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Protein

HAUS augmin-like complex subunit 6

Gene

HAUS6

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 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. Promotes the nucleation of microtubules from the spindle through recruitment of NEDD1 and gamma-tubulin.3 Publications

GO - Biological processi

  • cell division Source: UniProtKB-KW
  • centrosome organization Source: UniProtKB
  • G2/M transition of mitotic cell cycle Source: Reactome
  • mitotic nuclear division Source: UniProtKB-KW
  • spindle assembly Source: UniProtKB
Complete GO annotation...

Keywords - Biological processi

Cell cycle, Cell division, Mitosis

Enzyme and pathway databases

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

Names & Taxonomyi

Protein namesi
Recommended name:
HAUS augmin-like complex subunit 6
Gene namesi
Name:HAUS6
Synonyms:DGT6, FAM29A, KIAA1574
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 9

Organism-specific databases

HGNCiHGNC:25948. HAUS6.

Subcellular locationi

GO - Cellular componenti

  • centrosome Source: UniProtKB
  • cytoplasm Source: HPA
  • cytosol Source: Reactome
  • HAUS complex Source: UniProtKB
  • microtubule Source: UniProtKB-KW
  • microtubule organizing center Source: HPA
  • nucleoplasm Source: HPA
  • spindle Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton, Microtubule

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA165585815.

Polymorphism and mutation databases

DMDMi85700957.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 955955HAUS augmin-like complex subunit 6PRO_0000076217Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei406 – 4061PhosphoserineCombined sources
Modified residuei507 – 5071PhosphoserineCombined sources
Modified residuei552 – 5521PhosphoserineCombined sources
Modified residuei584 – 5841PhosphothreonineCombined sources
Modified residuei715 – 7151PhosphoserineCombined sources
Modified residuei805 – 8051PhosphoserineCombined sources

Post-translational modificationi

Phosphorylated during mitosis.1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiQ7Z4H7.
MaxQBiQ7Z4H7.
PaxDbiQ7Z4H7.
PRIDEiQ7Z4H7.

PTM databases

iPTMnetiQ7Z4H7.
PhosphoSiteiQ7Z4H7.

Expressioni

Gene expression databases

BgeeiQ7Z4H7.
CleanExiHS_FAM29A.
ExpressionAtlasiQ7Z4H7. baseline and differential.
GenevisibleiQ7Z4H7. HS.

Organism-specific databases

HPAiHPA020960.
HPA020965.

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. Interacts with PLK1 and NEDD1.3 Publications

Protein-protein interaction databases

BioGridi120160. 57 interactions.
DIPiDIP-48830N.
IntActiQ7Z4H7. 49 interactions.
MINTiMINT-4994775.
STRINGi9606.ENSP00000369871.

Structurei

3D structure databases

ProteinModelPortaliQ7Z4H7.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili188 – 21932Sequence analysisAdd
BLAST

Sequence similaritiesi

Belongs to the HAUS6 family.Curated

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiENOG410IIH0. Eukaryota.
ENOG4111YMT. LUCA.
GeneTreeiENSGT00390000008250.
HOVERGENiHBG059896.
InParanoidiQ7Z4H7.
KOiK16589.
OMAiIQMDTEH.
OrthoDBiEOG7XDBHC.
PhylomeDBiQ7Z4H7.
TreeFamiTF325931.

