Q5T200 (ZC3HD_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Zinc finger CCCH domain-containing protein 13

Gene names

Name:	ZC3H13
Synonyms:	KIAA0853

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	1668 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.6 Ref.7 Ref.8 Ref.9 Ref.10 Ref.11 Ref.12 Ref.13 Ref.14 Ref.15 Ref.16
Sequence similarities	Contains 1 C3H1-type zinc finger.

Ontologies

Keywords
Coding sequence diversity	Alternative splicing Polymorphism
Domain	Coiled coil Repeat Zinc-finger
Ligand	Metal-binding Zinc
PTM	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
SCHIP1	Q9P0W5	2	EBI-2679720,EBI-1397509

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q5T200-1)

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.

Note: Gene prediction confirmed by EST data.

Isoform 2 (identifier: Q5T200-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1440-1440: E → EA
     1558-1563: DADNLF → GSFILL
     1564-1668: Missing.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 1668	1668	Zinc finger CCCH domain-containing protein 13		PRO_0000050778
Regions
	Zinc finger	36 – 64	29	C3H1-type
	Coiled coil	645 – 789	145	Potential
	Coiled coil	1300 – 1366	67	Potential
	Compositional bias	204 – 242	39	Ser-rich
	Compositional bias	316 – 349	34	Ser-rich
	Compositional bias	350 – 652	303	Arg/Ser-rich
	Compositional bias	653 – 842	190	Arg/Glu-rich
	Compositional bias	957 – 1028	72	Lys-rich
	Compositional bias	1189 – 1295	107	Ser-rich
Amino acid modifications
	Modified residue	64	1	Phosphoserine Ref.8
	Modified residue	77	1	Phosphoserine Ref.8
	Modified residue	198	1	Phosphoserine Ref.8 Ref.14
	Modified residue	207	1	Phosphoserine Ref.6 Ref.8 Ref.14 Ref.15
	Modified residue	209	1	Phosphoserine Ref.6 Ref.8 Ref.14 Ref.15
	Modified residue	238	1	Phosphoserine Ref.10 Ref.15
	Modified residue	241	1	Phosphoserine Ref.10
	Modified residue	242	1	Phosphoserine Ref.7 Ref.14 Ref.15 Ref.16
	Modified residue	263	1	Phosphothreonine Ref.7 Ref.8 Ref.9 Ref.14 Ref.15
	Modified residue	265	1	Phosphoserine Ref.7 Ref.8 Ref.9 Ref.14 Ref.15
	Modified residue	316	1	Phosphoserine Ref.8
	Modified residue	317	1	Phosphothreonine Ref.8 Ref.15
	Modified residue	318	1	Phosphoserine Ref.14 Ref.15
	Modified residue	325	1	Phosphoserine Ref.8 Ref.14 Ref.15
	Modified residue	354	1	Phosphothreonine Ref.9 Ref.14
	Modified residue	356	1	Phosphoserine Ref.9 Ref.14
	Modified residue	364	1	Phosphothreonine Ref.14
	Modified residue	370	1	Phosphoserine Ref.14 Ref.15
	Modified residue	372	1	Phosphoserine Ref.14 Ref.15
	Modified residue	381	1	Phosphoserine Ref.14 Ref.15
	Modified residue	492	1	Phosphoserine Ref.8
	Modified residue	581	1	Phosphoserine Ref.11
	Modified residue	831	1	Phosphoserine Ref.14
	Modified residue	833	1	Phosphoserine Ref.14
	Modified residue	837	1	Phosphoserine Ref.14
	Modified residue	845	1	Phosphoserine Ref.14
	Modified residue	848	1	Phosphoserine Ref.14
	Modified residue	853	1	Phosphoserine Ref.14
	Modified residue	875	1	Phosphoserine Ref.8 Ref.14 Ref.15
	Modified residue	877	1	Phosphoserine Ref.8 Ref.12 Ref.14 Ref.15
	Modified residue	984	1	Phosphothreonine Ref.15
	Modified residue	986	1	Phosphoserine Ref.14 Ref.15 Ref.16
	Modified residue	993	1	Phosphoserine Ref.8 Ref.9 Ref.13 Ref.14 Ref.15 Ref.16
	Modified residue	1010	1	Phosphoserine Ref.14
	Modified residue	1014	1	Phosphoserine Ref.14 Ref.15 Ref.16
	Modified residue	1017	1	Phosphoserine Ref.14 Ref.15 Ref.16
	Modified residue	1056	1	Phosphoserine Ref.11
	Modified residue	1208	1	Phosphoserine Ref.12
	Modified residue	1279	1	Phosphoserine Ref.8
	Modified residue	1288	1	Phosphoserine Ref.8
	Modified residue	1318	1	Phosphothreonine Ref.8
	Modified residue	1364	1	Phosphoserine Ref.16
	Modified residue	1382	1	Phosphoserine Ref.11
	Modified residue	1657	1	Phosphoserine Ref.11
Natural variations
	Alternative sequence	1440	1	E → EA in isoform 2.		VSP_027202
	Alternative sequence	1558 – 1563	6	DADNLF → GSFILL in isoform 2.		VSP_014252
	Alternative sequence	1564 – 1668	105	Missing in isoform 2.		VSP_014253
	Natural variant	1429	1	E → D. Ref.1 Ref.3 Ref.4 Ref.5 Corresponds to variant rs9534264 [ dbSNP | Ensembl ].		VAR_022727
Experimental info
	Sequence conflict	702 – 704	3	EKE → KAR in BAA74876. Ref.5
	Sequence conflict	967	1	I → K in CAD38544. Ref.3

