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Q9UPT8

- ZC3H4_HUMAN

UniProt

Q9UPT8 - ZC3H4_HUMAN

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Protein

Zinc finger CCCH domain-containing protein 4

Gene

ZC3H4

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli

Functioni

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri390 – 41728C3H1-type 1PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri419 – 44628C3H1-type 2PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri447 – 47024C3H1-type 3PROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

  1. metal ion binding Source: UniProtKB-KW
  2. 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 4
Gene namesi
Name:ZC3H4
Synonyms:C19orf7, KIAA1064
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 19

Organism-specific databases

HGNCiHGNC:17808. ZC3H4.

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA162409534.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 13031303Zinc finger CCCH domain-containing protein 4PRO_0000234068Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei72 – 721Phosphothreonine1 Publication
Modified residuei75 – 751Phosphothreonine1 Publication
Modified residuei76 – 761Phosphoserine1 Publication
Modified residuei92 – 921Phosphoserine1 Publication
Modified residuei94 – 941Phosphoserine1 Publication
Modified residuei155 – 1551Phosphotyrosine1 Publication
Modified residuei807 – 8071Phosphoserine2 Publications
Modified residuei808 – 8081Phosphoserine1 Publication
Modified residuei904 – 9041Phosphoserine2 Publications
Modified residuei908 – 9081Phosphoserine1 Publication
Modified residuei1104 – 11041Phosphoserine1 Publication
Modified residuei1106 – 11061Phosphothreonine1 Publication
Modified residuei1108 – 11081Phosphoserine1 Publication
Modified residuei1114 – 11141Phosphoserine3 Publications
Modified residuei1269 – 12691Phosphoserine2 Publications
Modified residuei1275 – 12751Phosphoserine4 Publications

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ9UPT8.
PaxDbiQ9UPT8.
PRIDEiQ9UPT8.

PTM databases

PhosphoSiteiQ9UPT8.

Miscellaneous databases

PMAP-CutDBQ9UPT8.

Expressioni

Gene expression databases

BgeeiQ9UPT8.
CleanExiHS_ZC3H4.
GenevestigatoriQ9UPT8.

Organism-specific databases

HPAiHPA040934.
HPA041068.

Interactioni

Protein-protein interaction databases

BioGridi116818. 19 interactions.
IntActiQ9UPT8. 2 interactions.
STRINGi9606.ENSP00000253048.

Structurei

Secondary structure

1
1303
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Turni426 – 4305Combined sources
Beta strandi440 – 4478Combined sources
Helixi450 – 4534Combined sources
Beta strandi464 – 4663Combined sources
Helixi472 – 48716Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2CQENMR-A417-501[»]
ProteinModelPortaliQ9UPT8.
SMRiQ9UPT8. Positions 417-503.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9UPT8.

Family & Domainsi

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili95 – 12834Sequence AnalysisAdd
BLAST
Coiled coili767 – 80034Sequence AnalysisAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi5 – 5147Pro-richAdd
BLAST
Compositional biasi233 – 374142Gly-richAdd
BLAST
Compositional biasi506 – 690185Pro-richAdd
BLAST
Compositional biasi1129 – 113810Poly-Gly

Sequence similaritiesi

Contains 3 C3H1-type zinc fingers.PROSITE-ProRule annotation

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri390 – 41728C3H1-type 1PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri419 – 44628C3H1-type 2PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri447 – 47024C3H1-type 3PROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

Coiled coil, Repeat, Zinc-finger

Phylogenomic databases

eggNOGiNOG245027.
GeneTreeiENSGT00530000063288.
HOGENOMiHOG000231733.
HOVERGENiHBG108366.
InParanoidiQ9UPT8.
OMAiEGDTGNW.
OrthoDBiEOG7ZWD14.
PhylomeDBiQ9UPT8.
TreeFamiTF321641.

