ID R144A_HUMAN Reviewed; 292 AA. AC P50876; D6W4Y6; Q585H5; DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. DT 23-OCT-2007, sequence version 2. DT 21-SEP-2011, entry version 100. DE RecName: Full=Probable E3 ubiquitin-protein ligase RNF144A; DE EC=6.3.2.-; DE AltName: Full=RING finger protein 144A; DE AltName: Full=UbcM4-interacting protein 4; DE AltName: Full=Ubiquitin-conjugating enzyme 7-interacting protein 4; GN Name=RNF144A; Synonyms=KIAA0161, RNF144, UBCE7IP4; 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 MRNA], AND VARIANT ALA-4. RC TISSUE=Bone marrow; RX MEDLINE=96281124; PubMed=8724849; DOI=10.1093/dnares/3.1.17; RA Nagase T., Seki N., Ishikawa K., Tanaka A., Nomura N.; RT "Prediction of the coding sequences of unidentified human genes. V. RT The coding sequences of 40 new genes (KIAA0161-KIAA0200) deduced by RT analysis of cDNA clones from human cell line KG-1."; RL DNA Res. 3:17-24(1996). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15815621; DOI=10.1038/nature03466; RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., RA Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., RA Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., RA Kremitzki C., Oddy L., Du H., Sun H., Bradshaw-Cordum H., Ali J., RA Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., RA Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., RA Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., RA Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., RA Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., RA Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., RA Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., RA Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., RA Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., RA Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., RA Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., RA Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., RA Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., RA Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., RA McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., RA Waterston R.H., Wilson R.K.; RT "Generation and annotation of the DNA sequences of human chromosomes 2 RT and 4."; RL Nature 434:724-731(2005). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT ALA-4. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R., RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., RA Venter J.C.; RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT ALA-4. RC TISSUE=Ovary; 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 [5] RP INTERACTION WITH UBE2L3. RX MEDLINE=99358765; PubMed=10431818; DOI=10.1016/S0014-5793(99)00823-6; RA Martinez-Noel G., Niedenthal R., Tamura T., Harbers K.; RT "A family of structurally related RING finger proteins interacts RT specifically with the ubiquitin-conjugating enzyme UbcM4."; RL FEBS Lett. 454:257-261(1999). RN [6] RP STRUCTURE BY NMR OF 20-100. RG RIKEN structural genomics initiative (RSGI); RT "Solution structure of the RING finger domain of the human UbcM4- RT interacting protein 4."; RL Submitted (NOV-2004) to the PDB data bank. CC -!- FUNCTION: E3 ubiquitin-protein ligase which accepts ubiquitin from CC E2 ubiquitin-conjugating enzymes UBE2L3 and UBE2L6 in the form of CC a thioester and then directly transfers the ubiquitin to targeted CC substrates (By similarity). CC -!- PATHWAY: Protein modification; protein ubiquitination. CC -!- SUBUNIT: Interacts with UBE2L3. CC -!- SUBCELLULAR LOCATION: Membrane; Single-pass membrane protein CC (Potential). CC -!- SIMILARITY: Belongs to the RBR family. RNF144 subfamily. CC -!- SIMILARITY: Contains 1 IBR-type zinc finger. CC -!- SIMILARITY: Contains 2 RING-type zinc fingers. CC -!- CAUTION: Lacks the His residue in the RING-type domain 2 that is CC one of the conserved features of the family. CC -!- SEQUENCE CAUTION: CC Sequence=BAA11478.2; Type=Erroneous initiation; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; D79983; BAA11478.2; ALT_INIT; mRNA. DR EMBL; AC068481; AAX82010.1; -; Genomic_DNA. DR EMBL; CH471053; EAX01030.1; -; Genomic_DNA. DR EMBL; CH471053; EAX01031.1; -; Genomic_DNA. DR EMBL; BC050373; AAH50373.1; -; mRNA. DR IPI; IPI00220842; -. DR RefSeq; NP_055561.2; NM_014746.3. DR UniGene; Hs.22146; -. DR PDB; 1WIM; NMR; -; A=20-100. DR PDBsum; 1WIM; -. DR ProteinModelPortal; P50876; -. DR SMR; P50876; 20-157, 179-230. DR IntAct; P50876; 6. DR STRING; P50876; -. DR PRIDE; P50876; -. DR Ensembl; ENST00000320892; ENSP00000321330; ENSG00000151692. DR GeneID; 9781; -. DR KEGG; hsa:9781; -. DR UCSC; uc002qys.1; human. DR CTD; 9781; -. DR GeneCards; GC02P006974; -. DR HGNC; HGNC:20457; RNF144A. DR neXtProt; NX_P50876; -. DR PharmGKB; PA162401542; -. DR eggNOG; prNOG07763; -. DR GeneTree; ENSGT00550000074424; -. DR HOGENOM; HBG314219; -. DR HOVERGEN; HBG052072; -. DR InParanoid; P50876; -. DR OMA; CKCSKGD; -. DR OrthoDB; EOG4WWRK1; -. DR PhylomeDB; P50876; -. DR NextBio; 36828; -. DR ArrayExpress; P50876; -. DR Bgee; P50876; -. DR CleanEx; HS_RNF144A; -. DR Genevestigator; P50876; -. DR GO; GO:0005794; C:Golgi apparatus; IDA:UniProtKB. DR GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW. DR GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR InterPro; IPR002867; Znf_C6HC. DR InterPro; IPR001841; Znf_RING. DR InterPro; IPR017907; Znf_RING_CS. DR Pfam; PF01485; IBR; 2. DR SMART; SM00647; IBR; 2. DR SMART; SM00184; RING; 2. DR PROSITE; PS00518; ZF_RING_1; 1. DR PROSITE; PS50089; ZF_RING_2; 1. PE 1: Evidence at protein level; KW 3D-structure; Complete proteome; Ligase; Membrane; Metal-binding; KW Polymorphism; Reference proteome; Repeat; Transmembrane; KW Transmembrane helix; Ubl conjugation pathway; Zinc; Zinc-finger. FT CHAIN 1 292 Probable E3 ubiquitin-protein ligase FT RNF144A. FT /FTId=PRO_0000056298. FT TRANSMEM 250 270 Helical; (Potential). FT ZN_FING 20 70 RING-type 1; atypical. FT ZN_FING 91 156 IBR-type. FT ZN_FING 185 214 RING-type 2; degenerate. FT VARIANT 4 4 T -> A (in dbSNP:rs364891). FT /FTId=VAR_035375. FT STRAND 21 23 FT HELIX 29 31 FT STRAND 32 35 FT TURN 36 39 FT STRAND 40 43 FT HELIX 44 57 FT HELIX 78 84 FT HELIX 87 99 SQ SEQUENCE 292 AA; 32890 MW; E5BE7BC9560DCF93 CRC64; MTTTRYRPTW DLALDPLVSC KLCLGEYPVE QMTTIAQCQC IFCTLCLKQY VELLIKEGLE TAISCPDAAC PKQGHLQENE IECMVAAEIM QRYKKLQFER EVLFDPCRTW CPASTCQAVC QLQDVGLQTP QPVQCKACRM EFCSTCKASW HPGQGCPETM PITFLPGETS AAFKMEEDDA PIKRCPKCKV YIERDEGCAQ MMCKNCKHAF CWYCLESLDD DFLLIHYDKG PCRNKLGHSR ASVIWHRTQV VGIFAGFGLL LLVASPFLLL ATPFVLCCKC KCSKGDDDPL PT //