HAUS5_HUMAN
ID HAUS5_HUMAN Reviewed; 633 AA.
AC O94927; B2RXK1; Q6P2P7; Q7L3D5; Q96CT8;
DT 07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 07-JUN-2005, sequence version 2.
DT 03-AUG-2022, entry version 157.
DE RecName: Full=HAUS augmin-like complex subunit 5;
GN Name=HAUS5; Synonyms=KIAA0841;
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=Brain;
RX PubMed=10048485; DOI=10.1093/dnares/5.6.355;
RA Nagase T., Ishikawa K., Suyama M., Kikuno R., Hirosawa M., Miyajima N.,
RA Tanaka A., Kotani H., Nomura N., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XII. The
RT complete sequences of 100 new cDNA clones from brain which code for large
RT proteins in vitro.";
RL DNA Res. 5:355-364(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Brain, Colon carcinoma, and Leukocyte;
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 [3]
RP IDENTIFICATION IN THE HAUS AUGMIN-LIKE COMPLEX, FUNCTION, AND SUBCELLULAR
RP LOCATION.
RX PubMed=19427217; DOI=10.1016/j.cub.2009.04.033;
RA Lawo S., Bashkurov M., Mullin M., Ferreria M.G., Kittler R., Habermann B.,
RA Tagliaferro A., Poser I., Hutchins J.R.A., Hegemann B., Pinchev D.,
RA Buchholz F., Peters J.-M., Hyman A.A., Gingras A.-C., Pelletier L.;
RT "HAUS, the 8-subunit human augmin complex, regulates centrosome and spindle
RT integrity.";
RL Curr. Biol. 19:816-826(2009).
RN [4]
RP IDENTIFICATION IN THE HAUS AUGMIN-LIKE COMPLEX, FUNCTION, AND SUBCELLULAR
RP LOCATION.
RX PubMed=19369198; DOI=10.1073/pnas.0901587106;
RA Uehara R., Nozawa R.-S., Tomioka A., Petry S., Vale R.D., Obuse C.,
RA Goshima G.;
RT "The augmin complex plays a critical role in spindle microtubule generation
RT for mitotic progression and cytokinesis in human cells.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:6998-7003(2009).
RN [5]
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 [6]
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 [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-71, AND IDENTIFICATION BY
RP MASS 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 [8]
RP INTERACTION WITH EML3, AND SUBCELLULAR LOCATION.
RX PubMed=30723163; DOI=10.1074/jbc.ra118.007164;
RA Luo J., Yang B., Xin G., Sun M., Zhang B., Guo X., Jiang Q., Zhang C.;
RT "The microtubule-associated protein EML3 regulates mitotic spindle assembly
RT by recruiting the Augmin complex to spindle microtubules.";
RL J. Biol. Chem. 294:5643-5656(2019).
CC -!- FUNCTION: Contributes to mitotic spindle assembly, maintenance of
CC centrosome integrity and completion of cytokinesis as part of the HAUS
CC augmin-like complex. {ECO:0000269|PubMed:19369198,
CC ECO:0000269|PubMed:19427217}.
CC -!- SUBUNIT: Component of the HAUS augmin-like complex. The complex
CC interacts with the gamma-tubulin ring complex and this interaction is
CC required for spindle assembly. Interacts with EML3 (phosphorylated at
CC 'Thr-881') (PubMed:30723163). {ECO:0000269|PubMed:19369198,
CC ECO:0000269|PubMed:19427217, ECO:0000269|PubMed:30723163}.
