RN212_HUMAN
ID RN212_HUMAN Reviewed; 297 AA.
AC Q495C1; C9J8N0; Q495C0; Q86W82; Q8IY99; Q8N8U7;
DT 06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2005, sequence version 1.
DT 03-AUG-2022, entry version 123.
DE RecName: Full=Probable E3 SUMO-protein ligase RNF212;
DE EC=2.3.2.-;
DE AltName: Full=Probable E3 SUMO-protein transferase RNF212 {ECO:0000305};
DE AltName: Full=RING finger protein 212;
GN Name=RNF212;
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 [LARGE SCALE MRNA] (ISOFORM 5).
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 [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., 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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2; 3 AND 4).
RC TISSUE=Brain, and 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 project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP ASSOCIATION WITH RRQTL1.
RX PubMed=18239089; DOI=10.1126/science.1152422;
RA Kong A., Thorleifsson G., Stefansson H., Masson G., Helgason A.,
RA Gudbjartsson D.F., Jonsdottir G.M., Gudjonsson S.A., Sverrisson S.,
RA Thorlacius T., Jonasdottir A., Hardarson G.A., Palsson S.T., Frigge M.L.,
RA Gulcher J.R., Thorsteinsdottir U., Stefansson K.;
RT "Sequence variants in the RNF212 gene associate with genome-wide
RT recombination rate.";
RL Science 319:1398-1401(2008).
CC -!- FUNCTION: SUMO E3 ligase that acts as a regulator of crossing-over
CC during meiosis: required to couple chromosome synapsis to the formation
CC of crossover-specific recombination complexes. Localizes to
CC recombination sites and stabilizes meiosis-specific recombination
CC factors, such as MutS-gamma complex proteins (MSH4 and MSH5) and TEX11.
CC May mediate sumoylation of target proteins MSH4 and/or MSH5, leading to
CC enhance their binding to recombination sites. Acts as a limiting factor
CC for crossover designation and/or reinforcement and plays an antagonist
CC role with CCNB1IP1/HEI10 in the regulation of meiotic recombination (By
CC similarity). {ECO:0000250}.
CC -!- PATHWAY: Protein modification; protein sumoylation.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Chromosome {ECO:0000250}.
CC Note=Associates to the synaptonemal complex. Localizes to a minority of
CC double-strand breaks (DSBs) sites. Marks crossover sites during
CC midpachynema (By similarity). {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=6;
CC Name=1;
CC IsoId=Q495C1-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q495C1-2; Sequence=VSP_022840, VSP_022841;
CC Name=3;
CC IsoId=Q495C1-3; Sequence=VSP_022843;
CC Name=4;
CC IsoId=Q495C1-4; Sequence=VSP_022839;
CC Name=5;
CC IsoId=Q495C1-5; Sequence=VSP_022842, VSP_022844;
CC Name=6;
CC IsoId=Q495C1-6; Sequence=VSP_046301;
CC -!- POLYMORPHISM: Genetic variations in RNF212 influence recombination
CC rate, designated recombination rate quantitative trait locus 1 (RRQTL1)
CC [MIM:612042]. {ECO:0000269|PubMed:18239089}.
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DR EMBL; AK096160; BAC04714.1; -; mRNA.
DR EMBL; AC019103; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC092535; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC036250; AAH36250.2; -; mRNA.
DR EMBL; BC050356; AAH50356.2; -; mRNA.
DR EMBL; BC101258; AAI01259.1; -; mRNA.
DR EMBL; BC101259; AAI01260.1; -; mRNA.
DR EMBL; BC101260; AAI01261.1; -; mRNA.
DR EMBL; BC101261; AAI01262.1; -; mRNA.
DR CCDS; CCDS3345.1; -. [Q495C1-5]
DR CCDS; CCDS46996.1; -. [Q495C1-1]
DR CCDS; CCDS54704.1; -. [Q495C1-6]
DR RefSeq; NP_001124506.1; NM_001131034.3. [Q495C1-1]
DR RefSeq; NP_001180247.1; NM_001193318.2. [Q495C1-6]
DR RefSeq; NP_919420.1; NM_194439.4. [Q495C1-5]
DR AlphaFoldDB; Q495C1; -.
DR SMR; Q495C1; -.
DR BioGRID; 130126; 24.
DR IntAct; Q495C1; 1.
DR STRING; 9606.ENSP00000389709; -.
DR iPTMnet; Q495C1; -.
DR PhosphoSitePlus; Q495C1; -.