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified December 21, 2004. Version 1. Checksum: B7E8118D3B5954D6	FASTA	1,668	196,635
	10 20 30 40 50 60 MSKIRRKVTV ENTKTISDST SRRPSVFERL GPSTGSTAET QCRNWLKTGN CLYGNTCRFV 70 80 90 100 110 120 HGPSPRGKGY SSNYRRSPER PTGDLRERMK NKRQDVDTEP QKRNTEESSS PVRKESSRGR 130 140 150 160 170 180 HREKEDIKIT KERTPESEEE NVEWETNRDD SDNGDINYDY VHELSLEMKR QKIQRELMKL 190 200 210 220 230 240 EQENMEKREE IIIKKEVSPE VVRSKLSPSP SLRKSSKSPK RKSSPKSSSA SKKDRKTSAV 250 260 270 280 290 300 SSPLLDQQRN SKTNQSKKKG PRTPSPPPPI PEDIALGKKY KEKYKVKDRI EEKTRDGKDR 310 320 330 340 350 360 GRDFERQREK RDKPRSTSPA GQHHSPISSR HHSSSSQSGS SIQRHSPSPR RKRTPSPSYQ 370 380 390 400 410 420 RTLTPPLRRS ASPYPSHSLS SPQRKQSPPR HRSPMREKGR HDHERTSQSH DRRHERREDT 430 440 450 460 470 480 RGKRDREKDS REEREYEQDQ SSSRDHRDDR EPRDGRDRRD ARDTRDRREL RDSRDMRDSR 490 500 510 520 530 540 EMRDYSRDTK ESRDPRDSRS TRDAHDYRDR EGRDTHRKED TYPEESRSYG RNHLREESSR 550 560 570 580 590 600 TEIRNESRNE SRSEIRNDRM GRSRGRVPEL PEKGSRGSRG SQIDSHSSNS NYHDSWETRS 610 620 630 640 650 660 SYPERDRYPE RDNRDQARDS SFERRHGERD RRDNRERDQR PSSPIRHQGR NDELERDERR 670 680 690 700 710 720 EERRVDRVDD RRDERARERD RERERDRERE RERERERDRE REKERELERE RARERERERE 730 740 750 760 770 780 KERDRERDRD RDHDRERERE RERDREKERE REREERERER ERERERERER ERERERARER 790 800 810 820 830 840 DKERERQRDW EDKDKGRDDR REKREEIRED RNPRDGHDER KSKKRYRNEG SPSPRQSPKR 850 860 870 880 890 900 RREHSPDSDA YNSGDDKNEK HRLLSQVVRP QESRSLSPSH LTEDRQGRWK EEDRKPERKE 910 920 930 940 950 960 SSRRYEEQEL KEKVSSVDKQ REQTEILESS RMRAQDIIGH HQSEDRETSD RAHDENKKKA 970 980 990 1000 1010 1020 KIQKKPIKKK KEDDVGIERG NIETTSEDGQ VFSPKKGQKK KSIEKKRKKS KGDSDISDEE 1030 1040 1050 1060 1070 1080 AAQQSKKKRG PRTPPITTKE ELVEMCNGKN GILEDSQKKE DTAFSDWSDE DVPDRTEVTE 1090 1100 1110 1120 1130 1140 AEHTATATTP GSTPSPLSSL LPPPPPVATA TATTVPATLA ATTAAAATSF STSAITISTS 1150 1160 1170 1180 1190 1200 ATPTNTTNNT FANEDSHRKC HRTRVEKVET PHVTIEDAQH RKPMDQKRSS SLGSNRSNRS 1210 1220 1230 1240 1250 1260 HTSGRLRSPS NDSAHRSGDD QSGRKRVLHS GSRDREKTKS LEITGERKSR IDQLKRGEPS 1270 1280 1290 1300 1310 1320 RSTSSDRQDS RSHSSRRSSP ESDRQVHSRS GSFDSRDRLQ ERDRYEHDRE RERERRDTRQ 1330 1340 1350 1360 1370 1380 REWDRDADKD WPRNRDRDRL RERERERERD KRRDLDRERE RLISDSVERD RDRDRDRTFE 1390 1400 1410 1420 1430 1440 SSQIESVKRC EAKLEGEHER DLESTSRDSL ALDKERMDKD LGSVQGFEET NKSERTESLE 1450 1460 1470 1480 1490 1500 GDDESKLDDA HSLGSGAGEG YEPISDDELD EILAGDAEKR EDQQDEEKMP DPLDVIDVDW 1510 1520 1530 1540 1550 1560 SGLMPKHPKE PREPGAALLK FTPGAVMLRV GISKKLAGSE LFAKVKETCQ RLLEKPKDAD 1570 1580 1590 1600 1610 1620 NLFEHELGAL NMAALLRKEE RASLLSNLGP CCKALCFRRD SAIRKQLVKN EKGTIKQAYT 1630 1640 1650 1660 SAPMVDNELL RLSLRLFKRK TTCHAPGHEK TEDNKLSQSS IQQELCVS
	Isoform 2 [UniParc]. Checksum: EDF7A3EA9DB7448B	FASTA	1,564	184,869