Family and domain databases

InterProiIPR026797. HAUS_6.
IPR028163. HAUS_6_N.
[Graphical view]
PANTHERiPTHR16151. PTHR16151. 1 hit.
PfamiPF14661. HAUS6_N. 1 hit.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q7Z4H7-1) [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
MSSASVTAFE KEHLWMYLQA LGFEPGPATI ACGKIVSHTH LGVNMFDKLN
60 70 80 90 100
RDAFHIISYF LFQVLDQSLT KEVFKFCWPP FDQKSDTEFR KHCCEWIKRI
110 120 130 140 150
SGECGSSFPQ VVGSLFLSPG GPKFIHLMYH FARFVAMKYI KSNSKNSSHH
160 170 180 190 200
FVETFNIKPQ DLHKCIARCH FARSRFLQIL QRQDCVTQKY QENAQLSVKQ
210 220 230 240 250
VRNLRSECIG LENQIKKMEP YDDHSNMEEK IQKVRSLWAS VNETLMFLEK
260 270 280 290 300
EREVVSSVLS LVNQYALDGT NVAINIPRLL LDKIEKQMFQ LHIGNVYEAG
310 320 330 340 350
KLNLLTVIQL LNEVLKVMKY ERCQADQARL TVDLHYLEKE TKFQKERLSD
360 370 380 390 400
LKHMRYRIKD DLTTIRHSVV EKQGEWHKKW KEFLGLSPFS LIKGWTPSVD
410 420 430 440 450
LLPPMSPLSF DPASEEVYAK SILCQYPASL PDAHKQHNQE NGCRGDSDTL
460 470 480 490 500
GALHDLANSP ASFLSQSVSS SDRNSVTVLE KDTKMGTPKE KNEAISKKIP
510 520 530 540 550
EFEVENSPLS DVAKNTESSA FGGSLPAKKS DPFQKEQDHL VEEVARAVLS
560 570 580 590 600
DSPQLSEGKE IKLEELIDSL GSNPFLTRNQ IPRTPENLIT EIRSSWRKAI
610 620 630 640 650
EMEENRTKEP IQMDAEHREV LPESLPVLHN QREFSMADFL LETTVSDFGQ
660 670 680 690 700
SHLTEEKVIS DCECVPQKHV LTSHIDEPPT QNQSDLLNKK VICKQDLECL
710 720 730 740 750
AFTKLSETSR METFSPAVGN RIDVMGGSEE EFMKILDHLE VSCNKPSTNK
760 770 780 790 800
TMLWNSFQIS SGISSKSFKD NDFGILHETL PEEVGHLSFN SSSSSEANFK
810 820 830 840 850
LEPNSPMHGG TLLEDVVGGR QTTPESDFNL QALRSRYEAL KKSLSKKREE
860 870 880 890 900
SYLSNSQTPE RHKPELSPTP QNVQTDDTLN FLDTCDLHTE HIKPSLRTSI
910 920 930 940 950
GERKRSLSPL IKFSPVEQRL RTTIACSLGE LPNLKEEDIL NKSLDAKEPP

SDLTR
Length:955
Mass (Da):108,621
Last modified:January 24, 2006 - v2
Checksum:i8EA52C24BA818C00
GO
Isoform 2 (identifier: Q7Z4H7-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     589-606: ITEIRSSWRKAIEMEENR → SKLIMLSVTFFFHRHNHC
     607-955: Missing.

Show »
Length:606
Mass (Da):69,328
Checksum:i6BA4D3414DC9072C
GO
Isoform 3 (identifier: Q7Z4H7-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     355-389: Missing.

Note: No experimental confirmation available.
Show »
Length:920
Mass (Da):104,310
Checksum:i01F0DAA9DC32D0CB
GO

Sequence cautioni

The sequence AAH26178.1 differs from that shown.Contaminating sequence. Potential poly-A sequence.Curated
The sequence AAI11042.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence BAA90922.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence BAB14334.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence BAB14388.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence BAG63294.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti82 – 821D → E in AAQ09022 (Ref. 1) Curated
Sequence conflicti183 – 1831Missing in AAI11042 (PubMed:15164053).Curated
Sequence conflicti297 – 2971Y → H in BAG63294 (PubMed:14702039).Curated
Sequence conflicti347 – 3471R → G in BAB14334 (PubMed:14702039).Curated
Sequence conflicti409 – 4091S → L in BAB14388 (PubMed:14702039).Curated
Sequence conflicti615 – 6151A → V in AAH10632 (PubMed:15489334).Curated
Sequence conflicti615 – 6151A → V in AAI14493 (PubMed:15489334).Curated
Sequence conflicti686 – 6861L → M in BAB14388 (PubMed:14702039).Curated
Sequence conflicti936 – 9383EED → GKV in BAB14334 (PubMed:14702039).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti552 – 5521S → T.
Corresponds to variant rs41269003 [ dbSNP | Ensembl ].
VAR_062243
Natural varianti674 – 6741H → Q.1 Publication
Corresponds to variant rs10511670 [ dbSNP | Ensembl ].
VAR_024926
Natural varianti761 – 7611S → I.1 Publication
Corresponds to variant rs4977493 [ dbSNP | Ensembl ].
VAR_024927

