HAUS7_HUMAN
ID HAUS7_HUMAN Reviewed; 358 AA.
AC Q99871; B4DUH6; D3DWT9; Q96HS8; Q9NP54; Q9UFH9;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 23-FEB-2022, sequence version 4.
DT 03-AUG-2022, entry version 168.
DE RecName: Full=HAUS augmin-like complex subunit 7;
DE AltName: Full=26S proteasome-associated UCH37-interacting protein 1;
DE AltName: Full=UCHL5-interacting protein;
DE AltName: Full=X-linked protein STS1769;
GN Name=HAUS7; Synonyms=UCHL5IP, UIP1;
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 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 [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 276-358 (ISOFORM 2).
RC TISSUE=Bone, and Oligodendroglioma;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC TISSUE=Rectum;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), INTERACTION WITH UCHL5, AND TISSUE
RP SPECIFICITY.
RX PubMed=11163772; DOI=10.1016/s0014-5793(00)02436-4;
RA Li T., Duan W., Yang H., Lee M.K., Bte Mustafa F., Lee B.H., Teo T.S.;
RT "Identification of two proteins, S14 and UIP1, that interact with UCH37.";
RL FEBS Lett. 488:201-205(2001).
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 82-358 (ISOFORM 1).
RC TISSUE=Fetal brain;
RX PubMed=9099879; DOI=10.1016/s0378-1119(96)00772-x;
RA Esposito T., Ciccodicola A., Flagiello L., Matarazzo M.R., Migliaccio C.,
RA Cifarelli R.A., Visone R., Campanile C., Mazzarella R., Schlessinger D.,
RA D'Urso M., D'Esposito M.;
RT "Expressed STSs and transcription of human Xq28.";
RL Gene 187:185-191(1997).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 132-358 (ISOFORM 3).
RC TISSUE=Testis;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-16, AND IDENTIFICATION BY
RP 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 [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [10]
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 [11]
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 [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-16, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE 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 [13]
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 UCHL5 (PubMed:11163772).
CC Interacts with EML3 (phosphorylated at 'Thr-881') (PubMed:30723163).
CC {ECO:0000269|PubMed:11163772, ECO:0000269|PubMed:19369198,
CC ECO:0000269|PubMed:19427217, ECO:0000269|PubMed:30723163}.
CC -!- INTERACTION:
CC Q99871; P18848: ATF4; NbExp=3; IntAct=EBI-395719, EBI-492498;
CC Q99871; O75190-2: DNAJB6; NbExp=3; IntAct=EBI-395719, EBI-12593112;
CC Q99871; Q6W0C5: DPPA3; NbExp=3; IntAct=EBI-395719, EBI-12082590;
CC Q99871; Q7Z4H7: HAUS6; NbExp=3; IntAct=EBI-395719, EBI-2558196;
CC Q99871; O43464: HTRA2; NbExp=3; IntAct=EBI-395719, EBI-517086;
CC Q99871; P42858: HTT; NbExp=18; IntAct=EBI-395719, EBI-466029;
CC Q99871; O14901: KLF11; NbExp=3; IntAct=EBI-395719, EBI-948266;
CC Q99871; P28331-2: NDUFS1; NbExp=3; IntAct=EBI-395719, EBI-6190702;
CC Q99871; Q9BVL2: NUP58; NbExp=3; IntAct=EBI-395719, EBI-2811583;
CC Q99871; Q9BZ23-2: PANK2; NbExp=3; IntAct=EBI-395719, EBI-25929070;
CC Q99871; P41219: PRPH; NbExp=3; IntAct=EBI-395719, EBI-752074;
CC Q99871; Q7Z699: SPRED1; NbExp=3; IntAct=EBI-395719, EBI-5235340;
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=3;
CC Name=1;
CC IsoId=Q99871-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q99871-2; Sequence=VSP_037669;
CC Name=3;
CC IsoId=Q99871-3; Sequence=VSP_040920, VSP_040921;
CC -!- TISSUE SPECIFICITY: Detected in spleen, thymus, testis, ovary, small
CC intestine and colon, with highest levels of expression in testis and
CC ovary. {ECO:0000269|PubMed:11163772}.
CC -!- SIMILARITY: Belongs to the HAUS7 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH08141.3; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=CAA67665.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=CAA67665.1; Type=Miscellaneous discrepancy; Note=Chimera. The N-terminal part of the clone up to position 91 maps to another chromosome.; Evidence={ECO:0000305};
CC Sequence=EAW72866.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=EAW72868.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=EAW72869.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=EAW72871.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; U82695; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471172; EAW72866.1; ALT_INIT; Genomic_DNA.
DR EMBL; CH471172; EAW72868.1; ALT_INIT; Genomic_DNA.
DR EMBL; CH471172; EAW72869.1; ALT_INIT; Genomic_DNA.
DR EMBL; CH471172; EAW72871.1; ALT_INIT; Genomic_DNA.
DR EMBL; BC008141; AAH08141.3; ALT_INIT; mRNA.
DR EMBL; CA441020; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AK300650; BAG62338.1; -; mRNA.
DR EMBL; AF267739; AAF75785.1; -; mRNA.
DR EMBL; X99270; CAA67665.1; ALT_SEQ; mRNA.
DR EMBL; AL122036; CAB59176.1; -; mRNA.
DR CCDS; CCDS35438.1; -. [Q99871-1]
DR PIR; T34551; T34551.
