LOCUS       NP_001093869            1337 aa            linear   PRI 19-SEP-2024
DEFINITION  sister chromatid cohesion protein PDS5 homolog A isoform 1 [Homo
            sapiens].
ACCESSION   NP_001093869
VERSION     NP_001093869.1
DBSOURCE    REFSEQ: accession NM_001100399.2
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1337)
  AUTHORS   van Ruiten,M.S., van Gent,D., Sedeno Cacciatore,A., Fauster,A.,
            Willems,L., Hekkelman,M.L., Hoekman,L., Altelaar,M.,
            Haarhuis,J.H.I., Brummelkamp,T.R., de Wit,E. and Rowland,B.D.
  TITLE     The cohesin acetylation cycle controls chromatin loop length
            through a PDS5A brake mechanism
  JOURNAL   Nat Struct Mol Biol 29 (6), 586-591 (2022)
   PUBMED   35710836
  REMARK    GeneRIF: The cohesin acetylation cycle controls chromatin loop
            length through a PDS5A brake mechanism.
REFERENCE   2  (residues 1 to 1337)
  AUTHORS   Wang,Y., Yao,J., Zhu,Y., Zhao,X., Lv,J. and Sun,F.
  TITLE     Knockdown of CDCA5 suppresses malignant progression of breast
            cancer cells by regulating PDS5A
  JOURNAL   Mol Med Rep 25 (6) (2022)
   PUBMED   35506437
  REMARK    GeneRIF: Knockdown of CDCA5 suppresses malignant progression of
            breast cancer cells by regulating PDS5A.
REFERENCE   3  (residues 1 to 1337)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   4  (residues 1 to 1337)
  AUTHORS   Zhang,N., Coutinho,L.E. and Pati,D.
  TITLE     PDS5A and PDS5B in Cohesin Function and Human Disease
  JOURNAL   Int J Mol Sci 22 (11), 5868 (2021)
   PUBMED   34070827
  REMARK    GeneRIF: PDS5A and PDS5B in Cohesin Function and Human Disease.
            Review article
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 1337)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   6  (residues 1 to 1337)
  AUTHORS   Losada,A., Yokochi,T. and Hirano,T.
  TITLE     Functional contribution of Pds5 to cohesin-mediated cohesion in
            human cells and Xenopus egg extracts
  JOURNAL   J Cell Sci 118 (Pt 10), 2133-2141 (2005)
   PUBMED   15855230
REFERENCE   7  (residues 1 to 1337)
  AUTHORS   Rankin,S., Ayad,N.G. and Kirschner,M.W.
  TITLE     Sororin, a substrate of the anaphase-promoting complex, is required
            for sister chromatid cohesion in vertebrates
  JOURNAL   Mol Cell 18 (2), 185-200 (2005)
   PUBMED   15837422
  REMARK    Erratum:[Mol Cell. 2005 May 27;18(5):609]
REFERENCE   8  (residues 1 to 1337)
  AUTHORS   Kumar,D., Sakabe,I., Patel,S., Zhang,Y., Ahmad,I., Gehan,E.A.,
            Whiteside,T.L. and Kasid,U.
  TITLE     SCC-112, a novel cell cycle-regulated molecule, exhibits reduced
            expression in human renal carcinomas
  JOURNAL   Gene 328, 187-196 (2004)
   PUBMED   15019998
  REMARK    GeneRIF: Findings suggest that the SCC-112 gene expression is
            likely to be associated with normal cell growth and proliferation.
REFERENCE   9  (residues 1 to 1337)
  AUTHORS   Gregson,H.C., Schmiesing,J.A., Kim,J.S., Kobayashi,T., Zhou,S. and
            Yokomori,K.
  TITLE     A potential role for human cohesin in mitotic spindle aster
            assembly
  JOURNAL   J Biol Chem 276 (50), 47575-47582 (2001)
   PUBMED   11590136
REFERENCE   10 (residues 1 to 1337)
  AUTHORS   Sumara,I., Vorlaufer,E., Gieffers,C., Peters,B.H. and Peters,J.M.
  TITLE     Characterization of vertebrate cohesin complexes and their
            regulation in prophase
  JOURNAL   J Cell Biol 151 (4), 749-762 (2000)
   PUBMED   11076961
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BC041361.1, AC098591.4 and
            BC114218.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: The protein encoded by this gene binds to the cohesin
            complex and associates with chromatin through most of the cell
            cycle. The encoded protein may play a role in regulating sister
            chromatid cohesion during mitosis. Two transcript variants encoding
            different isoforms have been found for this gene. [provided by
            RefSeq, May 2010].
