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Q5T200 (ZC3HD_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 86. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Zinc finger CCCH domain-containing protein 13
Gene names
Name:ZC3H13
Synonyms:KIAA0853
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1668 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Sequence similarities

Contains 1 C3H1-type zinc finger.

Ontologies

Keywords
   Coding sequence diversityAlternative splicing
Polymorphism
   DomainCoiled coil
Repeat
Zinc-finger
   LigandMetal-binding
Zinc
   PTMPhosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Molecular_functionmetal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

poly(A) RNA binding

Inferred from direct assay PubMed 22681889. Source: UniProtKB

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

SCHIP1Q9P0W52EBI-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.
Note: Contains a phosphoserine at position 1453. Contains a phosphoserine at position 1456. Contains a phosphoserine at position 1466.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 16681668Zinc finger CCCH domain-containing protein 13
PRO_0000050778

Regions

Zinc finger36 – 6429C3H1-type
Coiled coil645 – 789145 Potential
Coiled coil1300 – 136667 Potential
Compositional bias204 – 24239Ser-rich
Compositional bias316 – 34934Ser-rich
Compositional bias350 – 652303Arg/Ser-rich
Compositional bias653 – 842190Arg/Glu-rich
Compositional bias957 – 102872Lys-rich
Compositional bias1189 – 1295107Ser-rich

Amino acid modifications

Modified residue641Phosphoserine Ref.14
Modified residue1981Phosphoserine Ref.7 Ref.14 Ref.15
Modified residue2071Phosphoserine Ref.11 Ref.14
Modified residue2091Phosphoserine Ref.11 Ref.14
Modified residue2371Phosphothreonine Ref.15
Modified residue2421Phosphoserine Ref.8 Ref.11 Ref.13 Ref.14 Ref.15
Modified residue2631Phosphothreonine Ref.6 Ref.7 Ref.8 Ref.13 Ref.14 Ref.15
Modified residue2651Phosphoserine Ref.6 Ref.7 Ref.8 Ref.13 Ref.14 Ref.15
Modified residue3161Phosphoserine Ref.11
Modified residue3181Phosphoserine Ref.11
Modified residue3251Phosphoserine Ref.11 Ref.15
Modified residue3281Phosphoserine Ref.15
Modified residue3541Phosphothreonine Ref.11
Modified residue3641Phosphothreonine Ref.11
Modified residue3701Phosphoserine Ref.11 Ref.14 Ref.15
Modified residue3721Phosphoserine Ref.11 Ref.14 Ref.15
Modified residue3811Phosphoserine Ref.11 Ref.14 Ref.15
Modified residue8311Phosphoserine Ref.11
Modified residue8331Phosphoserine Ref.11
Modified residue8371Phosphoserine Ref.11
Modified residue8451Phosphoserine Ref.11 Ref.14 Ref.15
Modified residue8481Phosphoserine Ref.11 Ref.14 Ref.15
Modified residue8531Phosphoserine Ref.11 Ref.14 Ref.15
Modified residue8751Phosphoserine Ref.11
Modified residue8771Phosphoserine Ref.11 Ref.14 Ref.15
Modified residue8821Phosphothreonine Ref.15
Modified residue9861Phosphoserine Ref.11 Ref.13 Ref.15
Modified residue9931Phosphoserine Ref.8 Ref.11 Ref.13 Ref.14 Ref.15
Modified residue10101Phosphoserine Ref.11 Ref.14 Ref.15
Modified residue10141Phosphoserine Ref.11 Ref.13 Ref.14
Modified residue10171Phosphoserine Ref.11 Ref.13 Ref.14 Ref.15
Modified residue11701Phosphothreonine Ref.14
Modified residue11911Phosphoserine Ref.15
Modified residue11941Phosphoserine Ref.15
Modified residue12081Phosphoserine Ref.14 Ref.15
Modified residue12101Phosphoserine Ref.15
Modified residue12301Phosphoserine Ref.14
Modified residue13641Phosphoserine Ref.14
Modified residue13661Phosphoserine Ref.14
Modified residue13821Phosphoserine Ref.9
Modified residue14381Phosphoserine Ref.14
Modified residue14651Phosphoserine Ref.15

