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Protein

Zinc finger CCCH domain-containing protein 13

Gene

ZC3H13

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Acts as component of the WTAP complex that is involved in RNA processing and cell cycle (PubMed:24100041).1 Publication

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri36 – 6429C3H1-typePROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

  • metal ion binding Source: UniProtKB-KW
  • poly(A) RNA binding Source: UniProtKB
Complete GO annotation...

Keywords - Ligandi

Metal-binding, Zinc

Names & Taxonomyi

Protein namesi
Recommended name:
Zinc finger CCCH domain-containing protein 13
Gene namesi
Name:ZC3H13
Synonyms:KIAA0853
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 13

Organism-specific databases

HGNCiHGNC:20368. ZC3H13.

Subcellular locationi

GO - Cellular componenti

  • nuclear speck Source: UniProtKB
  • nucleoplasm Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA134907656.

Polymorphism and mutation databases

BioMutaiZC3H13.
DMDMi68052314.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 16681668Zinc finger CCCH domain-containing protein 13PRO_0000050778Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei64 – 641PhosphoserineCombined sources
Cross-linki194 – 194Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei198 – 1981PhosphoserineCombined sources
Modified residuei207 – 2071PhosphoserineCombined sources
Modified residuei209 – 2091PhosphoserineCombined sources
Modified residuei237 – 2371PhosphothreonineCombined sources
Modified residuei242 – 2421PhosphoserineCombined sources
Modified residuei263 – 2631PhosphothreonineCombined sources
Modified residuei265 – 2651PhosphoserineCombined sources
Modified residuei316 – 3161PhosphoserineCombined sources
Modified residuei318 – 3181PhosphoserineCombined sources
Modified residuei325 – 3251PhosphoserineCombined sources
Modified residuei328 – 3281PhosphoserineCombined sources
Modified residuei354 – 3541PhosphothreonineCombined sources
Modified residuei364 – 3641PhosphothreonineCombined sources
Modified residuei370 – 3701PhosphoserineCombined sources
Modified residuei372 – 3721PhosphoserineCombined sources
Modified residuei381 – 3811PhosphoserineCombined sources
Modified residuei831 – 8311PhosphoserineCombined sources
Modified residuei833 – 8331PhosphoserineCombined sources
Modified residuei837 – 8371PhosphoserineCombined sources
Modified residuei845 – 8451PhosphoserineCombined sources
Modified residuei848 – 8481PhosphoserineCombined sources
Modified residuei853 – 8531PhosphoserineCombined sources
Modified residuei875 – 8751PhosphoserineCombined sources
Modified residuei877 – 8771PhosphoserineCombined sources
Modified residuei882 – 8821PhosphothreonineCombined sources
Modified residuei986 – 9861PhosphoserineCombined sources
Modified residuei993 – 9931PhosphoserineCombined sources
Modified residuei1010 – 10101PhosphoserineCombined sources
Modified residuei1014 – 10141PhosphoserineCombined sources
Modified residuei1017 – 10171PhosphoserineCombined sources
Modified residuei1170 – 11701PhosphothreonineCombined sources
Modified residuei1191 – 11911PhosphoserineCombined sources
Modified residuei1194 – 11941PhosphoserineCombined sources
Modified residuei1208 – 12081PhosphoserineCombined sources
Modified residuei1210 – 12101PhosphoserineCombined sources
Modified residuei1230 – 12301PhosphoserineCombined sources
Modified residuei1364 – 13641PhosphoserineCombined sources
Modified residuei1366 – 13661PhosphoserineCombined sources
Modified residuei1382 – 13821PhosphoserineCombined sources
Modified residuei1438 – 14381PhosphoserineCombined sources
Modified residuei1465 – 14651PhosphoserineCombined sources
Isoform 2 (identifier: Q5T200-2)
Modified residuei1453 – 14531PhosphoserineCombined sources
Modified residuei1456 – 14561PhosphoserineCombined sources
Modified residuei1466 – 14661PhosphoserineCombined sources

Keywords - PTMi

Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiQ5T200.
MaxQBiQ5T200.
PaxDbiQ5T200.
PRIDEiQ5T200.

PTM databases

iPTMnetiQ5T200.
PhosphoSiteiQ5T200.

Miscellaneous databases

PMAP-CutDBQ5T200.

Expressioni

Gene expression databases

BgeeiQ5T200.
CleanExiHS_ZC3H13.
ExpressionAtlasiQ5T200. baseline and differential.
GenevisibleiQ5T200. HS.

Organism-specific databases

HPAiHPA039340.
HPA040140.
HPA047806.

