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Protein

HAUS augmin-like complex subunit 5

Gene

Haus5

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 3 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

Enzyme and pathway databases

ReactomeiR-MMU-2565942. Regulation of PLK1 Activity at G2/M Transition.
R-MMU-380259. Loss of Nlp from mitotic centrosomes.
R-MMU-380270. Recruitment of mitotic centrosome proteins and complexes.
R-MMU-5620912. Anchoring of the basal body to the plasma membrane.
R-MMU-8854518. AURKA Activation by TPX2.

Names & Taxonomyi

Protein namesi
Recommended name:
HAUS augmin-like complex subunit 5
Gene namesi
Name:Haus5
Synonyms:Kiaa0841
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 7

Organism-specific databases

MGIiMGI:1919159. Haus5.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton, Microtubule

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 619619HAUS augmin-like complex subunit 5PRO_0000050777Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionineBy similarity

Keywords - PTMi

Acetylation

Proteomic databases

EPDiQ9D786.
MaxQBiQ9D786.
PaxDbiQ9D786.
PeptideAtlasiQ9D786.
PRIDEiQ9D786.

PTM databases

iPTMnetiQ9D786.
PhosphoSiteiQ9D786.

Expressioni

Gene expression databases

BgeeiQ9D786.
CleanExiMM_2310022K01RIK.
GenevisibleiQ9D786. 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

STRINGi10090.ENSMUSP00000019697.

Structurei

3D structure databases

ProteinModelPortaliQ9D786.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili73 – 10836Sequence analysisAdd
BLAST
Coiled coili310 – 39586Sequence analysisAdd
BLAST
Coiled coili550 – 59041Sequence analysisAdd
BLAST

Sequence similaritiesi

Belongs to the HAUS5 family.Curated

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiENOG410IJZU. Eukaryota.
ENOG410ZKR5. LUCA.
GeneTreeiENSGT00390000012508.
HOGENOMiHOG000112852.
HOVERGENiHBG081829.
InParanoidiQ9D786.
KOiK16588.
OMAiWAYVLRH.
OrthoDBiEOG7060QF.
PhylomeDBiQ9D786.
TreeFamiTF333977.

Family and domain databases

InterProiIPR029131. HAUS5.
IPR026215. HAUS5_metazoa.
[Graphical view]
PfamiPF14817. HAUS5. 1 hit.
[Graphical view]
PRINTSiPR02091. HAUSAUGMINL5.

Sequences (2)i

Sequence statusi: Complete.

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

Isoform 1 (identifier: Q9D786-1) [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
MELTQKEREL SRWAAEEMEV PLAARPREST LRRLCLSQGA DIWAYIVQHV
60 70 80 90 100
RSQRNIKKIQ GNLLWHAYQD NPKIHRKLEL EATVARLRAE NQELDQSLEL
110 120 130 140 150
MDQESEAQDV AMTQTLQSLK DTQHRALLLQ AQAGAVRRQQ RGLQDPMQRL
160 170 180 190 200
QNQLKHLQDM QRKAKVDVTF GPVVSAAPAL EPEVLGDVRA ACTLRTQFLQ
210 220 230 240 250
NLLTPRARGG SILSPCDDHV GTSYQQWLTS VETLLTNHPA GHVLAALEYL
260 270 280 290 300
AAERESEIRS LCYGDGLKEE ELSRPQAPES SNSSQVLPST VHLIQEGWQA
310 320 330 340 350
VGALVTQRSA LLSERQVLTG RLQRLVEEVK RLLLGSSERK VLLLGLRHSG
360 370 380 390 400
LLAELKALHA QSQELESAVG QRHLLLRELQ AKRQRILQWR QLVEDRQEQI
410 420 430 440 450
RLLIKGNSAS KTRLSRGPEE VLALIDQKLV PTSEAVAPQS QELLRCLKEE
460 470 480 490 500
AKHLPRVLLG PLLPYHVKGL KPLSRILPSI HQLHPTNPRA SSLILLSHTL
510 520 530 540 550
GLPVGKASEL LLPRAASLQQ DLLFLQDQLG LRRGNLCVKT SLPPGPSTQE
560 570 580 590 600
LLQMQVSQEK EQNENVGQTL KKLSNLLKQA LEQIPELQGI VQDWWEQPSQ
610
AALPEEICQG LSLPQCQLR
Length:619
Mass (Da):69,572
Last modified:June 1, 2001 - v1
Checksum:i2D1201F6CB8CA28E
GO
Isoform 2 (identifier: Q9D786-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     507-517: ASELLLPRAAS → TSWVSEEEISV
     518-619: Missing.

