RN103_HUMAN
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 03-AUG-2022, entry version 153.
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; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC 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., Kikuno R.,
RA Kuma K., Ohkubo K., Hosokawa Y., Ibata Y., Abe T., Miyata T., Matsubara K.,
RA 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., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., 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., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA 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., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., 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., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., 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., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 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 project:
RT 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., 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-associated
RT degradation pathway.";
RL Biochem. Biophys. Res. Commun. 374:737-741(2008).
CC -!- FUNCTION: Acts as an E2-dependent E3 ubiquitin-protein ligase, probably
CC involved in the ER-associated protein degradation pathway.
CC {ECO:0000269|PubMed:10500182, ECO:0000269|PubMed:18675248}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine +
CC [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-
CC cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.;
CC EC=2.3.2.27;
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC -!- SUBUNIT: Interacts with DERL1 and VCP. {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 not
CC in the cerebral cortex. {ECO:0000269|PubMed:9070305}.
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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 AlphaFoldDB; O00237; -.
DR SMR; O00237; -.
DR BioGRID; 113601; 26.
DR IntAct; O00237; 10.
DR STRING; 9606.ENSP00000237455; -.
DR iPTMnet; O00237; -.
DR PhosphoSitePlus; O00237; -.
DR BioMuta; RNF103; -.
DR jPOST; O00237; -.
DR PaxDb; O00237; -.
DR PeptideAtlas; O00237; -.
DR PRIDE; O00237; -.
DR ProteomicsDB; 47801; -.
DR Antibodypedia; 34817; 128 antibodies from 21 providers.
DR DNASU; 7844; -.
DR Ensembl; ENST00000237455.5; ENSP00000237455.4; ENSG00000239305.7.
DR GeneID; 7844; -.
DR KEGG; hsa:7844; -.
DR MANE-Select; ENST00000237455.5; ENSP00000237455.4; NM_005667.4; NP_005658.1.
DR UCSC; uc002srn.4; human.
DR CTD; 7844; -.
DR DisGeNET; 7844; -.
DR GeneCards; RNF103; -.
DR HGNC; HGNC:12859; RNF103.
DR HPA; ENSG00000239305; Low tissue specificity.
DR MIM; 602507; gene.
DR neXtProt; NX_O00237; -.
DR OpenTargets; ENSG00000239305; -.
DR PharmGKB; PA37448; -.
DR VEuPathDB; HostDB:ENSG00000239305; -.
DR eggNOG; KOG0800; Eukaryota.
DR GeneTree; ENSGT00390000006413; -.
DR HOGENOM; CLU_031351_0_0_1; -.
DR InParanoid; O00237; -.
DR OMA; IYKTPSY; -.
DR OrthoDB; 1487241at2759; -.
DR PhylomeDB; O00237; -.
DR TreeFam; TF329229; -.
DR PathwayCommons; O00237; -.
DR Reactome; R-HSA-901032; ER Quality Control Compartment (ERQC).
DR SignaLink; O00237; -.
DR UniPathway; UPA00143; -.
DR BioGRID-ORCS; 7844; 22 hits in 1118 CRISPR screens.
DR GenomeRNAi; 7844; -.
DR Pharos; O00237; Tbio.
DR PRO; PR:O00237; -.
DR Proteomes; UP000005640; Chromosome 2.
DR RNAct; O00237; protein.
DR Bgee; ENSG00000239305; Expressed in middle temporal gyrus and 208 other tissues.
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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; TAS:Reactome.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; IDA:UniProtKB.
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 Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR042494; RNF103.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR15302; PTHR15302; 1.
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 Endoplasmic reticulum; Membrane; Metal-binding; Reference proteome;
KW Transferase; Transmembrane; Transmembrane helix; Ubl conjugation pathway;
KW Zinc; Zinc-finger.
FT CHAIN 1..685
FT /note="E3 ubiquitin-protein ligase RNF103"
FT /id="PRO_0000056084"
FT TRANSMEM 6..26
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 326..346
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 366..386
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 411..431
FT /note="Helical"
FT /evidence="ECO:0000255"
FT ZN_FING 621..663
FT /note="RING-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT REGION 526..550
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 529..543
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MUTAGEN 621
FT /note="C->S: Loss of E2-dependent ubiquitination."
FT /evidence="ECO:0000269|PubMed:10500182"
FT CONFLICT 22
FT /note="F -> L (in Ref. 3; BAG36861)"
FT /evidence="ECO:0000305"
FT CONFLICT 251
FT /note="S -> P (in Ref. 5; AAH35053)"
FT /evidence="ECO:0000305"
FT CONFLICT 287
FT /note="S -> P (in Ref. 3; BAG36861)"
FT /evidence="ECO:0000305"
FT CONFLICT 502
FT /note="P -> H (in Ref. 5; AAH35053)"
FT /evidence="ECO:0000305"
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
