PARVB_HUMAN
ID PARVB_HUMAN Reviewed; 364 AA.
AC Q9HBI1; B0QYM8; B0QYN1; B2R9X6; Q5TGJ5; Q86X93; Q96PN1; Q9NSP7; Q9UGT3;
AC Q9Y368; Q9Y3L6; Q9Y3L7;
DT 23-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 183.
DE RecName: Full=Beta-parvin;
DE AltName: Full=Affixin;
GN Name=PARVB; ORFNames=CGI-56;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND VARIANT ALA-58.
RC TISSUE=Skeletal muscle;
RA Carnio L., Hannigan G.E.;
RT "CLINT, Calponin homology domain protein binding to integrin-linked kinase,
RT ILK1.";
RL Submitted (SEP-2000) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, INTERACTION WITH ILK,
RP SUBCELLULAR LOCATION, PHOSPHORYLATION, AND TISSUE SPECIFICITY.
RX PubMed=11402068; DOI=10.1083/jcb.153.6.1251;
RA Yamaji S., Suzuki A., Sugiyama Y., Koide Y., Yoshida M., Kanamori H.,
RA Mohri H., Ohno S., Ishigatsubo Y.;
RT "A novel integrin-linked kinase-binding protein, affixin, is involved in
RT the early stage of cell-substrate interaction.";
RL J. Cell Biol. 153:1251-1264(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=11171322; DOI=10.1242/jcs.114.3.525;
RA Olski T.M., Noegel A.A., Korenbaum E.;
RT "Parvin, a 42 kDa focal adhesion protein, related to the alpha-actinin
RT superfamily.";
RL J. Cell Sci. 114:525-538(2001).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RX PubMed=10810093; DOI=10.1101/gr.10.5.703;
RA Lai C.-H., Chou C.-Y., Ch'ang L.-Y., Liu C.-S., Lin W.-C.;
RT "Identification of novel human genes evolutionarily conserved in
RT Caenorhabditis elegans by comparative proteomics.";
RL Genome Res. 10:703-713(2000).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT ALA-58.
RC TISSUE=Colon;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=10591208; DOI=10.1038/990031;
RA Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M.,
RA Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C.,
RA Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E.,
RA Bridgeman A.M., Buck D., Burgess J., Burrill W.D., Burton J., Carder C.,
RA Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G.,
RA Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V.,
RA Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M.,
RA Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A.,
RA Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C.,
RA Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E.,
RA Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F.,
RA Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M.,
RA Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A.,
RA Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D.,
RA Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y.,
RA Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S.,
RA Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E.,
RA Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L.,
RA Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L.,
RA Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N.,
RA Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A.,
RA Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L.,
RA Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P.,
RA Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P.,
RA Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q.,
RA Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J.,
RA Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J.,
RA Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D.,
RA Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T.,
RA Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P.,
RA Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K.,
RA Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R.,
RA Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L.,
RA McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J.,
RA Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E.,
RA Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P.,
RA Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y.,
RA Wright H.;
RT "The DNA sequence of human chromosome 22.";
RL Nature 402:489-495(1999).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3), NUCLEOTIDE
RP SEQUENCE [LARGE SCALE MRNA] OF 1-238 (ISOFORM 2), AND VARIANT ALA-58.
RC TISSUE=Brain, Leukocyte, and Skin;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 15-364 (ISOFORM 1).
RX PubMed=12529303; DOI=10.1101/gr.695703;
RA Collins J.E., Goward M.E., Cole C.G., Smink L.J., Huckle E.J., Knowles S.,
RA Bye J.M., Beare D.M., Dunham I.;
RT "Reevaluating human gene annotation: a second-generation analysis of
RT chromosome 22.";
RL Genome Res. 13:27-36(2003).
RN [10]
RP TISSUE SPECIFICITY.
RX PubMed=11722847; DOI=10.1016/s0378-1119(01)00743-0;
RA Korenbaum E., Olski T.M., Noegel A.A.;
RT "Genomic organization and expression profile of the parvin family of focal
RT adhesion proteins in mice and humans.";
RL Gene 279:69-79(2001).
RN [11]
RP FUNCTION, AND INTERACTION WITH ARHGEF6.
