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Protein

HAUS augmin-like complex subunit 3

Gene

Haus3

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Contributes to mitotic spindle assembly, maintenance of centrosome integrity and completion of cytokinesis as part of the HAUS augmin-like complex.By similarity

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Cell cycle, Cell division, Mitosis

Names & Taxonomyi

Protein namesi
Recommended name:
HAUS augmin-like complex subunit 3
Gene namesi
Name:Haus3
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 5

Organism-specific databases

MGIiMGI:2387633. Haus3.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton, Microtubule

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedBy similarity
Chaini2 – 570569HAUS augmin-like complex subunit 3PRO_0000301952Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserineBy similarity

Keywords - PTMi

Acetylation

Proteomic databases

EPDiQ8QZX2.
MaxQBiQ8QZX2.
PaxDbiQ8QZX2.
PRIDEiQ8QZX2.

PTM databases

PhosphoSiteiQ8QZX2.

Expressioni

Gene expression databases

BgeeiQ8QZX2.
CleanExiMM_BC023882.
ExpressionAtlasiQ8QZX2. baseline and differential.
GenevisibleiQ8QZX2. MM.

Interactioni

Subunit structurei

Component of the HAUS augmin-like complex. The complex interacts with the gamma-tubulin ring complex and this interaction is required for spindle assembly (By similarity).By similarity

Protein-protein interaction databases

BioGridi231085. 3 interactions.
IntActiQ8QZX2. 5 interactions.
MINTiMINT-4116362.
STRINGi10090.ENSMUSP00000049973.

Structurei

3D structure databases

ProteinModelPortaliQ8QZX2.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili90 – 12435Sequence analysisAdd
BLAST
Coiled coili154 – 17825Sequence analysisAdd
BLAST
Coiled coili284 – 33653Sequence analysisAdd
BLAST
Coiled coili458 – 49538Sequence analysisAdd
BLAST

Sequence similaritiesi

Belongs to the HAUS3 family.Curated

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiENOG410IG8W. Eukaryota.
ENOG4111N2F. LUCA.
GeneTreeiENSGT00390000011904.
HOGENOMiHOG000054217.
InParanoidiQ8QZX2.
KOiK16586.
OMAiEQFHQVE.
OrthoDBiEOG71P2C7.
PhylomeDBiQ8QZX2.
TreeFamiTF331151.

Family and domain databases

InterProiIPR026206. HAUS3.
IPR032733. HAUS3_N.
[Graphical view]
PANTHERiPTHR19378. PTHR19378. 1 hit.
PfamiPF14932. HAUS-augmin3. 1 hit.
[Graphical view]
PRINTSiPR02089. HAUSAUGMINL3.

Sequences (2)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q8QZX2-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MSCGNEFVET LKKIGYPKAD ILNGEDFDWL FEDVEDESFL KWFCGNVNEQ
60 70 80 90 100
NVLSEKELEA FSDLQRSGKP ILEGTALDEV LRTCKTFDLK TCKLDDKEIQ
110 120 130 140 150
ILEDEVQTLQ KLNNSKIQRR NKYQLMVSET SYRFLALNAK QEEATKKLKQ
160 170 180 190 200
KQGFLNSVNT KLSNELQGLT EEVNNLMIFF RNSNLSERTN PMVFLSQFPL
210 220 230 240 250
GKYISQEEQS TAALTLYTKK QFFQGMHEVV ESSNEDNFQL LDIQTPSICD
260 270 280 290 300
NEEILRERRL EMARLQMACI CVQKQIIYLK TSNLSMKSSI KWAEENLNRL
310 320 330 340 350
TNEVIDKENL DAEISSLNSE ILKLEEQITH IKDKVLPAVV KEYAQLLNMP
360 370 380 390 400
VVKGDFELQI AKQDYYTARQ ELVLNELIKQ KASFELVQLS YEIELRKHWD
410 420 430 440 450
TYRQLESLVQ QLSQRNTVLC QHLAVLSDIP ASEQLTSRTP IDTKDHSTHR
460 470 480 490 500
LYELLEGDNK KKELFITHEH LEEVAEKLKQ DVSVIQDQLA VSTQEHFFFL
510 520 530 540 550
SKLNNDVDML CDALYRGGNQ LLLCDQELKE HFHQVESQLN ELHHLLTDIL
560 570
ADVKTKRRIL ATNKLHQVER
Length:570
Mass (Da):66,308
Last modified:June 1, 2002 - v1
Checksum:iBAA32FB3003E3B3F
GO
Isoform 2 (identifier: Q8QZX2-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     527-570: ELKEHFHQVESQLNELHHLLTDILADVKTKRRILATNKLHQVER → VSVYLKI