Interactioni

Subunit structurei

Component of the WTAP complex composed of WTAP, ZC3H13, CBLL1, KIAA1429, RBM15, BCLAF1 and THRAP3 (PubMed:24100041).1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
SCHIP1Q9P0W52EBI-2679720,EBI-1397509

Protein-protein interaction databases

BioGridi116719. 56 interactions.
IntActiQ5T200. 13 interactions.
MINTiMINT-3306871.
STRINGi9606.ENSP00000282007.

Structurei

3D structure databases

ProteinModelPortaliQ5T200.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili645 – 789145Sequence analysisAdd
BLAST
Coiled coili1300 – 136667Sequence analysisAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi204 – 24239Ser-richAdd
BLAST
Compositional biasi316 – 34934Ser-richAdd
BLAST
Compositional biasi350 – 652303Arg/Ser-richAdd
BLAST
Compositional biasi653 – 842190Arg/Glu-richAdd
BLAST
Compositional biasi957 – 102872Lys-richAdd
BLAST
Compositional biasi1189 – 1295107Ser-richAdd
BLAST

Sequence similaritiesi

Contains 1 C3H1-type zinc finger.PROSITE-ProRule annotation

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri36 – 6429C3H1-typePROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

Coiled coil, Repeat, Zinc-finger

Phylogenomic databases

eggNOGiKOG1874. Eukaryota.
ENOG410XQ2A. LUCA.
GeneTreeiENSGT00730000111163.
HOVERGENiHBG107115.
InParanoidiQ5T200.
OMAiHQSEDRD.
OrthoDBiEOG7DC23Q.
PhylomeDBiQ5T200.
TreeFamiTF332670.

Family and domain databases

Gene3Di4.10.1000.10. 1 hit.
InterProiIPR000571. Znf_CCCH.
[Graphical view]
PfamiPF00642. zf-CCCH. 1 hit.
[Graphical view]
SMARTiSM00356. ZnF_C3H1. 1 hit.
[Graphical view]
SUPFAMiSSF90229. SSF90229. 1 hit.
PROSITEiPS50103. ZF_C3H1. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q5T200-1) [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
MSKIRRKVTV ENTKTISDST SRRPSVFERL GPSTGSTAET QCRNWLKTGN
60 70 80 90 100
CLYGNTCRFV HGPSPRGKGY SSNYRRSPER PTGDLRERMK NKRQDVDTEP
110 120 130 140 150
QKRNTEESSS PVRKESSRGR HREKEDIKIT KERTPESEEE NVEWETNRDD
160 170 180 190 200
SDNGDINYDY VHELSLEMKR QKIQRELMKL EQENMEKREE IIIKKEVSPE
210 220 230 240 250
VVRSKLSPSP SLRKSSKSPK RKSSPKSSSA SKKDRKTSAV SSPLLDQQRN
260 270 280 290 300
SKTNQSKKKG PRTPSPPPPI PEDIALGKKY KEKYKVKDRI EEKTRDGKDR
310 320 330 340 350
GRDFERQREK RDKPRSTSPA GQHHSPISSR HHSSSSQSGS SIQRHSPSPR
360 370 380 390 400
RKRTPSPSYQ RTLTPPLRRS ASPYPSHSLS SPQRKQSPPR HRSPMREKGR
410 420 430 440 450
HDHERTSQSH DRRHERREDT RGKRDREKDS REEREYEQDQ SSSRDHRDDR
460 470 480 490 500
EPRDGRDRRD ARDTRDRREL RDSRDMRDSR EMRDYSRDTK ESRDPRDSRS
510 520 530 540 550
TRDAHDYRDR EGRDTHRKED TYPEESRSYG RNHLREESSR TEIRNESRNE
560 570 580 590 600
SRSEIRNDRM GRSRGRVPEL PEKGSRGSRG SQIDSHSSNS NYHDSWETRS
610 620 630 640 650
SYPERDRYPE RDNRDQARDS SFERRHGERD RRDNRERDQR PSSPIRHQGR
660 670 680 690 700
NDELERDERR EERRVDRVDD RRDERARERD RERERDRERE RERERERDRE
710 720 730 740 750
REKERELERE RARERERERE KERDRERDRD RDHDRERERE RERDREKERE
760 770 780 790 800
REREERERER ERERERERER ERERERARER DKERERQRDW EDKDKGRDDR
810 820 830 840 850
REKREEIRED RNPRDGHDER KSKKRYRNEG SPSPRQSPKR RREHSPDSDA
860 870 880 890 900
YNSGDDKNEK HRLLSQVVRP QESRSLSPSH LTEDRQGRWK EEDRKPERKE
910 920 930 940 950
SSRRYEEQEL KEKVSSVDKQ REQTEILESS RMRAQDIIGH HQSEDRETSD
960 970 980 990 1000
RAHDENKKKA KIQKKPIKKK KEDDVGIERG NIETTSEDGQ VFSPKKGQKK
1010 1020 1030 1040 1050
KSIEKKRKKS KGDSDISDEE AAQQSKKKRG PRTPPITTKE ELVEMCNGKN
1060 1070 1080 1090 1100
GILEDSQKKE DTAFSDWSDE DVPDRTEVTE AEHTATATTP GSTPSPLSSL
1110 1120 1130 1140 1150
LPPPPPVATA TATTVPATLA ATTAAAATSF STSAITISTS ATPTNTTNNT
1160 1170 1180 1190 1200
FANEDSHRKC HRTRVEKVET PHVTIEDAQH RKPMDQKRSS SLGSNRSNRS
1210 1220 1230 1240 1250
HTSGRLRSPS NDSAHRSGDD QSGRKRVLHS GSRDREKTKS LEITGERKSR
1260 1270 1280 1290 1300
IDQLKRGEPS RSTSSDRQDS RSHSSRRSSP ESDRQVHSRS GSFDSRDRLQ
1310 1320 1330 1340 1350
ERDRYEHDRE RERERRDTRQ REWDRDADKD WPRNRDRDRL RERERERERD
1360 1370 1380 1390 1400
KRRDLDRERE RLISDSVERD RDRDRDRTFE SSQIESVKRC EAKLEGEHER
1410 1420 1430 1440 1450
DLESTSRDSL ALDKERMDKD LGSVQGFEET NKSERTESLE GDDESKLDDA
1460 1470 1480 1490 1500
HSLGSGAGEG YEPISDDELD EILAGDAEKR EDQQDEEKMP DPLDVIDVDW
1510 1520 1530 1540 1550
SGLMPKHPKE PREPGAALLK FTPGAVMLRV GISKKLAGSE LFAKVKETCQ
1560 1570 1580 1590 1600
RLLEKPKDAD NLFEHELGAL NMAALLRKEE RASLLSNLGP CCKALCFRRD
1610 1620 1630 1640 1650
SAIRKQLVKN EKGTIKQAYT SAPMVDNELL RLSLRLFKRK TTCHAPGHEK
1660
TEDNKLSQSS IQQELCVS
Note: Gene prediction confirmed by EST data.
Length:1,668
Mass (Da):196,635
Last modified:December 21, 2004 - v1
Checksum:iB7E8118D3B5954D6
GO
Isoform 2 (identifier: Q5T200-2) [UniParc]FASTAAdd to basket