RX PubMed=15005707; DOI=10.1111/j.1356-9597.2004.00717.x;
RA Mishima W., Suzuki A., Yamaji S., Yoshimi R., Ueda A., Kaneko T.,
RA Tanaka J., Miwa Y., Ohno S., Ishigatsubo Y.;
RT "The first CH domain of affixin activates Cdc42 and Rac1 through alphaPIX,
RT a Cdc42/Rac1-specific guanine nucleotide exchanging factor.";
RL Genes Cells 9:193-204(2004).
RN [12]
RP FUNCTION, AND INTERACTION WITH ILK.
RX PubMed=15284246; DOI=10.1074/jbc.m401563200;
RA Zhang Y., Chen K., Tu Y., Wu C.;
RT "Distinct roles of two structurally closely related focal adhesion
RT proteins, alpha-parvins and beta-parvins, in regulation of cell morphology
RT and survival.";
RL J. Biol. Chem. 279:41695-41705(2004).
RN [13]
RP INTERACTION WITH ACTN2, SUBCELLULAR LOCATION, AND FUNCTION.
RX PubMed=15159419; DOI=10.1083/jcb.200308141;
RA Yamaji S., Suzuki A., Kanamori H., Mishima W., Yoshimi R., Takasaki H.,
RA Takabayashi M., Fujimaki K., Fujisawa S., Ohno S., Ishigatsubo Y.;
RT "Affixin interacts with alpha-actinin and mediates integrin signaling for
RT reorganization of F-actin induced by initial cell-substrate interaction.";
RL J. Cell Biol. 165:539-551(2004).
RN [14]
RP INTERACTION WITH DYSF.
RX PubMed=15835269; DOI=10.1093/jnen/64.4.334;
RA Matsuda C., Kameyama K., Tagawa K., Ogawa M., Suzuki A., Yamaji S.,
RA Okamoto H., Nishino I., Hayashi Y.K.;
RT "Dysferlin interacts with affixin (beta-parvin) at the sarcolemma.";
RL J. Neuropathol. Exp. Neurol. 64:334-340(2005).
RN [15]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH ARHGEF6 AND ARHGEF7.
RX PubMed=18325335; DOI=10.1016/j.febslet.2008.01.064;
RA Matsuda C., Kameyama K., Suzuki A., Mishima W., Yamaji S., Okamoto H.,
RA Nishino I., Hayashi Y.K.;
RT "Affixin activates Rac1 via betaPIX in C2C12 myoblast.";
RL FEBS Lett. 582:1189-1196(2008).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-54, VARIANT [LARGE SCALE
RP ANALYSIS] ALA-58, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the
RT kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [17]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [18]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [19]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-7, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [20]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 235-364 IN COMPLEX WITH PXN,
RP SUBCELLULAR LOCATION, MUTAGENESIS OF VAL-256 AND PHE-299, AND INTERACTION
RP WITH ILK AND PXN.
RX PubMed=22869380; DOI=10.1074/jbc.m112.367342;
RA Stiegler A.L., Draheim K.M., Li X., Chayen N.E., Calderwood D.A.,
RA Boggon T.J.;
RT "Structural basis for paxillin binding and focal adhesion targeting of
RT beta-parvin.";
RL J. Biol. Chem. 287:32566-32577(2012).
CC -!- FUNCTION: Adapter protein that plays a role in integrin signaling via
CC ILK and in activation of the GTPases CDC42 and RAC1 by guanine exchange
CC factors, such as ARHGEF6. Is involved in the reorganization of the
CC actin cytoskeleton and formation of lamellipodia. Plays a role in cell
CC adhesion, cell spreading, establishment or maintenance of cell
CC polarity, and cell migration. {ECO:0000269|PubMed:11402068,
CC ECO:0000269|PubMed:15005707, ECO:0000269|PubMed:15159419,
CC ECO:0000269|PubMed:15284246, ECO:0000269|PubMed:18325335}.
CC -!- SUBUNIT: Interacts with DYSF. Interacts with ILK, ARHGEF6, PXN (via LD
CC motifs), ACTN2 and actin. {ECO:0000269|PubMed:11402068,
CC ECO:0000269|PubMed:15005707, ECO:0000269|PubMed:15159419,
CC ECO:0000269|PubMed:15284246, ECO:0000269|PubMed:15835269,
CC ECO:0000269|PubMed:18325335, ECO:0000269|PubMed:22869380}.
