HAUS3_MOUSE
ID HAUS3_MOUSE Reviewed; 570 AA.
AC Q8QZX2; Q3TSW5; Q8BQL2; Q8CIH1;
DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 121.
DE RecName: Full=HAUS augmin-like complex subunit 3;
GN Name=Haus3;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 271-554 (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Embryo, and Thymus;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=FVB/N; TISSUE=Mammary tumor;
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 BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Spleen;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
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:0000250}.
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 (By similarity). Interacts with EML3
CC (phosphorylated at 'Thr-882') (By similarity).
CC {ECO:0000250|UniProtKB:Q68CZ6}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing
CC center, centrosome {ECO:0000250|UniProtKB:Q68CZ6}. Cytoplasm,
CC cytoskeleton, spindle {ECO:0000250|UniProtKB:Q68CZ6}. Note=Localizes to
CC interphase centrosomes and to mitotic spindle microtubules.
CC {ECO:0000250|UniProtKB:Q68CZ6}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8QZX2-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8QZX2-2; Sequence=VSP_027887;
CC -!- SIMILARITY: Belongs to the HAUS3 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAE36560.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AK049414; BAC33742.1; -; mRNA.
DR EMBL; AK161756; BAE36560.1; ALT_INIT; mRNA.
DR EMBL; BC023882; AAH23882.1; -; mRNA.
DR EMBL; BC025497; AAH25497.1; -; mRNA.
DR EMBL; BC027393; AAH27393.1; -; mRNA.
DR CCDS; CCDS19211.1; -. [Q8QZX2-1]
DR RefSeq; NP_666271.1; NM_146159.1. [Q8QZX2-1]
DR AlphaFoldDB; Q8QZX2; -.
DR SMR; Q8QZX2; -.
DR BioGRID; 231085; 5.
DR IntAct; Q8QZX2; 4.
DR STRING; 10090.ENSMUSP00000049973; -.
DR PhosphoSitePlus; Q8QZX2; -.
DR EPD; Q8QZX2; -.
DR MaxQB; Q8QZX2; -.
DR PaxDb; Q8QZX2; -.
DR PeptideAtlas; Q8QZX2; -.
DR PRIDE; Q8QZX2; -.
DR ProteomicsDB; 270940; -. [Q8QZX2-1]
DR ProteomicsDB; 270941; -. [Q8QZX2-2]
DR Antibodypedia; 43178; 134 antibodies from 23 providers.
DR Ensembl; ENSMUST00000060049; ENSMUSP00000049973; ENSMUSG00000079555. [Q8QZX2-1]
DR GeneID; 231123; -.
DR KEGG; mmu:231123; -.
DR UCSC; uc008xbv.3; mouse. [Q8QZX2-1]
DR CTD; 79441; -.
DR MGI; MGI:2387633; Haus3.
DR VEuPathDB; HostDB:ENSMUSG00000079555; -.
DR eggNOG; ENOG502R4I5; Eukaryota.
DR GeneTree; ENSGT00390000011904; -.
DR HOGENOM; CLU_031795_0_0_1; -.
DR InParanoid; Q8QZX2; -.
DR OMA; SFLEWFC; -.
DR OrthoDB; 380555at2759; -.
DR PhylomeDB; Q8QZX2; -.
DR TreeFam; TF331151; -.
DR Reactome; R-MMU-2565942; Regulation of PLK1 Activity at G2/M Transition.
DR Reactome; R-MMU-380259; Loss of Nlp from mitotic centrosomes.
DR Reactome; R-MMU-380270; Recruitment of mitotic centrosome proteins and complexes.
DR Reactome; R-MMU-380284; Loss of proteins required for interphase microtubule organization from the centrosome.
DR Reactome; R-MMU-380320; Recruitment of NuMA to mitotic centrosomes.
DR Reactome; R-MMU-5620912; Anchoring of the basal body to the plasma membrane.
DR Reactome; R-MMU-8854518; AURKA Activation by TPX2.
DR BioGRID-ORCS; 231123; 22 hits in 73 CRISPR screens.
DR PRO; PR:Q8QZX2; -.
DR Proteomes; UP000000589; Chromosome 5.
DR RNAct; Q8QZX2; protein.
DR Bgee; ENSMUSG00000079555; Expressed in primary oocyte and 265 other tissues.
DR ExpressionAtlas; Q8QZX2; baseline and differential.
DR Genevisible; Q8QZX2; MM.
DR GO; GO:0005813; C:centrosome; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0070652; C:HAUS complex; ISS:UniProtKB.
DR GO; GO:0072686; C:mitotic spindle; IBA:GO_Central.
DR GO; GO:1990498; C:mitotic spindle microtubule; ISS:UniProtKB.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0007098; P:centrosome cycle; ISS:UniProtKB.
DR GO; GO:0051225; P:spindle assembly; ISS:UniProtKB.
DR InterPro; IPR026206; HAUS3.
DR InterPro; IPR032733; HAUS3_N.
DR PANTHER; PTHR19378; PTHR19378; 1.
DR Pfam; PF14932; HAUS-augmin3; 1.
DR PRINTS; PR02089; HAUSAUGMINL3.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Cell cycle; Cell division; Coiled coil;
KW Cytoplasm; Cytoskeleton; Microtubule; Mitosis; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q68CZ6"
FT CHAIN 2..570
FT /note="HAUS augmin-like complex subunit 3"
FT /id="PRO_0000301952"
FT COILED 90..124
FT /evidence="ECO:0000255"
FT COILED 154..178
FT /evidence="ECO:0000255"
FT COILED 284..336
FT /evidence="ECO:0000255"
FT COILED 458..495
FT /evidence="ECO:0000255"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000250|UniProtKB:Q68CZ6"
FT VAR_SEQ 527..570
FT /note="ELKEHFHQVESQLNELHHLLTDILADVKTKRRILATNKLHQVER -> VSVY
FT LKI (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_027887"
FT CONFLICT 31
FT /note="F -> L (in Ref. 2; AAH23882)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 570 AA; 66308 MW; BAA32FB3003E3B3F CRC64;
MSCGNEFVET LKKIGYPKAD ILNGEDFDWL FEDVEDESFL KWFCGNVNEQ NVLSEKELEA
FSDLQRSGKP ILEGTALDEV LRTCKTFDLK TCKLDDKEIQ ILEDEVQTLQ KLNNSKIQRR
NKYQLMVSET SYRFLALNAK QEEATKKLKQ KQGFLNSVNT KLSNELQGLT EEVNNLMIFF
RNSNLSERTN PMVFLSQFPL GKYISQEEQS TAALTLYTKK QFFQGMHEVV ESSNEDNFQL
LDIQTPSICD NEEILRERRL EMARLQMACI CVQKQIIYLK TSNLSMKSSI KWAEENLNRL
TNEVIDKENL DAEISSLNSE ILKLEEQITH IKDKVLPAVV KEYAQLLNMP VVKGDFELQI
AKQDYYTARQ ELVLNELIKQ KASFELVQLS YEIELRKHWD TYRQLESLVQ QLSQRNTVLC
QHLAVLSDIP ASEQLTSRTP IDTKDHSTHR LYELLEGDNK KKELFITHEH LEEVAEKLKQ
DVSVIQDQLA VSTQEHFFFL SKLNNDVDML CDALYRGGNQ LLLCDQELKE HFHQVESQLN
ELHHLLTDIL ADVKTKRRIL ATNKLHQVER
