Q9UPT8 (ZC3H4_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Zinc finger CCCH domain-containing protein 4

Gene names

Name:	ZC3H4
Synonyms:	C19orf7, KIAA1064

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	1303 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Sequence similarities	Contains 3 C3H1-type zinc fingers.
Sequence caution	The sequence BAA83016.2 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
Coding sequence diversity	Polymorphism
Domain	Coiled coil Repeat Zinc-finger
Ligand	Metal-binding Zinc
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Molecular_function	nucleic acid binding Inferred from electronic annotation. Source: InterPro zinc ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 1303

1303

Zinc finger CCCH domain-containing protein 4

PRO_0000234068

Regions

Zinc finger

390 – 417

28

C3H1-type 1

Zinc finger

419 – 446

28

C3H1-type 2

Zinc finger

447 – 470

24

C3H1-type 3

Coiled coil

95 – 128

34

Potential

Coiled coil

767 – 800

34

Potential

Compositional bias

5 – 51

47

Pro-rich

Compositional bias

233 – 374

142

Gly-rich

Compositional bias

506 – 690

185

Pro-rich

Compositional bias

1129 – 1138

10

Poly-Gly

Amino acid modifications

Modified residue

72

1

Phosphothreonine Ref.6

Modified residue

75

1

Phosphothreonine Ref.8

Modified residue

76

1

Phosphoserine Ref.8

Modified residue

92

1

Phosphoserine Ref.10

Modified residue

94

1

Phosphoserine Ref.10

Modified residue

155

1

Phosphotyrosine Ref.8

Modified residue

807

1

Phosphoserine Ref.8 Ref.9

Modified residue

808

1

Phosphoserine Ref.9

Modified residue

888

1

Phosphoserine By similarity

Modified residue

904

1

Phosphoserine Ref.8 Ref.10

Modified residue

908

1

Phosphoserine Ref.8

Modified residue

1104

1

Phosphoserine Ref.9

Modified residue

1106

1

Phosphothreonine Ref.8

Modified residue

1108

1

Phosphoserine Ref.8

Modified residue

1114

1

Phosphoserine Ref.8 Ref.9 Ref.10

Modified residue

1269

1

Phosphoserine Ref.5 Ref.9

Modified residue

1275

1

Phosphoserine Ref.5 Ref.7 Ref.8 Ref.12

Natural variations

Natural variant

287

1

E → K.
Corresponds to variant rs192824 [ dbSNP | Ensembl ].

VAR_052964

Natural variant

464

1

M → V.
Corresponds to variant rs402833 [ dbSNP | Ensembl ].

VAR_052965

Natural variant

1228

1

A → G.
Corresponds to variant rs309195 [ dbSNP | Ensembl ].

VAR_052966

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

1303

Helix Strand Turn

Details...

