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Q86VM9 (ZCH18_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 69. 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·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Zinc finger CCCH domain-containing protein 18
Alternative name(s):
Nuclear protein NHN1
Gene names
Name:ZC3H18
Synonyms:NHN1
OrganismHomo sapiens (Human)
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length953 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Subcellular location

Nucleus By similarity.

Sequence similarities

Contains 1 C3H1-type zinc finger.

Ontologies

Keywords
   Cellular componentNucleus
   Coding sequence diversityAlternative splicing
Polymorphism
   DomainCoiled coil
Zinc-finger
   LigandMetal-binding
Zinc
   PTMPhosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Cellular componentnucleus

Inferred from direct assay. Source: HPA

   Molecular functionnucleic acid binding

Inferred from electronic annotation. Source: InterPro

zinc ion binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q86VM9-1)

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.
Isoform 2 (identifier: Q86VM9-2)

The sequence of this isoform differs from the canonical sequence as follows:
     228-228: M → MKDVVTPLSTLLPPISNSIPFRGQV
     412-469: NRQRERERERERDRERERRQRERERERERERDKERQRRKEEWERERAKRDEKDRQHRD → RE
     683-953: TLSGSGSGSG...RKRAKIPGKA → LIKEAGSAMN...PARCLGGRSC

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 953953Zinc finger CCCH domain-containing protein 18
PRO_0000311242

Regions

Zinc finger219 – 24527C3H1-type
Coiled coil105 – 13430 Potential
Coiled coil399 – 46466 Potential
Coiled coil921 – 95030 Potential
Compositional bias201 – 2044Poly-Asp
Compositional bias259 – 29638Pro-rich
Compositional bias532 – 746215Ser-rich

Amino acid modifications

Modified residue461Phosphoserine Ref.4 Ref.9 Ref.11 Ref.12 Ref.14
Modified residue671Phosphoserine Ref.4 Ref.11 Ref.14
Modified residue741Phosphoserine Ref.4 Ref.11
Modified residue781Phosphoserine Ref.4 Ref.11
Modified residue831Phosphoserine Ref.4
Modified residue951Phosphoserine Ref.11
Modified residue1091Phosphothreonine Ref.11
Modified residue1101Phosphoserine Ref.11
Modified residue4871Phosphoserine Ref.4 Ref.7
Modified residue5321Phosphoserine Ref.4 Ref.5 Ref.10 Ref.11 Ref.12
Modified residue5341Phosphoserine Ref.4 Ref.5 Ref.6 Ref.8 Ref.10 Ref.11 Ref.12 Ref.13 Ref.14
Modified residue5991Phosphoserine Ref.4
Modified residue6011Phosphoserine Ref.4
Modified residue6031Phosphoserine Ref.4
Modified residue6041Phosphoserine Ref.4
Modified residue6051Phosphoserine Ref.4
Modified residue6071Phosphoserine Ref.4
Modified residue6091Phosphoserine Ref.4
Modified residue6111Phosphothreonine Ref.4
Modified residue6131Phosphoserine Ref.4
Modified residue6771Phosphothreonine Ref.4
Modified residue8421Phosphoserine Ref.4
Modified residue8521Phosphoserine By similarity
Modified residue8571Phosphoserine Ref.4
Modified residue8681Phosphoserine Ref.4 Ref.6 Ref.10 Ref.13
Modified residue8931Phosphoserine Ref.4

Natural variations

Alternative sequence2281M → MKDVVTPLSTLLPPISNSIP FRGQV in isoform 2.
VSP_029453
Alternative sequence412 – 46958NRQRE…RQHRD → RE in isoform 2.
VSP_029454
Alternative sequence683 – 953271TLSGS…IPGKA → LIKEAGSAMNHQTRTGRALL QPSGPTHPQTEVLGTGSQVG DWAPRSQSGREARTPKPLQP RLTGSASCHPSPRAPARSRA CPAKPRIPAPPAPNQGRPAR CLGGRSC in isoform 2.
VSP_029455
Natural variant3681A → T.
Corresponds to variant rs34808360 [ dbSNP | Ensembl ].
VAR_037188
Natural variant4401R → H. Ref.3
Corresponds to variant rs17855686 [ dbSNP | Ensembl ].
VAR_037189

