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Q9NVM9 (ASUN_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified March 19, 2014. Version 83. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Protein asunder homolog
Alternative name(s):
Cell cycle regulator Mat89Bb homolog
Germ cell tumor 1
Sarcoma antigen NY-SAR-95
Gene names
Name:ASUN
Synonyms:C12orf11, GCT1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length706 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Crucial regulator of the mitotic cell cycle and development. At prophase, required for dynein anchoring to the nuclear envelope important for proper centrosome-nucleus coupling. At G2/M phase, may be required for proper spindle formation and execution of cytokinesis. Ref.6 Ref.12

Subunit structure

Interacts with PAFAH1B1; this interaction may be required for proper recruitment of dynein complexes to the nuclear envelope at prophase. Ref.12

Subcellular location

Cytoplasm Ref.12.

Tissue specificity

Widely expressed. Tends to be up-regulated in seminomas compared to normal testis. Ref.5

Miscellaneous

RNAi in HeLa cells results in a multinucleated phenotype.

Sequence similarities

Belongs to the asunder family.

Sequence caution

The sequence AAO65180.1 differs from that shown. Reason: Frameshift at positions 414, 445, 483, 498 and 507.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

CBFBQ139512EBI-741429,EBI-718750

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 706706Protein asunder homolog
PRO_0000089845

Regions

Coiled coil567 – 62256 Potential

Amino acid modifications

Modified residue6261Phosphoserine Ref.7 Ref.8 Ref.9

Natural variations

Natural variant661M → T.
Corresponds to variant rs2306852 [ dbSNP | Ensembl ].
VAR_050864
Natural variant2271S → P in a colorectal cancer sample; somatic mutation. Ref.13
VAR_035673

Experimental info

Sequence conflict291E → G in BAA91725. Ref.1
Sequence conflict531T → P in BAA91725. Ref.1
Sequence conflict751L → P in BAA91725. Ref.1
Sequence conflict4541K → R in BAA91721. Ref.1
Sequence conflict4571R → P in BAA91721. Ref.1
Sequence conflict4591W → R in BAA91725. Ref.1
Sequence conflict4841E → K in AAO65180. Ref.3
Sequence conflict4901D → N in AAO65180. Ref.3
Sequence conflict6991E → K in AAH03081. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Q9NVM9 [UniParc].

Last modified July 19, 2005. Version 2.
Checksum: 925C733184461EA6

FASTA70680,225
        10         20         30         40         50         60 
MKIFSESHKT VFVVDHCPYM AESCRQHVEF DMLVKNRTQG IIPLAPISKS LWTCSVESSM 

        70         80         90        100        110        120 
EYCRIMYDIF PFKKLVNFIV SDSGAHVLNS WTQEDQNLQE LMAALAAVGP PNPRADPECC 

       130        140        150        160        170        180 
SILHGLVAAV ETLCKITEYQ HEARTLLMEN AERVGNRGRI ICITNAKSDS HVRMLEDCVQ 

       190        200        210        220        230        240 
ETIHEHNKLA ANSDHLMQIQ KCELVLIHTY PVGEDSLVSD RSKKELSPVL TSEVHSVRAG 

       250        260        270        280        290        300 
RHLATKLNIL VQQHFDLAST TITNIPMKEE QHANTSANYD VELLHHKDAH VDFLKSGDSH 

       310        320        330        340        350        360 
LGGGSREGSF KETITLKWCT PRTNNIELHY CTGAYRISPV DVNSRPSSCL TNFLLNGRSV 

       370        380        390        400        410        420 
LLEQPRKSGS KVISHMLSSH GGEIFLHVLS SSRSILEDPP SISEGCGGRV TDYRITDFGE 

       430        440        450        460        470        480 
FMRENRLTPF LDPRYKIDGS LEVPLERAKD QLEKHTRYWP MIISQTTIFN MQAVVPLASV 

       490        500        510        520        530        540 
IVKESLTEED VLNCQKTIYN LVDMERKNDP LPISTVGTRG KGPKRDEQYR IMWNELETLV 

       550        560        570        580        590        600 
RAHINNSEKH QRVLECLMAC RSKPPEEEER KKRGRKREDK EDKSEKAVKD YEQEKSWQDS 

       610        620        630        640        650        660 
ERLKGILERG KEELAEAEII KDSPDSPEPP NKKPLVEMDE TPQVEKSKGP VSLLSLWSNR 

