MYO1B_HUMAN
ID MYO1B_HUMAN Reviewed; 1136 AA.
AC O43795; O43794; Q7Z6L5;
DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-2005, sequence version 3.
DT 03-AUG-2022, entry version 194.
DE RecName: Full=Unconventional myosin-Ib;
DE AltName: Full=MYH-1c;
DE AltName: Full=Myosin I alpha;
DE Short=MMI-alpha;
DE Short=MMIa;
GN Name=MYO1B;
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 [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=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 [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 644-1136 (ISOFORM 2), AND VARIANT LYS-969.
RA Zorn E., Hercend T.;
RT "A mutated non conventional class I myosin peptide elicits a dominant CTL
RT response in a regressive human primary melanoma lesion.";
RL Submitted (DEC-1997) to the EMBL/GenBank/DDBJ databases.
RN [3]
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 [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-60, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [5]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-287, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25218447; DOI=10.1038/nsmb.2890;
RA Hendriks I.A., D'Souza R.C., Yang B., Verlaan-de Vries M., Mann M.,
RA Vertegaal A.C.;
RT "Uncovering global SUMOylation signaling networks in a site-specific
RT manner.";
RL Nat. Struct. Mol. Biol. 21:927-936(2014).
RN [6]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-287, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25114211; DOI=10.1073/pnas.1413825111;
RA Impens F., Radoshevich L., Cossart P., Ribet D.;
RT "Mapping of SUMO sites and analysis of SUMOylation changes induced by
RT external stimuli.";
RL Proc. Natl. Acad. Sci. U.S.A. 111:12432-12437(2014).
RN [7]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-287, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25755297; DOI=10.1074/mcp.o114.044792;
RA Xiao Z., Chang J.G., Hendriks I.A., Sigurdsson J.O., Olsen J.V.,
RA Vertegaal A.C.;
RT "System-wide analysis of SUMOylation dynamics in response to replication
RT stress reveals novel small ubiquitin-like modified target proteins and
RT acceptor lysines relevant for genome stability.";
RL Mol. Cell. Proteomics 14:1419-1434(2015).
RN [8]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-287, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=28112733; DOI=10.1038/nsmb.3366;
RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
RA Nielsen M.L.;
RT "Site-specific mapping of the human SUMO proteome reveals co-modification
RT with phosphorylation.";
RL Nat. Struct. Mol. Biol. 24:325-336(2017).
RN [9]
RP VARIANTS [LARGE SCALE ANALYSIS] GLY-385 AND ILE-385.
RX PubMed=16959974; DOI=10.1126/science.1133427;
RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P.,
RA Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V.,
RA Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H.,
RA Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W.,
RA Velculescu V.E.;
RT "The consensus coding sequences of human breast and colorectal cancers.";
RL Science 314:268-274(2006).
CC -!- FUNCTION: Motor protein that may participate in process critical to
CC neuronal development and function such as cell migration, neurite
CC outgrowth and vesicular transport. {ECO:0000250}.
CC -!- INTERACTION:
CC O43795; Q7Z3K3: POGZ; NbExp=3; IntAct=EBI-351119, EBI-1389308;
CC O43795; P51687: SUOX; NbExp=3; IntAct=EBI-351119, EBI-3921347;
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=O43795-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O43795-2; Sequence=VSP_012759;
CC -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC superfamily. Myosin family. {ECO:0000305}.
CC -!- CAUTION: Represents an unconventional myosin. This protein should not
CC be confused with the conventional myosin-1 (MYH1). {ECO:0000305}.
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DR EMBL; BC053558; AAH53558.1; -; mRNA.
DR EMBL; AJ001381; CAA04712.1; -; mRNA.
DR EMBL; AJ001382; CAA04713.1; -; mRNA.
DR CCDS; CCDS2311.1; -. [O43795-2]
DR CCDS; CCDS46477.1; -. [O43795-1]
DR RefSeq; NP_001123630.1; NM_001130158.2. [O43795-1]
DR RefSeq; NP_001155291.1; NM_001161819.2. [O43795-1]
DR RefSeq; NP_036355.2; NM_012223.4. [O43795-2]
DR RefSeq; XP_005246629.1; XM_005246572.1. [O43795-1]
DR AlphaFoldDB; O43795; -.
DR SMR; O43795; -.
DR BioGRID; 110567; 224.
DR IntAct; O43795; 101.
DR MINT; O43795; -.
DR STRING; 9606.ENSP00000376132; -.
DR GlyGen; O43795; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; O43795; -.
DR MetOSite; O43795; -.
DR PhosphoSitePlus; O43795; -.
DR SwissPalm; O43795; -.
DR BioMuta; MYO1B; -.
DR EPD; O43795; -.
DR jPOST; O43795; -.
DR MassIVE; O43795; -.
DR MaxQB; O43795; -.
DR PaxDb; O43795; -.
DR PeptideAtlas; O43795; -.
DR PRIDE; O43795; -.
