O75152 (ZC11A_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Zinc finger CCCH domain-containing protein 11A

Gene names

Name:	ZC3H11A
Synonyms:	KIAA0663, ZC3HDC11A

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	810 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Post-translational modification	Phosphorylated upon DNA damage, probably by ATM or ATR. Ref.5 Ref.6 Ref.7 Ref.8 Ref.9 Ref.10 Ref.11 Ref.12 Ref.13 Ref.14 Ref.15
Sequence similarities	Contains 3 C3H1-type zinc fingers.
Sequence caution	The sequence BAA31638.2 differs from that shown. Reason: Erroneous initiation. The sequence CAH10553.1 differs from that shown. Reason: Contaminating sequence. Potential poly-A sequence.

Ontologies

Keywords
Coding sequence diversity	Polymorphism
Domain	Coiled coil Repeat Zinc-finger
Ligand	Metal-binding Zinc
PTM	Acetylation Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Molecular function	nucleic acid binding Inferred from electronic annotation. Source: InterPro protein binding Inferred from physical interaction. Source: IntAct zinc ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
MLH1	P40692	3	EBI-748480,EBI-744248

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 810	810	Zinc finger CCCH domain-containing protein 11A		PRO_0000213905
Regions
	Zinc finger	2 – 29	28	C3H1-type 1
	Zinc finger	31 – 57	27	C3H1-type 2
	Zinc finger	60 – 86	27	C3H1-type 3
	Coiled coil	362 – 423	62	Potential
	Compositional bias	161 – 168	8	Poly-Asp
Amino acid modifications
	Modified residue	108	1	Phosphoserine Ref.7 Ref.8 Ref.10 Ref.13 Ref.14 Ref.15
	Modified residue	116	1	Phosphoserine Ref.10
	Modified residue	132	1	Phosphoserine Ref.5 Ref.7 Ref.8 Ref.11 Ref.12 Ref.13 Ref.14
	Modified residue	149	1	Phosphoserine Ref.11
	Modified residue	171	1	Phosphoserine Ref.11 Ref.13
	Modified residue	290	1	Phosphoserine Ref.6 Ref.13
	Modified residue	321	1	Phosphothreonine Ref.13
	Modified residue	495	1	Phosphoserine Ref.8
	Modified residue	738	1	Phosphoserine Ref.15
	Modified residue	758	1	Phosphoserine Ref.6 Ref.9 Ref.13
	Modified residue	759	1	Phosphoserine Ref.9 Ref.13
	Modified residue	761	1	Phosphoserine Ref.9
	Modified residue	762	1	Phosphothreonine Ref.9
	Modified residue	764	1	N6-acetyllysine Ref.16
	Modified residue	768	1	Phosphoserine Ref.13
Natural variations
	Natural variant	640	1	T → N. Corresponds to variant rs11240604 [ dbSNP | Ensembl ].		VAR_052967
Experimental info
	Sequence conflict	80	1	C → Y in CAH10553. Ref.3
	Sequence conflict	246	1	P → L in CAH10530. Ref.3
	Sequence conflict	266	1	L → P in CAH10525. Ref.3
	Sequence conflict	277	1	R → G in CAH10530. Ref.3
	Sequence conflict	409	1	V → G in CAH10525. Ref.3
	Sequence conflict	412	1	E → K in CAH10525. Ref.3
	Sequence conflict	616	1	S → P in CAH10566. Ref.3

Sequences

	Sequence		Length	Mass (Da)
	O75152 [UniParc]. Last modified August 16, 2005. Version 3. Checksum: 9048ABC7F4A372FB	FASTA	810	89,131
	10 20 30 40 50 60 MPNQGEDCYF FFYSTCTKGD SCPFRHCEAA IGNETVCTLW QEGRCFRQVC RFRHMEIDKK 70 80 90 100 110 120 RSEIPCYWEN QPTGCQKLNC AFHHNRGRYV DGLFLPPSKT VLPTVPESPE EEVKASQLSV 130 140 150 160 170 180 QQNKLSVQSN PSPQLRSVMK VESSENVPSP THPPVVINAA DDDEDDDDQF SEEGDETKTP 190 200 210 220 230 240 TLQPTPEVHN GLRVTSVRKP AVNIKQGECL NFGIKTLEEI KSKKMKEKSK KQGEGSSGVS 250 260 270 280 290 300 SLLLHPEPVP GPEKENVRTV VRTVTLSTKQ GEEPLVRLSL TERLGKRKFS AGGDSDPPLK 310 320 330 340 350 360 RSLAQRLGKK VEAPETNIDK TPKKAQVSKS LKERLGMSAD PDNEDATDKV NKVGEIHVKT 370 380 390 400 410 420 LEEILLERAS QKRGELQTKL KTEGPSKTDD STSGARSSST IRIKTFSEVL AEKKHRQQEA 430 440 450 460 470 480 ERQKSKKDTT CIKLKIDSEI KKTVVLPPIV ASRGQSEEPA GKTKSMQEVH IKTLEEIKLE 490 500 510 520 530 540 KALRVQQSSE SSTSSPSQHE ATPGARRLLR ITKRTGMKEE KNLQEGNEVD SQSSIRTEAK 550 560 570 580 590 600 EASGETTGVD ITKIQVKRCE TMREKHMQKQ QEREKSVLTP LRGDVASCNT QVAEKPVLTA 610 620 630 640 650 660 VPGITRHLTK RLPTKSSQKV EVETSGIGDS LLNVKCAAQT LEKRGKAKPK VNVKPSVVKV 670 680 690 700 710 720 VSSPKLAPKR KAVEMHAAVI AAVKPLSSSS VLQEPPAKKA AVAVVPLVSE DKSVTVPEAE 730 740 750 760 770 780 NPRDSLVLPP TQSSSDSSPP EVSGPSSSQM SMKTRRLSSA STGKPPLSVE DDFEKLIWEI 790 800 810 SGGKLEAEID LDPGKDEDDL LLELSEMIDS

