ITBP2_HUMAN
ID ITBP2_HUMAN Reviewed; 347 AA.
AC Q9UKP3; Q32N04; Q549J7;
DT 31-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 150.
DE RecName: Full=Integrin beta-1-binding protein 2;
DE AltName: Full=Melusin;
GN Name=ITGB1BP2; ORFNames=MSTP015;
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 1).
RC TISSUE=Skeletal muscle;
RX PubMed=10506186; DOI=10.1074/jbc.274.41.29282;
RA Brancaccio M., Guazzone S., Menini N., Sibona E., Hirsch E., De Andrea M.,
RA Rocchi M., Altruda F., Tarone G., Silengo L.;
RT "Melusin is a new muscle-specific interactor for beta(1) integrin
RT cytoplasmic domain.";
RL J. Biol. Chem. 274:29282-29288(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Heart;
RA Liu Y.Q., Liu B., Zhao B., Wang X.Y., Song L., Ye J., Sheng H., Gao Y.,
RA Zhang C.L., Zhang J., Wei Y.J., Sun Y.H., Jiang Y.X., Zhao X.W., Liu S.,
RA Liu L.S., Ding J.F., Gao R.L., Wu Q.Y., Qiang B.Q., Yuan J.G., Liew C.C.,
RA Zhao M.S., Hui R.T.;
RT "Homo sapiens normal heart MST015.";
RL Submitted (NOV-1998) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15772651; DOI=10.1038/nature03440;
RA Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D.,
RA Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L.,
RA Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.,
RA Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A.,
RA Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P.,
RA Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D.,
RA Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D.,
RA Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L.,
RA Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P.,
RA Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G.,
RA Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J.,
RA Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D.,
RA Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L.,
RA Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z.,
RA Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
RA Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S.,
RA Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O.,
RA Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H.,
RA Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T.,
RA Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L.,
RA Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R.,
RA Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y.,
RA Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K.,
RA Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J.,
RA Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L.,
RA Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S.,
RA Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A.,
RA Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L.,
RA Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D.,
RA Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H.,
RA McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S.,
RA Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C.,
RA Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S.,
RA Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V.,
RA Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K.,
RA Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K.,
RA Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D.,
RA Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R.,
RA Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B.,
RA Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C.,
RA d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q.,
RA Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N.,
RA Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A.,
RA Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J.,
RA Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A.,
RA Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F.,
RA Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L.,
RA Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S.,
RA Rogers J., Bentley D.R.;
RT "The DNA sequence of the human X chromosome.";
RL Nature 434:325-337(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
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).
CC -!- FUNCTION: May play a role during maturation and/or organization of
CC muscles cells.
CC -!- SUBUNIT: Interacts with beta-1 integrin subunit. This interaction is
CC regulated by divalent cations, and it occurs only in absence of
CC calcium.
CC -!- INTERACTION:
CC Q9UKP3; Q9BRP1: PDCD2L; NbExp=2; IntAct=EBI-5659717, EBI-2372173;
CC Q9UKP3; P10276: RARA; NbExp=2; IntAct=EBI-5659717, EBI-413374;
CC Q9UKP3-2; P21333-2: FLNA; NbExp=3; IntAct=EBI-25856470, EBI-9641086;
CC Q9UKP3-2; P04792: HSPB1; NbExp=3; IntAct=EBI-25856470, EBI-352682;
CC Q9UKP3-2; O60333-2: KIF1B; NbExp=3; IntAct=EBI-25856470, EBI-10975473;
CC Q9UKP3-2; Q8N2W9: PIAS4; NbExp=3; IntAct=EBI-25856470, EBI-473160;
CC Q9UKP3-2; O60260-5: PRKN; NbExp=3; IntAct=EBI-25856470, EBI-21251460;
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9UKP3-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9UKP3-2; Sequence=VSP_056379;
CC -!- TISSUE SPECIFICITY: Expressed in skeletal and cardiac muscles but not
CC in other tissues.
CC -!- DOMAIN: The tail domain binds to the cytoplasmic domain of both
CC integrin beta-1a and beta-1d isoforms. The presence of Ca(2+) ions does
CC not prevent binding of a fragment consisting of the second cysteine
CC rich repeat and the tail domain but prevents the binding of the full-
CC length protein.
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DR EMBL; AF140690; AAF01676.1; -; mRNA.
DR EMBL; AF110225; AAL36913.1; -; mRNA.
DR EMBL; AL590762; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC108901; AAI08902.1; -; mRNA.
DR CCDS; CCDS14411.1; -. [Q9UKP3-1]
DR RefSeq; NP_036410.1; NM_012278.2. [Q9UKP3-1]
DR AlphaFoldDB; Q9UKP3; -.
DR SMR; Q9UKP3; -.
DR BioGRID; 117742; 22.
DR IntAct; Q9UKP3; 27.
DR STRING; 9606.ENSP00000362935; -.
DR iPTMnet; Q9UKP3; -.
DR PhosphoSitePlus; Q9UKP3; -.
DR BioMuta; ITGB1BP2; -.
DR DMDM; 20138790; -.
DR MassIVE; Q9UKP3; -.
DR PaxDb; Q9UKP3; -.
DR PeptideAtlas; Q9UKP3; -.
DR PRIDE; Q9UKP3; -.
DR ProteomicsDB; 61614; -.
DR ProteomicsDB; 84827; -. [Q9UKP3-1]
DR Antibodypedia; 13542; 220 antibodies from 29 providers.
DR DNASU; 26548; -.
DR Ensembl; ENST00000373829.8; ENSP00000362935.3; ENSG00000147166.11. [Q9UKP3-1]
DR Ensembl; ENST00000538820.1; ENSP00000440289.1; ENSG00000147166.11. [Q9UKP3-2]
DR GeneID; 26548; -.