DR ProteomicsDB; 49172; -. [O43795-1]
DR ProteomicsDB; 49173; -. [O43795-2]
DR Antibodypedia; 2858; 127 antibodies from 32 providers.
DR DNASU; 4430; -.
DR Ensembl; ENST00000304164.8; ENSP00000306382.4; ENSG00000128641.19. [O43795-1]
DR Ensembl; ENST00000339514.8; ENSP00000341903.4; ENSG00000128641.19. [O43795-2]
DR Ensembl; ENST00000392318.8; ENSP00000376132.3; ENSG00000128641.19. [O43795-1]
DR GeneID; 4430; -.
DR KEGG; hsa:4430; -.
DR MANE-Select; ENST00000392318.8; ENSP00000376132.3; NM_001130158.3; NP_001123630.1.
DR UCSC; uc002usq.3; human. [O43795-1]
DR CTD; 4430; -.
DR DisGeNET; 4430; -.
DR GeneCards; MYO1B; -.
DR HGNC; HGNC:7596; MYO1B.
DR HPA; ENSG00000128641; Tissue enhanced (liver).
DR MalaCards; MYO1B; -.
DR MIM; 606537; gene.
DR neXtProt; NX_O43795; -.
DR OpenTargets; ENSG00000128641; -.
DR PharmGKB; PA31398; -.
DR VEuPathDB; HostDB:ENSG00000128641; -.
DR eggNOG; KOG0164; Eukaryota.
DR GeneTree; ENSGT00940000155752; -.
DR HOGENOM; CLU_000192_7_7_1; -.
DR InParanoid; O43795; -.
DR OMA; PLYGNEY; -.
DR PhylomeDB; O43795; -.
DR TreeFam; TF312960; -.
DR PathwayCommons; O43795; -.
DR SignaLink; O43795; -.
DR BioGRID-ORCS; 4430; 12 hits in 1072 CRISPR screens.
DR ChiTaRS; MYO1B; human.
DR GeneWiki; MYO1B; -.
DR GenomeRNAi; 4430; -.
DR Pharos; O43795; Tbio.
DR PRO; PR:O43795; -.
DR Proteomes; UP000005640; Chromosome 2.
DR RNAct; O43795; protein.
DR Bgee; ENSG00000128641; Expressed in endometrium epithelium and 205 other tissues.
DR ExpressionAtlas; O43795; baseline and differential.
DR Genevisible; O43795; HS.
DR GO; GO:0015629; C:actin cytoskeleton; IBA:GO_Central.
DR GO; GO:0005884; C:actin filament; IDA:UniProtKB.
DR GO; GO:0045177; C:apical part of cell; IEA:Ensembl.
DR GO; GO:0005903; C:brush border; ISS:UniProtKB.
DR GO; GO:0071944; C:cell periphery; ISS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005769; C:early endosome; IDA:UniProtKB.
DR GO; GO:0010008; C:endosome membrane; IDA:UniProtKB.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0030175; C:filopodium; ISS:UniProtKB.
DR GO; GO:0005902; C:microvillus; IBA:GO_Central.
DR GO; GO:0016459; C:myosin complex; IEA:UniProtKB-KW.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IDA:HPA.
DR GO; GO:0051015; F:actin filament binding; IMP:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IMP:UniProtKB.
DR GO; GO:0045296; F:cadherin binding; HDA:BHF-UCL.
DR GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
DR GO; GO:0000146; F:microfilament motor activity; IMP:UniProtKB.
DR GO; GO:0005547; F:phosphatidylinositol-3,4,5-trisphosphate binding; ISS:UniProtKB.
DR GO; GO:0005546; F:phosphatidylinositol-4,5-bisphosphate binding; ISS:UniProtKB.
DR GO; GO:0051017; P:actin filament bundle assembly; ISS:UniProtKB.
DR GO; GO:0007015; P:actin filament organization; IMP:UniProtKB.
DR GO; GO:0030048; P:actin filament-based movement; ISS:UniProtKB.
DR GO; GO:0006892; P:post-Golgi vesicle-mediated transport; IMP:UniProtKB.
DR GO; GO:0030050; P:vesicle transport along actin filament; IBA:GO_Central.
DR CDD; cd01378; MYSc_Myo1; 1.
DR Gene3D; 3.40.850.10; -; 1.
DR InterPro; IPR000048; IQ_motif_EF-hand-BS.
DR InterPro; IPR036961; Kinesin_motor_dom_sf.
DR InterPro; IPR001609; Myosin_head_motor_dom.
DR InterPro; IPR010926; Myosin_TH1.
DR InterPro; IPR036072; MYSc_Myo1.
DR InterPro; IPR027417; P-loop_NTPase.
DR Pfam; PF00612; IQ; 2.
DR Pfam; PF00063; Myosin_head; 1.
DR Pfam; PF06017; Myosin_TH1; 1.
DR PRINTS; PR00193; MYOSINHEAVY.
DR SMART; SM00015; IQ; 6.
DR SMART; SM00242; MYSc; 1.