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Prediction of the coding sequences of unidentified human genes. X. The complete sequences of 100 new cDNA clones from brain which can code for large proteins in vitro." Ishikawa K., Nagase T., Suyama M., Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O. DNA Res. 5:169-176(1998) [PubMed: 9734811] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Brain.
[2]	Ohara O., Suyama M., Nagase T., Ishikawa K. Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases Cited for: SEQUENCE REVISION.
[3]	"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: 17974005] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Fetal kidney and Retina.
[4]	"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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Kidney and Placenta.
[5]	"Large-scale characterization of HeLa cell nuclear phosphoproteins." Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J., Li J., Cohn M.A., Cantley L.C., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004) [PubMed: 15302935] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-132, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[6]	"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: 17081983] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-290 AND SER-758, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[7]	"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: 16964243] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-108 AND SER-132, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[8]	"Phosphoproteome analysis of the human mitotic spindle." Nousiainen M., Sillje H.H.W., Sauer G., Nigg E.A., Koerner R. Proc. Natl. Acad. Sci. U.S.A. 103:5391-5396(2006) [PubMed: 16565220] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-108; SER-132 AND SER-495, MASS SPECTROMETRY. Tissue: Cervix adenocarcinoma.
[9]	"Global proteomic profiling of phosphopeptides using electron transfer dissociation tandem mass spectrometry." Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A. Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007) [PubMed: 17287340] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-758; SER-759; SER-761 AND THR-762, MASS SPECTROMETRY. Tissue: Embryonic kidney.
[10]	"ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage." Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J. Science 316:1160-1166(2007) [PubMed: 17525332] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-108 AND SER-116, MASS SPECTROMETRY. Tissue: Embryonic kidney.
[11]	"Evaluation of the low-specificity protease elastase for large-scale phosphoproteome analysis." Wang B., Malik R., Nigg E.A., Korner R. Anal. Chem. 80:9526-9533(2008) [PubMed: 19007248] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-132; SER-149 AND SER-171, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[12]	"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: 18220336] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-132, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[13]	"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: 18669648] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-108; SER-132; SER-171; SER-290; THR-321; SER-758; SER-759 AND SER-768, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[14]	"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: 19413330] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-108 AND SER-132, MASS SPECTROMETRY. Tissue: Embryonic kidney.
[15]	"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: 19690332] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-108 AND SER-738, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[16]	"Lysine acetylation targets protein complexes and co-regulates major cellular functions." Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T., Olsen J.V., Mann M. Science 325:834-840(2009) [PubMed: 19608861] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-764, MASS SPECTROMETRY.
[17]	"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: 21269460] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AB014563 mRNA. Translation: BAA31638.2. Different initiation. CR627439 mRNA. Translation: CAH10525.1. CR627446 mRNA. Translation: CAH10530.1. BX648271 mRNA. Translation: CAH10553.1. Sequence problems. BX649148 mRNA. Translation: CAH10566.1. BC014268 mRNA. Translation: AAH14268.1.
IPI	IPI00328306.
PIR	T00368.
RefSeq	NP_055642.3. NM_014827.4.
UniGene	Hs.532399.
3D structure databases
ProteinModelPortal	O75152.
SMR	O75152. Positions 6-87.
ModBase	Search...
Protein-protein interaction databases
IntAct	O75152. 1 interaction.
MINT	MINT-1444822.
STRING	O75152.
PTM databases
PhosphoSite	O75152.
Proteomic databases
PRIDE	O75152.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000332127; ENSP00000333253; ENSG00000058673. ENST00000367210; ENSP00000356179; ENSG00000058673. ENST00000367212; ENSP00000356181; ENSG00000058673. ENST00000367214; ENSP00000356183; ENSG00000058673.
GeneID	9877.
KEGG	hsa:9877.
UCSC	uc001hac.1. human.
Organism-specific databases
CTD	9877.
GeneCards	GC01P203765.
H-InvDB	HIX0001492.
HGNC	HGNC:29093. ZC3H11A.
HPA	HPA026439. HPA028490. HPA028526.
MIM	613513. gene.
neXtProt	NX_O75152.
PharmGKB	PA142670535.
HUGE	Search...
GenAtlas	Search...
Phylogenomic databases
eggNOG	prNOG14555.
HOVERGEN	HBG082979.
InParanoid	O75152.
OMA	GKRKFSV.
OrthoDB	EOG4HQDJF.
Gene expression databases
ArrayExpress	O75152.
Bgee	O75152.
CleanEx	HS_ZC3H11A.
Genevestigator	O75152.
GermOnline	ENSG00000058673. Homo sapiens.
Family and domain databases
InterPro	IPR000571. Znf_CCCH. [Graphical view]
SMART	SM00356. ZnF_C3H1. 3 hits. [Graphical view]
PROSITE	PS50103. ZF_C3H1. 2 hits. [Graphical view]
ProtoNet	Search...
Other
NextBio	37225.
SOURCE	Search...

Entry information

Entry name

ZC11A_HUMAN

Accession

Primary (citable) accession number: O75152
Secondary accession number(s): Q6AHY4 , Q6AHY9, Q6AW79, Q6AWA1, Q6PJK4, Q86XZ7

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 16, 2005
Last sequence update:	August 16, 2005
Last modified:	January 25, 2012
This is version 92 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.