ZCHC7_HUMAN
ID ZCHC7_HUMAN Reviewed; 543 AA.
AC Q8N3Z6; B2RCI4; D3DRQ0; Q5T0Q8; Q5T0Q9; Q5T0R0; Q8N2M1; Q8N4J2; Q8TBK8;
AC Q9H648; Q9P0F0;
DT 07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 14-APR-2009, sequence version 2.
DT 03-AUG-2022, entry version 156.
DE RecName: Full=Zinc finger CCHC domain-containing protein 7;
DE AltName: Full=TRAMP-like complex RNA-binding factor ZCCHC7;
GN Name=ZCCHC7; ORFNames=HSPC086;
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 1).
RC TISSUE=Embryo, and Small intestine;
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=15164053; DOI=10.1038/nature02465;
RA Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L.,
RA Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R.,
RA Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S.,
RA Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K.,
RA Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y.,
RA Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C.,
RA Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E.,
RA Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M.,
RA Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J.,
RA Frankish A., Frankland J.A., French L., Fricker D.G., Garner P.,
RA Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
RA Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
RA Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
RA Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
RA Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
RA Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S.,
RA Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J.,
RA Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E.,
RA McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V.,
RA Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S.,
RA Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K.,
RA Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J.,
RA Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M.,
RA West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L.,
RA Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
RA Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J.,
RA Dunham I.;
RT "DNA sequence and analysis of human chromosome 9.";
RL Nature 429:369-374(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Brain, and Mammary gland;
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 340-446.
RC TISSUE=Umbilical cord blood;
RA Ye M., Zhang Q.-H., Zhou J., Shen Y., Wu X.-Y., Guan Z.Q., Wang L.,
RA Fan H.-Y., Mao Y.-F., Dai M., Huang Q.-H., Chen S.-J., Chen Z.;
RT "Human partial CDS from CD34+ stem cells.";
RL Submitted (MAY-1999) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-482, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [7]
RP IDENTIFICATION IN A TRAMP-LIKE COMPLEX, SUBUNIT, AND SUBCELLULAR LOCATION.
RX PubMed=21855801; DOI=10.1016/j.molcel.2011.06.028;
RA Lubas M., Christensen M.S., Kristiansen M.S., Domanski M., Falkenby L.G.,
RA Lykke-Andersen S., Andersen J.S., Dziembowski A., Jensen T.H.;
RT "Interaction profiling identifies the human nuclear exosome targeting
RT complex.";
RL Mol. Cell 43:624-637(2011).
RN [8]
RP REVIEW ON RNA EXOSOMES.
RX PubMed=22817747; DOI=10.1042/bst20120061;
RA Sloan K.E., Schneider C., Watkins N.J.;
RT "Comparison of the yeast and human nuclear exosome complexes.";
RL Biochem. Soc. Trans. 40:850-855(2012).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-485, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [10]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-417, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25218447; DOI=10.1038/nsmb.2890;
RA Hendriks I.A., D'Souza R.C., Yang B., Verlaan-de Vries M., Mann M.,
RA Vertegaal A.C.;
RT "Uncovering global SUMOylation signaling networks in a site-specific
RT manner.";
RL Nat. Struct. Mol. Biol. 21:927-936(2014).
RN [11]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-417, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25772364; DOI=10.1016/j.celrep.2015.02.033;
RA Hendriks I.A., Treffers L.W., Verlaan-de Vries M., Olsen J.V.,
RA Vertegaal A.C.;
RT "SUMO-2 orchestrates chromatin modifiers in response to DNA damage.";
RL Cell Rep. 10:1778-1791(2015).
RN [12]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-131; LYS-139; LYS-141; LYS-239;
RP LYS-254; LYS-339; LYS-412; LYS-417; LYS-435; LYS-478; LYS-487; LYS-490;
RP LYS-493 AND LYS-537, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RX PubMed=28112733; DOI=10.1038/nsmb.3366;
RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
RA Nielsen M.L.;
RT "Site-specific mapping of the human SUMO proteome reveals co-modification
RT with phosphorylation.";
RL Nat. Struct. Mol. Biol. 24:325-336(2017).