CC -!- INTERACTION:
CC Q9HBI1; Q8K4I3: Arhgef6; Xeno; NbExp=3; IntAct=EBI-1047679, EBI-6272809;
CC Q9HBI1; Q9ES28: Arhgef7; Xeno; NbExp=10; IntAct=EBI-1047679, EBI-642580;
CC -!- SUBCELLULAR LOCATION: Cell junction, focal adhesion. Cell membrane;
CC Peripheral membrane protein; Cytoplasmic side. Cytoplasm, cytoskeleton.
CC Cell projection, lamellipodium. Cytoplasm, myofibril, sarcomere.
CC Cytoplasm, myofibril, sarcomere, Z line. Note=Constituent of focal
CC adhesions. Detected at the tips of the leading edge of cells.
CC Colocalizes with F-actin at the tips of lamellipodia.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q9HBI1-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9HBI1-2; Sequence=VSP_041336;
CC Name=3;
CC IsoId=Q9HBI1-3; Sequence=VSP_045555;
CC -!- TISSUE SPECIFICITY: Expressed predominantly in heart and skeletal
CC muscle. {ECO:0000269|PubMed:11402068, ECO:0000269|PubMed:11722847}.
CC -!- SIMILARITY: Belongs to the parvin family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAD34051.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=BG743702; Type=Frameshift; Evidence={ECO:0000305};
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/PARVBID46486ch22q13.html";
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AF303887; AAL08219.1; -; mRNA.
DR EMBL; AB048276; BAB62077.1; -; mRNA.
DR EMBL; AF237769; AAG27171.1; -; mRNA.
DR EMBL; AF151814; AAD34051.1; ALT_FRAME; mRNA.
DR EMBL; AK313957; BAG36673.1; -; mRNA.
DR EMBL; AL031595; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL033543; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; Z82178; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; Z82174; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL035398; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471138; EAW73328.1; -; Genomic_DNA.
DR EMBL; BC039811; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; BC046103; AAH46103.2; -; mRNA.
DR EMBL; BG743702; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AL159142; CAB76900.1; -; mRNA.
DR CCDS; CCDS14056.1; -. [Q9HBI1-1]
DR CCDS; CCDS46724.1; -. [Q9HBI1-2]
DR CCDS; CCDS58808.1; -. [Q9HBI1-3]
DR RefSeq; NP_001003828.1; NM_001003828.2. [Q9HBI1-2]
DR RefSeq; NP_001230314.1; NM_001243385.1. [Q9HBI1-3]
DR RefSeq; NP_001230315.1; NM_001243386.1.
DR RefSeq; NP_037459.2; NM_013327.4. [Q9HBI1-1]
DR PDB; 4EDL; X-ray; 2.10 A; A/B/C/D/E/F=235-364.
DR PDB; 4EDM; X-ray; 2.00 A; A/B=235-364.
DR PDB; 4EDN; X-ray; 2.90 A; A/B/C/D/E/F/G/H/I/J=235-364.
DR PDBsum; 4EDL; -.
DR PDBsum; 4EDM; -.
DR PDBsum; 4EDN; -.
DR AlphaFoldDB; Q9HBI1; -.
DR SMR; Q9HBI1; -.
DR BioGRID; 118912; 23.
DR CORUM; Q9HBI1; -.
DR IntAct; Q9HBI1; 13.
DR MINT; Q9HBI1; -.
DR STRING; 9606.ENSP00000384515; -.
DR iPTMnet; Q9HBI1; -.
DR PhosphoSitePlus; Q9HBI1; -.
DR BioMuta; PARVB; -.
DR DMDM; 20139178; -.
DR EPD; Q9HBI1; -.
DR jPOST; Q9HBI1; -.
DR MassIVE; Q9HBI1; -.
DR MaxQB; Q9HBI1; -.
DR PaxDb; Q9HBI1; -.
DR PeptideAtlas; Q9HBI1; -.
DR PRIDE; Q9HBI1; -.
DR ProteomicsDB; 2670; -.
DR ProteomicsDB; 81559; -. [Q9HBI1-1]
DR ProteomicsDB; 81560; -. [Q9HBI1-2]
DR Antibodypedia; 27615; 228 antibodies from 27 providers.
DR DNASU; 29780; -.