Natural variations

Alternative sequence14401E → EA in isoform 2.
VSP_027202
Alternative sequence1558 – 15636DADNLF → GSFILL in isoform 2.
VSP_014252
Alternative sequence1564 – 1668105Missing in isoform 2.
VSP_014253
Natural variant14291E → D. Ref.1 Ref.3 Ref.4 Ref.5
Corresponds to variant rs9534264 [ dbSNP | Ensembl ].
VAR_022727

Experimental info

Sequence conflict702 – 7043EKE → KAR in BAA74876. Ref.5
Sequence conflict9671I → K in CAD38544. Ref.3

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified December 21, 2004. Version 1.
Checksum: B7E8118D3B5954D6

FASTA1,668196,635
        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 

« Hide

Isoform 2 [UniParc].

Checksum: EDF7A3EA9DB7448B
Show »

FASTA1,564184,869

References

« Hide '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. expand/collapse author list , 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]"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 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. expand/collapse author list , Tampe J., Heubner D., Wambutt R., Korn B., Klein M., Poustka A.
Genome Res. 11:422-435(2001) [PubMed] [Europe PMC] [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] [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]"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] [Europe PMC] [Abstract]
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]"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-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-265; 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].
+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.
RefSeqNP_055885.3. NM_015070.4.
XP_005266368.1. XM_005266311.1.
XP_005266369.1. XM_005266312.1.
UniGeneHs.136102.

3D structure databases

ProteinModelPortalQ5T200.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid116719. 41 interactions.
IntActQ5T200. 7 interactions.
MINTMINT-3306871.
STRING9606.ENSP00000282007.

PTM databases

PhosphoSiteQ5T200.

Polymorphism databases

DMDM68052314.

Proteomic databases

PaxDbQ5T200.
PRIDEQ5T200.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000242848; ENSP00000242848; ENSG00000123200. [Q5T200-1]
ENST00000282007; ENSP00000282007; ENSG00000123200. [Q5T200-2]
GeneID23091.
KEGGhsa:23091.
UCSCuc001vas.1. human. [Q5T200-2]
uc001vat.1. human. [Q5T200-1]

Organism-specific databases

CTD23091.
GeneCardsGC13M046528.
H-InvDBHIX0000705.
HIX0011294.
HIX0039579.
HGNCHGNC:20368. ZC3H13.
HPAHPA039340.
HPA040140.
HPA047806.
neXtProtNX_Q5T200.
PharmGKBPA134907656.
HUGESearch...
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG301709.
HOVERGENHBG107115.
InParanoidQ5T200.
OMASYQRTIT.
OrthoDBEOG7DC23Q.
PhylomeDBQ5T200.
TreeFamTF332670.

Gene expression databases

ArrayExpressQ5T200.
BgeeQ5T200.
CleanExHS_ZC3H13.
GenevestigatorQ5T200.

Family and domain databases

Gene3D4.10.1000.10. 1 hit.
InterProIPR000571. Znf_CCCH.
[Graphical view]
PfamPF00642. zf-CCCH. 1 hit.
[Graphical view]
SMARTSM00356. ZnF_C3H1. 1 hit.
[Graphical view]
PROSITEPS50103. ZF_C3H1. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSZC3H13. human.
GeneWikiZC3H13.
GenomeRNAi23091.
NextBio44243.
PMAP-CutDBQ5T200.
PROQ5T200.

Entry information

Entry nameZC3HD_HUMAN
AccessionPrimary (citable) accession number: Q5T200
Secondary accession number(s): A2A323 expand/collapse secondary AC list , O94936, Q5T1Z9, Q7Z7J3, Q8NDT6, Q9H0L6
Entry history
Integrated into UniProtKB/Swiss-Prot: June 21, 2005
Last sequence update: December 21, 2004
Last modified: April 16, 2014
This is version 86 of the entry and version 1 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

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 13

Human chromosome 13: entries, gene names and cross-references to MIM