CDCA7_HUMAN
ID CDCA7_HUMAN Reviewed; 371 AA.
AC Q9BWT1; B4DLP8; B4DV66; Q53EW5; Q580W9; Q658K4; Q658N4; Q8NBY9; Q96BV8;
AC Q96SP5;
DT 05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 148.
DE RecName: Full=Cell division cycle-associated protein 7;
DE AltName: Full=Protein JPO1;
GN Name=CDCA7; Synonyms=JPO1;
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] (ISOFORM 1), FUNCTION, MISCELLANEOUS, TISSUE
RP SPECIFICITY, AND SUBCELLULAR LOCATION.
RX PubMed=11598121; DOI=10.1074/jbc.m107357200;
RA Prescott J.E., Osthus R.C., Lee L.A., Lewis B.C., Shim H., Barrett J.F.,
RA Guo Q., Hawkins A.L., Griffin C.A., Dang C.V.;
RT "A novel c-Myc-responsive gene, JPO1, participates in neoplastic
RT transformation.";
RL J. Biol. Chem. 276:48276-48284(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2; 4; 5 AND 6).
RC TISSUE=Placenta, 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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.;
RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3), AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 155-371 (ISOFORM 1).
RC TISSUE=Lymph node, and Stomach;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [5]
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Kidney, and Pancreas;
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 [7]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 90-371.
RX PubMed=12188893; DOI=10.2174/1568009013334241;
RA Walker M.G.;
RT "Drug target discovery by gene expression analysis: cell cycle genes.";
RL Curr. Cancer Drug Targets 1:73-83(2001).
RN [8]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=15994934; DOI=10.1158/0008-5472.can-05-0536;
RA Osthus R.C., Karim B., Prescott J.E., Smith B.D., McDevitt M., Huso D.L.,
RA Dang C.V.;
RT "The Myc target gene JPO1/CDCA7 is frequently overexpressed in human tumors
RT and has limited transforming activity in vivo.";
RL Cancer Res. 65:5620-5627(2005).
RN [9]
RP FUNCTION, AND REGION.
RX PubMed=16580749; DOI=10.1016/j.bbaexp.2006.02.004;
RA Goto Y., Hayashi R., Muramatsu T., Ogawa H., Eguchi I., Oshida Y.,
RA Ohtani K., Yoshida K.;
RT "JPO1/CDCA7, a novel transcription factor E2F1-induced protein, possesses
RT intrinsic transcriptional regulator activity.";
RL Biochim. Biophys. Acta 1759:60-68(2006).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-190, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-142 AND THR-163, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and 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 [12]
RP FUNCTION, INTERACTION WITH MYC; YWHAE AND YWHAZ, SUBCELLULAR LOCATION,
RP NUCLEAR LOCALIZATION SIGNAL, PHOSPHORYLATION AT THR-163, AND MUTAGENESIS OF
RP ARG-158; PRO-159; ARG-160; ARG-161; ARG-162; THR-163; PHE-164; PRO-165;
RP ARG-171; ARG-176; ARG-182 AND ARG-184.
RX PubMed=23166294; DOI=10.1128/mcb.00276-12;
RA Gill R.M., Gabor T.V., Couzens A.L., Scheid M.P.;
RT "The MYC-associated protein CDCA7 is phosphorylated by AKT to regulate MYC-
RT dependent apoptosis and transformation.";
RL Mol. Cell. Biol. 33:498-513(2013).
RN [13]
RP INVOLVEMENT IN ICF3, AND VARIANTS ICF3 CYS-274; HIS-274; VAL-294 AND
RP HIS-304.
RX PubMed=26216346; DOI=10.1038/ncomms8870;
RA Thijssen P.E., Ito Y., Grillo G., Wang J., Velasco G., Nitta H., Unoki M.,
RA Yoshihara M., Suyama M., Sun Y., Lemmers R.J., de Greef J.C., Gennery A.,
RA Picco P., Kloeckener-Gruissem B., Guengoer T., Reisli I., Picard C.,
RA Kebaili K., Roquelaure B., Iwai T., Kondo I., Kubota T.,
RA van Ostaijen-Ten Dam M.M., van Tol M.J., Weemaes C., Francastel C.,
RA van der Maarel S.M., Sasaki H.;
RT "Mutations in CDCA7 and HELLS cause immunodeficiency-centromeric
RT instability-facial anomalies syndrome.";
RL Nat. Commun. 6:7870-7870(2015).