Experimental info

Sequence conflict2511Y → H in BAB71237. Ref.1

Sequences

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

Last modified November 24, 2009. Version 2.
Checksum: F12E87B342E1F892

FASTA953106,378
        10         20         30         40         50         60 
MDVAESPERD PHSPEDEEQP QGLSDDDILR DSGSDQDLDG AGVRASDLED EESAARGPSQ 

        70         80         90        100        110        120 
EEEDNHSDEE DRASEPKSQD QDSEVNELSR GPTSSPCEEE GDEGEEDRTS DLRDEASSVT 

       130        140        150        160        170        180 
RELDEHELDY DEEVPEEPAP AVQEDEAEKA GAEDDEEKGE GTPREEGKAG VQSVGEKESL 

       190        200        210        220        230        240 
EAAKEKKKED DDGEIDDGEI DDDDLEEGEV KDPSDRKVRP RPTCRFFMKG NCTWGMNCRF 

       250        260        270        280        290        300 
IHPGVNDKGN YSLITKADPF PPNGAPPLGP HPLMPANPWG GPVVDEILPP PPPEPPTESA 

       310        320        330        340        350        360 
WERGLRHAKE VLKKATIRKE QEPDFEEKRF TVTIGEDERE FDKENEVFRD WNSRIPRDVR 

       370        380        390        400        410        420 
DTVLEPYADP YYDYEIERFW RGGQYENFRV QYTETEPYHN YRERERERER ENRQRERERE 

       430        440        450        460        470        480 
RERDRERERR QRERERERER ERDKERQRRK EEWERERAKR DEKDRQHRDR DREKEREKEK 

       490        500        510        520        530        540 
GKPKPRSPQP PSRQAEPPKK EAATTGPQVK RADEWKDPWR RSKSPKKKLG VSVSPSRARR 

       550        560        570        580        590        600 
RRKTSASSAS ASNSSRSSSR SSSYSGSGSS RSRSRSSSYS SYSSRSSRHS SFSGSRSRSR 

       610        620        630        640        650        660 
SFSSSPSPSP TPSPHRPSIR TKGEPAPPPG KAGEKSVKKP APPPAPPQAT KTTAPVPEPT 

       670        680        690        700        710        720 
KPGDPREARR KERPARTPPR RRTLSGSGSG SGSSYSGSSS RSRSLSVSSV SSVSSATSSS 

       730        740        750        760        770        780 
SSAHSVDSED MYADLASPVS SASSRSPAPA QTRKEKGKSK KEDGVKEEKR KRDSSTQPPK 

       790        800        810        820        830        840 
SAKPPAGGKS SQQPSTPQQA PPGQPQQGTF VAHKEIKLTL LNKAADKGSR KRYEPSDKDR 

       850        860        870        880        890        900 
QSPPPAKRPN TSPDRGSRDR KSGGRLGSPK PERQRGQNSK APAAPADRKR QLSPQSKSSS 

       910        920        930        940        950 
KVTSVPGKAS DPGAASTKSG KASTLSRREE LLKQLKAVED AIARKRAKIP GKA 

« Hide

Isoform 2 [UniParc].

Checksum: 883B3D5A20DCBC4F
Show »