            
            Transcript Variant: This variant (1) represents the longest
            transcript and encodes the longest isoform (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC114218.1, AB621803.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000303538.13/ ENSP00000303427.8
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1337
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="4"
                     /map="4p14"
     Protein         1..1337
                     /product="sister chromatid cohesion protein PDS5 homolog A
                     isoform 1"
                     /note="sister chromatid cohesion protein PDS5 homolog A;
                     sister chromatid cohesion protein 112; cell
                     proliferation-inducing gene 54 protein; PDS5, regulator of
                     cohesion maintenance, homolog A"
                     /calculated_mol_wt=150700
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine.
                     /evidence=ECO:0007744|PubMed:19413330; propagated from
                     UniProtKB/Swiss-Prot (Q29RF7.1)"
     Region          39..1109
                     /region_name="PDS5"
                     /note="Sister chromatid cohesion protein PDS5 protein;
                     pfam20168"
                     /db_xref="CDD:466319"
     Site            order(263..264,267,270..271,300..301,304,307..308,313,
                     341..342,345,348,378..379,382,385..386,416..417)
                     /site_type="other"
                     /note="putative peptide binding site [polypeptide
                     binding]"
                     /db_xref="CDD:293787"
     Region          283..313
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     Region          323..349
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     Region          360..386
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     Region          393..429
                     /region_name="HEAT. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q29RF7.1)"
     Site            1097
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q29RF7.1)"
     Site            1146
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (Q29RF7.1)"
     Region          1150..1337
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q29RF7.1)"
     Site            1195
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q29RF7.1)"
     Site            1208
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q29RF7.1)"
     Site            1211
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (Q29RF7.1)"
     Site            1290
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (Q29RF7.1)"
     Site            1305
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:16964243,
                     ECO:0007744|PubMed:17081983, ECO:0007744|PubMed:17924679,
                     ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q29RF7.1)"
     CDS             1..1337
                     /gene="PDS5A"
                     /gene_synonym="PIG54; SCC-112; SCC112"
                     /coded_by="NM_001100399.2:496..4509"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS47045.1"
                     /db_xref="GeneID:23244"
                     /db_xref="HGNC:HGNC:29088"
                     /db_xref="MIM:613200"
ORIGIN      
        1 mdftaqpkpa talcgvvsad gkiayppgvk eitdkittde mikrlkmvvk tfmdmdqdse
       61 dekqqylpla lhlasefflr npnkdvrllv accladifri yapeapytsh dklkdiflfi
      121 trqlkgledt kspqfnryfy llenlawvks ynicfeledc neifiqlfrt lfsvinnshn
      181 kkvqmhmldl mssiimegdg vtqelldsil inlipahknl nkqsfdlakv llkrtvqtie
      241 acianffnqv lvlgrssvsd lsehvfdliq elfaidphll lsvmpqlefk lksndgeerl
      301 avvrllaklf gskdsdlatq nrplwqcflg rfndihvpvr lesvkfashc lmnhpdlakd
      361 lteylkvrsh dpeeairhdv ivtiitaakr dlalvndqll gfvrertldk rwrvrkeamm
      421 glaqlykkyc lhgeagkeaa ekvswikdkl lhiyyqnsid dkllvekifa qylvphnlet
      481 eermkclyyl yasldpnavk alnemwkcqn mlrshvrell dlhkqptsea ncsamfgklm
      541 tiaknlpdpg kaqdfvkkfn qvlgddeklr sqlellispt csckqadicv reiarklanp
      601 kqptnpflem vkflleriap vhidseaisa lvklmnksie gtaddeeegv spdtairsgl
      661 ellkvlsfth ptsfhsaety esllqclrme ddkvaeaaiq ifrntghkie tdlpqirstl
      721 ipilhqkakr gtphqakqav hcihaiftnk evqlaqifep lsrslnadvp eqlitplvsl
      781 ghismlapdq faspmksvva nfivkdllmn drstgekngk lwspdeevsp evlakvqaik
      841 llvrwllgmk nnqsksanst lrllsamlvs egdlteqkri sksdmsrlrl aagsaimkla
      901 qepcyheiit peqfqlcalv indecyqvrq ifaqklhkal vklllpleym aifalcakdp
      961 vkerraharq cllknisirr eyikqnpmat ekllsllpey vvpymihlla hdpdftrsqd
     1021 vdqlrdikec lwfmlevlmt knennshafm kkmaeniklt rdaqspdesk tneklytvcd
     1081 valcvinsks alcnadspkd pvlpmkfftq pekdfcndks yiseetrvll ltgkpkpagv
     1141 lgavnkplsa tgrkpyvrst gtetgsninv nselnpstgn rsreqsseaa etgvseneen
     1201 pvriisvtpv knidpvknke insdqatqgn issdrgkkrt vtaagaeniq qktdekvdes
     1261 gppapskprr grrpksesqg natknddlnk pinkgrkraa vgqespggle agnakapklq
     1321 dlakkaapae rqidlqr
//
