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Protein

HAUS augmin-like complex subunit 8

Gene

Haus8

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

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 8
Alternative name(s):
HEC1/NDC80-interacting centrosome-associated protein 1
Sarcoma antigen NY-SAR-48 homolog
Gene namesi
Name:Haus8
Synonyms:Hice1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 8

Organism-specific databases

MGIiMGI:1923728. Haus8.

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 – 373372HAUS augmin-like complex subunit 8PRO_0000319938Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanineBy similarity
Modified residuei99 – 991PhosphoserineBy similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiQ99L00.
MaxQBiQ99L00.
PaxDbiQ99L00.
PRIDEiQ99L00.

PTM databases

iPTMnetiQ99L00.
PhosphoSiteiQ99L00.

Expressioni

Gene expression databases

BgeeiQ99L00.
CleanExiMM_2410004L22RIK.
ExpressionAtlasiQ99L00. baseline and differential.
GenevisibleiQ99L00. 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. Associates with microtubules. The interaction with microtubules is strong during mitosis, while it is weak or absent during interphase. It is unclear whether this interaction is direct or indirect (By similarity).By similarity

Protein-protein interaction databases

BioGridi218144. 5 interactions.
IntActiQ99L00. 5 interactions.
STRINGi10090.ENSMUSP00000040802.

Family & Domainsi

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili130 – 20475Sequence analysisAdd
BLAST

Sequence similaritiesi

Belongs to the HAUS8 family.Curated

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiENOG410IEK2. Eukaryota.
ENOG4112BWM. LUCA.
GeneTreeiENSGT00390000010974.
HOGENOMiHOG000112854.
InParanoidiQ99L00.
KOiK16591.
OMAiESRYLQY.
PhylomeDBiQ99L00.
TreeFamiTF332998.

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: Q99L00-1) [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
MADSSERDAG KSAAAGACAV PKTKGRRVQG RRVVESRYLQ YDKKAKKVSG
60 70 80 90 100
AAKEEKPPEG RKASTVPRSR EESQVMGTGN LQSTMLEGHG MNPPDLDLSA
110 120 130 140 150
IDDKILSRKA SWPDREMTDK AKSTSFISCD KKRILRKKRR DLQETMDMME
160 170 180 190 200
SQTLLMTLLS VKMENNLALL EERAEKDLAA MCHEKERLQR QALELRRQLL
210 220 230 240 250
LRQKHQELAA TLDAQIEVLS PLQPVLERFK EEYMTLGRAL DTTRHELPMQ
260 270 280 290 300
AVHMEGSGQE LLDDLEPALR ITLQLLGDLS ICSPYATAQV QGASAQEPGA
310 320 330 340 350
STQLSCLLKE LKGLVTEKDL ELRRLVSQVV ELSSQASKEA ALMNQEVWEE
360 370
AEGALTSSQW YFSPDACRDD SPS
Length:373
Mass (Da):41,653
Last modified:February 26, 2008 - v2
Checksum:i9F9896D057BD885E
GO
Isoform 2 (identifier: Q99L00-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     71-71: Missing.

Show »
Length:372
Mass (Da):41,524
Checksum:i1AB41E066AEEA7B4
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti50 – 501G → V in AAH03935 (PubMed:15489334).Curated
Sequence conflicti259 – 2591Q → R in BAB26909 (PubMed:16141072).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei71 – 711Missing in isoform 2. 1 PublicationVSP_031544

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK010398 mRNA. Translation: BAB26909.1.
BC003935 mRNA. Translation: AAH03935.1.
CCDSiCCDS22389.1. [Q99L00-2]
CCDS52579.1. [Q99L00-1]
RefSeqiNP_001156514.1. NM_001163042.1. [Q99L00-1]
NP_083897.2. NM_029621.3. [Q99L00-2]
UniGeneiMm.27355.

Genome annotation databases

EnsembliENSMUST00000035960; ENSMUSP00000040802; ENSMUSG00000035439. [Q99L00-1]
ENSMUST00000110071; ENSMUSP00000105698; ENSMUSG00000035439. [Q99L00-2]
GeneIDi76478.
KEGGimmu:76478.
UCSCiuc009mcg.2. mouse. [Q99L00-2]
uc009mch.2. mouse. [Q99L00-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK010398 mRNA. Translation: BAB26909.1.
BC003935 mRNA. Translation: AAH03935.1.
CCDSiCCDS22389.1. [Q99L00-2]
CCDS52579.1. [Q99L00-1]
RefSeqiNP_001156514.1. NM_001163042.1. [Q99L00-1]
NP_083897.2. NM_029621.3. [Q99L00-2]
UniGeneiMm.27355.

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi218144. 5 interactions.
IntActiQ99L00. 5 interactions.
STRINGi10090.ENSMUSP00000040802.

PTM databases

iPTMnetiQ99L00.
PhosphoSiteiQ99L00.

Proteomic databases

EPDiQ99L00.
MaxQBiQ99L00.
PaxDbiQ99L00.
PRIDEiQ99L00.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000035960; ENSMUSP00000040802; ENSMUSG00000035439. [Q99L00-1]
ENSMUST00000110071; ENSMUSP00000105698; ENSMUSG00000035439. [Q99L00-2]
GeneIDi76478.
KEGGimmu:76478.
UCSCiuc009mcg.2. mouse. [Q99L00-2]
uc009mch.2. mouse. [Q99L00-1]

Organism-specific databases

CTDi93323.
MGIiMGI:1923728. Haus8.

Phylogenomic databases

eggNOGiENOG410IEK2. Eukaryota.
ENOG4112BWM. LUCA.
GeneTreeiENSGT00390000010974.
HOGENOMiHOG000112854.
InParanoidiQ99L00.
KOiK16591.
OMAiESRYLQY.
PhylomeDBiQ99L00.
TreeFamiTF332998.

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

PROiQ99L00.
SOURCEiSearch...

Gene expression databases

BgeeiQ99L00.
CleanExiMM_2410004L22RIK.
ExpressionAtlasiQ99L00. baseline and differential.
GenevisibleiQ99L00. MM.

Family and domain databases

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).
    Strain: C57BL/6J.
  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).
    Tissue: Mammary tumor.
  3. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Spleen.

Entry informationi

Entry nameiHAUS8_MOUSE
AccessioniPrimary (citable) accession number: Q99L00
Secondary accession number(s): Q9CWT4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 26, 2008
Last sequence update: February 26, 2008
Last modified: June 8, 2016
This is version 84 of the entry and version 2 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.