ID   DCC1_HUMAN              Reviewed;         393 AA.
AC   Q9BVC3; Q969N5;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-FEB-2008, sequence version 2.
DT   03-AUG-2022, entry version 144.
DE   RecName: Full=Sister chromatid cohesion protein DCC1;
DE   AltName: Full=Defective in sister chromatid cohesion protein 1 homolog;
GN   Name=DSCC1; Synonyms=DCC1; ORFNames=UNQ9337/PRO34008;
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], AND VARIANT ARG-376.
RX   PubMed=12975309; DOI=10.1101/gr.1293003;
RA   Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J.,
RA   Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P.,
RA   Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S., Huang A.,
RA   Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D.,
RA   Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L.,
RA   Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C.,
RA   Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J.,
RA   Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M.;
RT   "The secreted protein discovery initiative (SPDI), a large-scale effort to
RT   identify novel human secreted and transmembrane proteins: a bioinformatics
RT   assessment.";
RL   Genome Res. 13:2265-2270(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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], AND VARIANT ARG-376.
RC   TISSUE=Brain, and Placenta;
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   FUNCTION, AND INTERACTION WITH CTF8 AND CTF18.
RX   PubMed=12766176; DOI=10.1074/jbc.m211591200;
RA   Merkle C.J., Karnitz L.M., Henry-Sanchez J.T., Chen J.;
RT   "Cloning and characterization of hCTF18, hCTF8, and hDCC1. Human homologs
RT   of a Saccharomyces cerevisiae complex involved in sister chromatid cohesion
RT   establishment.";
RL   J. Biol. Chem. 278:30051-30056(2003).
RN   [5]
RP   INTERACTION WITH DDX11.
RX   PubMed=18499658; DOI=10.1074/jbc.m802696200;
RA   Farina A., Shin J.H., Kim D.H., Bermudez V.P., Kelman Z., Seo Y.S.,
RA   Hurwitz J.;
RT   "Studies with the human cohesin establishment factor, ChlR1. Association of
RT   ChlR1 with Ctf18-RFC and Fen1.";
RL   J. Biol. Chem. 283:20925-20936(2008).
RN   [6]
RP   FUNCTION IN DNA REPLICATION AND SISTER CHROMATID COHESION.
RX   PubMed=19907496; DOI=10.1038/nature08550;
RA   Terret M.E., Sherwood R., Rahman S., Qin J., Jallepalli P.V.;
RT   "Cohesin acetylation speeds the replication fork.";
RL   Nature 462:231-234(2009).
RN   [7]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA   Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA   Bennett K.L., Superti-Furga G., Colinge J.;
RT   "Initial characterization of the human central proteome.";
RL   BMC Syst. Biol. 5:17-17(2011).
CC   -!- FUNCTION: Loads PCNA onto primed templates regulating velocity, spacing
CC       and restart activity of replication forks. May couple DNA replication
CC       to sister chromatid cohesion through regulation of the acetylation of
CC       the cohesin subunit SMC3. {ECO:0000269|PubMed:12766176,
CC       ECO:0000269|PubMed:19907496}.
CC   -!- SUBUNIT: Component of the CTF18-RFC complex which consists of CTF8,
CC       CTF18, DSCC1 and the RFC complex (PubMed:12766176). Interacts with CTF8
CC       and CTF18 (PubMed:12766176). Interacts with DDX11 (PubMed:18499658).
CC       {ECO:0000269|PubMed:12766176, ECO:0000269|PubMed:18499658}.
CC   -!- INTERACTION:
CC       Q9BVC3; P22607: FGFR3; NbExp=3; IntAct=EBI-11143782, EBI-348399;
CC       Q9BVC3; Q9UMX0: UBQLN1; NbExp=3; IntAct=EBI-11143782, EBI-741480;
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the DCC1 family. {ECO:0000305}.
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DR   EMBL; AY358866; AAQ89225.1; -; mRNA.
DR   EMBL; AK054585; BAB70767.1; -; mRNA.
DR   EMBL; BC001316; AAH01316.1; -; mRNA.
DR   EMBL; BC001531; AAH01531.1; -; mRNA.
DR   CCDS; CCDS6330.1; -.
DR   RefSeq; NP_076999.2; NM_024094.2.
DR   AlphaFoldDB; Q9BVC3; -.
DR   SMR; Q9BVC3; -.
DR   BioGRID; 122526; 61.
DR   CORUM; Q9BVC3; -.
DR   IntAct; Q9BVC3; 18.
DR   STRING; 9606.ENSP00000322180; -.
DR   iPTMnet; Q9BVC3; -.
DR   MetOSite; Q9BVC3; -.
DR   PhosphoSitePlus; Q9BVC3; -.
DR   BioMuta; DSCC1; -.
DR   DMDM; 167012058; -.
DR   EPD; Q9BVC3; -.
DR   jPOST; Q9BVC3; -.
DR   MassIVE; Q9BVC3; -.
DR   MaxQB; Q9BVC3; -.
DR   PaxDb; Q9BVC3; -.
DR   PeptideAtlas; Q9BVC3; -.