RN [14]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-204, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE 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 -!- FUNCTION: Participates in MYC-mediated cell transformation and
CC apoptosis; induces anchorage-independent growth and clonogenicity in
CC lymphoblastoid cells. Insufficient to induce tumorigenicity when
CC overexpressed but contributes to MYC-mediated tumorigenesis. May play a
CC role as transcriptional regulator. {ECO:0000269|PubMed:11598121,
CC ECO:0000269|PubMed:15994934, ECO:0000269|PubMed:16580749,
CC ECO:0000269|PubMed:23166294}.
CC -!- SUBUNIT: Interacts with MYC (via C-terminus), YWHAE and YWHAZ.
CC {ECO:0000269|PubMed:23166294}.
CC -!- INTERACTION:
CC Q9BWT1; P42858: HTT; NbExp=3; IntAct=EBI-7054803, EBI-466029;
CC Q9BWT1; O76024: WFS1; NbExp=3; IntAct=EBI-7054803, EBI-720609;
CC -!- SUBCELLULAR LOCATION: Nucleus. Cytoplasm. Note=Predominantly nuclear
CC with some expression also seen in the cytoplasm. Predominantly
CC cytoplasmic when phosphorylated at Thr-163.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=6;
CC Name=1; Synonyms=isoform 2 variant;
CC IsoId=Q9BWT1-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9BWT1-2; Sequence=VSP_020394;
CC Name=3;
CC IsoId=Q9BWT1-3; Sequence=VSP_020397;
CC Name=4;
CC IsoId=Q9BWT1-4; Sequence=VSP_020395, VSP_020396;
CC Name=5;
CC IsoId=Q9BWT1-5; Sequence=VSP_054407;
CC Name=6;
CC IsoId=Q9BWT1-6; Sequence=VSP_054408;
CC -!- TISSUE SPECIFICITY: Ubiquitous with higher level in thymus and small
CC intestine. Overexpressed in a large number of tumors, in blood from
CC patients with acute myelogenous leukemia (AML) and in chronic
CC myelogenous leukemia (CML) blast crisis. {ECO:0000269|PubMed:11598121,
CC ECO:0000269|PubMed:15994934}.
CC -!- INDUCTION: Activated by MYC and possibly E2F1.
CC -!- PTM: Phosphorylation at Thr-163 promotes interaction with YWHAE and
CC YWHAZ, dissociation from MYC and sequestration in the cytoplasm. In
CC vitro, phosphorylated at Thr-163 by AKT. {ECO:0000269|PubMed:23166294}.
CC -!- DISEASE: Immunodeficiency-centromeric instability-facial anomalies
CC syndrome 3 (ICF3) [MIM:616910]: A rare disorder characterized by a
CC variable immunodeficiency resulting in recurrent infections, facial
CC anomalies, and branching of chromosomes 1, 9, and 16. Other variable
CC symptoms include growth retardation, failure to thrive, and psychomotor
CC retardation. Laboratory studies show limited hypomethylation of DNA in
CC a small fraction of the genome in some, but not all, patients.
CC {ECO:0000269|PubMed:26216346}. Note=The disease may be caused by
CC variants affecting the gene represented in this entry.
CC -!- MISCELLANEOUS: CDCA7 expression is correlated with MYC expression in
CC lymphoblastoid, lymphoma and breast cancer cell lines.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAH56357.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AY029179; AAK31591.1; -; mRNA.
DR EMBL; AK027628; BAB55245.1; -; mRNA.
DR EMBL; AK027642; BAB55258.1; -; mRNA.
DR EMBL; AK075134; BAC11425.1; -; mRNA.
DR EMBL; AK297097; BAG59610.1; -; mRNA.