CC -!- SUBUNIT: Component of a nucleolar TRAMP-like complex, an ATP-dependent
CC exosome regulatory complex consisting of a helicase (MTREX), an
CC oligadenylate polymerase (TENT4B or TENT4A), and a substrate specific
CC RNA-binding factor (ZCCHC7 or ZCCHC8). Several TRAMP-like complexes
CC exist with specific compositions and are associated with nuclear, or
CC nucleolar RNA exosomes. {ECO:0000269|PubMed:21855801}.
CC -!- INTERACTION:
CC Q8N3Z6; Q9H257: CARD9; NbExp=3; IntAct=EBI-7265024, EBI-751319;
CC Q8N3Z6; Q8TF65: GIPC2; NbExp=3; IntAct=EBI-7265024, EBI-712067;
CC Q8N3Z6; Q9HAQ2: KIF9; NbExp=3; IntAct=EBI-7265024, EBI-8472129;
CC Q8N3Z6; Q5T753: LCE1E; NbExp=3; IntAct=EBI-7265024, EBI-11955335;
CC Q8N3Z6; Q9HC98-4: NEK6; NbExp=3; IntAct=EBI-7265024, EBI-11750983;
CC Q8N3Z6; P63165: SUMO1; NbExp=3; IntAct=EBI-7265024, EBI-80140;
CC Q8N3Z6; Q8WV44: TRIM41; NbExp=3; IntAct=EBI-7265024, EBI-725997;
CC Q8N3Z6; P63279: UBE2I; NbExp=3; IntAct=EBI-7265024, EBI-80168;
CC Q8N3Z6; P15622-3: ZNF250; NbExp=3; IntAct=EBI-7265024, EBI-10177272;
CC Q8N3Z6; Q59GP6; NbExp=3; IntAct=EBI-7265024, EBI-10243413;
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:21855801}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8N3Z6-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8N3Z6-2; Sequence=VSP_013841, VSP_013842;
CC -!- CAUTION: It is uncertain whether Met-1 or Met-2 is the initiator.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH36940.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAB15418.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
CC Sequence=BAC11087.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAG37581.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AK026264; BAB15418.1; ALT_SEQ; mRNA.
DR EMBL; AK074608; BAC11087.1; ALT_INIT; mRNA.
DR EMBL; AK315128; BAG37581.1; ALT_INIT; mRNA.
DR EMBL; AL512604; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL158155; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471071; EAW58288.1; -; Genomic_DNA.
DR EMBL; CH471071; EAW58289.1; -; Genomic_DNA.
DR EMBL; BC022434; AAH22434.1; -; mRNA.
DR EMBL; BC036940; AAH36940.1; ALT_INIT; mRNA.
DR EMBL; AF161349; AAF28909.1; -; mRNA.
DR CCDS; CCDS6608.2; -. [Q8N3Z6-1]
DR RefSeq; NP_001276048.1; NM_001289119.1. [Q8N3Z6-1]
DR RefSeq; NP_001276049.1; NM_001289120.1. [Q8N3Z6-1]
DR RefSeq; NP_001276050.1; NM_001289121.1. [Q8N3Z6-1]
DR RefSeq; NP_115602.2; NM_032226.2. [Q8N3Z6-1]
DR RefSeq; XP_005251665.1; XM_005251608.4. [Q8N3Z6-1]
DR RefSeq; XP_005251669.1; XM_005251612.2. [Q8N3Z6-1]
DR AlphaFoldDB; Q8N3Z6; -.
DR BioGRID; 123934; 102.
DR ELM; Q8N3Z6; -.
DR IntAct; Q8N3Z6; 29.
DR MINT; Q8N3Z6; -.
