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Q9BT25

- HAUS8_HUMAN

UniProt

Q9BT25 - HAUS8_HUMAN

Protein

HAUS augmin-like complex subunit 8

Gene

HAUS8

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 85 (01 Oct 2014)
      Sequence version 3 (05 May 2009)
      Previous versions | rss
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    Functioni

    Contributes to mitotic spindle assembly, maintenance of centrosome integrity and completion of cytokinesis as part of the HAUS augmin-like complex.3 Publications

    GO - Biological processi

    1. centrosome organization Source: UniProtKB
    2. mitotic nuclear division Source: UniProtKB-KW
    3. spindle assembly Source: UniProtKB

    Keywords - Biological processi

    Cell cycle, Cell division, Mitosis

    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
    Gene namesi
    Name:HAUS8
    Synonyms:HICE1
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 19

    Organism-specific databases

    HGNCiHGNC:30532. HAUS8.

    Subcellular locationi

    Cytoplasm. Cytoplasmcytoskeletonmicrotubule organizing centercentrosome. Cytoplasmcytoskeletonspindle. Cytoplasmcytoskeletonspindle pole
    Note: During interphase, primarily cytoplasmic and associates with centrosomes and with the mitotic spindles, preferentially at the spindle pole vicinity. During anaphase and telophase, additionally associates with the spindle midzone and midbody, respectively.

    GO - Cellular componenti

    1. centrosome Source: UniProtKB
    2. cytoplasm Source: UniProtKB-SubCell
    3. HAUS complex Source: UniProtKB
    4. microtubule Source: UniProtKB-KW
    5. spindle pole Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasm, Cytoskeleton, Microtubule

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA165393466.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 410409HAUS augmin-like complex subunit 8PRO_0000319937Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanine1 Publication
    Modified residuei105 – 1051Phosphoserine1 Publication

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiQ9BT25.
    PaxDbiQ9BT25.
    PRIDEiQ9BT25.

    PTM databases

    PhosphoSiteiQ9BT25.

    Expressioni

    Gene expression databases

    ArrayExpressiQ9BT25.
    BgeeiQ9BT25.
    GenevestigatoriQ9BT25.

    Organism-specific databases

    HPAiHPA039406.

    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.2 Publications

    Protein-protein interaction databases

    BioGridi125017. 10 interactions.
    DIPiDIP-48834N.
    IntActiQ9BT25. 9 interactions.
    STRINGi9606.ENSP00000253669.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9BT25.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili156 – 20853Sequence AnalysisAdd
    BLAST

    Sequence similaritiesi

    Belongs to the HAUS8 family.Curated

    Keywords - Domaini

    Coiled coil

    Phylogenomic databases

    eggNOGiNOG47763.
    HOGENOMiHOG000112854.
    InParanoidiQ9BT25.
    KOiK16591.
    OMAiESRYLQY.
    OrthoDBiEOG7JHM6B.
    PhylomeDBiQ9BT25.
    TreeFamiTF332998.

    Sequences (3)i

    Sequence statusi: Complete.

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

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q9BT25-1) [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

    MADSSGRGAG KPATGPTNSS SAKKKDKRVQ GGRVIESRYL QYEKKTTQKA    50
    PAGDGSQTRG KMSEGGRKSS LLQKSKADSS GVGKGDLQST LLEGHGTAPP 100
    DLDLSAINDK SIVKKTPQLA KTISKKPEST SFSAPRKKSP DLSEAMEMME 150
    SQTLLLTLLS VKMENNLAEF ERRAEKNLLI MCKEKEKLQK KAHELKRRLL 200
    LSQRKRELAD VLDAQIEMLS PFEAVATRFK EQYRTFATAL DTTRHELPVR 250
    SIHLEGDGQQ LLDALQHELV TTQRLLGELD VGDSEENVQV LDLLSELKDV 300
    TAKKDLELRR SFAQVLELSA EASKEAALAN QEVWEETQGM APPSRWYFNQ 350
    DSACRESGGA PKNTPLSEDD NPGASSAPAQ ATFISPSEDF SSSSQAEVPP 400
    SLSRSGRDLS 410
    Length:410
    Mass (Da):44,857
    Last modified:May 5, 2009 - v3
    Checksum:i05D7B175523E5DA5
    GO
    Isoform 2 (identifier: Q9BT25-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-61: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:349
    Mass (Da):38,464
    Checksum:iA16103E23892C1AC
    GO
    Isoform 3 (identifier: Q9BT25-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         77-77: Missing.