DR EMBL; AK300949; BAG62578.1; -; mRNA.
DR EMBL; AK223524; BAD97244.1; -; mRNA.
DR EMBL; AL833728; CAH56253.1; -; mRNA.
DR EMBL; AL834186; CAH56357.1; ALT_FRAME; mRNA.
DR EMBL; AC092573; AAX82003.1; -; Genomic_DNA.
DR EMBL; BC015124; AAH15124.1; -; mRNA.
DR EMBL; BC027966; AAH27966.1; -; mRNA.
DR EMBL; BG354580; -; NOT_ANNOTATED_CDS; mRNA.
DR CCDS; CCDS2252.1; -. [Q9BWT1-2]
DR CCDS; CCDS2253.1; -. [Q9BWT1-1]
DR RefSeq; NP_114148.3; NM_031942.4. [Q9BWT1-2]
DR RefSeq; NP_665809.1; NM_145810.2. [Q9BWT1-1]
DR AlphaFoldDB; Q9BWT1; -.
DR BioGRID; 123792; 11.
DR IntAct; Q9BWT1; 6.
DR MINT; Q9BWT1; -.
DR iPTMnet; Q9BWT1; -.
DR PhosphoSitePlus; Q9BWT1; -.
DR BioMuta; CDCA7; -.
DR DMDM; 74733461; -.
DR EPD; Q9BWT1; -.
DR jPOST; Q9BWT1; -.
DR MassIVE; Q9BWT1; -.
DR MaxQB; Q9BWT1; -.
DR PaxDb; Q9BWT1; -.
DR PeptideAtlas; Q9BWT1; -.
DR PRIDE; Q9BWT1; -.
DR ProteomicsDB; 4548; -.
DR ProteomicsDB; 5247; -.
DR ProteomicsDB; 79309; -. [Q9BWT1-1]
DR ProteomicsDB; 79310; -. [Q9BWT1-2]
DR ProteomicsDB; 79311; -. [Q9BWT1-3]
DR ProteomicsDB; 79312; -. [Q9BWT1-4]
DR Antibodypedia; 1585; 110 antibodies from 23 providers.
DR DNASU; 83879; -.
DR Ensembl; ENST00000306721.8; ENSP00000306968.3; ENSG00000144354.14. [Q9BWT1-2]
DR Ensembl; ENST00000347703.7; ENSP00000272789.4; ENSG00000144354.14. [Q9BWT1-1]
DR Ensembl; ENST00000410019.3; ENSP00000386833.3; ENSG00000144354.14. [Q9BWT1-5]
DR Ensembl; ENST00000410101.7; ENSP00000386656.3; ENSG00000144354.14. [Q9BWT1-6]
DR GeneID; 83879; -.
DR KEGG; hsa:83879; -.
DR MANE-Select; ENST00000306721.8; ENSP00000306968.3; NM_031942.5; NP_114148.3. [Q9BWT1-2]
DR UCSC; uc002uic.2; human. [Q9BWT1-1]
DR CTD; 83879; -.
DR DisGeNET; 83879; -.
DR GeneCards; CDCA7; -.
DR HGNC; HGNC:14628; CDCA7.
DR HPA; ENSG00000144354; Tissue enhanced (intestine, lymphoid tissue).
DR MalaCards; CDCA7; -.
DR MIM; 609937; gene.
DR MIM; 616910; phenotype.
DR neXtProt; NX_Q9BWT1; -.
DR OpenTargets; ENSG00000144354; -.
DR Orphanet; 2268; ICF syndrome.
DR PharmGKB; PA26280; -.
DR VEuPathDB; HostDB:ENSG00000144354; -.
DR eggNOG; ENOG502QQPE; Eukaryota.
DR GeneTree; ENSGT00940000155436; -.
DR HOGENOM; CLU_035988_2_0_1; -.
DR InParanoid; Q9BWT1; -.
DR OMA; NICGSAR; -.
DR OrthoDB; 1462540at2759; -.
DR PhylomeDB; Q9BWT1; -.