       670        680        690        700 
INTANSRKHQ EFAGRLNSVN NRAELYQHLK EENGMETTEN GKASRQ 

« Hide

References

« Hide 'large scale' references
[1]"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. expand/collapse author list , 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].
[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].
Tissue: Eye and Lymph.
[3]"Immunomic analysis of human sarcoma."
Lee S.-Y., Obata Y., Yoshida M., Stockert E., Williamson B., Jungbluth A.A., Chen Y.-T., Old L.J., Scanlan M.J.
Proc. Natl. Acad. Sci. U.S.A. 100:2651-2656(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 269-513.
[4]"The full-ORF clone resource of the German cDNA consortium."
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I.
BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 568-706.
Tissue: Testis.
[5]"Genomic and expression analysis of the 12p11-p12 amplicon using EST arrays identifies two novel amplified and overexpressed genes."
Bourdon V., Naef F., Rao P.H., Reuter V., Mok S.C., Bosl G.J., Koul S., Murty V.V., Kucherlapati R.S., Chaganti R.S.
Cancer Res. 62:6218-6223(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: TISSUE SPECIFICITY.
[6]"Drosophila genome-scale screen for PAN GU kinase substrates identifies Mat89Bb as a cell cycle regulator."
Lee L.A., Lee E., Anderson M.A., Vardy L., Tahinci E., Ali S.M., Kashevsky H., Benasutti M., Kirschner M.W., Orr-Weaver T.L.
Dev. Cell 8:435-442(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[7]"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-626, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[8]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-626, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[9]"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-626, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[10]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[11]"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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[12]"Human Asunder promotes dynein recruitment and centrosomal tethering to the nucleus at mitotic entry."
Jodoin J.N., Shboul M., Sitaram P., Zein-Sabatto H., Reversade B., Lee E., Lee L.A.
Mol. Biol. Cell 23:4713-4724(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH PAFAH1B1, SUBCELLULAR LOCATION.
[13]"The consensus coding sequences of human breast and colorectal cancers."
Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V. expand/collapse author list , Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., Velculescu V.E.
Science 314:268-274(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT [LARGE SCALE ANALYSIS] PRO-227.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AK001492 mRNA. Translation: BAA91721.1.
AK001499 mRNA. Translation: BAA91725.1.
BC003081 mRNA. Translation: AAH03081.1.
BC008368 mRNA. Translation: AAH08368.1.
AY211927 mRNA. Translation: AAO65180.1. Frameshift.
AL137401 mRNA. Translation: CAB70726.1.
PIRT46457.
RefSeqNP_060634.2. NM_018164.2.
UniGeneHs.505077.

3D structure databases

ProteinModelPortalQ9NVM9.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid120846. 12 interactions.
IntActQ9NVM9. 4 interactions.
MINTMINT-6782559.
STRING9606.ENSP00000261191.

PTM databases

PhosphoSiteQ9NVM9.

Polymorphism databases

DMDM71153010.

Proteomic databases

PaxDbQ9NVM9.
PeptideAtlasQ9NVM9.
PRIDEQ9NVM9.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000261191; ENSP00000261191; ENSG00000064102.
GeneID55726.
KEGGhsa:55726.
UCSCuc001rhk.4. human.

Organism-specific databases

CTD55726.
GeneCardsGC12M027059.
H-InvDBHIX0010501.
HGNCHGNC:20174. ASUN.
HPAHPA039543.
MIM615079. gene.
neXtProtNX_Q9NVM9.
PharmGKBPA134892469.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG301038.
HOGENOMHOG000046389.
InParanoidQ9NVM9.
OMAGRIICLT.
OrthoDBEOG7TF78D.
PhylomeDBQ9NVM9.
TreeFamTF105815.

Gene expression databases

ArrayExpressQ9NVM9.
BgeeQ9NVM9.
CleanExHS_C12orf11.
GenevestigatorQ9NVM9.

Family and domain databases

InterProIPR019355. Cell_cycle_regulator_Mat89Bb.
[Graphical view]
PfamPF10221. DUF2151. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GeneWikiC12orf11.
GenomeRNAi55726.
NextBio60635.
SOURCESearch...

Entry information

Entry nameASUN_HUMAN
AccessionPrimary (citable) accession number: Q9NVM9
Secondary accession number(s): Q86WE2 expand/collapse secondary AC list , Q96HM2, Q9BTX2, Q9NTB6, Q9NVM5
Entry history
Integrated into UniProtKB/Swiss-Prot: July 19, 2005
Last sequence update: July 19, 2005
Last modified: March 19, 2014
This is version 83 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 12

Human chromosome 12: entries, gene names and cross-references to MIM