SHRM1_HUMAN
ID SHRM1_HUMAN Reviewed; 852 AA.
AC Q2M3G4; B7WP40; B7ZL01; Q8TDP0; Q8TF41;
DT 01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 21-FEB-2006, sequence version 1.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=Protein Shroom1;
DE AltName: Full=Apical protein 2;
GN Name=SHROOM1; Synonyms=APXL2, KIAA1960;
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).
RC TISSUE=Brain;
RA Karlen S., Staub O., Rohrbach B., Braathen L.R.;
RT "The cytoplasmic tail of the melanoma cell adhesion molecule MCAM mediates
RT selective binding of APXL2, a new member of the Apx/Shroom actin-binding
RT protein family.";
RL Submitted (OCT-2000) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=11853319; DOI=10.1093/dnares/8.6.319;
RA Nagase T., Kikuno R., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XXII. The
RT complete sequences of 50 new cDNA clones which code for large proteins.";
RL DNA Res. 8:319-327(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15372022; DOI=10.1038/nature02919;
RA Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S.,
RA Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M.,
RA She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S.,
RA Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M.,
RA Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M.,
RA Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T.,
RA Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A.,
RA Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R.,
RA Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L.,
RA Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N.,
RA Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J.,
RA Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A.,
RA Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M.;
RT "The DNA sequence and comparative analysis of human chromosome 5.";
RL Nature 431:268-274(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Liver;
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 [6]
RP NOMENCLATURE.
RX PubMed=16615870; DOI=10.1186/1471-2121-7-18;
RA Hagens O., Ballabio A., Kalscheuer V., Kraehenbuhl J.-P., Schiaffino M.V.,
RA Smith P., Staub O., Hildebrand J.D., Wallingford J.B.;
RT "A new standard nomenclature for proteins related to Apx and Shroom.";
RL BMC Cell Biol. 7:18-18(2006).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [9]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP 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 [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-18; THR-103; SER-166; SER-190
RP AND SER-224, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Cervix carcinoma, and 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 [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-103; SER-133 AND SER-137, AND
RP IDENTIFICATION BY 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).
CC -!- FUNCTION: May be involved in the assembly of microtubule arrays during
CC cell elongation. {ECO:0000250}.
CC -!- SUBUNIT: Interacts with F-actin. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q2M3G4-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q2M3G4-2; Sequence=VSP_024962;
CC -!- DOMAIN: The ASD1 domain mediates F-actin binding. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the shroom family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB85546.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AF314142; AAM15526.1; -; mRNA.
DR EMBL; AB075840; BAB85546.1; ALT_INIT; mRNA.
DR EMBL; AC004775; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471062; EAW62311.1; -; Genomic_DNA.
DR EMBL; CH471062; EAW62312.1; -; Genomic_DNA.
DR EMBL; BC104914; AAI04915.1; -; mRNA.
DR EMBL; BC104916; AAI04917.1; -; mRNA.
DR EMBL; BC143494; AAI43495.1; -; mRNA.
DR CCDS; CCDS4161.1; -. [Q2M3G4-2]
DR CCDS; CCDS54902.1; -. [Q2M3G4-1]
DR RefSeq; NP_001166171.1; NM_001172700.1. [Q2M3G4-1]
DR RefSeq; NP_597713.2; NM_133456.2. [Q2M3G4-2]
DR RefSeq; XP_005271942.1; XM_005271885.4. [Q2M3G4-1]
DR RefSeq; XP_005271943.1; XM_005271886.3. [Q2M3G4-1]
DR RefSeq; XP_011541469.1; XM_011543167.2. [Q2M3G4-1]
DR AlphaFoldDB; Q2M3G4; -.
DR SMR; Q2M3G4; -.
DR BioGRID; 126408; 19.
DR DIP; DIP-42367N; -.
DR IntAct; Q2M3G4; 10.
DR MINT; Q2M3G4; -.
DR STRING; 9606.ENSP00000367950; -.
DR iPTMnet; Q2M3G4; -.
DR PhosphoSitePlus; Q2M3G4; -.
DR BioMuta; SHROOM1; -.
DR DMDM; 121941488; -.
DR EPD; Q2M3G4; -.
DR jPOST; Q2M3G4; -.
DR MassIVE; Q2M3G4; -.
DR MaxQB; Q2M3G4; -.
DR PaxDb; Q2M3G4; -.
DR PeptideAtlas; Q2M3G4; -.
DR PRIDE; Q2M3G4; -.
DR ProteomicsDB; 61376; -. [Q2M3G4-1]
DR ProteomicsDB; 61377; -. [Q2M3G4-2]
DR Antibodypedia; 64246; 54 antibodies from 21 providers.
DR DNASU; 134549; -.
DR Ensembl; ENST00000319854.7; ENSP00000324245.3; ENSG00000164403.15. [Q2M3G4-2]
DR Ensembl; ENST00000378679.8; ENSP00000367950.3; ENSG00000164403.15. [Q2M3G4-1]
DR Ensembl; ENST00000617339.4; ENSP00000478436.1; ENSG00000164403.15. [Q2M3G4-1]
DR GeneID; 134549; -.
DR KEGG; hsa:134549; -.
DR MANE-Select; ENST00000378679.8; ENSP00000367950.3; NM_001172700.2; NP_001166171.1.
DR UCSC; uc003kxx.3; human. [Q2M3G4-1]
DR CTD; 134549; -.
DR DisGeNET; 134549; -.
DR GeneCards; SHROOM1; -.
DR HGNC; HGNC:24084; SHROOM1.
DR HPA; ENSG00000164403; Group enriched (brain, liver, prostate, urinary bladder).
DR MIM; 611179; gene.