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. 3 hits.
[Graphical view]
PROSITEiPS50103. ZF_C3H1. 3 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9UPT8-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MEAAPGTPPP PPSESPPPPS PPPPSTPSPP PCSPDARPAT PHLLHHRLPL
60 70 80 90 100
PDDREDGELE EGELEDDGAE ETQDTSGGPE RSRKEKGEKH HSDSDEEKSH
110 120 130 140 150
RRLKRKRKKE REKEKRRSKK RRKSKHKRHA SSSDDFSDFS DDSDFSPSEK
160 170 180 190 200
GHRKYREYSP PYAPSHQQYP PSHATPLPKK AYSKMDSKSY GMYEDYENEQ
210 220 230 240 250
YGEYEGDEEE DMGKEDYDDF TKELNQYRRA KEGSSRGRGS RGRGRGYRGR
260 270 280 290 300
GSRGGSRGRG MGRGSRGRGR GSMGGDHPED EEDFYEEEMD YGESEEPMGD
310 320 330 340 350
DDYDEYSKEL NQYRRSKDSR GRGLSRGRGR GSRGRGKGMG RGRGRGGSRG
360 370 380 390 400
GMNKGGMNDD EDFYDEDMGD GGGGSYRSRD HDKPHQQSDK KGKVICKYFV
410 420 430 440 450
EGRCTWGDHC NFSHDIELPK KRELCKFYIT GFCARAENCP YMHGDFPCKL
460 470 480 490 500
YHTTGNCING DDCMFSHDPL TEETRELLDK MLADDAEAGA EDEKEVEELK
510 520 530 540 550
KQGINPLPKP PPGVGLLPTP PRPPGPQAPT SPNGRPMQGG PPPPPPPPPP
560 570 580 590 600
PPGPPQMPMP VHEPLSPQQL QQQDMYNKKI PSLFEIVVRP TGQLAEKLGV
610 620 630 640 650
RFPGPGGPPG PMGPGPNMGP PGPMGGPMHP DMHPDMHPDM HPDMHADMHA
660 670 680 690 700
DMPMGPGMNP GPPMGPGGPP MMPYGPGDSP HSGMMPPIPP AQNFYENFYQ
710 720 730 740 750
QQEGMEMEPG LLGDAEDYGH YEELPGEPGE HLFPEHPLEP DSFSEGGPPG
760 770 780 790 800
RPKPGAGVPD FLPSAQRALY LRIQQKQQEE EERARRLAES SKQDRENEEG
810 820 830 840 850
DTGNWYSSDE DEGGSSVTSI LKTLRQQTSS RPPASVGELS SSGLGDPRLQ
860 870 880 890 900
KGHPTGSRLA DPRLSRDPRL TRHVEASGGS GPGDSGPSDP RLARALPTSK
910 920 930 940 950
PEGSLHSSPV GPSSSKGSGP PPTEEEEGER ALREKAVNIP LDPLPGHPLR
960 970 980 990 1000
DPRSQLQQFS HIKKDVTLSK PSFARTVLWN PEDLIPLPIP KQDAVPPVPA
1010 1020 1030 1040 1050
ALQSMPTLDP RLHRAATAGP PNARQRPGAS TDSSTQGANL PDFELLSRIL
1060 1070 1080 1090 1100
KTVNATGSSA APGSSDKPSD PRVRKAPTDP RLQKPTDSTA SSRAAKPGPA
1110 1120 1130 1140 1150
EAPSPTASPS GDASPPATAP YDPRVLAAGG LGQGGGGGQS SVLSGISLYD
1160 1170 1180 1190 1200
PRTPNAGGKA TEPAADTGAQ PKGAEGNGKS SASKAKEPPF VRKSALEQPE
1210 1220 1230 1240 1250
TGKAGADGGT PTDRYNSYNR PRPKAAAAPA ATTATPPPEG APPQPGVHNL
1260 1270 1280 1290 1300
PVPTLFGTVK QTPKTGSGSP FAGNSPAREG EQDAASLKDV FKGFDPTASP

FCQ
Length:1,303
Mass (Da):140,257
Last modified:May 2, 2006 - v3
Checksum:iA6DAE368F543FF4D
GO

Sequence cautioni

The sequence BAA83016.2 differs from that shown. Reason: Erroneous initiation. Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti287 – 2871E → K.
Corresponds to variant rs192824 [ dbSNP | Ensembl ].
VAR_052964
Natural varianti464 – 4641M → V.
Corresponds to variant rs402833 [ dbSNP | Ensembl ].
VAR_052965
Natural varianti1228 – 12281A → G.
Corresponds to variant rs309195 [ dbSNP | Ensembl ].
VAR_052966

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB028987 mRNA. Translation: BAA83016.2. Different initiation.
AL050155 mRNA. Translation: CAB43296.1.
CCDSiCCDS42582.1.
PIRiT08781.
RefSeqiNP_055983.1. NM_015168.1.
XP_006723176.1. XM_006723113.1.
UniGeneiHs.104661.

