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UniProtKB/Swiss-Prot entry Q9NPA5


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name ZF64A_HUMAN
Primary accession number Q9NPA5
Secondary accession numbers Q9NTS7 Q9NVH4
Integrated into Swiss-Prot on April 30, 2003
Sequence was last modified on October 17, 2006 (Sequence version 3)
Annotations were last modified on    June 16, 2009 (Entry version 75)
Name and origin of the protein
Protein name Zinc finger protein 64 homolog, isoforms 1 and 2
Synonyms Zfp-64
Zinc finger protein 338
Gene name
Name: ZFP64
Synonyms: ZNF338
From
Homo sapiens (Human) [TaxID: 9606] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2), AND VARIANT ASN-451.
TISSUE=Neuron;
DOI=10.1038/ng1285; PubMed=14702039 [NCBI, ExPASy, EBI, Israel, Japan]
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., 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.;
"Complete sequencing and characterization of 21,243 full-length human cDNAs.";
Nat. Genet. 36:40-45(2004).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
DOI=10.1038/414865a; PubMed=11780052 [NCBI, ExPASy, EBI, Israel, Japan]
Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R., Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L., Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P., Bird C.P., Blakey S.E., Bridgeman A.M., Brown A.J., Buck D., Burrill W.D., Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G., Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E., Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D., Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P., Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E., Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J., Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D., Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S., Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D., Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A., Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T., Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I., Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M., Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D., Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M., Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A., Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L., Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L., Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.;
"The DNA sequence and comparative analysis of human chromosome 20.";
Nature 414:865-871(2001).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT ASN-451.
TISSUE=Lymph;
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[4]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-473 AND SER-487, AND MASS SPECTROMETRY.
DOI=10.1126/science.1140321; PubMed=17525332 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage.";
Science 316:1160-1166(2007).
[5]
STRUCTURE BY NMR OF 339-397, AND ZINC-BINDING SITES.
RIKEN structural genomics initiative (RSGI);
"Solution structure of the C2H2 type zinc-binding domain of human zinc finger protein 64, isoforms 1 and 2.";
Submitted (MAY-2005) to the PDB data bank.
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
AK001596; BAA91777.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK001744; BAA91876.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL121771; CAB90276.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL121771; CAB90277.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC012759; AAH12759.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC041622; AAH41622.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
IPI IPI00018906; -.
IPI00254471; -.
RefSeq NP_060667.2; -.
NP_071371.3; -.
NP_955458.1; -.
NP_955459.2; -.
UniGene Hs.473082
3D structure databases
PDB
1X5W; NMR; -; A=341-397.[ExPASy / RCSB / EBI]
2DMD; NMR; -; A=174-256.[ExPASy / RCSB / EBI]
Detailed list of linked structures.
PDBsum 1X5W; -.
2DMD; -.
ModBase Q9NPA5.
Protein-protein interaction databases
IntAct Q9NPA5; 4.
PTM databases
PhosphoSite Q9NPA5; -.
Organism-specific databases
GeneCards GC20M050133; -.
HGNC HGNC:15940; ZFP64.
GenAtlas ZFP64.
PharmGKB PA38060; -.
Gene expression databases
ArrayExpress Q9NPA5; -.
Bgee Q9NPA5; -.
CleanEx HS_ZFP64; -.
GermOnline ENSG00000020256; Homo sapiens.
Ontologies
GO
GO:0005634; Cellular component: nucleus (inferred from electronic annotation from UniProtKB-SubCell).
GO:0003677; Molecular function: DNA binding (inferred from electronic annotation from UniProtKB-KW).
GO:0008270; Molecular function: zinc ion binding (inferred from electronic annotation from UniProtKB-KW).
GO:0006355; Biological process: regulation of transcription, DNA-dependent (inferred from electronic annotation from UniProtKB-KW).
GO:0006350; Biological process: transcription (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.
Family and domain databases
InterPro IPR007087; Znf_C2H2.
IPR015880; Znf_C2H2-like.
IPR013087; Znf_C2H2/integrase_DNA-bd.
Graphical view of domain structure.
Gene3D G3DSA:3.30.160.60; Znf_C2H2/integrase_DNA-bd; 3.
Pfam PF00096; zf-C2H2; 9.
Pfam graphical view of domain structure.
ProDom PD000003; Znf_C2H2; 1.
[Domain structure / List of seq. sharing at least 1 domain]
SMART SM00355; ZnF_C2H2; 11.
SMART graphical view of domain structure.
PROSITE PS00028; ZINC_FINGER_C2H2_1; 5.
PS50157; ZINC_FINGER_C2H2_2; 9.
PROSITE graphical view of domain structure (profiles).
Proteomic databases
PRIDE Q9NPA5; -.
Genome annotation databases
Ensembl ENSG00000020256; Homo sapiens. [Contig view]
GeneID 55734; -.
KEGG hsa:55734; -.
Phylogenomic databases
HOGENOM Q9NPA5; -.
HOVERGEN Q9NPA5; -.
OMA Q9NPA5; HPALLCP.
Other
NextBio 60666; -.
ProtoNet Q9NPA5.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Alternative splicing; DNA-binding; Metal-binding; Nucleus; Phosphoprotein; Polymorphism; Repeat; Transcription; Transcription regulation; Zinc; Zinc-finger.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
CHAIN   1   681  681     Zinc finger protein 64 homolog, isoforms 1 and 2. PRO_0000047307
ZN_FING   175   197  23     C2H2-type 1. 
ZN_FING   203   225  23     C2H2-type 2. 
ZN_FING   231   253  23     C2H2-type 3. 
ZN_FING   259   281  23     C2H2-type 4. 
ZN_FING   287   310  24     C2H2-type 5. 
ZN_FING   315   337  23     C2H2-type 6. 
ZN_FING   343   365  23     C2H2-type 7. 
ZN_FING   371   394  24     C2H2-type 8. 
ZN_FING   425   447  23     C2H2-type 9. 
METAL   345   345        Zinc 1. 
METAL   348   348        Zinc 1. 
METAL   361   361        Zinc 1. 
METAL   365   365        Zinc 1. 
METAL   373   373        Zinc 2. 
METAL   376   376        Zinc 2. 
METAL   389   389        Zinc 2. 
METAL   394   394        Zinc 2. 
MOD_RES   473   473        Phosphothreonine. 
MOD_RES   487   487        Phosphoserine. 
VAR_SEQ   96   149        Missing (in isoform 2). VSP_007284
VARIANT   68    68  1     Q -> P (in dbSNP:rs7353222 [NCBI]). VAR_028019 
VARIANT   139   139  1     P -> L (in dbSNP:rs6021773 [NCBI]). VAR_028020 
VARIANT   425   425  1     F -> Y (in dbSNP:rs16996517 [NCBI]). VAR_028021 
VARIANT   451   451  1     S -> N (in dbSNP:rs3746414 [NCBI]). VAR_028022 
TURN   178   180  3      
HELIX   187   193  7      
HELIX   194   196  3      
STRAND   202   204  3      
STRAND   206   208  3      
STRAND   211   214  4      
HELIX   215   224  10      
STRAND   234   237  4      
STRAND   239   242  4      
HELIX   243   250  8      
STRAND   342   344  3      
STRAND   346   349  4      
STRAND   351   354  4      
HELIX   355   362  8      
HELIX   363   365  3      
STRAND   370   372  3      
STRAND   374   377  4      
STRAND   379   382  4      
HELIX   383   394  12      
STRAND   395   397  3      
Sequence information
Length: 681 AA [This is the length of the unprocessed precursor] Molecular weight: 74644 Da [This is the MW of the unprocessed precursor] CRC64: 949C2DB54BB97E2E [This is a checksum on the sequence]
        10         20         30         40         50         60 
MNASSEGESF AGSVQIPGGT TVLVELTPDI HICGICKQQF NNLDAFVAHK QSGCQLTGTS 