DR neXtProt; NX_Q2M3G4; -.
DR OpenTargets; ENSG00000164403; -.
DR PharmGKB; PA147357345; -.
DR VEuPathDB; HostDB:ENSG00000164403; -.
DR eggNOG; ENOG502SM3B; Eukaryota.
DR GeneTree; ENSGT00940000160656; -.
DR InParanoid; Q2M3G4; -.
DR OMA; EHPLHEH; -.
DR OrthoDB; 729991at2759; -.
DR PhylomeDB; Q2M3G4; -.
DR TreeFam; TF335754; -.
DR PathwayCommons; Q2M3G4; -.
DR SignaLink; Q2M3G4; -.
DR BioGRID-ORCS; 134549; 9 hits in 1078 CRISPR screens.
DR ChiTaRS; SHROOM1; human.
DR GenomeRNAi; 134549; -.
DR Pharos; Q2M3G4; Tdark.
DR PRO; PR:Q2M3G4; -.
DR Proteomes; UP000005640; Chromosome 5.
DR RNAct; Q2M3G4; protein.
DR Bgee; ENSG00000164403; Expressed in pancreatic ductal cell and 173 other tissues.
DR ExpressionAtlas; Q2M3G4; baseline and differential.
DR Genevisible; Q2M3G4; HS.
DR GO; GO:0005912; C:adherens junction; IBA:GO_Central.
DR GO; GO:0043296; C:apical junction complex; IBA:GO_Central.
DR GO; GO:0016324; C:apical plasma membrane; IBA:GO_Central.
DR GO; GO:0030864; C:cortical actin cytoskeleton; IBA:GO_Central.
DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR GO; GO:0051015; F:actin filament binding; ISS:HGNC.
DR GO; GO:0045159; F:myosin II binding; ISS:HGNC.
DR GO; GO:0051017; P:actin filament bundle assembly; ISS:HGNC.
DR GO; GO:0007015; P:actin filament organization; IBA:GO_Central.
DR GO; GO:0000902; P:cell morphogenesis; ISS:HGNC.
DR InterPro; IPR014800; ASD1_dom.
DR InterPro; IPR014799; ASD2_dom.
DR InterPro; IPR027685; Shroom_fam.
DR PANTHER; PTHR15012; PTHR15012; 2.
DR Pfam; PF08688; ASD1; 1.
DR Pfam; PF08687; ASD2; 1.
DR PROSITE; PS51306; ASD1; 1.
DR PROSITE; PS51307; ASD2; 1.
PE 1: Evidence at protein level;
KW Acetylation; Actin-binding; Alternative splicing; Cytoplasm; Cytoskeleton;
KW Microtubule; Phosphoprotein; Reference proteome.
FT CHAIN 1..852
FT /note="Protein Shroom1"
FT /id="PRO_0000286061"
FT DOMAIN 145..233
FT /note="ASD1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00637"
FT DOMAIN 543..825
FT /note="ASD2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00638"
FT REGION 34..54
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 81..109
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 125..218
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 276..320
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 399..431
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 464..496
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 823..852
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 464..495
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 830..852
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0007744|PubMed:22814378"
FT MOD_RES 18
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 103
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 133
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 137
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 166
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 190
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 224
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT VAR_SEQ 742..746
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|Ref.1"
FT /id="VSP_024962"
FT VARIANT 180
FT /note="P -> L (in dbSNP:rs2292030)"
FT /id="VAR_032061"
FT CONFLICT 129
FT /note="A -> V (in Ref. 1; AAM15526)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 852 AA; 90786 MW; 43DFAF54E8355877 CRC64;
MEALGPGGDR ASPASSTSSL DLWHLSMRAD SAYSSFSAAS GGPEPRTQSP GTDLLPYLDW
DYVRVVWGGP GPAPPDAALC TSPRPRPAVA ARSGPQPTEV PGTPGPLNRQ ATPLLYALAA
EAEAAAQAAE PPSPPASRAA YRQRLQGAQR RVLRETSFQR KELRMSLPAR LRPTVPARPP
ATHPRSASLS HPGGEGEPAR SRAPAPGTAG RGPLANQQRK WCFSEPGKLD RVGRGGGPAR
ECLGEACSSS GLPGPEPLEF QHPALAKFED HEVGWLPETQ PQGSMNLDSG SLKLGDAFRP
ASRSRSASGE VLGSWGGSGG TIPIVQAVPQ GAETPRPLFQ TKLSRFLPQK EAAVMYPAEL
PQSSPADSEQ RVSETCIVPA WLPSLPDEVF LEEAPLVRMR SPPDPHASQG PPASVHASDQ
PYGTGLGQRT GQVTVPTEYP LHECPGTAGA DDCWQGVNGS VGISRPTSHT PTGTANDNIP
TIDPTGLTTN PPTAAESDLL KPVPADALGL SGNDTPGPSH NTALARGTGQ PGSRPTWPSQ
CLEELVQELA RLDPSLCDPL ASQPSPEPPL GLLDGLIPLA EVRAAMRPAC GEAGEEAAST
FEPGSYQFSF TQLLPAPREE TRLENPATHP VLDQPCGQGL PAPNNSIQGK KVELAARLQK
MLQDLHTEQE RLQGEAQAWA RRQAALEAAV RQACAPQELE RFSRFMADLE RVLGLLLLLG
SRLARVRRAL ARAASDSDPD EQASLLQRLR LLQRQEEDAK ELKEHVARRE RAVREVLVRA
LPVEELRVYC ALLAGKAAVL AQQRNLDERI RLLQDQLDAI RDDLGHHAPS PSPARPPGTC
PPVQPPFPLL LT