DR KEGG; hsa:26548; -.
DR MANE-Select; ENST00000373829.8; ENSP00000362935.3; NM_012278.4; NP_036410.1.
DR UCSC; uc004dzr.2; human. [Q9UKP3-1]
DR CTD; 26548; -.
DR DisGeNET; 26548; -.
DR GeneCards; ITGB1BP2; -.
DR HGNC; HGNC:6154; ITGB1BP2.
DR HPA; ENSG00000147166; Tissue enhanced (heart muscle, skeletal muscle, tongue).
DR MIM; 300332; gene.
DR neXtProt; NX_Q9UKP3; -.
DR OpenTargets; ENSG00000147166; -.
DR PharmGKB; PA29954; -.
DR VEuPathDB; HostDB:ENSG00000147166; -.
DR eggNOG; KOG1667; Eukaryota.
DR GeneTree; ENSGT00940000159429; -.
DR HOGENOM; CLU_040079_0_0_1; -.
DR InParanoid; Q9UKP3; -.
DR OMA; TVRNDFY; -.
DR OrthoDB; 1163528at2759; -.
DR PhylomeDB; Q9UKP3; -.
DR TreeFam; TF105394; -.
DR PathwayCommons; Q9UKP3; -.
DR SignaLink; Q9UKP3; -.
DR BioGRID-ORCS; 26548; 13 hits in 703 CRISPR screens.
DR ChiTaRS; ITGB1BP2; human.
DR GenomeRNAi; 26548; -.
DR Pharos; Q9UKP3; Tbio.
DR PRO; PR:Q9UKP3; -.
DR Proteomes; UP000005640; Chromosome X.
DR RNAct; Q9UKP3; protein.
DR Bgee; ENSG00000147166; Expressed in right atrium auricular region and 113 other tissues.
DR Genevisible; Q9UKP3; HS.
DR GO; GO:0030018; C:Z disc; IBA:GO_Central.
DR GO; GO:0005509; F:calcium ion binding; IEA:Ensembl.
DR GO; GO:0005178; F:integrin binding; IEA:Ensembl.
DR GO; GO:0017124; F:SH3 domain binding; IEA:UniProtKB-KW.
DR GO; GO:0008270; F:zinc ion binding; IBA:GO_Central.
DR GO; GO:0007517; P:muscle organ development; TAS:ProtInc.
DR GO; GO:0007165; P:signal transduction; TAS:ProtInc.
DR Gene3D; 2.60.40.790; -; 1.
DR InterPro; IPR007051; CHORD_dom.
DR InterPro; IPR039790; CHORD_protein.
DR InterPro; IPR007052; CS_dom.
DR InterPro; IPR008978; HSP20-like_chaperone.
DR PANTHER; PTHR12621; PTHR12621; 1.
DR Pfam; PF04968; CHORD; 2.
DR Pfam; PF04969; CS; 1.
DR SUPFAM; SSF49764; SSF49764; 1.
DR PROSITE; PS51401; CHORD; 2.
DR PROSITE; PS51203; CS; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Metal-binding; Reference proteome; Repeat;
KW SH3-binding; Zinc.
FT CHAIN 1..347
FT /note="Integrin beta-1-binding protein 2"
FT /id="PRO_0000084267"
FT DOMAIN 5..64
FT /note="CHORD 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00734"
FT DOMAIN 149..208
FT /note="CHORD 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00734"
FT DOMAIN 215..304
FT /note="CS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00547"
FT REGION 319..347
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 28..31
FT /note="SH3-binding"
FT /evidence="ECO:0000255"
FT MOTIF 70..78
FT /note="SH3-binding"
FT /evidence="ECO:0000255"
FT MOTIF 158..161
FT /note="SH2-binding"
FT /evidence="ECO:0000255"
FT MOTIF 172..175
FT /note="SH3-binding"
FT /evidence="ECO:0000255"
FT MOTIF 234..237
FT /note="SH2-binding"
FT /evidence="ECO:0000255"
FT COMPBIAS 321..347
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 5
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00734"
FT BINDING 10
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00734"
FT BINDING 24
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00734"
FT BINDING 27
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00734"
FT BINDING 42
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00734"
FT BINDING 43
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00734"
FT BINDING 59
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00734"
FT BINDING 64
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00734"
FT BINDING 149
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00734"
FT BINDING 154
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00734"
FT BINDING 168
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00734"
FT BINDING 171
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00734"
FT BINDING 186
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00734"
FT BINDING 187
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00734"
FT BINDING 203
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00734"
FT BINDING 208
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00734"
FT VAR_SEQ 3..21
FT /note="LLCRNKGCGQHFDPNTNLP -> T (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_056379"
SQ SEQUENCE 347 AA; 38382 MW; 1D0A94931821E74D CRC64;
MSLLCRNKGC GQHFDPNTNL PDSCCHHPGV PIFHDALKGW SCCRKRTVDF SEFLNIKGCT
MGPHCAEKLP EAPQPEGPAT SSSLQEQKPL NVIPKSAETL RRERPKSELP LKLLPLNISQ
ALEMALEQKE LDQEPGAGLD SLIRTGSSCQ NPGCDAVYQG PESDATPCTY HPGAPRFHEG
MKSWSCCGIQ TLDFGAFLAQ PGCRVGRHDW GKQLPASCRH DWHQTDSLVV VTVYGQIPLP
AFNWVKASQT ELHVHIVFDG NRVFQAQMKL WGVINVEQSS VFLMPSRVEI SLVKADPGSW
AQLEHPDALA KKARAGVVLE MDEEESDDSD DDLSWTEEEE EEEAMGE