DR TreeFam; TF101076; -.
DR PathwayCommons; Q9BWT1; -.
DR SignaLink; Q9BWT1; -.
DR SIGNOR; Q9BWT1; -.
DR BioGRID-ORCS; 83879; 13 hits in 1085 CRISPR screens.
DR ChiTaRS; CDCA7; human.
DR GeneWiki; CDCA7; -.
DR GenomeRNAi; 83879; -.
DR Pharos; Q9BWT1; Tbio.
DR PRO; PR:Q9BWT1; -.
DR Proteomes; UP000005640; Chromosome 2.
DR RNAct; Q9BWT1; protein.
DR Bgee; ENSG00000144354; Expressed in ileal mucosa and 147 other tissues.
DR ExpressionAtlas; Q9BWT1; baseline and differential.
DR Genevisible; Q9BWT1; HS.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR GO; GO:0042127; P:regulation of cell population proliferation; IDA:MGI.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:InterPro.
DR InterPro; IPR033576; CDCA7.
DR InterPro; IPR040221; CDCA7/CDA7L.
DR InterPro; IPR018866; Znf-4CXXC_R1.
DR PANTHER; PTHR31169; PTHR31169; 1.
DR PANTHER; PTHR31169:SF2; PTHR31169:SF2; 1.
DR Pfam; PF10497; zf-4CXXC_R1; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Apoptosis; Cytoplasm; Disease variant;
KW Isopeptide bond; Nucleus; Phosphoprotein; Reference proteome;
KW Transcription; Transcription regulation; Ubl conjugation.
FT CHAIN 1..371
FT /note="Cell division cycle-associated protein 7"
FT /id="PRO_0000249310"
FT REGION 60..110
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 140..188
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 146..170
FT /note="Interaction with MYC"
FT /evidence="ECO:0000269|PubMed:23166294"
FT REGION 247..371
FT /note="Mediates transcriptional activity"
FT MOTIF 160..176
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000269|PubMed:23166294"
FT COMPBIAS 87..109
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 167..181
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 142
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 163
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:23166294,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 190
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT CROSSLNK 204
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VAR_SEQ 8..49
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_054407"
FT VAR_SEQ 49
FT /note="T -> TKPKFRSDISEELANVFYEDSDNESFCGFSESEVQDVLDHCGFLQKP
FT RPDVTNELAGIFHADSDDESFCGFSESEIQDGM (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_020394"
FT VAR_SEQ 49
FT /note="T -> TKPRPDVTNELAGIFHADSDDESFCGFSESEIQDGM (in
FT isoform 6)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_054408"
FT VAR_SEQ 155..207
FT /note="QSRRPRRRTFPGVASRRNPERRARPLTRSRSRILGSLDALPMEEEEEEDKYM
FT L -> VSTSSCLYTVVFWAHLRSICVVFKNLISLFVWPSRQTKGTQRKPPDRSLDDPP
FT (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_020395"
FT VAR_SEQ 208..371
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_020396"
FT VAR_SEQ 267..316
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:17974005"
FT /id="VSP_020397"
FT VARIANT 274
FT /note="R -> C (in ICF3; dbSNP:rs879253738)"
FT /evidence="ECO:0000269|PubMed:26216346"
FT /id="VAR_076578"
FT VARIANT 274
FT /note="R -> H (in ICF3; dbSNP:rs370384522)"
FT /evidence="ECO:0000269|PubMed:26216346"
FT /id="VAR_076579"
FT VARIANT 294
FT /note="G -> V (in ICF3; unknown pathological significance)"
FT /evidence="ECO:0000269|PubMed:26216346"
FT /id="VAR_076580"
FT VARIANT 304
FT /note="R -> H (in ICF3; unknown pathological significance;
FT dbSNP:rs772929976)"
FT /evidence="ECO:0000269|PubMed:26216346"
FT /id="VAR_076581"
FT MUTAGEN 158
FT /note="R->A: Does not affect phosphorylation or interaction
FT with YHWAE and YHWAZ."