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei355 – 38935Missing in isoform 3. 1 PublicationVSP_040919Add
BLAST
Alternative sequencei589 – 60618ITEIR…MEENR → SKLIMLSVTFFFHRHNHC in isoform 2. 1 PublicationVSP_017017Add
BLAST
Alternative sequencei607 – 955349Missing in isoform 2. 1 PublicationVSP_017018Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF533709 mRNA. Translation: AAQ09022.1.
AF537091 mRNA. Translation: AAN05700.1.
AK000067 mRNA. Translation: BAA90922.1. Different initiation.
AK022964 mRNA. Translation: BAB14334.1. Different initiation.
AK023068 mRNA. Translation: BAB14388.1. Different initiation.
AK301852 mRNA. Translation: BAG63294.1. Different initiation.
AK056458 mRNA. Translation: BAG51716.1.
AL356000, AL591206 Genomic DNA. Translation: CAH72133.1.
AL591206, AL356000 Genomic DNA. Translation: CAI12264.1.
BC010632 mRNA. Translation: AAH10632.1.
BC026178 mRNA. Translation: AAH26178.1. Sequence problems.
BC065935 mRNA. Translation: AAH65935.1.
BC071625 mRNA. Translation: AAH71625.1.
BC111041 mRNA. Translation: AAI11042.1. Different initiation.
BC113981 mRNA. Translation: AAI13982.1.
BC114492 mRNA. Translation: AAI14493.1.
AB046794 mRNA. Translation: BAB13400.1.
CCDSiCCDS6489.1. [Q7Z4H7-1]
RefSeqiNP_001257819.1. NM_001270890.1. [Q7Z4H7-3]
NP_060115.3. NM_017645.4. [Q7Z4H7-1]
UniGeneiHs.533468.

Genome annotation databases

EnsembliENST00000380502; ENSP00000369871; ENSG00000147874. [Q7Z4H7-1]
GeneIDi54801.
KEGGihsa:54801.
UCSCiuc003znk.5. human. [Q7Z4H7-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF533709 mRNA. Translation: AAQ09022.1.
AF537091 mRNA. Translation: AAN05700.1.
AK000067 mRNA. Translation: BAA90922.1. Different initiation.
AK022964 mRNA. Translation: BAB14334.1. Different initiation.
AK023068 mRNA. Translation: BAB14388.1. Different initiation.
AK301852 mRNA. Translation: BAG63294.1. Different initiation.
AK056458 mRNA. Translation: BAG51716.1.
AL356000, AL591206 Genomic DNA. Translation: CAH72133.1.
AL591206, AL356000 Genomic DNA. Translation: CAI12264.1.
BC010632 mRNA. Translation: AAH10632.1.
BC026178 mRNA. Translation: AAH26178.1. Sequence problems.
BC065935 mRNA. Translation: AAH65935.1.
BC071625 mRNA. Translation: AAH71625.1.
BC111041 mRNA. Translation: AAI11042.1. Different initiation.
BC113981 mRNA. Translation: AAI13982.1.
BC114492 mRNA. Translation: AAI14493.1.
AB046794 mRNA. Translation: BAB13400.1.
CCDSiCCDS6489.1. [Q7Z4H7-1]
RefSeqiNP_001257819.1. NM_001270890.1. [Q7Z4H7-3]
NP_060115.3. NM_017645.4. [Q7Z4H7-1]
UniGeneiHs.533468.

3D structure databases

ProteinModelPortaliQ7Z4H7.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi120160. 57 interactions.
DIPiDIP-48830N.
IntActiQ7Z4H7. 49 interactions.
MINTiMINT-4994775.
STRINGi9606.ENSP00000369871.

PTM databases

iPTMnetiQ7Z4H7.
PhosphoSiteiQ7Z4H7.

Polymorphism and mutation databases

DMDMi85700957.

Proteomic databases

EPDiQ7Z4H7.
MaxQBiQ7Z4H7.
PaxDbiQ7Z4H7.
PRIDEiQ7Z4H7.

Protocols and materials databases

DNASUi54801.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000380502; ENSP00000369871; ENSG00000147874. [Q7Z4H7-1]
GeneIDi54801.
KEGGihsa:54801.
UCSCiuc003znk.5. human. [Q7Z4H7-1]

Organism-specific databases

CTDi54801.
GeneCardsiHAUS6.
HGNCiHGNC:25948. HAUS6.
HPAiHPA020960.
HPA020965.
MIMi613433. gene.
neXtProtiNX_Q7Z4H7.
PharmGKBiPA165585815.
HUGEiSearch...
GenAtlasiSearch...