Genome annotation databases

EnsembliENST00000253048; ENSP00000253048; ENSG00000130749.
GeneIDi23211.
KEGGihsa:23211.
UCSCiuc002pga.4. human.

Polymorphism databases

DMDMi94707996.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB028987 mRNA. Translation: BAA83016.2 . Different initiation.
AL050155 mRNA. Translation: CAB43296.1 .
CCDSi CCDS42582.1.
PIRi T08781.
RefSeqi NP_055983.1. NM_015168.1.
XP_006723176.1. XM_006723113.1.
UniGenei Hs.104661.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2CQE NMR - A 417-501 [» ]
ProteinModelPortali Q9UPT8.
SMRi Q9UPT8. Positions 417-503.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 116818. 19 interactions.
IntActi Q9UPT8. 2 interactions.
STRINGi 9606.ENSP00000253048.

PTM databases

PhosphoSitei Q9UPT8.

Polymorphism databases

DMDMi 94707996.

Proteomic databases

MaxQBi Q9UPT8.
PaxDbi Q9UPT8.
PRIDEi Q9UPT8.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000253048 ; ENSP00000253048 ; ENSG00000130749 .
GeneIDi 23211.
KEGGi hsa:23211.
UCSCi uc002pga.4. human.

Organism-specific databases

CTDi 23211.
GeneCardsi GC19M047569.
HGNCi HGNC:17808. ZC3H4.
HPAi HPA040934.
HPA041068.
neXtProti NX_Q9UPT8.
PharmGKBi PA162409534.
HUGEi Search...
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG245027.
GeneTreei ENSGT00530000063288.
HOGENOMi HOG000231733.
HOVERGENi HBG108366.
InParanoidi Q9UPT8.
OMAi EGDTGNW.
OrthoDBi EOG7ZWD14.
PhylomeDBi Q9UPT8.
TreeFami TF321641.

Miscellaneous databases

ChiTaRSi ZC3H4. human.
EvolutionaryTracei Q9UPT8.
GenomeRNAii 23211.
NextBioi 44759.
PMAP-CutDB Q9UPT8.
PROi Q9UPT8.

Gene expression databases

Bgeei Q9UPT8.
CleanExi HS_ZC3H4.
Genevestigatori Q9UPT8.

Family and domain databases

Gene3Di 4.10.1000.10. 1 hit.
InterProi IPR000571. Znf_CCCH.
[Graphical view ]
Pfami PF00642. zf-CCCH. 1 hit.
[Graphical view ]
SMARTi SM00356. ZnF_C3H1. 3 hits.
[Graphical view ]
PROSITEi PS50103. ZF_C3H1. 3 hits.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Prediction of the coding sequences of unidentified human genes. XIV. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro."
    Kikuno R., Nagase T., Ishikawa K., Hirosawa M., Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O.
    DNA Res. 6:197-205(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Brain.
  2. "Construction of expression-ready cDNA clones for KIAA genes: manual curation of 330 KIAA cDNA clones."
    Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T.
    DNA Res. 9:99-106(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: SEQUENCE REVISION.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 993-1303.
    Tissue: Uterus.
  4. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  5. "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-1269 AND SER-1275, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  6. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-72, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic kidney.
  7. "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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1275, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  8. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-75; SER-76; TYR-155; SER-807; SER-904; SER-908; THR-1106; SER-1108; SER-1114 AND SER-1275, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  9. "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].
  10. "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-807; SER-808; SER-1104; SER-1114 AND SER-1269, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  11. "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-92; SER-94; SER-904 AND SER-1114, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  12. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  13. "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-1275, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  14. "Solution structure of the zinc-finger domain in KIAA1064 protein."
    RIKEN structural genomics initiative (RSGI)
    Submitted (NOV-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: STRUCTURE BY NMR OF 417-501 IN COMPLEX WITH ZINC.

Entry informationi

Entry nameiZC3H4_HUMAN
AccessioniPrimary (citable) accession number: Q9UPT8
Secondary accession number(s): Q9Y420
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 2, 2006
Last sequence update: May 2, 2006
Last modified: October 29, 2014
This is version 112 of the entry and version 3 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

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 19
    Human chromosome 19: 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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  5. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3