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

Show »
Length:1,564
Mass (Da):184,869
Checksum:iEDF7A3EA9DB7448B
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti702 – 7043EKE → KAR in BAA74876 (PubMed:10048485).Curated
Sequence conflicti967 – 9671I → K in CAD38544 (PubMed:17974005).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti1429 – 14291E → D.4 Publications
Corresponds to variant rs9534264 [ dbSNP | Ensembl ].
VAR_022727

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1440 – 14401E → EA in isoform 2. 2 PublicationsVSP_027202
Alternative sequencei1558 – 15636DADNLF → GSFILL in isoform 2. 2 PublicationsVSP_014252
Alternative sequencei1564 – 1668105Missing in isoform 2. 2 PublicationsVSP_014253Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS9400.1. [Q5T200-2]
RefSeqiNP_055885.3. NM_015070.4. [Q5T200-2]
XP_005266368.1. XM_005266311.2. [Q5T200-1]
XP_005266369.1. XM_005266312.1. [Q5T200-2]
UniGeneiHs.136102.

Genome annotation databases

EnsembliENST00000242848; ENSP00000242848; ENSG00000123200. [Q5T200-1]
ENST00000282007; ENSP00000282007; ENSG00000123200. [Q5T200-2]
GeneIDi23091.
KEGGihsa:23091.
UCSCiuc001vas.3. human. [Q5T200-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS9400.1. [Q5T200-2]
RefSeqiNP_055885.3. NM_015070.4. [Q5T200-2]
XP_005266368.1. XM_005266311.2. [Q5T200-1]
XP_005266369.1. XM_005266312.1. [Q5T200-2]
UniGeneiHs.136102.

3D structure databases

ProteinModelPortaliQ5T200.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi116719. 56 interactions.
IntActiQ5T200. 13 interactions.
MINTiMINT-3306871.
STRINGi9606.ENSP00000282007.

PTM databases

iPTMnetiQ5T200.
PhosphoSiteiQ5T200.

Polymorphism and mutation databases

BioMutaiZC3H13.
DMDMi68052314.