	10 20 30 40 50 60 MSKIRRKVTV ENTKTISDST SRRPSVFERL GPSTGSTAET QCRNWLKTGN CLYGNTCRFV 70 80 90 100 110 120 HGPSPRGKGY SSNYRRSPER PTGDLRERMK NKRQDVDTEP QKRNTEESSS PVRKESSRGR 130 140 150 160 170 180 HREKEDIKIT KERTPESEEE NVEWETNRDD SDNGDINYDY VHELSLEMKR QKIQRELMKL 190 200 210 220 230 240 EQENMEKREE IIIKKEVSPE VVRSKLSPSP SLRKSSKSPK RKSSPKSSSA SKKDRKTSAV 250 260 270 280 290 300 SSPLLDQQRN SKTNQSKKKG PRTPSPPPPI PEDIALGKKY KEKYKVKDRI EEKTRDGKDR 310 320 330 340 350 360 GRDFERQREK RDKPRSTSPA GQHHSPISSR HHSSSSQSGS SIQRHSPSPR RKRTPSPSYQ 370 380 390 400 410 420 RTLTPPLRRS ASPYPSHSLS SPQRKQSPPR HRSPMREKGR HDHERTSQSH DRRHERREDT 430 440 450 460 470 480 RGKRDREKDS REEREYEQDQ SSSRDHRDDR EPRDGRDRRD ARDTRDRREL RDSRDMRDSR 490 500 510 520 530 540 EMRDYSRDTK ESRDPRDSRS TRDAHDYRDR EGRDTHRKED TYPEESRSYG RNHLREESSR 550 560 570 580 590 600 TEIRNESRNE SRSEIRNDRM GRSRGRVPEL PEKGSRGSRG SQIDSHSSNS NYHDSWETRS 610 620 630 640 650 660 SYPERDRYPE RDNRDQARDS SFERRHGERD RRDNRERDQR PSSPIRHQGR NDELERDERR 670 680 690 700 710 720 EERRVDRVDD RRDERARERD RERERDRERE RERERERDRE REKERELERE RARERERERE 730 740 750 760 770 780 KERDRERDRD RDHDRERERE RERDREKERE REREERERER ERERERERER ERERERARER 790 800 810 820 830 840 DKERERQRDW EDKDKGRDDR REKREEIRED RNPRDGHDER KSKKRYRNEG SPSPRQSPKR 850 860 870 880 890 900 RREHSPDSDA YNSGDDKNEK HRLLSQVVRP QESRSLSPSH LTEDRQGRWK EEDRKPERKE 910 920 930 940 950 960 SSRRYEEQEL KEKVSSVDKQ REQTEILESS RMRAQDIIGH HQSEDRETSD RAHDENKKKA 970 980 990 1000 1010 1020 KIQKKPIKKK KEDDVGIERG NIETTSEDGQ VFSPKKGQKK KSIEKKRKKS KGDSDISDEE 1030 1040 1050 1060 1070 1080 AAQQSKKKRG PRTPPITTKE ELVEMCNGKN GILEDSQKKE DTAFSDWSDE DVPDRTEVTE 1090 1100 1110 1120 1130 1140 AEHTATATTP GSTPSPLSSL LPPPPPVATA TATTVPATLA ATTAAAATSF STSAITISTS 1150 1160 1170 1180 1190 1200 ATPTNTTNNT FANEDSHRKC HRTRVEKVET PHVTIEDAQH RKPMDQKRSS SLGSNRSNRS 1210 1220 1230 1240 1250 1260 HTSGRLRSPS NDSAHRSGDD QSGRKRVLHS GSRDREKTKS LEITGERKSR IDQLKRGEPS 1270 1280 1290 1300 1310 1320 RSTSSDRQDS RSHSSRRSSP ESDRQVHSRS GSFDSRDRLQ ERDRYEHDRE RERERRDTRQ 1330 1340 1350 1360 1370 1380 REWDRDADKD WPRNRDRDRL RERERERERD KRRDLDRERE RLISDSVERD RDRDRDRTFE 1390 1400 1410 1420 1430 1440 SSQIESVKRC EAKLEGEHER DLESTSRDSL ALDKERMDKD LGSVQGFEET NKSERTESLE 1450 1460 1470 1480 1490 1500 AGDDESKLDD AHSLGSGAGE GYEPISDDEL DEILAGDAEK REDQQDEEKM PDPLDVIDVD 1510 1520 1530 1540 1550 1560 WSGLMPKHPK EPREPGAALL KFTPGAVMLR VGISKKLAGS ELFAKVKETC QRLLEKPKGS FILL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	Shan Y.X., Yu L. Submitted (APR-2003) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), VARIANT ASP-1429.
[2]	"The DNA sequence and analysis of human chromosome 13." Dunham A., Matthews L.H., Burton J., Ashurst J.L., Howe K.L., Ashcroft K.J., Beare D.M., Burford D.C., Hunt S.E., Griffiths-Jones S., Jones M.C., Keenan S.J., Oliver K., Scott C.E., Ainscough R., Almeida J.P., Ambrose K.D., Andrews D.T. , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Bannerjee R., Barlow K.F., Bates K., Beasley H., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burrill W., Carder C., Carter N.P., Chapman J.C., Clamp M.E., Clark S.Y., Clarke G., Clee C.M., Clegg S.C., Cobley V., Collins J.E., Corby N., Coville G.J., Deloukas P., Dhami P., Dunham I., Dunn M., Earthrowl M.E., Ellington A.G., Faulkner L., Frankish A.G., Frankland J., French L., Garner P., Garnett J., Gilbert J.G.R., Gilson C.J., Ghori J., Grafham D.V., Gribble S.M., Griffiths C., Hall R.E., Hammond S., Harley J.L., Hart E.A., Heath