    Note: Gene prediction based on EST data.

    Show »
    Length:409
    Mass (Da):44,786
    Checksum:i414269CC2C9C254F
    GO

    Sequence cautioni

    The sequence AAO65172.1 differs from that shown. Reason: Frameshift at positions 222, 241, 269, 278 and 279.
    The sequence AAH10176.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.
    The sequence AAO65172.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti38 – 381R → P in AAH04398. (PubMed:15489334)Curated
    Sequence conflicti88 – 881Q → QLQ no nucleotide entry (PubMed:18362163)Curated
    Sequence conflicti268 – 2681E → D in AAO65172. (PubMed:12601173)Curated
    Sequence conflicti272 – 2721T → I no nucleotide entry (PubMed:18362163)Curated
    Sequence conflicti272 – 2721T → L in AAO65172. (PubMed:12601173)Curated
    Sequence conflicti275 – 2751L → F no nucleotide entry (PubMed:18362163)Curated
    Sequence conflicti354 – 3552Missing no nucleotide entry (PubMed:18362163)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti83 – 831G → R.2 Publications
    Corresponds to variant rs1130222 [ dbSNP | Ensembl ].
    VAR_039056

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 6161Missing in isoform 2. CuratedVSP_031543Add
    BLAST
    Alternative sequencei77 – 771Missing in isoform 3. CuratedVSP_047167

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK295994 mRNA. Translation: BAG58769.1.
    AC020908 Genomic DNA. No translation available.
    CH471106 Genomic DNA. Translation: EAW84570.1.
    CH471106 Genomic DNA. Translation: EAW84571.1.
    AY211919 mRNA. Translation: AAO65172.1. Sequence problems.
    BC004398 mRNA. Translation: AAH04398.1.
    BC010176 mRNA. Translation: AAH10176.1. Different initiation.
    CCDSiCCDS32948.1. [Q9BT25-1]
    CCDS46009.1. [Q9BT25-3]
    RefSeqiNP_001011699.1. NM_001011699.1. [Q9BT25-3]
    NP_219485.1. NM_033417.1. [Q9BT25-1]
    UniGeneiHs.404088.

    Genome annotation databases

    EnsembliENST00000253669; ENSP00000253669; ENSG00000131351. [Q9BT25-1]
    ENST00000448593; ENSP00000395298; ENSG00000131351. [Q9BT25-3]
    ENST00000593360; ENSP00000470829; ENSG00000131351. [Q9BT25-2]
    GeneIDi93323.
    KEGGihsa:93323.
    UCSCiuc002nfe.3. human. [Q9BT25-1]

    Polymorphism databases

    DMDMi229462967.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK295994 mRNA. Translation: BAG58769.1 .
    AC020908 Genomic DNA. No translation available.
    CH471106 Genomic DNA. Translation: EAW84570.1 .
    CH471106 Genomic DNA. Translation: EAW84571.1 .
    AY211919 mRNA. Translation: AAO65172.1 . Sequence problems.
    BC004398 mRNA. Translation: AAH04398.1 .
    BC010176 mRNA. Translation: AAH10176.1 . Different initiation.
    CCDSi CCDS32948.1. [Q9BT25-1 ]
    CCDS46009.1. [Q9BT25-3 ]
    RefSeqi NP_001011699.1. NM_001011699.1. [Q9BT25-3 ]
    NP_219485.1. NM_033417.1. [Q9BT25-1 ]
    UniGenei Hs.404088.

