ID ZN135_HUMAN Reviewed; 658 AA. AC P52742; Q5U5L3; DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. DT 18-MAY-2010, sequence version 3. DT 05-OCT-2010, entry version 84. DE RecName: Full=Zinc finger protein 135; DE AltName: Full=Zinc finger protein 61; DE AltName: Full=Zinc finger protein 78-like 1; GN Name=ZNF135; Synonyms=ZNF61, ZNF78L1; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15057824; DOI=10.1038/nature02399; RA Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., RA Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., RA Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., RA Caenepeel S., Carrano A.V., Caoile C., Chan Y.M., Christensen M., RA Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., RA Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M., RA Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T., RA Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H., RA Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S., RA Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J., RA Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M., RA Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J., RA Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D., RA Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A., RA Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I., RA Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E., RA Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M., RA Rubin E.M., Lucas S.M.; RT "The DNA sequence and biology of human chromosome 19."; RL Nature 428:529-535(2004). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT ASP-22. RC TISSUE=Testis; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA] OF 166-658. RC TISSUE=Insulinoma; RX MEDLINE=96044430; PubMed=7557990; DOI=10.1006/geno.1995.1040; RA Tommerup N., Vissing H.; RT "Isolation and fine mapping of 16 novel human zinc finger-encoding RT cDNAs identify putative candidate genes for developmental and RT malignant disorders."; RL Genomics 27:259-264(1995). CC -!- FUNCTION: May be involved in transcriptional regulation. CC -!- SUBCELLULAR LOCATION: Nucleus (Potential). CC -!- SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein CC family. CC -!- SIMILARITY: Contains 16 C2H2-type zinc fingers. CC -!- SIMILARITY: Contains 1 KRAB domain. CC -!- SEQUENCE CAUTION: CC Sequence=AAC50254.1; Type=Frameshift; Positions=207, 558, 563; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; BC046434; AAH46434.1; -; mRNA. DR EMBL; U09413; AAC50254.1; ALT_FRAME; mRNA. DR IPI; IPI00395473; -. DR PIR; I38600; I38600. DR UniGene; Hs.85863; -. DR ProteinModelPortal; P52742; -. DR STRING; P52742; -. DR Ensembl; ENST00000313434; ENSP00000321406; ENSG00000176293. DR UCSC; uc002qre.1; human. DR GeneCards; GC19P058571; -. DR HGNC; HGNC:12919; ZNF135. DR HPA; HPA006961; -. DR MIM; 604077; gene. DR PharmGKB; PA37507; -. DR eggNOG; prNOG16961; -. DR HOVERGEN; HBG018163; -. DR InParanoid; P52742; -. DR PhylomeDB; P52742; -. DR NextBio; 29824; -. DR ArrayExpress; P52742; -. DR Bgee; P52742; -. DR CleanEx; HS_ZNF135; -. DR Genevestigator; P52742; -. DR GermOnline; ENSG00000176293; Homo sapiens. DR GO; GO:0005634; C:nucleus; NAS:UniProtKB. DR GO; GO:0003700; F:transcription factor activity; NAS:UniProtKB. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0006355; P:regulation of transcription, DNA-dependent; NAS:UniProtKB. DR GO; GO:0006350; P:transcription; IEA:UniProtKB-KW. DR InterPro; IPR001909; Krueppel-associated_box. DR InterPro; IPR007087; Znf_C2H2. DR InterPro; IPR015880; Znf_C2H2-like. DR InterPro; IPR013087; Znf_C2H2/integrase_DNA-bd. DR Gene3D; G3DSA:3.30.160.60; Znf_C2H2/integrase_DNA-bd; 16. DR Pfam; PF01352; KRAB; 1. DR Pfam; PF00096; zf-C2H2; 13. DR SMART; SM00349; KRAB; 1. DR SMART; SM00355; ZnF_C2H2; 16. DR SUPFAM; SSF109640; Krueppel-associated_box; 1. DR PROSITE; PS50805; KRAB; 1. DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 16. DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 16. PE 2: Evidence at transcript level; KW Complete proteome; DNA-binding; Metal-binding; Nucleus; Polymorphism; KW Repeat; Transcription; Transcription regulation; Zinc; Zinc-finger. FT CHAIN 1 658 Zinc finger protein 135. FT /FTId=PRO_0000047419. FT DOMAIN 14 85 KRAB. FT ZN_FING 214 236 C2H2-type 1. FT ZN_FING 242 264 C2H2-type 2. FT ZN_FING 270 292 C2H2-type 3. FT ZN_FING 298 320 C2H2-type 4. FT ZN_FING 326 348 C2H2-type 5. FT ZN_FING 354 376 C2H2-type 6. FT ZN_FING 382 404 C2H2-type 7. FT ZN_FING 410 432 C2H2-type 8. FT ZN_FING 438 460 C2H2-type 9. FT ZN_FING 466 488 C2H2-type 10. FT ZN_FING 494 516 C2H2-type 11. FT ZN_FING 522 544 C2H2-type 12. FT ZN_FING 550 572 C2H2-type 13. FT ZN_FING 578 600 C2H2-type 14. FT ZN_FING 606 628 C2H2-type 15. FT ZN_FING 634 656 C2H2-type 16. FT VARIANT 22 22 G -> D (in dbSNP:rs1469087). FT /FTId=VAR_052774. FT VARIANT 507 507 S -> L (in dbSNP:rs2228277). FT /FTId=VAR_052775. FT VARIANT 517 517 T -> A (in dbSNP:rs2228278). FT /FTId=VAR_052776. FT VARIANT 579 579 G -> R (in dbSNP:rs2228279). FT /FTId=VAR_052777. FT VARIANT 592 592 S -> L (in dbSNP:rs2228275). FT /FTId=VAR_052778. FT CONFLICT 166 166 G -> R (in Ref. 2; AAC50254). SQ SEQUENCE 658 AA; 75261 MW; ED6A4FB042CB3CE5 CRC64; MTPGVRVSTD PEQVTFEDVV VGFSQEEWGQ LKPAQRTLYR DVMLDTFRLL VSVGHWLPKP NVISLLEQEA ELWAVESRLP QGVYPDLETR PKVKLSVLKQ GISEEISNSV ILVERFLWDG LWYCRGEDTE GHWEWSCESL ESLAVPVAFT PVKTPVLEQW QRNGFGENIS LNPDLPHQPM TPERQSPHTW GTRGKREKPD LNVLQKTCVK EKPYKCQECG KAFSHSSALI EHHRTHTGER PYECHECLKG FRNSSALTKH QRIHTGEKPY KCTQCGRTFN QIAPLIQHQR THTGEKPYEC SECGKSFSFR SSFSQHERTH TGEKPYECSE CGKAFRQSIH LTQHLRIHTG EKPYQCGECG KAFSHSSSLT KHQRIHTGEK PYECHECGKA FTQITPLIQH QRTHTGEKPY ECGECGKAFS QSTLLTEHRR IHTGEKPYGC NECGKTFSHS SSLSQHERTH TGEKPYECSQ CGKAFRQSTH LTQHQRIHTG EKPYECNDCG KAFSHSSSLT KHQRIHTGEK PYECNQCGRA FSQLAPLIQH QRIHTGEKPY ECNQCGRAFS QSSLLIEHQR IHTKEKPYGC NECGKSFSHS SSLSQHERTH TGEKPYECHD CGKSFRQSTH LTQHRRIHTG EKPYACRDCG KAFTHSSSLT KHQRTHTG //