ID RN103_HUMAN Reviewed; 685 AA.
AC O00237; A6NFV6; B2RAG4; Q53SU6; Q8IVB9;
DT 31-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1997, sequence version 1.
DT 10-MAY-2017, entry version 127.
DE RecName: Full=E3 ubiquitin-protein ligase RNF103;
DE EC=2.3.2.27;
DE AltName: Full=KF-1;
DE Short=hKF-1;
DE AltName: Full=RING finger protein 103;
DE AltName: Full=RING-type E3 ubiquitin transferase RNF103 {ECO:0000305};
DE AltName: Full=Zinc finger protein 103 homolog;
DE Short=Zfp-103;
GN Name=RNF103; Synonyms=ZFP103;
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 [MRNA], AND TISSUE SPECIFICITY.
RC TISSUE=Brain;
RX PubMed=9070305; DOI=10.1006/bbrc.1996.6033;
RA Yasojima K., Tsujimura A., Mizuno T., Shigeyoshi Y., Inazawa J.,
RA Kikuno R., Kuma K., Ohkubo K., Hosokawa Y., Ibata Y., Abe T.,
RA Miyata T., Matsubara K., Nakajima K., Hashimoto-Gotoh T.;
RT "Cloning of human and mouse cDNAs encoding novel zinc finger proteins
RT expressed in cerebellum and hippocampus.";
RL Biochem. Biophys. Res. Commun. 231:481-487(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC TISSUE=Peripheral blood;
RA Tsujimura A., Hashimoto-Gotoh T.;
RT "Structure of human kf-1 genomic DNA.";
RL Submitted (DEC-2000) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
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 [6]
RP FUNCTION, AND MUTAGENESIS OF CYS-621.
RX PubMed=10500182; DOI=10.1073/pnas.96.20.11364;
RA Lorick K.L., Jensen J.P., Fang S., Ong A.M., Hatakeyama S.,
RA Weissman A.M.;
RT "RING fingers mediate ubiquitin-conjugating enzyme (E2)-dependent
RT ubiquitination.";
RL Proc. Natl. Acad. Sci. U.S.A. 96:11364-11369(1999).
RN [7]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH DERL1 AND VCP.
RX PubMed=18675248; DOI=10.1016/j.bbrc.2008.07.126;
RA Maruyama Y., Yamada M., Takahashi K., Yamada M.;
RT "Ubiquitin ligase Kf-1 is involved in the endoplasmic reticulum-
RT associated degradation pathway.";
RL Biochem. Biophys. Res. Commun. 374:737-741(2008).
CC -!- FUNCTION: Acts as an E2-dependent E3 ubiquitin-protein ligase,
CC probably involved in the ER-associated protein degradation
CC pathway. {ECO:0000269|PubMed:10500182,
CC ECO:0000269|PubMed:18675248}.
CC -!- CATALYTIC ACTIVITY: S-ubiquitinyl-[E2 ubiquitin-conjugating
CC enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-
CC conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor
CC protein]-L-lysine.
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC -!- SUBUNIT: Interacts with DERL1 and VCP.
CC {ECO:0000269|PubMed:18675248}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:18675248}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:18675248}.
CC -!- TISSUE SPECIFICITY: Highly expressed in the normal cerebellum but
CC not in the cerebral cortex. {ECO:0000269|PubMed:9070305}.
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; D76444; BAA19739.1; -; mRNA.
DR EMBL; AB052743; BAB20900.1; -; Genomic_DNA.
DR EMBL; AK314180; BAG36861.1; -; mRNA.
DR EMBL; AC015971; AAX93079.1; -; Genomic_DNA.
DR EMBL; BC035053; AAH35053.1; -; mRNA.
DR EMBL; BC110333; AAI10334.1; -; mRNA.
DR CCDS; CCDS33237.1; -.
DR PIR; JC5392; JC5392.
DR RefSeq; NP_001185880.1; NM_001198951.1.
DR RefSeq; NP_001185881.1; NM_001198952.1.
DR RefSeq; NP_005658.1; NM_005667.3.
DR UniGene; Hs.469199; -.
DR UniGene; Hs.731426; -.
DR ProteinModelPortal; O00237; -.
DR SMR; O00237; -.
DR BioGrid; 113601; 13.
DR IntAct; O00237; 9.
DR STRING; 9606.ENSP00000237455; -.
DR iPTMnet; O00237; -.
DR PhosphoSitePlus; O00237; -.
DR BioMuta; RNF103; -.
DR PaxDb; O00237; -.
DR PeptideAtlas; O00237; -.
DR PRIDE; O00237; -.
DR DNASU; 7844; -.
DR Ensembl; ENST00000237455; ENSP00000237455; ENSG00000239305.
DR GeneID; 7844; -.
DR KEGG; hsa:7844; -.
DR UCSC; uc002srn.4; human.
DR CTD; 7844; -.
DR DisGeNET; 7844; -.
DR GeneCards; RNF103; -.
DR HGNC; HGNC:12859; RNF103.
DR HPA; HPA057922; -.
DR MIM; 602507; gene.
DR neXtProt; NX_O00237; -.
DR OpenTargets; ENSG00000239305; -.
DR PharmGKB; PA37448; -.