DR STRING; 9606.ENSP00000443113; -.
DR iPTMnet; Q8N3Z6; -.
DR PhosphoSitePlus; Q8N3Z6; -.
DR BioMuta; ZCCHC7; -.
DR DMDM; 226693603; -.
DR EPD; Q8N3Z6; -.
DR jPOST; Q8N3Z6; -.
DR MassIVE; Q8N3Z6; -.
DR MaxQB; Q8N3Z6; -.
DR PaxDb; Q8N3Z6; -.
DR PeptideAtlas; Q8N3Z6; -.
DR PRIDE; Q8N3Z6; -.
DR ProteomicsDB; 71857; -. [Q8N3Z6-1]
DR ProteomicsDB; 71858; -. [Q8N3Z6-2]
DR Antibodypedia; 11966; 96 antibodies from 17 providers.
DR DNASU; 84186; -.
DR Ensembl; ENST00000336755.10; ENSP00000337839.5; ENSG00000147905.18. [Q8N3Z6-1]
DR Ensembl; ENST00000534928.5; ENSP00000443113.2; ENSG00000147905.18. [Q8N3Z6-1]
DR GeneID; 84186; -.
DR KEGG; hsa:84186; -.
DR MANE-Select; ENST00000336755.10; ENSP00000337839.5; NM_032226.3; NP_115602.2.
DR UCSC; uc003zzq.4; human. [Q8N3Z6-1]
DR CTD; 84186; -.
DR DisGeNET; 84186; -.
DR GeneCards; ZCCHC7; -.
DR HGNC; HGNC:26209; ZCCHC7.
DR HPA; ENSG00000147905; Low tissue specificity.
DR neXtProt; NX_Q8N3Z6; -.
DR OpenTargets; ENSG00000147905; -.
DR PharmGKB; PA128394734; -.
DR VEuPathDB; HostDB:ENSG00000147905; -.
DR eggNOG; KOG4400; Eukaryota.
DR GeneTree; ENSGT00950000183041; -.
DR HOGENOM; CLU_029787_0_0_1; -.
DR InParanoid; Q8N3Z6; -.
DR OMA; SHAYCYN; -.
DR PhylomeDB; Q8N3Z6; -.
DR TreeFam; TF329448; -.
DR PathwayCommons; Q8N3Z6; -.
DR SignaLink; Q8N3Z6; -.
DR BioGRID-ORCS; 84186; 49 hits in 1075 CRISPR screens.
DR ChiTaRS; ZCCHC7; human.
DR GenomeRNAi; 84186; -.
DR Pharos; Q8N3Z6; Tbio.
DR PRO; PR:Q8N3Z6; -.
DR Proteomes; UP000005640; Chromosome 9.
DR RNAct; Q8N3Z6; protein.
DR Bgee; ENSG00000147905; Expressed in calcaneal tendon and 178 other tissues.
DR ExpressionAtlas; Q8N3Z6; baseline and differential.
DR Genevisible; Q8N3Z6; HS.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0005730; C:nucleolus; IDA:HPA.
DR GO; GO:0031499; C:TRAMP complex; IBA:GO_Central.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0043629; P:ncRNA polyadenylation; IBA:GO_Central.
DR GO; GO:0071031; P:nuclear mRNA surveillance of mRNA 3'-end processing; IBA:GO_Central.
DR GO; GO:0071039; P:nuclear polyadenylation-dependent CUT catabolic process; IBA:GO_Central.
DR GO; GO:0071035; P:nuclear polyadenylation-dependent rRNA catabolic process; IBA:GO_Central.
DR GO; GO:0071036; P:nuclear polyadenylation-dependent snoRNA catabolic process; IBA:GO_Central.
DR GO; GO:0071037; P:nuclear polyadenylation-dependent snRNA catabolic process; IBA:GO_Central.
DR GO; GO:0071038; P:nuclear polyadenylation-dependent tRNA catabolic process; IBA:GO_Central.