        70         80         90        100        110        120 
AAAPSTVQFV SEETVPATQT QTTTRTITSE TQTITVSAPE FVFEHGYQTY LPTESNENQT 

       130        140        150        160        170        180 
ATVISLPAKS RTKKPTTPPA QKRLNCCYPG CQFKTAYGMK DMERHLKIHT GDKPHKCEVC 

       190        200        210        220        230        240 
GKCFSRKDKL KTHMRCHTGV KPYKCKTCDY AAADSSSLNK HLRIHSDERP FKCQICPYAS 

       250        260        270        280        290        300 
RNSSQLTVHL RSHTGDAPFQ CWLCSAKFKI SSDLKRHMRV HSGEKPFKCE FCNVRCTMKG 

       310        320        330        340        350        360 
NLKSHIRIKH SGNNFKCPHC DFLGDSKATL RKHSRVHQSE HPEKCSECSY SCSSKAALRI 

       370        380        390        400        410        420 
HERIHCTDRP FKCNYCSFDT KQPSNLSKHM KKFHGDMVKT EALERKDTGR QSSRQVAKLD 

       430        440        450        460        470        480 
AKKSFHCDIC DASFMREDSL RSHKRQHSEY SESKNSDVTV LQFQIDPSKQ PATPLTVGHL 

       490        500        510        520        530        540 
QVPLQPSQVP QFSEGRVKII VGHQVPQANT IVQAAAAAVN IVPPALVAQN PEELPGNSRL 

       550        560        570        580        590        600 
QILRQVSLIA PPQSSRCPSE AGAMTQPAVL LTTHEQTDGA TLHQTLIPTA SGGPQEGSGN 

       610        620        630        640        650        660 
QTFITSSGIT CTDFEGLNAL IQEGTAEVTV VSDGGQNIAV ATTAPPVFSS SSQQELPKQT 

       670        680 
YSIIQGAAHP ALLCPADSIP D 

Q9NPA5 in FASTA format

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BLAST logo BLAST submission on ExPASy/SIB
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Tools Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
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