Phylogenomic databases

eggNOGiENOG410IIH0. Eukaryota.
ENOG4111YMT. LUCA.
GeneTreeiENSGT00390000008250.
HOVERGENiHBG059896.
InParanoidiQ7Z4H7.
KOiK16589.
OMAiIQMDTEH.
OrthoDBiEOG7XDBHC.
PhylomeDBiQ7Z4H7.
TreeFamiTF325931.

Enzyme and pathway databases

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

Miscellaneous databases

ChiTaRSiHAUS6. human.
GeneWikiiFAM29A.
GenomeRNAii54801.
PROiQ7Z4H7.
SOURCEiSearch...

Gene expression databases

BgeeiQ7Z4H7.
CleanExiHS_FAM29A.
ExpressionAtlasiQ7Z4H7. baseline and differential.
GenevisibleiQ7Z4H7. HS.

Family and domain databases

InterProiIPR026797. HAUS_6.
IPR028163. HAUS_6_N.
[Graphical view]
PANTHERiPTHR16151. PTHR16151. 1 hit.
PfamiPF14661. HAUS6_N. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Ding P., Han W., Wang L., Wang Y., Qiu X., Xu M., Ma D.
    Submitted (JUL-2002) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Tissue: Testis.
  2. Guo J.H., Chen L., Yu L.
    Submitted (AUG-2002) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Brain.
  3. "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), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 288-955 (ISOFORM 3), VARIANT GLN-674.
    Tissue: Colon and Teratocarcinoma.
  4. "DNA sequence and analysis of human chromosome 9."
    Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S., Bagguley C.L.
    , Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A., Frankland J.A., French L., Fricker D.G., Garner P., Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S., Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E., Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D., Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E., Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K., Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M., Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J., Dunham I.
    Nature 429:369-374(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "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), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 251-955 (ISOFORM 2), VARIANT ILE-761.
    Tissue: Duodenum, Eye, Skin and Uterus.
  6. "Prediction of the coding sequences of unidentified human genes. XVIII. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro."
    Nagase T., Kikuno R., Nakayama M., Hirosawa M., Ohara O.
    DNA Res. 7:273-281(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 286-955 (ISOFORM 1).
    Tissue: Brain.
  7. "Augmin: a protein complex required for centrosome-independent microtubule generation within the spindle."
    Goshima G., Mayer M., Zhang N., Stuurman N., Vale R.D.
    J. Cell Biol. 181:421-429(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION, SUBCELLULAR LOCATION.
  8. "A probability-based approach for high-throughput protein phosphorylation analysis and site localization."
    Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.
    Nat. Biotechnol. 24:1285-1292(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-552, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  9. "FAM29A promotes microtubule amplification via recruitment of the NEDD1-gamma-tubulin complex to the mitotic spindle."
    Zhu H., Coppinger J.A., Jang C.-Y., Yates J.R. III, Fang G.
    J. Cell Biol. 183:835-848(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH PLK1 AND NEDD1, PHOSPHORYLATION, SUBCELLULAR LOCATION.
  10. "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis."
    Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III
    J. Proteome Res. 7:1346-1351(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-584 AND SER-805, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  11. "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-507, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  12. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-507; SER-552; THR-584 AND SER-715, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  13. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  14. Cited for: IDENTIFICATION IN THE HAUS AUGMIN-LIKE COMPLEX, FUNCTION, SUBCELLULAR LOCATION.
  15. "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.
  16. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
    Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
    Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-406 AND SER-552, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  17. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
    Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-507; SER-552 AND THR-584, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  18. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  19. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
    Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
    Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-552, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiHAUS6_HUMAN
AccessioniPrimary (citable) accession number: Q7Z4H7
Secondary accession number(s): B3KPK4
, B4DX82, Q05CG1, Q14CB6, Q14CD9, Q2TA91, Q6IQ10, Q6NZX5, Q8IZQ4, Q96FN0, Q9H950, Q9H998, Q9HCJ8, Q9NXT8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 24, 2006
Last sequence update: January 24, 2006
Last modified: June 8, 2016
This is version 110 of the entry and version 2 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 9
    Human chromosome 9: 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

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.