Note: No experimental confirmation available.
Show »
Length:533
Mass (Da):61,847
Checksum:iC4DD46DE66FF4E6F
GO

Sequence cautioni

The sequence BAE36560.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti31 – 311F → L in AAH23882 (PubMed:15489334).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei527 – 57044ELKEH…HQVER → VSVYLKI in isoform 2. 1 PublicationVSP_027887Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK049414 mRNA. Translation: BAC33742.1.
AK161756 mRNA. Translation: BAE36560.1. Different initiation.
BC023882 mRNA. Translation: AAH23882.1.
BC025497 mRNA. Translation: AAH25497.1.
BC027393 mRNA. Translation: AAH27393.1.
CCDSiCCDS19211.1. [Q8QZX2-1]
RefSeqiNP_666271.1. NM_146159.1. [Q8QZX2-1]
UniGeneiMm.319286.

Genome annotation databases

EnsembliENSMUST00000060049; ENSMUSP00000049973; ENSMUSG00000079555. [Q8QZX2-1]
GeneIDi231123.
KEGGimmu:231123.
UCSCiuc008xbv.3. mouse. [Q8QZX2-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK049414 mRNA. Translation: BAC33742.1.
AK161756 mRNA. Translation: BAE36560.1. Different initiation.
BC023882 mRNA. Translation: AAH23882.1.
BC025497 mRNA. Translation: AAH25497.1.
BC027393 mRNA. Translation: AAH27393.1.
CCDSiCCDS19211.1. [Q8QZX2-1]
RefSeqiNP_666271.1. NM_146159.1. [Q8QZX2-1]
UniGeneiMm.319286.

3D structure databases

ProteinModelPortaliQ8QZX2.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi231085. 3 interactions.
IntActiQ8QZX2. 5 interactions.
MINTiMINT-4116362.
STRINGi10090.ENSMUSP00000049973.

PTM databases

PhosphoSiteiQ8QZX2.

Proteomic databases

EPDiQ8QZX2.
MaxQBiQ8QZX2.
PaxDbiQ8QZX2.
PRIDEiQ8QZX2.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000060049; ENSMUSP00000049973; ENSMUSG00000079555. [Q8QZX2-1]
GeneIDi231123.
KEGGimmu:231123.
UCSCiuc008xbv.3. mouse. [Q8QZX2-1]

Organism-specific databases

CTDi79441.
MGIiMGI:2387633. Haus3.

Phylogenomic databases

eggNOGiENOG410IG8W. Eukaryota.
ENOG4111N2F. LUCA.
GeneTreeiENSGT00390000011904.
HOGENOMiHOG000054217.
InParanoidiQ8QZX2.
KOiK16586.
OMAiEQFHQVE.
OrthoDBiEOG71P2C7.
PhylomeDBiQ8QZX2.
TreeFamiTF331151.

Miscellaneous databases

NextBioi380409.
PROiQ8QZX2.
SOURCEiSearch...

Gene expression databases

BgeeiQ8QZX2.
CleanExiMM_BC023882.
ExpressionAtlasiQ8QZX2. baseline and differential.
GenevisibleiQ8QZX2. MM.

Family and domain databases

InterProiIPR026206. HAUS3.
IPR032733. HAUS3_N.
[Graphical view]
PANTHERiPTHR19378. PTHR19378. 1 hit.
PfamiPF14932. HAUS-augmin3. 1 hit.
[Graphical view]
PRINTSiPR02089. HAUSAUGMINL3.
ProtoNetiSearch...

Publicationsi

  1. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 271-554 (ISOFORM 1).
    Strain: C57BL/6J.
    Tissue: Embryo and Thymus.
  2. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Strain: FVB/N.
    Tissue: Mammary tumor.
  3. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Spleen.

Entry informationi

Entry nameiHAUS3_MOUSE
AccessioniPrimary (citable) accession number: Q8QZX2
Secondary accession number(s): Q3TSW5, Q8BQL2, Q8CIH1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 11, 2007
Last sequence update: June 1, 2002
Last modified: May 11, 2016
This is version 90 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.