FASTA75784,100

References

[1]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed: 14702039] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
Tissue: Brain.
[2]"The sequence and analysis of duplication-rich human chromosome 16."
Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G., Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E., Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J. expand/collapse author list , Buckingham J.M., Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C., Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M., Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M., Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E., Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H., Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y., Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J., Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D., Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S., Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A., Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M., Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H., Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A., Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J., DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J., Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M., Myers R.M., Rubin E.M., Pennacchio L.A.
Nature 432:988-994(2004) [PubMed: 15616553] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), VARIANT HIS-440.
Tissue: Cervix and Testis.
[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: 17081983] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-46; SER-67; SER-74; SER-78; SER-83; SER-487; SER-532; SER-534; SER-599; SER-601; SER-603; SER-604; SER-605; SER-607; SER-609; THR-611; SER-613; THR-677; SER-842; SER-857; SER-868 AND SER-893, MASS SPECTROMETRY.
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: 16964243] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-532 AND SER-534, MASS SPECTROMETRY.
Tissue: Cervix carcinoma.
[6]"Improved titanium dioxide enrichment of phosphopeptides from HeLa cells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra."
Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.
J. Proteome Res. 6:4150-4162(2007) [PubMed: 17924679] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-534 AND SER-868, MASS SPECTROMETRY.
Tissue: Cervix carcinoma.
[7]"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-487, MASS SPECTROMETRY.
Tissue: Embryonic kidney.
[8]"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-534, MASS SPECTROMETRY.
Tissue: Cervix carcinoma.
[9]"Phosphorylation analysis of primary human T lymphocytes using sequential IMAC and titanium oxide enrichment."
Carrascal M., Ovelleiro D., Casas V., Gay M., Abian J.
J. Proteome Res. 7:5167-5176(2008) [PubMed: 19367720] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-46, MASS SPECTROMETRY.
Tissue: T-cell.
[10]"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-532; SER-534 AND SER-868, MASS SPECTROMETRY.
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: 18669648] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-46; SER-67; SER-74; SER-78; SER-95; THR-109; SER-110; SER-532 AND SER-534, MASS SPECTROMETRY.
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: 19413330] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-46; SER-532 AND SER-534, MASS SPECTROMETRY.
Tissue: Embryonic kidney.
[13]"Large-scale proteomics analysis of the human kinome."
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G., Mann M., Daub H.
Mol. Cell. Proteomics 8:1751-1764(2009) [PubMed: 19369195] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-534 AND SER-868, MASS SPECTROMETRY.
[14]"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-46; SER-67 AND SER-534, MASS SPECTROMETRY.
Tissue: Leukemic T-cell.
[15]"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: 21269460] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AK056632 mRNA. Translation: BAB71237.1.
AC116552 Genomic DNA. No translation available.
BC001584 mRNA. Translation: AAH01584.1.
BC050463 mRNA. Translation: AAH50463.1.
IPIIPI00293312.
IPI00328929.
RefSeqNP_653205.3. NM_144604.3.
UniGeneHs.93670.

3D structure databases

ProteinModelPortalQ86VM9.
ModBaseSearch...

Protein-protein interaction databases

IntActQ86VM9. 3 interactions.

PTM databases

PhosphoSiteQ86VM9.

Polymorphism databases

DMDM269849528.

Proteomic databases

PRIDEQ86VM9.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000301011; ENSP00000301011; ENSG00000158545.
GeneID124245.
KEGGhsa:124245.
UCSCuc002fky.1. human.

Organism-specific databases

CTD124245.
GeneCardsGC16P088636.
H-InvDBHIX0013334.
HGNCHGNC:25091. ZC3H18.
HPAHPA040847.
HPA041327.
neXtProtNX_Q86VM9.
PharmGKBPA162409533.
GenAtlasSearch...

Phylogenomic databases

eggNOGprNOG10161.
GeneTreeENSGT00580000081375.
HOVERGENHBG103346.
InParanoidQ86VM9.
OrthoDBEOG46T31J.
PhylomeDBQ86VM9.

Gene expression databases

ArrayExpressQ86VM9.
BgeeQ86VM9.
CleanExHS_ZC3H18.
GenevestigatorQ86VM9.

Family and domain databases

InterProIPR000571. Znf_CCCH.
[Graphical view]
KOK13092.
SMARTSM00356. ZnF_C3H1. 1 hit.
[Graphical view]
PROSITEPS50103. ZF_C3H1. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio81250.

Entry information

Entry nameZCH18_HUMAN
AccessionPrimary (citable) accession number: Q86VM9
Secondary accession number(s): Q96DG4, Q96MP7
Entry history
Integrated into UniProtKB/Swiss-Prot: November 13, 2007
Last sequence update: November 24, 2009
Last modified: January 25, 2012
This is version 69 of the entry and version 2 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

Human chromosome 16

Human chromosome 16: entries, gene names and cross-references to MIM

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

SIMILARITY comments

Index of protein domains and families