DR Ensembl; ENST00000338758.12; ENSP00000342492.6; ENSG00000188677.15. [Q9HBI1-1]
DR Ensembl; ENST00000404989.1; ENSP00000384353.1; ENSG00000188677.15. [Q9HBI1-3]
DR Ensembl; ENST00000406477.7; ENSP00000384515.3; ENSG00000188677.15. [Q9HBI1-2]
DR GeneID; 29780; -.
DR KEGG; hsa:29780; -.
DR MANE-Select; ENST00000338758.12; ENSP00000342492.6; NM_013327.5; NP_037459.2.
DR UCSC; uc003bem.4; human. [Q9HBI1-1]
DR CTD; 29780; -.
DR DisGeNET; 29780; -.
DR GeneCards; PARVB; -.
DR HGNC; HGNC:14653; PARVB.
DR HPA; ENSG00000188677; Tissue enhanced (skeletal muscle, tongue).
DR MIM; 608121; gene.
DR neXtProt; NX_Q9HBI1; -.
DR OpenTargets; ENSG00000188677; -.
DR PharmGKB; PA32951; -.
DR VEuPathDB; HostDB:ENSG00000188677; -.
DR eggNOG; KOG3631; Eukaryota.
DR GeneTree; ENSGT00950000183194; -.
DR HOGENOM; CLU_047624_2_0_1; -.
DR InParanoid; Q9HBI1; -.
DR OMA; GWPLRWN; -.
DR OrthoDB; 871306at2759; -.
DR PhylomeDB; Q9HBI1; -.
DR TreeFam; TF314025; -.
DR PathwayCommons; Q9HBI1; -.
DR Reactome; R-HSA-446353; Cell-extracellular matrix interactions.
DR Reactome; R-HSA-446388; Regulation of cytoskeletal remodeling and cell spreading by IPP complex components.
DR SignaLink; Q9HBI1; -.
DR BioGRID-ORCS; 29780; 21 hits in 1077 CRISPR screens.
DR ChiTaRS; PARVB; human.
DR GeneWiki; PARVB; -.
DR GenomeRNAi; 29780; -.
DR Pharos; Q9HBI1; Tbio.
DR PRO; PR:Q9HBI1; -.
DR Proteomes; UP000005640; Chromosome 22.
DR RNAct; Q9HBI1; protein.
DR Bgee; ENSG00000188677; Expressed in hindlimb stylopod muscle and 158 other tissues.
DR ExpressionAtlas; Q9HBI1; baseline and differential.
DR Genevisible; Q9HBI1; HS.
DR GO; GO:0015629; C:actin cytoskeleton; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005925; C:focal adhesion; IDA:UniProtKB.
DR GO; GO:0030027; C:lamellipodium; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0030018; C:Z disc; IEA:UniProtKB-SubCell.
DR GO; GO:0003779; F:actin binding; IBA:GO_Central.
DR GO; GO:0031532; P:actin cytoskeleton reorganization; IMP:UniProtKB.
DR GO; GO:0030031; P:cell projection assembly; IMP:UniProtKB.
DR GO; GO:0007163; P:establishment or maintenance of cell polarity; IBA:GO_Central.
DR GO; GO:0071963; P:establishment or maintenance of cell polarity regulating cell shape; IMP:UniProtKB.
DR GO; GO:0030032; P:lamellipodium assembly; IMP:UniProtKB.
DR GO; GO:0034446; P:substrate adhesion-dependent cell spreading; IBA:GO_Central.
DR Gene3D; 1.10.418.10; -; 2.
DR InterPro; IPR001715; CH-domain.
DR InterPro; IPR036872; CH_dom_sf.
DR InterPro; IPR028433; Parvin.
DR PANTHER; PTHR12114; PTHR12114; 1.
DR Pfam; PF00307; CH; 2.
DR PIRSF; PIRSF039131; Parvin; 1.
DR SMART; SM00033; CH; 2.
DR SUPFAM; SSF47576; SSF47576; 1.
DR PROSITE; PS50021; CH; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Actin-binding; Alternative splicing; Cell adhesion;
KW Cell junction; Cell membrane; Cell projection; Cytoplasm; Cytoskeleton;
KW Membrane; Phosphoprotein; Reference proteome; Repeat.
