LOCUS       NP_001072113             620 aa            linear   PRI 28-APR-2025
DEFINITION  cell division cycle protein 16 homolog isoform 1 [Homo sapiens].
ACCESSION   NP_001072113
VERSION     NP_001072113.1
DBSOURCE    REFSEQ: accession NM_001078645.3
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 620)
  AUTHORS   Hu,F., Fong,K.O., Cheung,M.P.L., Liu,J.A., Liang,R., Li,T.W.,
            Sharma,R., Ip,P.P., Yang,X. and Cheung,M.
  TITLE     DEPDC1B Promotes Melanoma Angiogenesis and Metastasis through
            Sequestration of Ubiquitin Ligase CDC16 to Stabilize Secreted
            SCUBE3
  JOURNAL   Adv Sci (Weinh) 9 (10), e2105226 (2022)
   PUBMED   35088579
  REMARK    GeneRIF: DEPDC1B Promotes Melanoma Angiogenesis and Metastasis
            through Sequestration of Ubiquitin Ligase CDC16 to Stabilize
            Secreted SCUBE3.
REFERENCE   2  (residues 1 to 620)
  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   3  (residues 1 to 620)
  AUTHORS   Wu,H., Zhang,X., Shen,Q., Liu,Y., Gao,Y., Wang,G., Lv,M., Hua,R.,
            Xu,Y., Zhou,P., Wei,Z., Tao,F., He,X., Cao,Y. and Liu,M.
  TITLE     A homozygous loss-of-function mutation in FBXO43 causes human
            non-obstructive azoospermia
  JOURNAL   Clin Genet 101 (1), 55-64 (2022)
   PUBMED   34595750
REFERENCE   4  (residues 1 to 620)
  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   5  (residues 1 to 620)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   6  (residues 1 to 620)
  AUTHORS   Grossberger,R., Gieffers,C., Zachariae,W., Podtelejnikov,A.V.,
            Schleiffer,A., Nasmyth,K., Mann,M. and Peters,J.M.
  TITLE     Characterization of the DOC1/APC10 subunit of the yeast and the
            human anaphase-promoting complex
  JOURNAL   J Biol Chem 274 (20), 14500-14507 (1999)
   PUBMED   10318877
REFERENCE   7  (residues 1 to 620)
  AUTHORS   Kallio,M., Weinstein,J., Daum,J.R., Burke,D.J. and Gorbsky,G.J.
  TITLE     Mammalian p55CDC mediates association of the spindle checkpoint
            protein Mad2 with the cyclosome/anaphase-promoting complex, and is
            involved in regulating anaphase onset and late mitotic events
  JOURNAL   J Cell Biol 141 (6), 1393-1406 (1998)
   PUBMED   9628895
REFERENCE   8  (residues 1 to 620)
  AUTHORS   Yu,H., Peters,J.M., King,R.W., Page,A.M., Hieter,P. and
            Kirschner,M.W.
  TITLE     Identification of a cullin homology region in a subunit of the
            anaphase-promoting complex
  JOURNAL   Science 279 (5354), 1219-1222 (1998)
   PUBMED   9469815
REFERENCE   9  (residues 1 to 620)
  AUTHORS   Ollendorff,V. and Donoghue,D.J.
  TITLE     The serine/threonine phosphatase PP5 interacts with CDC16 and
            CDC27, two tetratricopeptide repeat-containing subunits of the
            anaphase-promoting complex
  JOURNAL   J Biol Chem 272 (51), 32011-32018 (1997)
   PUBMED   9405394
REFERENCE   10 (residues 1 to 620)
  AUTHORS   Tugendreich,S., Tomkiel,J., Earnshaw,W. and Hieter,P.
  TITLE     CDC27Hs colocalizes with CDC16Hs to the centrosome and mitotic
            spindle and is essential for the metaphase to anaphase transition
  JOURNAL   Cell 81 (2), 261-268 (1995)
   PUBMED   7736578
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DC391369.1, BQ051608.1,
            AW953481.1, BQ424567.1, AW662777.1 and BM663581.1.
            
            Summary: The protein encoded by this gene functions as a protein
            ubiquitin ligase and is a component of the multiprotein APC
            complex. The APC complex is a cyclin degradation system that
            governs exit from mitosis by targeting cell cycle proteins for
            degredation by the 26S proteasome. Each component protein of the
            APC complex is highly conserved among eukaryotic organisms. This
            protein, and other APC complex proteins, contain a
            tetratricopeptide repeat (TPR) domain; a protein domain that is
            often involved in protein-protein interactions and the assembly of
            multiprotein complexes. Multiple alternatively spliced transcript
            variants, encoding distinct proteins, have been identified.
            [provided by RefSeq, Jan 2016].
