PBDC1_HUMAN
ID PBDC1_HUMAN Reviewed; 233 AA.
AC Q9BVG4;
DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=Protein PBDC1;
DE AltName: Full=Polysaccharide biosynthesis domain-containing protein 1;
GN Name=PBDC1; Synonyms=CXorf26;
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].
RC TISSUE=Leiomyosarcoma, and Rhabdomyosarcoma;
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 [2]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-126, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic kidney;
RX PubMed=17525332; DOI=10.1126/science.1140321;
RA Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E.,
RA Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y.,
RA Gygi S.P., Elledge S.J.;
RT "ATM and ATR substrate analysis reveals extensive protein networks
RT responsive to DNA damage.";
RL Science 316:1160-1166(2007).
RN [3]
RP IDENTIFICATION BY 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 [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-197, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=18318008; DOI=10.1002/pmic.200700884;
RA Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D.,
RA Zou H., Gu J.;
RT "Large-scale phosphoproteome analysis of human liver tissue by enrichment
RT and fractionation of phosphopeptides with strong anion exchange
RT chromatography.";
RL Proteomics 8:1346-1361(2008).
RN [5]
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).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-181 AND SER-197, AND
RP IDENTIFICATION BY 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 [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-197, 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 [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-181 AND SER-197, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
CC -!- SIMILARITY: Belongs to the PBDC1 family. {ECO:0000305}.
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DR EMBL; BC001220; AAH01220.1; -; mRNA.
DR EMBL; BC051894; AAH51894.1; -; mRNA.
DR CCDS; CCDS14432.1; -.
DR RefSeq; NP_001287817.1; NM_001300888.1.
DR RefSeq; NP_057584.2; NM_016500.3.
DR AlphaFoldDB; Q9BVG4; -.
DR SMR; Q9BVG4; -.
DR BioGRID; 119416; 25.
DR IntAct; Q9BVG4; 15.
DR MINT; Q9BVG4; -.
DR STRING; 9606.ENSP00000362456; -.
DR GlyGen; Q9BVG4; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q9BVG4; -.
DR MetOSite; Q9BVG4; -.
DR PhosphoSitePlus; Q9BVG4; -.
DR BioMuta; PBDC1; -.
DR DMDM; 74733325; -.
DR EPD; Q9BVG4; -.
DR jPOST; Q9BVG4; -.
DR MassIVE; Q9BVG4; -.
DR MaxQB; Q9BVG4; -.
DR PaxDb; Q9BVG4; -.
DR PeptideAtlas; Q9BVG4; -.
DR PRIDE; Q9BVG4; -.
DR ProteomicsDB; 79200; -.
DR Antibodypedia; 507; 199 antibodies from 19 providers.
DR DNASU; 51260; -.
DR Ensembl; ENST00000373358.8; ENSP00000362456.3; ENSG00000102390.11.
DR GeneID; 51260; -.
DR KEGG; hsa:51260; -.
DR MANE-Select; ENST00000373358.8; ENSP00000362456.3; NM_016500.5; NP_057584.2.
DR UCSC; uc004ecl.2; human.
DR CTD; 51260; -.
DR GeneCards; PBDC1; -.
DR HGNC; HGNC:28790; PBDC1.
DR HPA; ENSG00000102390; Low tissue specificity.
DR neXtProt; NX_Q9BVG4; -.
DR OpenTargets; ENSG00000102390; -.
DR PharmGKB; PA128394657; -.
DR VEuPathDB; HostDB:ENSG00000102390; -.
DR eggNOG; KOG4093; Eukaryota.
DR GeneTree; ENSGT00390000016333; -.
DR HOGENOM; CLU_103791_0_0_1; -.
DR InParanoid; Q9BVG4; -.
DR OMA; MELMHGA; -.
DR OrthoDB; 1420225at2759; -.
DR PhylomeDB; Q9BVG4; -.
DR TreeFam; TF314442; -.
DR PathwayCommons; Q9BVG4; -.
DR SignaLink; Q9BVG4; -.
DR BioGRID-ORCS; 51260; 7 hits in 700 CRISPR screens.
DR ChiTaRS; PBDC1; human.
DR GenomeRNAi; 51260; -.
DR Pharos; Q9BVG4; Tdark.
DR PRO; PR:Q9BVG4; -.
DR Proteomes; UP000005640; Chromosome X.
DR RNAct; Q9BVG4; protein.
DR Bgee; ENSG00000102390; Expressed in epithelial cell of pancreas and 182 other tissues.
DR ExpressionAtlas; Q9BVG4; baseline and differential.
DR Genevisible; Q9BVG4; HS.
DR Gene3D; 1.10.3560.10; -; 1.
DR InterPro; IPR023139; PBDC1-like_dom_sf.
DR InterPro; IPR008476; PBDC1_metazoa/fungi.
DR InterPro; IPR021148; Polysacc_synth_dom.
DR PANTHER; PTHR13410; PTHR13410; 1.
DR Pfam; PF04669; Polysacc_synt_4; 1.
PE 1: Evidence at protein level;
KW Phosphoprotein; Reference proteome.
FT CHAIN 1..233
FT /note="Protein PBDC1"
FT /id="PRO_0000254105"
FT REGION 167..233
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 169..233
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 126
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17525332"
FT MOD_RES 181
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 197
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18318008,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
SQ SEQUENCE 233 AA; 26057 MW; 31FD39EC70B9A9C7 CRC64;
MAATSGTDEP VSGELVSVAH ALSLPAESYG NDPDIEMAWA MRAMQHAEVY YKLISSVDPQ
FLKLTKVDDQ IYSEFRKNFE TLRIDVLDPE ELKSESAKEK WRPFCLKFNG IVEDFNYGTL
LRLDCSQGYT EENTIFAPRI QFFAIEIARN REGYNKAVYI SVQDKEGEKG VNNGGEKRAD
SGEEENTKNG GEKGADSGEE KEEGINREDK TDKGGEKGKE ADKEINKSGE KAM