    3D structure databases

    ProteinModelPortali Q9BT25.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 125017. 10 interactions.
    DIPi DIP-48834N.
    IntActi Q9BT25. 9 interactions.
    STRINGi 9606.ENSP00000253669.

    PTM databases

    PhosphoSitei Q9BT25.

    Polymorphism databases

    DMDMi 229462967.

    Proteomic databases

    MaxQBi Q9BT25.
    PaxDbi Q9BT25.
    PRIDEi Q9BT25.

    Protocols and materials databases

    DNASUi 93323.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000253669 ; ENSP00000253669 ; ENSG00000131351 . [Q9BT25-1 ]
    ENST00000448593 ; ENSP00000395298 ; ENSG00000131351 . [Q9BT25-3 ]
    ENST00000593360 ; ENSP00000470829 ; ENSG00000131351 . [Q9BT25-2 ]
    GeneIDi 93323.
    KEGGi hsa:93323.
    UCSCi uc002nfe.3. human. [Q9BT25-1 ]

    Organism-specific databases

    CTDi 93323.
    GeneCardsi GC19M017160.
    H-InvDB HIX0014879.
    HGNCi HGNC:30532. HAUS8.
    HPAi HPA039406.
    MIMi 613434. gene.
    neXtProti NX_Q9BT25.
    PharmGKBi PA165393466.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG47763.
    HOGENOMi HOG000112854.
    InParanoidi Q9BT25.
    KOi K16591.
    OMAi ESRYLQY.
    OrthoDBi EOG7JHM6B.
    PhylomeDBi Q9BT25.
    TreeFami TF332998.

    Miscellaneous databases

    ChiTaRSi HAUS8. human.
    GenomeRNAii 93323.
    NextBioi 78044.
    PROi Q9BT25.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9BT25.
    Bgeei Q9BT25.
    Genevestigatori Q9BT25.

    Family and domain databases

    ProtoNeti Search...

    Publicationsi

    1. "Hice1, a novel microtubule-associated protein required for maintenance of spindle integrity and chromosomal stability in human cells."
      Wu G., Lin Y.-T., Wei R., Chen Y., Shan Z., Lee W.-H.
      Mol. Cell. Biol. 28:3652-3662(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, SUBCELLULAR LOCATION, VARIANT ARG-83.
    2. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
      Tissue: Subthalamic nucleus.
    3. "The DNA sequence and biology of human chromosome 19."
      Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S., Carrano A.V.
      , Caoile C., Chan Y.M., Christensen M., Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E., Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M., Rubin E.M., Lucas S.M.
      Nature 428:529-535(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-283 (ISOFORM 1).
    6. "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] OF 2-410 (ISOFORM 1), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 152-410 (ISOFORMS 1/2), VARIANT ARG-83.
      Tissue: Eye and Placenta.
    7. "Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
      Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
      Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-105, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    8. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
      Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
      Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
    9. Cited for: IDENTIFICATION IN THE HAUS AUGMIN-LIKE COMPLEX, FUNCTION, SUBCELLULAR LOCATION.
    10. "The augmin complex plays a critical role in spindle microtubule generation for mitotic progression and cytokinesis in human cells."
      Uehara R., Nozawa R.-S., Tomioka A., Petry S., Vale R.D., Obuse C., Goshima G.
      Proc. Natl. Acad. Sci. U.S.A. 106:6998-7003(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION IN THE HAUS AUGMIN-LIKE COMPLEX, FUNCTION, SUBCELLULAR LOCATION.
    11. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiHAUS8_HUMAN
    AccessioniPrimary (citable) accession number: Q9BT25
    Secondary accession number(s): B4DJA7
    , C9JBZ4, Q49AC4, Q86WF0, Q96FX3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 26, 2008
    Last sequence update: May 5, 2009
    Last modified: October 1, 2014
    This is version 85 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome 19
      Human chromosome 19: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3