DR RefSeq; NP_059988.3; NM_017518.7. [Q99871-1]
DR AlphaFoldDB; Q99871; -.
DR BioGRID; 120718; 121.
DR ComplexPortal; CPX-1847; HAUS complex.
DR CORUM; Q99871; -.
DR DIP; DIP-32974N; -.
DR IntAct; Q99871; 82.
DR MINT; Q99871; -.
DR STRING; 9606.ENSP00000359230; -.
DR GlyGen; Q99871; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q99871; -.
DR PhosphoSitePlus; Q99871; -.
DR BioMuta; HAUS7; -.
DR EPD; Q99871; -.
DR jPOST; Q99871; -.
DR MassIVE; Q99871; -.
DR MaxQB; Q99871; -.
DR PaxDb; Q99871; -.
DR PeptideAtlas; Q99871; -.
DR PRIDE; Q99871; -.
DR ProteomicsDB; 78508; -. [Q99871-1]
DR ProteomicsDB; 78509; -. [Q99871-2]
DR ProteomicsDB; 78510; -. [Q99871-3]
DR Antibodypedia; 461; 304 antibodies from 21 providers.
DR DNASU; 55559; -.
DR Ensembl; ENST00000370211.10; ENSP00000359230.6; ENSG00000213397.12. [Q99871-1]
DR GeneID; 55559; -.
DR MANE-Select; ENST00000370211.10; ENSP00000359230.6; NM_001385482.1; NP_001372411.1.
DR UCSC; uc004fho.3; human. [Q99871-1]
DR CTD; 55559; -.
DR DisGeNET; 55559; -.
DR GeneCards; HAUS7; -.
DR HGNC; HGNC:32979; HAUS7.
DR HPA; ENSG00000213397; Low tissue specificity.
DR MIM; 300540; gene.
DR neXtProt; NX_Q99871; -.
DR OpenTargets; ENSG00000213397; -.
DR PharmGKB; PA165756645; -.
DR VEuPathDB; HostDB:ENSG00000213397; -.
DR eggNOG; ENOG502RYVK; Eukaryota.
DR GeneTree; ENSGT00390000003937; -.
DR HOGENOM; CLU_065168_0_0_1; -.
DR InParanoid; Q99871; -.
DR OMA; PESDPWP; -.
DR OrthoDB; 1184888at2759; -.
DR PhylomeDB; Q99871; -.
DR TreeFam; TF333445; -.
DR PathwayCommons; Q99871; -.
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; Q99871; -.
DR SIGNOR; Q99871; -.
DR BioGRID-ORCS; 55559; 372 hits in 664 CRISPR screens.
DR ChiTaRS; HAUS7; human.
DR GenomeRNAi; 55559; -.
DR Pharos; Q99871; Tbio.
DR PRO; PR:Q99871; -.
DR Proteomes; UP000005640; Chromosome X.
DR RNAct; Q99871; protein.
DR Bgee; ENSG00000213397; Expressed in ascending aorta and 93 other tissues.
DR ExpressionAtlas; Q99871; baseline and differential.
DR Genevisible; Q99871; 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:0005730; C:nucleolus; IDA:HPA.
DR GO; GO:0005886; C:plasma membrane; IDA:HPA.
DR GO; GO:0051011; F:microtubule minus-end binding; IBA:GO_Central.
DR GO; GO:0031996; F:thioesterase binding; IPI: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; IPR029711; Haus7-like.
DR PANTHER; PTHR14352; PTHR14352; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell cycle; Cell division; Coiled coil; Cytoplasm;
KW Cytoskeleton; Microtubule; Mitosis; Phosphoprotein; Reference proteome.
FT CHAIN 1..358
FT /note="HAUS augmin-like complex subunit 7"
FT /id="PRO_0000097552"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 203..236
FT /evidence="ECO:0000255"
FT MOD_RES 16
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT VAR_SEQ 310
FT /note="Q -> QIPRGQPKKPALVTMTTVPTCATLPLAQGFRDVHFGFLSERLRAFQP
FT LTGWSCETPRSGM (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_037669"
FT VAR_SEQ 311..329
FT /note="LLQVVMAVADTSAKAVETV -> VRVPFPSPLTAPSPVHSD (in
FT isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:17974005"
FT /id="VSP_040920"
FT VAR_SEQ 330..358
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:17974005"
FT /id="VSP_040921"
SQ SEQUENCE 358 AA; 39794 MW; EFD0264BD6608F0F CRC64;
MAGQDAGCGR GGDDYSEDEG DSSVSRAAVE VFGKLKDLNC PFLEGLYITE PKTIQELLCS
PSEYRLEILE WMCTRVWPSL QDRFSSLKGV PTEVKIQEMT KLGHELMLCA PDDQELLKGC
ACAQKQLHFM DQLLDTIRSL TIGCSSCSSL MEHFEDTREK NEALLGELFS SPHLQMLLNP
ECDPWPLDMQ PLLNKQSDDW QWASASAKSE EEEKLAELAR QLQESAAKLH ALRTEYFAQH
EQGAAAGAAD ISTLDQKLRL VTSDFHQLIL AFLQVYDDEL GECCQRPGPD LHPCGPIIQA
THQNLTSYSQ LLQVVMAVAD TSAKAVETVK KQQGEQICWG GSSSVMSLAT KMNELMEK