DR BioMuta; RNF212; -.
DR DMDM; 121943260; -.
DR MaxQB; Q495C1; -.
DR PaxDb; Q495C1; -.
DR PeptideAtlas; Q495C1; -.
DR PRIDE; Q495C1; -.
DR ProteomicsDB; 61954; -. [Q495C1-1]
DR ProteomicsDB; 61956; -. [Q495C1-3]
DR ProteomicsDB; 61958; -. [Q495C1-5]
DR Antibodypedia; 22203; 127 antibodies from 25 providers.
DR DNASU; 285498; -.
DR Ensembl; ENST00000333673.5; ENSP00000327481.5; ENSG00000178222.13. [Q495C1-6]
DR Ensembl; ENST00000382968.9; ENSP00000372428.5; ENSG00000178222.13. [Q495C1-5]
DR Ensembl; ENST00000433731.7; ENSP00000389709.2; ENSG00000178222.13. [Q495C1-1]
DR Ensembl; ENST00000511620.5; ENSP00000426115.1; ENSG00000178222.13. [Q495C1-2]
DR GeneID; 285498; -.
DR KEGG; hsa:285498; -.
DR MANE-Select; ENST00000433731.7; ENSP00000389709.2; NM_001131034.4; NP_001124506.1.
DR UCSC; uc003gci.4; human. [Q495C1-1]
DR CTD; 285498; -.
DR DisGeNET; 285498; -.
DR GeneCards; RNF212; -.
DR HGNC; HGNC:27729; RNF212.
DR HPA; ENSG00000178222; Tissue enhanced (pancreas).
DR MalaCards; RNF212; -.
DR MIM; 612041; gene.
DR MIM; 612042; phenotype.
DR neXtProt; NX_Q495C1; -.
DR OpenTargets; ENSG00000178222; -.
DR PharmGKB; PA162401656; -.
DR VEuPathDB; HostDB:ENSG00000178222; -.
DR eggNOG; KOG4739; Eukaryota.
DR GeneTree; ENSGT00740000115581; -.
DR HOGENOM; CLU_074594_1_0_1; -.
DR InParanoid; Q495C1; -.
DR OMA; VCCNSCF; -.
DR OrthoDB; 1325661at2759; -.
DR PhylomeDB; Q495C1; -.
DR TreeFam; TF339477; -.
DR PathwayCommons; Q495C1; -.
DR SignaLink; Q495C1; -.
DR UniPathway; UPA00886; -.
DR BioGRID-ORCS; 285498; 12 hits in 1111 CRISPR screens.
DR ChiTaRS; RNF212; human.
DR GenomeRNAi; 285498; -.
DR Pharos; Q495C1; Tbio.
DR PRO; PR:Q495C1; -.
DR Proteomes; UP000005640; Chromosome 4.
DR RNAct; Q495C1; protein.
DR Bgee; ENSG00000178222; Expressed in body of pancreas and 101 other tissues.
DR ExpressionAtlas; Q495C1; baseline and differential.
DR Genevisible; Q495C1; HS.
DR GO; GO:0000795; C:synaptonemal complex; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0019789; F:SUMO transferase activity; IBA:GO_Central.
DR GO; GO:0051026; P:chiasma assembly; ISS:UniProtKB.
DR GO; GO:0007129; P:homologous chromosome pairing at meiosis; IBA:GO_Central.
DR GO; GO:0006311; P:meiotic gene conversion; ISS:UniProtKB.
DR GO; GO:0016925; P:protein sumoylation; IBA:GO_Central.
DR GO; GO:0007131; P:reciprocal meiotic recombination; ISS:UniProtKB.
DR InterPro; IPR042123; Zip3/RNF212-like.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR017907; Znf_RING_CS.
DR PANTHER; PTHR22663; PTHR22663; 1.
DR Pfam; PF14634; zf-RING_5; 1.
DR PROSITE; PS00518; ZF_RING_1; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; Chromosome; Coiled coil; Meiosis; Metal-binding;
KW Nucleus; Reference proteome; Transferase; Ubl conjugation pathway; Zinc;
KW Zinc-finger.