FT CHAIN 1..364
FT /note="Beta-parvin"
FT /id="PRO_0000121583"
FT DOMAIN 87..194
FT /note="Calponin-homology (CH) 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00044"
FT DOMAIN 254..361
FT /note="Calponin-homology (CH) 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00044"
FT REGION 1..57
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 7
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 54
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18691976"
FT VAR_SEQ 1..38
FT /note="MSSAPRSPTPRPRRMKKDESFLGKLGGTLARKRRAREV -> M (in
FT isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_045555"
FT VAR_SEQ 1..37
FT /note="MSSAPRSPTPRPRRMKKDESFLGKLGGTLARKRRARE -> MHHVFKDHQRG
FT EKRGFLSPENKNCRRLELRRGCSCSWGLCSQALMASLAGSLLPGSDRSGVETSEYAQGG
FT (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334, ECO:0000303|Ref.1"
FT /id="VSP_041336"
FT VARIANT 52
FT /note="P -> R (in dbSNP:rs34476853)"
FT /id="VAR_034369"
FT VARIANT 58
FT /note="V -> A (in dbSNP:rs1983609)"
FT /evidence="ECO:0000269|PubMed:14702039,
FT ECO:0000269|PubMed:15489334, ECO:0000269|Ref.1,
FT ECO:0007744|PubMed:18691976"
FT /id="VAR_017242"
FT MUTAGEN 256
FT /note="V->Q: Abolishes interaction with PXN."
FT /evidence="ECO:0000269|PubMed:22869380"
FT MUTAGEN 299
FT /note="F->D: Abolishes interaction with ILK. Abolishes
FT location at focal adhesion sites."
FT /evidence="ECO:0000269|PubMed:22869380"
FT CONFLICT 27
FT /note="G -> V (in Ref. 4; AAD34051)"
FT /evidence="ECO:0000305"
FT CONFLICT 59
FT /note="D -> M (in Ref. 4; AAD34051)"
FT /evidence="ECO:0000305"
FT CONFLICT 349
FT /note="T -> P (in Ref. 4; AAD34051)"
FT /evidence="ECO:0000305"
FT HELIX 243..246
FT /evidence="ECO:0007829|PDB:4EDM"
FT HELIX 250..252
FT /evidence="ECO:0007829|PDB:4EDN"
FT HELIX 254..268
FT /evidence="ECO:0007829|PDB:4EDM"
FT HELIX 269..271
FT /evidence="ECO:0007829|PDB:4EDM"
FT TURN 278..284
FT /evidence="ECO:0007829|PDB:4EDM"
FT HELIX 286..295
FT /evidence="ECO:0007829|PDB:4EDM"
FT HELIX 302..304
FT /evidence="ECO:0007829|PDB:4EDM"
FT HELIX 312..328
FT /evidence="ECO:0007829|PDB:4EDM"
FT HELIX 338..342
FT /evidence="ECO:0007829|PDB:4EDM"
FT HELIX 346..360
FT /evidence="ECO:0007829|PDB:4EDM"
FT CONFLICT Q9HBI1-2:4
FT /note="V -> G (in Ref. 8; BG743702)"
FT /evidence="ECO:0000305"
FT CONFLICT Q9HBI1-2:21
FT /note="N -> K (in Ref. 1; AAL08219)"
FT /evidence="ECO:0000305"
FT CONFLICT Q9HBI1-2:37
FT /note="W -> R (in Ref. 1; AAL08219)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 364 AA; 41714 MW; 4BA4B50C83083DC7 CRC64;
MSSAPRSPTP RPRRMKKDES FLGKLGGTLA RKRRAREVSD LQEEGKNAIN SPMSPALVDV
HPEDTQLEEN EERTMIDPTS KEDPKFKELV KVLLDWINDV LVEERIIVKQ LEEDLYDGQV
LQKLLEKLAG CKLNVAEVTQ SEIGQKQKLQ TVLEAVHDLL RPRGWALRWS VDSIHGKNLV
AILHLLVSLA MHFRAPIRLP EHVTVQVVVV RKREGLLHSS HISEELTTTT EMMMGRFERD
AFDTLFDHAP DKLSVVKKSL ITFVNKHLNK LNLEVTELET QFADGVYLVL LMGLLEDYFV
PLHHFYLTPE SFDQKVHNVS FAFELMLDGG LKKPKARPED VVNLDLKSTL RVLYNLFTKY
KNVE