            
            Transcript Variant: This variant (2) represents the longest
            transcript. Variants 1 and 2 encode the same 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 :: SRR1163655.264295.1,
                                           SRR1803616.84521.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000356221.8/ ENSP00000348554.3
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..620
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="13"
                     /map="13q34"
     Protein         1..620
                     /product="cell division cycle protein 16 homolog isoform
                     1"
                     /note="cell division cycle protein 16 homolog; cell
                     division cycle 16 homolog; anaphase-promoting complex,
                     subunit 6; cyclosome subunit 6"
                     /calculated_mol_wt=71525
     Region          4..33
                     /region_name="TPR 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q13042.2)"
     Region          15..94
                     /region_name="ANAPC3"
                     /note="Anaphase-promoting complex, cyclosome, subunit 3;
                     pfam12895"
                     /db_xref="CDD:463743"
     Region          36..65
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          37..62
                     /region_name="TPR 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q13042.2)"
     Region          70..94
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          70..93
                     /region_name="TPR 3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q13042.2)"
     Site            112
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:14657031; propagated from
                     UniProtKB/Swiss-Prot (Q13042.2)"
     Region          128..159
                     /region_name="TPR 4"
                     /note="propagated from UniProtKB/Swiss-Prot (Q13042.2)"
     Region          164..187
                     /region_name="TPR 5"
                     /note="propagated from UniProtKB/Swiss-Prot (Q13042.2)"
     Region          198..222
                     /region_name="TPR 6"
                     /note="propagated from UniProtKB/Swiss-Prot (Q13042.2)"
     Region          232..260
                     /region_name="TPR 7"
                     /note="propagated from UniProtKB/Swiss-Prot (Q13042.2)"
     Region          267..294
                     /region_name="TPR 8"
                     /note="propagated from UniProtKB/Swiss-Prot (Q13042.2)"
     Region          275..>440
                     /region_name="Spy"
                     /note="Predicted O-linked N-acetylglucosamine transferase,
                     SPINDLY family [Posttranslational modification, protein
                     turnover, chaperones]; COG3914"
                     /db_xref="CDD:443119"
     Region          298..329
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          299..329
                     /region_name="TPR 9"
                     /note="propagated from UniProtKB/Swiss-Prot (Q13042.2)"
     Region          334..362
                     /region_name="TPR 10"
                     /note="propagated from UniProtKB/Swiss-Prot (Q13042.2)"
     Region          336..362
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          367..397
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          369..397
                     /region_name="TPR 11"
                     /note="propagated from UniProtKB/Swiss-Prot (Q13042.2)"
     Region          373..>522
                     /region_name="TPR"
                     /note="Tetratricopeptide (TPR) repeat [General function
                     prediction only]; COG0457"
                     /db_xref="CDD:440225"
     Region          402..434
                     /region_name="TPR 12"
                     /note="propagated from UniProtKB/Swiss-Prot (Q13042.2)"
     Region          402..430
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(403,406..407,410..411,413,437,449..450,453..454,
                     456..457,480,483..484,487..488,491)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          435..474
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          442..474
                     /region_name="TPR 13"
                     /note="propagated from UniProtKB/Swiss-Prot (Q13042.2)"
     Region          479..508
                     /region_name="TPR 14"
                     /note="propagated from UniProtKB/Swiss-Prot (Q13042.2)"
     Region          479..506
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            490
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:14657031; propagated from
                     UniProtKB/Swiss-Prot (Q13042.2)"
     Site            560
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:14657031,
                     ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q13042.2)"
     Region          574..599
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q13042.2)"
     Site            581
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000269|PubMed:14657031,
                     ECO:0007744|PubMed:16964243, ECO:0007744|PubMed:18691976,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q13042.2)"
     Site            595
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:14657031; propagated from
                     UniProtKB/Swiss-Prot (Q13042.2)"
     Site            599
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000269|PubMed:14657031; propagated from
                     UniProtKB/Swiss-Prot (Q13042.2)"
     CDS             1..620
                     /gene="CDC16"
                     /gene_synonym="ANAPC6; APC6; CDC16Hs; CUT9"
                     /coded_by="NM_001078645.3:189..2051"
                     /note="isoform 1 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS9542.2"
                     /db_xref="GeneID:8881"
                     /db_xref="HGNC:HGNC:1720"
                     /db_xref="MIM:603461"
ORIGIN      
        1 mnlerlrkrv rqyldqqqyq salfwadkva slsreepqdi ywlaqclylt aqyhraahal
       61 rsrkldklye acrylaarch yaakehqqal dvldmeepin krlfekylkd esgfkdpssd
      121 wemsqssiks sicllrgkiy daldnrtlat ysykealkld vycfeafdll tshhmltaqe
      181 ekelleslpl sklcneeqel lrflfenklk kynkpsetvi pesvdglqen ldvvvslaer
      241 hyyncdfkmc ykltsvvmek dpfhasclpv higtlvelnk anelfylshk lvdlypsnpv
      301 swfavgcyyl mvghknehar rylskattle ktygpawiay ghsfaveseh dqamaayfta
      361 aqlmkgchlp mlyigleygl tnnsklaerf fsqalsiape dpfvmhevgv vafqngewkt
      421 aekwfldale kikaignevt vdkwepllnn lghvcrklkk yaealdyhrq alvlipqnas
      481 tysaigyihs lmgnfenavd yfhtalglrr ddtfsvtmlg hciemyigds eayigadikd
      541 klkcydfdvh tmktlkniis ppwdfrefev ekqtaeetgl tpletsrktp dsrpsleetf
      601 eiemnesdmm letsmsdhst
//