FT CHAIN 1..297
FT /note="Probable E3 SUMO-protein ligase RNF212"
FT /id="PRO_0000274612"
FT ZN_FING 7..46
FT /note="RING-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT COILED 91..124
FT /evidence="ECO:0000255"
FT VAR_SEQ 83..297
FT /note="ILEFQEKHRKRLLAFYREKISRLEESLRKSVLQIEQLQSMRSSQQTAFSTIK
FT SSVSTKPHGCLLPPHSSAPDRLESMEVDLSPSPIRKSEIAAGPARISMISPPQDGRMGP
FT HLTASFCFIPWLTLSKPPVPGECVISRGSPCFCIDVCPHWLLLLAFSSGRHGELTNSKT
FT LPIYAEVQRAVLFPFQQAEGTLDTFRTPAVSVVFPLCQFERKKSF -> YLRLSRGCCR
FT LKLCPATSSKEVPRGSTHGSQAAARDPQEHWVSTTRAPRPGCRRSQSQPEAQGNTIQDA
FT PHPLTLLHPSRTLIHTKSPWGQKLLEFIKHVCYHRHQSHRPCAPGWFCQVLQRPGAVSG
FT EKTQQTRPAPPATCLLCLSCLSGFRHGPWRWLAPAWAAQALPSDLVAPLFVSYTVEVSI
FT TNAGWSFPAAV (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_022839"
FT VAR_SEQ 83..297
FT /note="ILEFQEKHRKRLLAFYREKISRLEESLRKSVLQIEQLQSMRSSQQTAFSTIK
FT SSVSTKPHGCLLPPHSSAPDRLESMEVDLSPSPIRKSEIAAGPARISMISPPQDGRMGP
FT HLTASFCFIPWLTLSKPPVPGECVISRGSPCFCIDVCPHWLLLLAFSSGRHGELTNSKT
FT LPIYAEVQRAVLFPFQQAEGTLDTFRTPAVSVVFPLCQFERKKSF -> YLRLSRGCCR
FT LKLCPATSSKEVPRGSTHGSQAAARDPQEHWVSTTRAPRPGCRRSQSQPEAQGNTIQDA
FT PHPLTLLHPSRTLIHTKSPWGQKLLEFIKHVCYHRHQSHRPCAPGWFCQVLQRPGAVSG
FT EKTQQTRPAPPATCLLCLSCLSGFRHGPWRSQALPSDLVAPLFVSYTVEVSITNAGWSF
FT PAAV (in isoform 6)"
FT /evidence="ECO:0000305"
FT /id="VSP_046301"
FT VAR_SEQ 122
FT /note="M -> L (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_022840"
FT VAR_SEQ 124..297
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_022841"
FT VAR_SEQ 192..276
FT /note="GPHLTASFCFIPWLTLSKPPVPGECVISRGSPCFCIDVCPHWLLLLAFSSGR
FT HGELTNSKTLPIYAEVQRAVLFPFQQAEGTLDT -> APCARRVCHFQRFTMFLHRRLS
FT SLAAPPSVQFWKARGTHQL (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_022842"
FT VAR_SEQ 193..297
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_022843"
FT VAR_SEQ 277..297
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_022844"
FT VARIANT 263
FT /note="V -> I (in dbSNP:rs17728127)"
FT /id="VAR_059815"
FT CONFLICT 147
FT /note="P -> Q (in Ref. 3; AAH50356)"
FT /evidence="ECO:0000305"
FT CONFLICT Q495C1-4:144
FT /note="Q -> H (in Ref. 3; AAH36250)"
FT /evidence="ECO:0000305"
FT CONFLICT Q495C1-4:173
FT /note="Q -> R (in Ref. 3; AAH36250)"
FT /evidence="ECO:0000305"
FT CONFLICT Q495C1-4:219
FT /note="A -> D (in Ref. 3; AAH36250)"
FT /evidence="ECO:0000305"
FT CONFLICT Q495C1-4:269
FT /note="I -> V (in Ref. 3; AAH36250)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 297 AA; 33365 MW; 9ABF48A990D68FA7 CRC64;
MANWVFCNRC FQPPHRTSCF SLTNCGHVYC DACLGKGKKN ECLICKAPCR TVLLSKHTDA
DIQAFFMSID SLCKKYSRET SQILEFQEKH RKRLLAFYRE KISRLEESLR KSVLQIEQLQ
SMRSSQQTAF STIKSSVSTK PHGCLLPPHS SAPDRLESME VDLSPSPIRK SEIAAGPARI
SMISPPQDGR MGPHLTASFC FIPWLTLSKP PVPGECVISR GSPCFCIDVC PHWLLLLAFS
SGRHGELTNS KTLPIYAEVQ RAVLFPFQQA EGTLDTFRTP AVSVVFPLCQ FERKKSF