DR eggNOG; KOG0800; Eukaryota.
DR eggNOG; ENOG41121N2; LUCA.
DR GeneTree; ENSGT00390000006413; -.
DR HOGENOM; HOG000006578; -.
DR HOVERGEN; HBG054144; -.
DR InParanoid; O00237; -.
DR KO; K15695; -.
DR OMA; GKVHWEK; -.
DR OrthoDB; EOG091G0EZD; -.
DR PhylomeDB; O00237; -.
DR TreeFam; TF329229; -.
DR Reactome; R-HSA-901032; ER Quality Control Compartment (ERQC).
DR UniPathway; UPA00143; -.
DR GenomeRNAi; 7844; -.
DR PRO; PR:O00237; -.
DR Proteomes; UP000005640; Chromosome 2.
DR Bgee; ENSG00000239305; -.
DR CleanEx; HS_RNF103; -.
DR Genevisible; O00237; HS.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; TAS:Reactome.
DR GO; GO:0044322; C:endoplasmic reticulum quality control compartment; IEA:GOC.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:1904264; F:ubiquitin protein ligase activity involved in ERAD pathway; TAS:Reactome.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; IDA:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0007417; P:central nervous system development; TAS:ProtInc.
DR GO; GO:1904380; P:endoplasmic reticulum mannose trimming; TAS:Reactome.
DR GO; GO:0016567; P:protein ubiquitination; IDA:UniProtKB.
DR GO; GO:0030433; P:ubiquitin-dependent ERAD pathway; IDA:UniProtKB.
DR CDD; cd00162; RING; 1.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR Pfam; PF13639; zf-RING_2; 1.
DR SMART; SM00184; RING; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 1: Evidence at protein level;
KW Complete proteome; Endoplasmic reticulum; Membrane; Metal-binding;
KW Reference proteome; Transferase; Transmembrane; Transmembrane helix;
KW Ubl conjugation pathway; Zinc; Zinc-finger.
FT CHAIN 1 685 E3 ubiquitin-protein ligase RNF103.
FT /FTId=PRO_0000056084.
FT TRANSMEM 6 26 Helical. {ECO:0000255}.
FT TRANSMEM 326 346 Helical. {ECO:0000255}.
FT TRANSMEM 366 386 Helical. {ECO:0000255}.
FT TRANSMEM 411 431 Helical. {ECO:0000255}.
FT ZN_FING 621 663 RING-type. {ECO:0000255|PROSITE-
FT ProRule:PRU00175}.
FT MUTAGEN 621 621 C->S: Loss of E2-dependent
FT ubiquitination.
FT {ECO:0000269|PubMed:10500182}.
FT CONFLICT 22 22 F -> L (in Ref. 3; BAG36861).
FT {ECO:0000305}.
FT CONFLICT 251 251 S -> P (in Ref. 5; AAH35053).
FT {ECO:0000305}.
FT CONFLICT 287 287 S -> P (in Ref. 3; BAG36861).
FT {ECO:0000305}.
FT CONFLICT 502 502 P -> H (in Ref. 5; AAH35053).
FT {ECO:0000305}.
CC --------------------------------------------------------------------------
CC The following FT lines are automated annotations from the MyHits database.
CC --------------------------------------------------------------------------
FT MYHIT 621 663 iprf:ZF_RING_2 [T]
FT MYHIT 621 662 ismart:RING [T]
FT MYHIT 620 663 ipfam:zf-RING_2 [T]
SQ SEQUENCE 685 AA; 79405 MW; 5AE7283EB38F533F CRC64;
MWLKLFFLLL YFLVLFVLAR FFEAIVWYET GIFATQLVDP VALSFKKLKT ILECRGLGYS
GLPEKKDVRE LVEKSGDLME GELYSALKEE EASESVSSTN FSGEMHFYEL VEDTKDGIWL
VQVIANDRSP LVGKIHWEKM VKKVSRFGIR TGTFNCSSDP RYCRRRGWVR STLIMSVPQT
STSKGKVMLK EYSGRKIEVE HIFKWITAHA ASRIKTIYNA EHLKEEWNKS DQYWLKIYLF
ANLDQPPAFF SALSIKFTGR VEFIFVNVEN WDNKSYMTDI GIYNMPSYIL RTPEGIYRYG
NHTGEFISLQ AMDSFLRSLQ PEVNDLFVLS LVLVNLMAWM DLFITQGATI KRFVVLISTL
GTYNSLLIIS WLPVLGFLQL PYLDSFYEYS LKLLRYSNTT TLASWVRADW MFYSSHPALF
LSTYLGHGLL IDYFEKKRRR NNNNDEVNAN NLEWLSSLWD WYTSYLFHPI ASFQNFPVES
DWDEDPDLFL ERLAFPDLWL HPLIPTDYIK NLPMWRFKCL GVQSEEEMSE GSQDTENDSE
SENTDTLSSE KEVFEDKQSV LHNSPGTASH CDAEACSCAN KYCQTSPCER KGRSYGSYNT
NEDMEPDWLT WPADMLHCTE CVVCLENFEN GCLLMGLPCG HVFHQNCIVM WLAGGRHCCP
VCRWPSYKKK QPYAQHQPLS NDVPS
//
|