DR InterPro; IPR001878; Znf_CCHC.
DR InterPro; IPR036875; Znf_CCHC_sf.
DR Pfam; PF00098; zf-CCHC; 1.
DR SMART; SM00343; ZnF_C2HC; 4.
DR SUPFAM; SSF57756; SSF57756; 1.
DR PROSITE; PS50158; ZF_CCHC; 3.
PE 1: Evidence at protein level;
KW Alternative splicing; Isopeptide bond; Metal-binding; Nucleus;
KW Phosphoprotein; Reference proteome; Repeat; Ubl conjugation; Zinc;
KW Zinc-finger.
FT CHAIN 1..543
FT /note="Zinc finger CCHC domain-containing protein 7"
FT /id="PRO_0000150959"
FT ZN_FING 241..258
FT /note="CCHC-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00047"
FT ZN_FING 263..280
FT /note="CCHC-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00047"
FT ZN_FING 304..321
FT /note="CCHC-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00047"
FT ZN_FING 348..365
FT /note="CCHC-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00047"
FT REGION 51..71
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 414..543
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 419..435
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 441..475
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 499..537
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 482
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 485
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT CROSSLNK 131
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 139
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 141
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 239
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 254
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 339
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 412
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 417
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25218447,
FT ECO:0007744|PubMed:25772364, ECO:0007744|PubMed:28112733"
FT CROSSLNK 435
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 478
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 487
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 490
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 493
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 537
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VAR_SEQ 205..206
FT /note="ED -> QE (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_013841"
FT VAR_SEQ 207..543
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_013842"
FT VARIANT 118
FT /note="G -> D (in dbSNP:rs35119826)"
FT /id="VAR_054958"
FT VARIANT 539
FT /note="R -> K (in dbSNP:rs1051465)"
FT /id="VAR_054959"
FT CONFLICT 3
FT /note="F -> L (in Ref. 1; BAB15418)"
FT /evidence="ECO:0000305"
FT CONFLICT 65
FT /note="S -> P (in Ref. 4; AAH22434)"
FT /evidence="ECO:0000305"
FT CONFLICT 214
FT /note="D -> G (in Ref. 1; BAC11087)"
FT /evidence="ECO:0000305"
FT CONFLICT 233
FT /note="R -> W (in Ref. 1; BAC11087)"
FT /evidence="ECO:0000305"
FT CONFLICT 443
FT /note="N -> D (in Ref. 1; BAC11087)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 543 AA; 63052 MW; 1EDB6DD168C28EE6 CRC64;
MMFGGYETIE AYEDDLYRDE SSSELSVDSE VEFQLYSQIH YAQDLDDVIR EEEHEEKNSG
NSESSSSKPN QKKLIVLSDS EVIQLSDGSE VITLSDEDSI YRCKGKNVRV QAQENAHGLS
SSLQSNELVD KKCKSDIEKP KSEERSGVIR EVMIIEVSSS EEEESTISEG DNVESWMLLG
CEVDDKDDDI LLNLVGCENS VTEGEDGINW SISDKDIEAQ IANNRTPGRW TQRYYSANKN
IICRNCDKRG HLSKNCPLPR KVRRCFLCSR RGHLLYSCPA PLCEYCPVPK MLDHSCLFRH
SWDKQCDRCH MLGHYTDACT EIWRQYHLTT KPGPPKKPKT PSRPSALAYC YHCAQKGHYG
HECPEREVYD PSPVSPFICY YDDKYEIQER EKRLKQKIKV LKKNGVIPEP SKLPYIKAAN
ENPHHDIRKG RASWKSNRWP QENKETQKEM KNKNRNWEKH RKADRHREVD EDFPRGPKTY
SSPGSFKTQK PSKPFHRSSH YHTSREDKSP KEGKRGKQKK KERCWEDDDN DNLFLIKQRK
KKS