Turn

426 – 430

5

Beta strand

440 – 447

8

Helix

450 – 453

4

Beta strand

464 – 466

3

Helix

472 – 487

16

Sequences

	Sequence		Length	Mass (Da)
	Q9UPT8 [UniParc]. Last modified May 2, 2006. Version 3. Checksum: A6DAE368F543FF4D	FASTA	1,303	140,257
	10 20 30 40 50 60 MEAAPGTPPP PPSESPPPPS PPPPSTPSPP PCSPDARPAT PHLLHHRLPL PDDREDGELE 70 80 90 100 110 120 EGELEDDGAE ETQDTSGGPE RSRKEKGEKH HSDSDEEKSH RRLKRKRKKE REKEKRRSKK 130 140 150 160 170 180 RRKSKHKRHA SSSDDFSDFS DDSDFSPSEK GHRKYREYSP PYAPSHQQYP PSHATPLPKK 190 200 210 220 230 240 AYSKMDSKSY GMYEDYENEQ YGEYEGDEEE DMGKEDYDDF TKELNQYRRA KEGSSRGRGS 250 260 270 280 290 300 RGRGRGYRGR GSRGGSRGRG MGRGSRGRGR GSMGGDHPED EEDFYEEEMD YGESEEPMGD 310 320 330 340 350 360 DDYDEYSKEL NQYRRSKDSR GRGLSRGRGR GSRGRGKGMG RGRGRGGSRG GMNKGGMNDD 370 380 390 400 410 420 EDFYDEDMGD GGGGSYRSRD HDKPHQQSDK KGKVICKYFV EGRCTWGDHC NFSHDIELPK 430 440 450 460 470 480 KRELCKFYIT GFCARAENCP YMHGDFPCKL YHTTGNCING DDCMFSHDPL TEETRELLDK 490 500 510 520 530 540 MLADDAEAGA EDEKEVEELK KQGINPLPKP PPGVGLLPTP PRPPGPQAPT SPNGRPMQGG 550 560 570 580 590 600 PPPPPPPPPP PPGPPQMPMP VHEPLSPQQL QQQDMYNKKI PSLFEIVVRP TGQLAEKLGV 610 620 630 640 650 660 RFPGPGGPPG PMGPGPNMGP PGPMGGPMHP DMHPDMHPDM HPDMHADMHA DMPMGPGMNP 670 680 690 700 710 720 GPPMGPGGPP MMPYGPGDSP HSGMMPPIPP AQNFYENFYQ QQEGMEMEPG LLGDAEDYGH 730 740 750 760 770 780 YEELPGEPGE HLFPEHPLEP DSFSEGGPPG RPKPGAGVPD FLPSAQRALY LRIQQKQQEE 790 800 810 820 830 840 EERARRLAES SKQDRENEEG DTGNWYSSDE DEGGSSVTSI LKTLRQQTSS RPPASVGELS 850 860 870 880 890 900 SSGLGDPRLQ KGHPTGSRLA DPRLSRDPRL TRHVEASGGS GPGDSGPSDP RLARALPTSK 910 920 930 940 950 960 PEGSLHSSPV GPSSSKGSGP PPTEEEEGER ALREKAVNIP LDPLPGHPLR DPRSQLQQFS 970 980 990 1000 1010 1020 HIKKDVTLSK PSFARTVLWN PEDLIPLPIP KQDAVPPVPA ALQSMPTLDP RLHRAATAGP 1030 1040 1050 1060 1070 1080 PNARQRPGAS TDSSTQGANL PDFELLSRIL KTVNATGSSA APGSSDKPSD PRVRKAPTDP 1090 1100 1110 1120 1130 1140 RLQKPTDSTA SSRAAKPGPA EAPSPTASPS GDASPPATAP YDPRVLAAGG LGQGGGGGQS 1150 1160 1170 1180 1190 1200 SVLSGISLYD PRTPNAGGKA TEPAADTGAQ PKGAEGNGKS SASKAKEPPF VRKSALEQPE 1210 1220 1230 1240 1250 1260 TGKAGADGGT PTDRYNSYNR PRPKAAAAPA ATTATPPPEG APPQPGVHNL PVPTLFGTVK 1270 1280 1290 1300 QTPKTGSGSP FAGNSPAREG EQDAASLKDV FKGFDPTASP FCQ

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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]	"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 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, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[6]	"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 THR-72, MASS SPECTROMETRY. 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, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[8]	"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 THR-75; SER-76; TYR-155; SER-807; SER-904; SER-908; THR-1106; SER-1108; SER-1114 AND SER-1275, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[9]	"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, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[10]	"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, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[11]	"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] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[12]	"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, MASS SPECTROMETRY.
[13]	"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.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AB028987 mRNA. Translation: BAA83016.2. Different initiation.
AL050155 mRNA. Translation: CAB43296.1.

IPI

IPI00187011.

PIR

T08781.

RefSeq

NP_055983.1. NM_015168.1.

UniGene

Hs.104661.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2CQE	NMR	-	A	417-501	[»]

ProteinModelPortal

Q9UPT8.

ModBase

Search...

Protein-protein interaction databases

IntAct

Q9UPT8. 2 interactions.

STRING

9606.ENSP00000253048.

PTM databases

PhosphoSite

Q9UPT8.

Polymorphism databases

DMDM

94707996.

Proteomic databases

PaxDb

Q9UPT8.

PRIDE

Q9UPT8.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000253048; ENSP00000253048; ENSG00000130749.

GeneID

23211.

KEGG

hsa:23211.

UCSC

uc002pga.4. human.

Organism-specific databases

CTD

23211.

GeneCards

GC19M047569.

HGNC

HGNC:17808. ZC3H4.

HPA

HPA040934.
HPA041068.

neXtProt

NX_Q9UPT8.

PharmGKB

PA162409534.

HUGE

Search...

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG245027.

HOGENOM

HOG000231733.

HOVERGEN

HBG108366.

InParanoid

Q9UPT8.

OMA

SPNGRPM.

OrthoDB

EOG4Z62N1.

Gene expression databases

Bgee

Q9UPT8.

CleanEx

HS_ZC3H4.

Genevestigator

Q9UPT8.

GermOnline

ENSG00000130749. Homo sapiens.

Family and domain databases

InterPro

IPR000571. Znf_CCCH.
[Graphical view]

Pfam

PF00642. zf-CCCH. 1 hit.
[Graphical view]

SMART

SM00356. ZnF_C3H1. 3 hits.
[Graphical view]

PROSITE

PS50103. ZF_C3H1. 3 hits.
[Graphical view]

ProtoNet

Search...

Other

ChiTaRS

ZC3H4. human.

EvolutionaryTrace

Q9UPT8.

GenomeRNAi

23211.

NextBio

44759.

PMAP-CutDB

Q9UPT8.

Entry information

Entry name

ZC3H4_HUMAN

Accession

Primary (citable) accession number: Q9UPT8
Secondary accession number(s): Q9Y420

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 2, 2006
Last sequence update:	May 2, 2006
Last modified:	May 1, 2013
This is version 98 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.