Proteomic databases

EPDiQ5T200.
MaxQBiQ5T200.
PaxDbiQ5T200.
PRIDEiQ5T200.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000242848; ENSP00000242848; ENSG00000123200. [Q5T200-1]
ENST00000282007; ENSP00000282007; ENSG00000123200. [Q5T200-2]
GeneIDi23091.
KEGGihsa:23091.
UCSCiuc001vas.3. human. [Q5T200-1]

Organism-specific databases

CTDi23091.
GeneCardsiZC3H13.
H-InvDBHIX0000705.
HIX0011294.
HIX0039579.
HGNCiHGNC:20368. ZC3H13.
HPAiHPA039340.
HPA040140.
HPA047806.
MIMi616453. gene.
neXtProtiNX_Q5T200.
PharmGKBiPA134907656.
HUGEiSearch...
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG1874. Eukaryota.
ENOG410XQ2A. LUCA.
GeneTreeiENSGT00730000111163.
HOVERGENiHBG107115.
InParanoidiQ5T200.
OMAiHQSEDRD.
OrthoDBiEOG7DC23Q.
PhylomeDBiQ5T200.
TreeFamiTF332670.

Miscellaneous databases

ChiTaRSiZC3H13. human.
GeneWikiiZC3H13.
GenomeRNAii23091.
NextBioi44243.
PMAP-CutDBQ5T200.
PROiQ5T200.
SOURCEiSearch...

Gene expression databases

BgeeiQ5T200.
CleanExiHS_ZC3H13.
ExpressionAtlasiQ5T200. baseline and differential.
GenevisibleiQ5T200. HS.

Family and domain databases

Gene3Di4.10.1000.10. 1 hit.
InterProiIPR000571. Znf_CCCH.
[Graphical view]
PfamiPF00642. zf-CCCH. 1 hit.
[Graphical view]
SMARTiSM00356. ZnF_C3H1. 1 hit.
[Graphical view]
SUPFAMiSSF90229. SSF90229. 1 hit.
PROSITEiPS50103. ZF_C3H1. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 176-971, VARIANT ASP-1429.
    Tissue: Fetal brain.
  4. 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] [Europe PMC] [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] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-263 AND SER-265, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  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-198; THR-263 AND SER-265, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  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-242; THR-263; SER-265 AND SER-993, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  9. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1382, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic kidney.
  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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  11. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-207; SER-209; SER-242; SER-316; SER-318; SER-325; THR-354; 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, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1453; SER-1456 AND SER-1466 (ISOFORM 2), IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  12. "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].
  13. "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-242; THR-263; SER-986; SER-993; SER-1014 AND SER-1017, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  14. "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-64; SER-198; SER-207; SER-209; SER-242; THR-263; SER-265; SER-370; SER-372; SER-381; SER-845; SER-848; SER-853; SER-877; SER-993; SER-1010; SER-1014; SER-1017; THR-1170; SER-1208; SER-1230; SER-1364; SER-1366 AND SER-1438, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  15. "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-198; THR-237; SER-242; THR-263; SER-265; SER-325; SER-328; SER-370; SER-372; SER-381; SER-845; SER-848; SER-853; SER-877; THR-882; SER-986; SER-993; SER-1010; SER-1017; SER-1191; SER-1194; SER-1208; SER-1210 AND SER-1465, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  16. "Identification of Wilms' tumor 1-associating protein complex and its role in alternative splicing and the cell cycle."
    Horiuchi K., Kawamura T., Iwanari H., Ohashi R., Naito M., Kodama T., Hamakubo T.
    J. Biol. Chem. 288:33292-33302(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN THE WTAP COMPLEX, SUBCELLULAR LOCATION.
  17. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-242; SER-370; SER-372; SER-877; SER-1010; SER-1014; SER-1017 AND SER-1210, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  18. "Uncovering global SUMOylation signaling networks in a site-specific manner."
    Hendriks I.A., D'Souza R.C., Yang B., Verlaan-de Vries M., Mann M., Vertegaal A.C.
    Nat. Struct. Mol. Biol. 21:927-936(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-194, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  19. "SUMO-2 orchestrates chromatin modifiers in response to DNA damage."
    Hendriks I.A., Treffers L.W., Verlaan-de Vries M., Olsen J.V., Vertegaal A.C.
    Cell Rep. 10:1778-1791(2015) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-194, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  20. "System-wide analysis of SUMOylation dynamics in response to replication stress reveals novel small ubiquitin-like modified target proteins and acceptor lysines relevant for genome stability."
    Xiao Z., Chang J.G., Hendriks I.A., Sigurdsson J.O., Olsen J.V., Vertegaal A.C.
    Mol. Cell. Proteomics 14:1419-1434(2015) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-194, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiZC3HD_HUMAN
AccessioniPrimary (citable) accession number: Q5T200
Secondary accession number(s): A2A323
, O94936, Q5T1Z9, Q7Z7J3, Q8NDT6, Q9H0L6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 21, 2005
Last sequence update: December 21, 2004
Last modified: April 13, 2016
This is version 105 of the entry and version 1 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 13
    Human chromosome 13: 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.