CC -!- INTERACTION:
CC O94927; Q7Z4H7: HAUS6; NbExp=3; IntAct=EBI-2558224, EBI-2558196;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing
CC center, centrosome {ECO:0000269|PubMed:19369198,
CC ECO:0000269|PubMed:19427217}. Cytoplasm, cytoskeleton, spindle
CC {ECO:0000269|PubMed:19369198, ECO:0000269|PubMed:19427217,
CC ECO:0000269|PubMed:30723163}. Note=Localizes to interphase centrosomes
CC and to mitotic spindle microtubules. {ECO:0000269|PubMed:19369198,
CC ECO:0000269|PubMed:19427217, ECO:0000269|PubMed:30723163}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=O94927-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O94927-2; Sequence=VSP_013927, VSP_013928;
CC -!- SIMILARITY: Belongs to the HAUS5 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH13947.2; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAA74864.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AB020648; BAA74864.1; ALT_INIT; mRNA.
DR EMBL; BC013947; AAH13947.2; ALT_INIT; mRNA.
DR EMBL; BC064390; AAH64390.1; -; mRNA.
DR EMBL; BC157882; AAI57883.1; -; mRNA.
DR CCDS; CCDS42550.1; -. [O94927-1]
DR RefSeq; NP_056117.1; NM_015302.1. [O94927-1]
DR AlphaFoldDB; O94927; -.
DR SMR; O94927; -.
DR BioGRID; 116936; 164.
DR ComplexPortal; CPX-1847; HAUS complex.
DR CORUM; O94927; -.
DR DIP; DIP-48831N; -.
DR IntAct; O94927; 58.
DR MINT; O94927; -.
DR STRING; 9606.ENSP00000439056; -.
DR GlyGen; O94927; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; O94927; -.
DR MetOSite; O94927; -.
DR PhosphoSitePlus; O94927; -.
DR BioMuta; HAUS5; -.
DR EPD; O94927; -.
DR jPOST; O94927; -.
DR MassIVE; O94927; -.
DR MaxQB; O94927; -.
DR PaxDb; O94927; -.
DR PeptideAtlas; O94927; -.
DR PRIDE; O94927; -.
DR ProteomicsDB; 50563; -. [O94927-1]
DR ProteomicsDB; 50564; -. [O94927-2]
DR Antibodypedia; 54102; 93 antibodies from 18 providers.
DR DNASU; 23354; -.
DR Ensembl; ENST00000203166.10; ENSP00000439056.1; ENSG00000249115.9. [O94927-1]
DR Ensembl; ENST00000587439.5; ENSP00000466661.1; ENSG00000249115.9. [O94927-2]
DR GeneID; 23354; -.
DR KEGG; hsa:23354; -.
DR MANE-Select; ENST00000203166.10; ENSP00000439056.1; NM_015302.2; NP_056117.1.
DR UCSC; uc002oam.2; human. [O94927-1]
DR CTD; 23354; -.
DR DisGeNET; 23354; -.
DR GeneCards; HAUS5; -.
DR HGNC; HGNC:29130; HAUS5.
DR HPA; ENSG00000249115; Low tissue specificity.
DR MIM; 613432; gene.
DR neXtProt; NX_O94927; -.
DR OpenTargets; ENSG00000249115; -.
DR PharmGKB; PA165393415; -.
DR VEuPathDB; HostDB:ENSG00000249115; -.
DR eggNOG; ENOG502QVVA; Eukaryota.
DR GeneTree; ENSGT00390000012508; -.
DR HOGENOM; CLU_959627_0_0_1; -.
DR InParanoid; O94927; -.
DR OMA; PHEDHFG; -.
DR OrthoDB; 277862at2759; -.
DR PhylomeDB; O94927; -.
DR TreeFam; TF333977; -.
DR PathwayCommons; O94927; -.
DR Reactome; R-HSA-2565942; Regulation of PLK1 Activity at G2/M Transition.
DR Reactome; R-HSA-380259; Loss of Nlp from mitotic centrosomes.
DR Reactome; R-HSA-380270; Recruitment of mitotic centrosome proteins and complexes.
DR Reactome; R-HSA-380284; Loss of proteins required for interphase microtubule organization from the centrosome.
DR Reactome; R-HSA-380320; Recruitment of NuMA to mitotic centrosomes.
DR Reactome; R-HSA-5620912; Anchoring of the basal body to the plasma membrane.