P.D., Howden P.J., Huckle E.J., Hunt P.J., Hunt A.R., Johnson C., Johnson D., Kay M., Kimberley A.M., King A., Laird G.K., Langford C.J., Lawlor S., Leongamornlert D.A., Lloyd D.M., Lloyd C., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., McLaren S.J., McMurray A., Milne S., Moore M.J.F., Nickerson T., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K.M., Rice C.M., Searle S., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Steward C.A., Sycamore N., Tester J., Thomas D.W., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Wilming L., Wray P.W., Wright M.W., Young L., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Beck S., Bentley D.R., Rogers J., Ross M.T. Nature 428:522-528(2004) [PubMed: 15057823] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[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] OF 176-971, VARIANT ASP-1429. Tissue: Fetal brain.
[4]	"Towards a catalog of human genes and proteins: sequencing and analysis of 500 novel complete protein coding human cDNAs." Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S., Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H., Lauber J., Duesterhoeft A., Beyer A., Koehrer K., Strack N., Mewes H.-W., Ottenwaelder B., Obermaier B. , Tampe J., Heubner D., Wambutt R., Korn B., Klein M., Poustka A. Genome Res. 11:422-435(2001) [PubMed: 11230166] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 298-1668 (ISOFORM 2), VARIANT ASP-1429. Tissue: Testis.
[5]	"Prediction of the coding sequences of unidentified human genes. XII. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro." Nagase T., Ishikawa K., Suyama M., Kikuno R., Hirosawa M., Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O. DNA Res. 5:355-364(1998) [PubMed: 10048485] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 702-1668 (ISOFORM 1), VARIANT ASP-1429. Tissue: Brain.
[6]	"Robust phosphoproteomic profiling of tyrosine phosphorylation sites from human T cells using immobilized metal affinity chromatography and tandem mass spectrometry." Brill L.M., Salomon A.R., Ficarro S.B., Mukherji M., Stettler-Gill M., Peters E.C. Anal. Chem. 76:2763-2772(2004) [PubMed: 15144186] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-207 AND SER-209, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[7]	"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-242; THR-263 AND SER-265, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[8]	"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-64; SER-77; SER-198; SER-207; SER-209; THR-263; SER-265; SER-316; THR-317; SER-325; SER-492; SER-875; SER-877; SER-993; SER-1279; SER-1288 AND THR-1318, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[9]	"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 THR-263; SER-265; THR-354; SER-356 AND SER-993, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[10]	"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-238 AND SER-241, MASS SPECTROMETRY. Tissue: Embryonic kidney.
[11]	"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-581; SER-1056; SER-1382 AND SER-1657, MASS SPECTROMETRY. Tissue: Embryonic kidney.