DR   PRIDE; Q9BVC3; -.
DR   ProteomicsDB; 79193; -.
DR   TopDownProteomics; Q9BVC3; -.
DR   Antibodypedia; 26822; 209 antibodies from 23 providers.
DR   DNASU; 79075; -.
DR   Ensembl; ENST00000313655.5; ENSP00000322180.4; ENSG00000136982.6.
DR   GeneID; 79075; -.
DR   KEGG; hsa:79075; -.
DR   MANE-Select; ENST00000313655.5; ENSP00000322180.4; NM_024094.3; NP_076999.2.
DR   UCSC; uc003yov.4; human.
DR   CTD; 79075; -.
DR   DisGeNET; 79075; -.
DR   GeneCards; DSCC1; -.
DR   HGNC; HGNC:24453; DSCC1.
DR   HPA; ENSG00000136982; Tissue enhanced (lymphoid).
DR   MIM; 613203; gene.
DR   neXtProt; NX_Q9BVC3; -.
DR   OpenTargets; ENSG00000136982; -.
DR   PharmGKB; PA162384079; -.
DR   VEuPathDB; HostDB:ENSG00000136982; -.
DR   eggNOG; KOG0798; Eukaryota.
DR   GeneTree; ENSGT00390000017400; -.
DR   HOGENOM; CLU_034504_1_1_1; -.
DR   InParanoid; Q9BVC3; -.
DR   OMA; YVRTPED; -.
DR   OrthoDB; 1140219at2759; -.
DR   PhylomeDB; Q9BVC3; -.
DR   TreeFam; TF106104; -.
DR   PathwayCommons; Q9BVC3; -.
DR   Reactome; R-HSA-174411; Polymerase switching on the C-strand of the telomere.
DR   SignaLink; Q9BVC3; -.
DR   BioGRID-ORCS; 79075; 164 hits in 1083 CRISPR screens.
DR   ChiTaRS; DSCC1; human.
DR   GeneWiki; DCC1; -.
DR   GenomeRNAi; 79075; -.
DR   Pharos; Q9BVC3; Tbio.
DR   PRO; PR:Q9BVC3; -.
DR   Proteomes; UP000005640; Chromosome 8.
DR   RNAct; Q9BVC3; protein.
DR   Bgee; ENSG00000136982; Expressed in secondary oocyte and 187 other tissues.
DR   Genevisible; Q9BVC3; HS.
DR   GO; GO:0000785; C:chromatin; IDA:UniProtKB.
DR   GO; GO:0000775; C:chromosome, centromeric region; IDA:UniProtKB.
DR   GO; GO:0031390; C:Ctf18 RFC-like complex; IDA:UniProtKB.
DR   GO; GO:0005654; C:nucleoplasm; IDA:UniProtKB.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0032508; P:DNA duplex unwinding; IEA:GOC.
DR   GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR   GO; GO:0034088; P:maintenance of mitotic sister chromatid cohesion; IMP:UniProtKB.
DR   GO; GO:1900264; P:positive regulation of DNA-directed DNA polymerase activity; IDA:UniProtKB.
DR   GO; GO:0034421; P:post-translational protein acetylation; IMP:UniProtKB.
DR   GO; GO:0006275; P:regulation of DNA replication; IMP:UniProtKB.
DR   InterPro; IPR019128; Dcc1.
DR   PANTHER; PTHR13395; PTHR13395; 1.
DR   Pfam; PF09724; Dcc1; 1.
PE   1: Evidence at protein level;
KW   Cell cycle; DNA replication; DNA-binding; Nucleus; Reference proteome.
FT   CHAIN           1..393
FT                   /note="Sister chromatid cohesion protein DCC1"
FT                   /id="PRO_0000318064"
FT   VARIANT         376
FT                   /note="H -> R (in dbSNP:rs1055130)"
FT                   /evidence="ECO:0000269|PubMed:12975309,
FT                   ECO:0000269|PubMed:15489334"
FT                   /id="VAR_038682"
SQ   SEQUENCE   393 AA;  44825 MW;  AAF6C66B7151FA65 CRC64;
     MKRTRDEVDA TLQIAKLNAA ELLPAVHCLG FGPGASGAAA GDFCLLELEP TLCQQLEDGH
     SLVIRGDKDE QAVLCSKDKT YDLKIADTSN MLLFIPGCKT PDQLKKEDSH CNIIHTEIFG
     FSNNYWELRR RRPKLKKLKK LLMENPYEGP DSQKEKDSNS SKYTTEDLLD QIQASEEEIM
     TQLQVLNACK IGGYWRILEF DYEMKLLNHV TQLVDSESWS FGKVPLNTCL QELGPLEPEE
     MIEHCLKCYG KKYVDEGEVY FELDADKICR AAARMLLQNA VKFNLAEFQE VWQQSVPEGM
     VTSLDQLKGL ALVDRHSRPE IIFLLKVDDL PEDNQERFNS LFSLREKWTE EDIAPYIQDL
     CGEKQTIGAL LTKYSHSSMQ NGVKVYNSRR PIS