DR SUPFAM; SSF52540; SSF52540; 2.
DR PROSITE; PS50096; IQ; 5.
DR PROSITE; PS51456; MYOSIN_MOTOR; 1.
DR PROSITE; PS51757; TH1; 1.
PE 1: Evidence at protein level;
KW Actin-binding; Alternative splicing; ATP-binding; Calmodulin-binding;
KW Isopeptide bond; Motor protein; Myosin; Nucleotide-binding; Phosphoprotein;
KW Reference proteome; Repeat; Ubl conjugation.
FT CHAIN 1..1136
FT /note="Unconventional myosin-Ib"
FT /id="PRO_0000123442"
FT DOMAIN 15..701
FT /note="Myosin motor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00782"
FT DOMAIN 704..733
FT /note="IQ 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT DOMAIN 728..748
FT /note="IQ 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT DOMAIN 750..779
FT /note="IQ 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT DOMAIN 779..808
FT /note="IQ 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT DOMAIN 808..837
FT /note="IQ 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT DOMAIN 837..866
FT /note="IQ 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT DOMAIN 952..1136
FT /note="TH1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01093"
FT REGION 578..600
FT /note="Actin-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00782"
FT BINDING 108..115
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00782"
FT MOD_RES 60
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT CROSSLNK 287
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1); alternate"
FT /evidence="ECO:0007744|PubMed:25114211"
FT CROSSLNK 287
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0007744|PubMed:25114211,
FT ECO:0007744|PubMed:25218447, ECO:0007744|PubMed:25755297,
FT ECO:0007744|PubMed:28112733"
FT VAR_SEQ 795..852
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|Ref.2"
FT /id="VSP_012759"
FT VARIANT 385
FT /note="V -> G (in a colorectal cancer sample; somatic
FT mutation)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_036007"
FT VARIANT 385
FT /note="V -> I (in a colorectal cancer sample; somatic
FT mutation)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_036008"
FT VARIANT 969
FT /note="E -> K (in a melanoma patient)"
FT /evidence="ECO:0000269|Ref.2"
FT /id="VAR_014113"
SQ SEQUENCE 1136 AA; 131985 MW; 98B7F2357928218D CRC64;
MAKMEVKTSL LDNMIGVGDM VLLEPLNEET FINNLKKRFD HSEIYTYIGS VVISVNPYRS
LPIYSPEKVE EYRNRNFYEL SPHIFALSDE AYRSLRDQDK DQCILITGES GAGKTEASKL
VMSYVAAVCG KGAEVNQVKE QLLQSNPVLE AFGNAKTVRN DNSSRFGKYM DIEFDFKGDP
LGGVISNYLL EKSRVVKQPR GERNFHVFYQ LLSGASEELL NKLKLERDFS RYNYLSLDSA
KVNGVDDAAN FRTVRNAMQI VGFMDHEAES VLAVVAAVLK LGNIEFKPES RVNGLDESKI
KDKNELKEIC ELTGIDQSVL ERAFSFRTVE AKQEKVSTTL NVAQAYYARD ALAKNLYSRL
FSWLVNRINE SIKAQTKVRK KVMGVLDIYG FEIFEDNSFE QFIINYCNEK LQQIFIELTL
KEEQEEYIRE DIEWTHIDYF NNAIICDLIE NNTNGILAML DEECLRPGTV TDETFLEKLN
QVCATHQHFE SRMSKCSRFL NDTSLPHSCF RIQHYAGKVL YQVEGFVDKN NDLLYRDLSQ
AMWKASHALI KSLFPEGNPA KINLKRPPTA GSQFKASVAT LMKNLQTKNP NYIRCIKPND
KKAAHIFNEA LVCHQIRYLG LLENVRVRRA GYAFRQAYEP CLERYKMLCK QTWPHWKGPA
RSGVEVLFNE LEIPVEEYSF GRSKIFIRNP RTLFKLEDLR KQRLEDLATL IQKIYRGWKC
RTHFLLMKKS QIVIAAWYRR YAQQKRYQQT KSSALVIQSY IRGWKARKIL RELKHQKRCK
EAVTTIAAYW HGTQARRELR RLKEEARNKH AIAVIWAYWL GSKARRELKR LKEEARRKHA
VAVIWAYWLG LKVRREYRKF FRANAGKKIY EFTLQRIVQK YFLEMKNKMP SLSPIDKNWP
SRPYLFLDST HKELKRIFHL WRCKKYRDQF TDQQKLIYEE KLEASELFKD KKALYPSSVG
QPFQGAYLEI NKNPKYKKLK DAIEEKIIIA EVVNKINRAN GKSTSRIFLL TNNNLLLADQ
KSGQIKSEVP LVDVTKVSMS SQNDGFFAVH LKEGSEAASK GDFLFSSDHL IEMATKLYRT
TLSQTKQKLN IEISDEFLVQ FRQDKVCVKF IQGNQKNGSV PTCKRKNNRL LEVAVP
