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 27-MAR-2024, entry version 192. 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="https://atlasgeneticsoncology.org/gene/46486/PARVB"; 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; 26. DR CORUM; Q9HBI1; -. DR IntAct; Q9HBI1; 14. DR MINT; Q9HBI1; -. DR STRING; 9606.ENSP00000384515; -. DR iPTMnet; Q9HBI1; -. DR PhosphoSitePlus; Q9HBI1; -. DR SwissPalm; Q9HBI1; -. DR BioMuta; PARVB; -. DR DMDM; 20139178; -. DR EPD; Q9HBI1; -. DR jPOST; Q9HBI1; -. DR MassIVE; Q9HBI1; -. DR MaxQB; Q9HBI1; -. DR PaxDb; 9606-ENSP00000384515; -. DR PeptideAtlas; Q9HBI1; -. DR ProteomicsDB; 2670; -. DR ProteomicsDB; 81559; -. [Q9HBI1-1] DR ProteomicsDB; 81560; -. [Q9HBI1-2] DR Pumba; Q9HBI1; -. DR Antibodypedia; 27615; 274 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 AGR; HGNC:14653; -. 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; HKFHLAP; -. DR OrthoDB; 1328998at2759; -. 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 1155 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 160 other cell types or tissues. DR ExpressionAtlas; Q9HBI1; baseline and differential. DR GO; GO:0015629; C:actin cytoskeleton; IDA:HPA. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0005829; C:cytosol; IDA:HPA. 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:0030036; P:actin cytoskeleton organization; 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 CDD; cd21336; CH_PARVB_rpt1; 1. DR CDD; cd21338; CH_PARVB_rpt2; 1. DR Gene3D; 1.10.418.10; Calponin-like domain; 2. DR InterPro; IPR001715; CH_dom. DR InterPro; IPR036872; CH_dom_sf. DR InterPro; IPR028433; Parvin. DR PANTHER; PTHR12114:SF7; BETA-PARVIN; 1. DR PANTHER; PTHR12114; PARVIN; 1. DR Pfam; PF00307; CH; 2. DR PIRSF; PIRSF039131; Parvin; 1. DR SMART; SM00033; CH; 2. DR SUPFAM; SSF47576; Calponin-homology domain, CH-domain; 1. DR PROSITE; PS50021; CH; 2. DR Genevisible; Q9HBI1; HS. 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 //