FT /evidence="ECO:0000269|PubMed:23166294"
FT MUTAGEN 159
FT /note="P->A: Does not affect phosphorylation or interaction
FT with YHWAE and YHWAZ."
FT /evidence="ECO:0000269|PubMed:23166294"
FT MUTAGEN 160
FT /note="R->A: Abolishes phosphorylation and interaction with
FT YHWAE and YHWAZ."
FT /evidence="ECO:0000269|PubMed:23166294"
FT MUTAGEN 160
FT /note="R->E: Predominantly cytoplasmic."
FT /evidence="ECO:0000269|PubMed:23166294"
FT MUTAGEN 161
FT /note="R->A: Increased phosphorylation, binding to YHWAE
FT and YHWAZ, and cytoplasmic expression."
FT /evidence="ECO:0000269|PubMed:23166294"
FT MUTAGEN 161
FT /note="R->E: Predominantly cytoplasmic."
FT /evidence="ECO:0000269|PubMed:23166294"
FT MUTAGEN 162
FT /note="R->A: Does not affect phosphorylation or interaction
FT with YHWAE and YHWAZ."
FT /evidence="ECO:0000269|PubMed:23166294"
FT MUTAGEN 162
FT /note="R->E: Predominantly cytoplasmic."
FT /evidence="ECO:0000269|PubMed:23166294"
FT MUTAGEN 163
FT /note="T->A: Abolishes phosphorylation, interaction with
FT YHWAE and YHWAZ, and cytoplasmic localization."
FT /evidence="ECO:0000269|PubMed:23166294"
FT MUTAGEN 164
FT /note="F->A: Abolishes phosphorylation and interaction with
FT YHWAE and YHWAZ."
FT /evidence="ECO:0000269|PubMed:23166294"
FT MUTAGEN 165
FT /note="P->A: Abolishes phosphorylation, interaction with
FT YHWAE and YHWAZ, and cytoplasmic localization."
FT /evidence="ECO:0000269|PubMed:23166294"
FT MUTAGEN 171
FT /note="R->E: Predominantly cytoplasmic. Completely
FT cytoplasmic with no nuclear expression; when associated
FT with E-176."
FT /evidence="ECO:0000269|PubMed:23166294"
FT MUTAGEN 176
FT /note="R->E: Predominantly cytoplasmic. Completely
FT cytoplasmic with no nuclear expression; when associated
FT with E-171."
FT /evidence="ECO:0000269|PubMed:23166294"
FT MUTAGEN 182
FT /note="R->E: No effect on subcellular location."
FT /evidence="ECO:0000269|PubMed:23166294"
FT MUTAGEN 184
FT /note="R->E: No effect on subcellular location."
FT /evidence="ECO:0000269|PubMed:23166294"
FT CONFLICT 152
FT /note="S -> G (in Ref. 6; AAH15124)"
FT /evidence="ECO:0000305"
FT CONFLICT 320
FT /note="C -> W (in Ref. 3; BAD97244)"
FT /evidence="ECO:0000305"
FT CONFLICT Q9BWT1-2:63
FT /note="N -> S (in Ref. 2; BAB55245)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 371 AA; 42573 MW; 30A244E3057D9C43 CRC64;
MDARRVPQKD LRVKKNLKKF RYVKLISMET SSSSDDSCDS FASDNFANTR LQSVREGCRT
RSQCRHSGPL RVAMKFPARS TRGATNKKAE SRQPSENSVT DSNSDSEDES GMNFLEKRAL
NIKQNKAMLA KLMSELESFP GSFRGRHPLP GSDSQSRRPR RRTFPGVASR RNPERRARPL
TRSRSRILGS LDALPMEEEE EEDKYMLVRK RKTVDGYMNE DDLPRSRRSR SSVTLPHIIR
PVEEITEEEL ENVCSNSREK IYNRSLGSTC HQCRQKTIDT KTNCRNPDCW GVRGQFCGPC
LRNRYGEEVR DALLDPNWHC PPCRGICNCS FCRQRDGRCA TGVLVYLAKY HGFGNVHAYL
KSLKQEFEMQ A
