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Q96A19 (C102A_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 74. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Coiled-coil domain-containing protein 102A
Gene names
Name:CCDC102A
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length550 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

Ontologies

Keywords
   DomainCoiled coil
   PTMPhosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
None. [Check GOA]

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 550550Coiled-coil domain-containing protein 102A
PRO_0000274400

Regions

Coiled coil72 – 16190 Potential
Coiled coil263 – 396134 Potential
Coiled coil427 – 51892 Potential
Compositional bias27 – 6135Pro-rich

Amino acid modifications

Modified residue261Phosphoserine Ref.3 Ref.4
Modified residue281Phosphoserine Ref.3 Ref.4

Experimental info

Sequence conflict961R → W in AAH08285. Ref.2
Sequence conflict961R → W in AAH09941. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Q96A19 [UniParc].

Last modified May 18, 2010. Version 2.
Checksum: FB8D693B4B7E580A

FASTA55062,596
        10         20         30         40         50         60 
MSHGPSPRLA ESPQLSKGSL LTILGSPSPE RMGPADSLPP TPPSGTPSPG PPPALPLPPA 

        70         80         90        100        110        120 
PALLADGDWE SREELRLREL EEARARAAQM EKTMRRWSDC TANWREKWSK VRAERNRARE 

       130        140        150        160        170        180 
EVRQLRQRLD ALTKELAGAR RERQEAQGEC EARGRELARL RGARGVADQT RDGPEPEAER 

       190        200        210        220        230        240 
EPVRDVGSER PPGSQELELV ESLLKSMPEE SEDCWEARSL GAGGPRGSSG RQERSRLPWE 

       250        260        270        280        290        300 
DTAATEEEAS KLTALRLRLD ESQKVLLKER EDKLALSRNI EKLEGELSQW KIKYEELSKT 

       310        320        330        340        350        360 
KQEMLKQLSI LKEAHQDELG RMSEDLEDEL GARSSMDRKM AELRGEMERL QAENAAEWGR 

       370        380        390        400        410        420 
RERLETEKLG LERENKKLRA QVGDLEEALA RRRRQTASAL DCDLRASQAA LFEKNKELAD 

       430        440        450        460        470        480 
LKHVHGKLKK QFQEKVAELA HANRRVEQHE AEVKKLRLRV EELKKELAQA EDELDEAHNQ 

       490        500        510        520        530        540 
ARKLQRSLDE QTEQSENLQV QLEHLQSRLR RQQQNAPLFG KIRSARFGTE EAEDGTSDLD 

       550 
EDEDLQIQVA 

« Hide

References

[1]"The sequence and analysis of duplication-rich human chromosome 16."
Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G., Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E., Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J. expand/collapse author list , Buckingham J.M., Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C., Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M., Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M., Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E., Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H., Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y., Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J., Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D., Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S., Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A., Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M., Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H., Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A., Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J., DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J., Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M., Myers R.M., Rubin E.M., Pennacchio L.A.
Nature 432:988-994(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[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: Brain, Placenta and Uterus.
[3]"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-26 AND SER-28, MASS SPECTROMETRY.
Tissue: Cervix carcinoma.
[4]"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-26 AND SER-28, MASS SPECTROMETRY.
Tissue: Cervix carcinoma.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AC004382 Genomic DNA. No translation available.
BC004307 mRNA. Translation: AAH04307.1.
BC008285 mRNA. Translation: AAH08285.1.
BC009941 mRNA. Translation: AAH09941.1.
IPIIPI00059169.
RefSeqNP_149989.2. NM_033212.3.
UniGeneHs.644611.

3D structure databases

ProteinModelPortalQ96A19.
SMRQ96A19. Positions 360-502.
ModBaseSearch...

Protein-protein interaction databases

STRING9606.ENSP00000258214.

PTM databases

PhosphoSiteQ96A19.

Polymorphism databases

DMDM296434412.

Proteomic databases

PaxDbQ96A19.
PRIDEQ96A19.

Protocols and materials databases

DNASU92922.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000258214; ENSP00000258214; ENSG00000135736.
GeneID92922.
KEGGhsa:92922.
UCSCuc002elw.3. human.

Organism-specific databases

CTD92922.
GeneCardsGC16M057546.
H-InvDBHIX0013076.
HGNCHGNC:28097. CCDC102A.
HPAHPA040598.
HPA040958.
neXtProtNX_Q96A19.
PharmGKBPA144596469.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG131045.
HOGENOMHOG000008304.
HOVERGENHBG080941.
InParanoidQ96A19.
KOK16759.
OMAKSMPEES.
OrthoDBEOG4W9J42.
PhylomeDBQ96A19.

Gene expression databases

BgeeQ96A19.
CleanExHS_CCDC102A.
GenevestigatorQ96A19.

Family and domain databases

ProtoNetSearch...

Other

GenomeRNAi92922.
NextBio77916.

Entry information

Entry nameC102A_HUMAN
AccessionPrimary (citable) accession number: Q96A19
Secondary accession number(s): Q9BT74
Entry history
Integrated into UniProtKB/Swiss-Prot: February 6, 2007
Last sequence update: May 18, 2010
Last modified: May 1, 2013
This is version 74 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

Human chromosome 16

Human chromosome 16: entries, gene names and cross-references to MIM