Show »
Length:517
Mass (Da):58,182
Checksum:i595A0EBC76EC8177
GO

Sequence cautioni

The sequence AAH23723.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated
The sequence AAH89002.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti71 – 733NPK → SYQ in BAC98038 (PubMed:14621295).Curated
Sequence conflicti156 – 1561H → R in EDL24000 (Ref. 2) Curated
Sequence conflicti156 – 1561H → R in AAI18935 (PubMed:15489334).Curated
Sequence conflicti156 – 1561H → R in BAC98038 (PubMed:14621295).Curated
Sequence conflicti321 – 3211R → H in EDL24000 (Ref. 2) Curated
Sequence conflicti321 – 3211R → H in AAI18935 (PubMed:15489334).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei507 – 51711ASELLLPRAAS → TSWVSEEEISV in isoform 2. 1 PublicationVSP_013929Add
BLAST
Alternative sequencei518 – 619102Missing in isoform 2. 1 PublicationVSP_013930Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK009476 mRNA. Translation: BAB26314.1.
CH466593 Genomic DNA. Translation: EDL24000.1.
BC023723 mRNA. Translation: AAH23723.1. Different initiation.
BC089002 mRNA. Translation: AAH89002.1. Different initiation.
BC118934 mRNA. Translation: AAI18935.1.
BC118935 mRNA. Translation: AAI18936.1.
AK129228 Transcribed RNA. Translation: BAC98038.2.
CCDSiCCDS52180.1. [Q9D786-1]
RefSeqiNP_082275.1. NM_027999.1. [Q9D786-1]
UniGeneiMm.290410.

Genome annotation databases

EnsembliENSMUST00000019697; ENSMUSP00000019697; ENSMUSG00000078762. [Q9D786-1]
ENSMUST00000132862; ENSMUSP00000121739; ENSMUSG00000078762. [Q9D786-2]
GeneIDi71909.
KEGGimmu:71909.
UCSCiuc009gfs.2. mouse. [Q9D786-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK009476 mRNA. Translation: BAB26314.1.
CH466593 Genomic DNA. Translation: EDL24000.1.
BC023723 mRNA. Translation: AAH23723.1. Different initiation.
BC089002 mRNA. Translation: AAH89002.1. Different initiation.
BC118934 mRNA. Translation: AAI18935.1.
BC118935 mRNA. Translation: AAI18936.1.
AK129228 Transcribed RNA. Translation: BAC98038.2.
CCDSiCCDS52180.1. [Q9D786-1]
RefSeqiNP_082275.1. NM_027999.1. [Q9D786-1]
UniGeneiMm.290410.

3D structure databases

ProteinModelPortaliQ9D786.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000019697.

PTM databases

iPTMnetiQ9D786.
PhosphoSiteiQ9D786.

Proteomic databases

EPDiQ9D786.
MaxQBiQ9D786.
PaxDbiQ9D786.
PeptideAtlasiQ9D786.
PRIDEiQ9D786.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000019697; ENSMUSP00000019697; ENSMUSG00000078762. [Q9D786-1]
ENSMUST00000132862; ENSMUSP00000121739; ENSMUSG00000078762. [Q9D786-2]
GeneIDi71909.
KEGGimmu:71909.
UCSCiuc009gfs.2. mouse. [Q9D786-1]

Organism-specific databases

CTDi23354.
MGIiMGI:1919159. Haus5.
RougeiSearch...

Phylogenomic databases

eggNOGiENOG410IJZU. Eukaryota.
ENOG410ZKR5. LUCA.
GeneTreeiENSGT00390000012508.
HOGENOMiHOG000112852.
HOVERGENiHBG081829.
InParanoidiQ9D786.
KOiK16588.
OMAiWAYVLRH.
OrthoDBiEOG7060QF.
PhylomeDBiQ9D786.
TreeFamiTF333977.

Enzyme and pathway databases

ReactomeiR-MMU-2565942. Regulation of PLK1 Activity at G2/M Transition.
R-MMU-380259. Loss of Nlp from mitotic centrosomes.
R-MMU-380270. Recruitment of mitotic centrosome proteins and complexes.
R-MMU-5620912. Anchoring of the basal body to the plasma membrane.
R-MMU-8854518. AURKA Activation by TPX2.

Miscellaneous databases

PROiQ9D786.
SOURCEiSearch...

Gene expression databases

BgeeiQ9D786.
CleanExiMM_2310022K01RIK.
GenevisibleiQ9D786. MM.

Family and domain databases

InterProiIPR029131. HAUS5.
IPR026215. HAUS5_metazoa.
[Graphical view]
PfamiPF14817. HAUS5. 1 hit.
[Graphical view]
PRINTSiPR02091. HAUSAUGMINL5.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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 1).
    Strain: C57BL/6J.
    Tissue: Tongue.
  2. Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
    Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  3. "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] (ISOFORMS 1 AND 2).
    Strain: C57BL/6J and FVB/N.
    Tissue: Brain and Mammary tumor.
  4. "Prediction of the coding sequences of mouse homologues of KIAA gene: III. The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs identified by screening of terminal sequences of cDNA clones randomly sampled from size-fractionated libraries."
    Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S., Saga Y., Nagase T., Ohara O., Koga H.
    DNA Res. 10:167-180(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 71-619.
    Tissue: Embryonic tail.
  5. Okazaki N., Kikuno R., Nagase T., Ohara O., Koga H.
    Submitted (DEC-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: SEQUENCE REVISION.
  6. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Spleen.

Entry informationi

Entry nameiHAUS5_MOUSE
AccessioniPrimary (citable) accession number: Q9D786
Secondary accession number(s): Q08EB3
, Q0VF86, Q5HZI7, Q6ZQ35, Q8CIK2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 7, 2005
Last sequence update: June 1, 2001
Last modified: July 6, 2016
This is version 95 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.