DR Reactome; R-HSA-8854518; AURKA Activation by TPX2.
DR SignaLink; O94927; -.
DR SIGNOR; O94927; -.
DR BioGRID-ORCS; 23354; 732 hits in 1090 CRISPR screens.
DR ChiTaRS; HAUS5; human.
DR GenomeRNAi; 23354; -.
DR Pharos; O94927; Tbio.
DR PRO; PR:O94927; -.
DR Proteomes; UP000005640; Chromosome 19.
DR RNAct; O94927; protein.
DR Bgee; ENSG00000249115; Expressed in secondary oocyte and 192 other tissues.
DR ExpressionAtlas; O94927; baseline and differential.
DR Genevisible; O94927; HS.
DR GO; GO:0005813; C:centrosome; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0070652; C:HAUS complex; IDA:UniProtKB.
DR GO; GO:1990498; C:mitotic spindle microtubule; IDA:UniProtKB.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0007098; P:centrosome cycle; IMP:UniProtKB.
DR GO; GO:0051225; P:spindle assembly; IMP:UniProtKB.
DR InterPro; IPR029131; HAUS5.
DR InterPro; IPR026215; HAUS5_metazoa.
DR Pfam; PF14817; HAUS5; 1.
DR PRINTS; PR02091; HAUSAUGMINL5.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Cell cycle; Cell division; Coiled coil;
KW Cytoplasm; Cytoskeleton; Microtubule; Mitosis; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..633
FT /note="HAUS augmin-like complex subunit 5"
FT /id="PRO_0000050776"
FT REGION 264..286
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 73..110
FT /evidence="ECO:0000255"
FT COILED 375..403
FT /evidence="ECO:0000255"
FT COILED 551..592
FT /evidence="ECO:0000255"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0007744|PubMed:22814378"
FT MOD_RES 71
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT VAR_SEQ 275..290
FT /note="PQAPDQSDSSQTLPSM -> RAGGLWVCWSPSGAPS (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_013927"
FT VAR_SEQ 291..633
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_013928"
FT VARIANT 213
FT /note="P -> L (in dbSNP:rs2301596)"
FT /id="VAR_034038"
FT VARIANT 277
FT /note="A -> D (in dbSNP:rs2285412)"
FT /id="VAR_034039"
FT CONFLICT 556
FT /note="Q -> R (in Ref. 2; AAI57883)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 633 AA; 71682 MW; 23D8746F2A81ABCB CRC64;
MELAQEAREL GCWAVEEMGV PVAARAPEST LRRLCLGQGA DIWAYILQHV HSQRTVKKIR
GNLLWYGHQD SPQVRRKLEL EAAVTRLRAE IQELDQSLEL MERDTEAQDT AMEQARQHTQ
DTQRRALLLR AQAGAMRRQQ HTLRDPMQRL QNQLRRLQDM ERKAKVDVTF GSLTSAALGL
EPVVLRDVRT ACTLRAQFLQ NLLLPQAKRG SLPTPHDDHF GTSYQQWLSS VETLLTNHPP
GHVLAALEHL AAEREAEIRS LCSGDGLGDT EISRPQAPDQ SDSSQTLPSM VHLIQEGWRT
VGVLVSQRST LLKERQVLTQ RLQGLVEEVE RRVLGSSERQ VLILGLRRCC LWTELKALHD
QSQELQDAAG HRQLLLRELQ AKQQRILHWR QLVEETQEQV RLLIKGNSAS KTRLCRSPGE
VLALVQRKVV PTFEAVAPQS RELLRCLEEE VRHLPHILLG TLLRHRPGEL KPLPTVLPSI
HQLHPASPRG SSFIALSHKL GLPPGKASEL LLPAAASLRQ DLLLLQDQRS LWCWDLLHMK
TSLPPGLPTQ ELLQIQASQE KQQKENLGQA LKRLEKLLKQ ALERIPELQG IVGDWWEQPG
QAALSEELCQ GLSLPQWRLR WVQAQGALQK LCS