[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-877 AND SER-1208, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[13]	"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: 18691976] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-993, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[14]	"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-198; SER-207; SER-209; SER-242; THR-263; SER-265; SER-318; SER-325; THR-354; SER-356; THR-364; SER-370; SER-372; SER-381; SER-831; SER-833; SER-837; SER-845; SER-848; SER-853; SER-875; SER-877; SER-986; SER-993; SER-1010; SER-1014 AND SER-1017, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[15]	"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-207; SER-209; SER-238; SER-242; THR-263; SER-265; THR-317; SER-318; SER-325; SER-370; SER-372; SER-381; SER-875; SER-877; THR-984; SER-986; SER-993; SER-1014 AND SER-1017, MASS SPECTROMETRY. Tissue: Embryonic kidney.
[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: 19690332] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-242; SER-986; SER-993; SER-1014; SER-1017 AND SER-1364, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AY283618 mRNA. Translation: AAP37483.1. AL157758, AL445232 Genomic DNA. Translation: CAI10903.1. AL157758, AL445232 Genomic DNA. Translation: CAM13064.1. AL445232, AL157758 Genomic DNA. Translation: CAI16505.1. AL445232, AL157758 Genomic DNA. Translation: CAI16506.2. AL831833 mRNA. Translation: CAD38544.1. AL136745 mRNA. Translation: CAB66679.2. AB020660 mRNA. Translation: BAA74876.1.
IPI	IPI00016472. IPI00329547.
RefSeq	NP_055885.3. NM_015070.3.
UniGene	Hs.136102.
3D structure databases
ProteinModelPortal	Q5T200.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q5T200. 3 interactions.
MINT	MINT-3306871.
PTM databases
PhosphoSite	Q5T200.
Polymorphism databases
DMDM	68052314.
Proteomic databases
PRIDE	Q5T200.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000242848; ENSP00000242848; ENSG00000123200.
GeneID	23091.
KEGG	hsa:23091.
UCSC	uc001vas.1. human.
Organism-specific databases
CTD	23091.
GeneCards	GC13M046528.
HGNC	HGNC:20368. ZC3H13.
neXtProt	NX_Q5T200.
HUGE	Search...
GenAtlas	Search...
Phylogenomic databases
HOVERGEN	HBG107115.
InParanoid	Q5T200.
OMA	RSNRSHT.
OrthoDB	EOG4KSPJC.
Gene expression databases
ArrayExpress	Q5T200.
Bgee	Q5T200.
CleanEx	HS_ZC3H13.
Genevestigator	Q5T200.
GermOnline	ENSG00000123200. Homo sapiens.
Family and domain databases
InterPro	IPR000571. Znf_CCCH. [Graphical view]
Pfam	PF00642. zf-CCCH. 1 hit. [Graphical view]
SMART	SM00356. ZnF_C3H1. 1 hit. [Graphical view]
PROSITE	PS50103. ZF_C3H1. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	44243.
PMAP-CutDB	Q5T200.

Entry information

Entry name

ZC3HD_HUMAN

Accession

Primary (citable) accession number: Q5T200
Secondary accession number(s): A2A323 , O94936, Q5T1Z9, Q7Z7J3, Q8NDT6, Q9H0L6

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 21, 2005
Last sequence update:	December 21, 2004
Last modified:	January 25, 2012
This is version 66 of the entry and version 1 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.