linked kinase, ILK1."
      Carnio L., Hannigan G.E.
      Submitted (SEP-2000) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), VARIANT ALA-58.
      Tissue: Skeletal muscle.
    2. "A novel integrin-linked kinase-binding protein, affixin, is involved in the early stage of cell-substrate interaction."
      Yamaji S., Suzuki A., Sugiyama Y., Koide Y., Yoshida M., Kanamori H., Mohri H., Ohno S., Ishigatsubo Y.
      J. Cell Biol. 153:1251-1264(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, INTERACTION WITH ILK, SUBCELLULAR LOCATION, PHOSPHORYLATION, TISSUE SPECIFICITY.
    3. "Parvin, a 42 kDa focal adhesion protein, related to the alpha-actinin superfamily."
      Olski T.M., Noegel A.A., Korenbaum E.
      J. Cell Sci. 114:525-538(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    4. "Identification of novel human genes evolutionarily conserved in Caenorhabditis elegans by comparative proteomics."
      Lai C.-H., Chou C.-Y., Ch'ang L.-Y., Liu C.-S., Lin W.-C.
      Genome Res. 10:703-713(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    5. "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 1), VARIANT ALA-58.
      Tissue: Colon.
    6. "The DNA sequence of human chromosome 22."
      Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M., Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C., Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E., Bridgeman A.M.
      , Buck D., Burgess J., Burrill W.D., Burton J., Carder C., Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G., Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V., Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M., Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A., Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C., Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E., Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F., Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M., Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A., Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D., Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y., Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S., Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E., Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L., Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L., Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N., Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A., Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L., Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P., Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P., Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q., Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J., Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J., Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D., Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T., Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P., Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K., Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R., Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L., McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J., Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E., Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P., Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y., Wright H.
      Nature 402:489-495(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    7. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    8. "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] (ISOFORMS 1 AND 3), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-238 (ISOFORM 2), VARIANT ALA-58.
      Tissue: Brain, Leukocyte and Skin.
    9. "Reevaluating human gene annotation: a second-generation analysis of chromosome 22."
      Collins J.E., Goward M.E., Cole C.G., Smink L.J., Huckle E.J., Knowles S., Bye J.M., Beare D.M., Dunham I.
      Genome Res. 13:27-36(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 15-364 (ISOFORM 1).
    10. "Genomic organization and expression profile of the parvin family of focal adhesion proteins in mice and humans."
      Korenbaum E., Olski T.M., Noegel A.A.
      Gene 279:69-79(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: TISSUE SPECIFICITY.
    11. "The first CH domain of affixin activates Cdc42 and Rac1 through alphaPIX, a Cdc42/Rac1-specific guanine nucleotide exchanging factor."
      Mishima W., Suzuki A., Yamaji S., Yoshimi R., Ueda A., Kaneko T., Tanaka J., Miwa Y., Ohno S., Ishigatsubo Y.
      Genes Cells 9:193-204(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH ARHGEF6.
    12. "Distinct roles of two structurally closely related focal adhesion proteins, alpha-parvins and beta-parvins, in regulation of cell morphology and survival."
      Zhang Y., Chen K., Tu Y., Wu C.
      J. Biol. Chem. 279:41695-41705(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH ILK.
    13. "Affixin interacts with alpha-actinin and mediates integrin signaling for reorganization of F-actin induced by initial cell-substrate interaction."
      Yamaji S., Suzuki A., Kanamori H., Mishima W., Yoshimi R., Takasaki H., Takabayashi M., Fujimaki K., Fujisawa S., Ohno S., Ishigatsubo Y.
      J. Cell Biol. 165:539-551(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH ACTN2, SUBCELLULAR LOCATION, FUNCTION.
    14. "Dysferlin interacts with affixin (beta-parvin) at the sarcolemma."
      Matsuda C., Kameyama K., Tagawa K., Ogawa M., Suzuki A., Yamaji S., Okamoto H., Nishino I., Hayashi Y.K.
      J. Neuropathol. Exp. Neurol. 64:334-340(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH DYSF.
    15. Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH ARHGEF6 AND ARHGEF7.
    16. "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-54, VARIANT [LARGE SCALE ANALYSIS] ALA-58, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    17. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    18. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    19. "Structural basis for paxillin binding and focal adhesion targeting of beta-parvin."
      Stiegler A.L., Draheim K.M., Li X., Chayen N.E., Calderwood D.A., Boggon T.J.
      J. Biol. Chem. 287:32566-32577(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 235-364 IN COMPLEX WITH PXN, SUBCELLULAR LOCATION, MUTAGENESIS OF VAL-256 AND PHE-299, INTERACTION WITH ILK AND PXN.

    Entry informationi

    Entry nameiPARVB_HUMAN
    AccessioniPrimary (citable) accession number: Q9HBI1
    Secondary accession number(s): B0QYM8
    , B0QYN1, B2R9X6, Q5TGJ5, Q86X93, Q96PN1, Q9NSP7, Q9UGT3, Q9Y368, Q9Y3L6, Q9Y3L7
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 23, 2002
    Last sequence update: March 1, 2001
    Last modified: October 1, 2014
    This is version 126 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 22
      Human chromosome 22: 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