PDC10_HUMAN
ID PDC10_HUMAN Reviewed; 212 AA.
AC Q9BUL8; A8K515; D3DNN5; O14811;
DT 11-OCT-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 165.
DE RecName: Full=Programmed cell death protein 10;
DE AltName: Full=Cerebral cavernous malformations 3 protein;
DE AltName: Full=TF-1 cell apoptosis-related protein 15;
GN Name=PDCD10; Synonyms=CCM3, TFAR15;
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], AND VARIANT ALA-102.
RA Wang Y.G., Liu H.T., Ma D.L., Zhang Y.M.;
RT "cDNA cloning and expression of an apoptosis-related gene, human TFAR-15
RT gene.";
RL Sci. China, Ser. C, Life Sci. 42:323-329(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16641997; DOI=10.1038/nature04728;
RA Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J.,
RA Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P.,
RA Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A.,
RA Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L.,
RA Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G.,
RA Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W.,
RA Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M.,
RA Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P.,
RA Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H.,
RA Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J.,
RA Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W.,
RA Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B.,
RA Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O.,
RA Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B.,
RA Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H.,
RA Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J.,
RA Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X.,
RA Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R.,
RA Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.;
RT "The DNA sequence, annotation and analysis of human chromosome 3.";
RL Nature 440:1194-1198(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Skin, and Urinary bladder;
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 PROTEIN SEQUENCE OF 36-45 AND 117-124, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC TISSUE=Platelet;
RA Bienvenut W.V., Claeys D.;
RL Submitted (NOV-2005) to UniProtKB.
RN [8]
RP FUNCTION, TISSUE SPECIFICITY, AND INVOLVEMENT IN CCM3.
RX PubMed=15543491; DOI=10.1086/426952;
RA Bergametti F., Denier C., Labauge P., Arnoult M., Boetto S., Clanet M.,
RA Coubes P., Echenne B., Ibrahim R., Irthum B., Jacquet G., Lonjon M.,
RA Moreau J.J., Neau J.P., Parker F., Tremoulet M., Tournier-Lasserve E.;
RT "Mutations within the programmed cell death 10 gene cause cerebral
RT cavernous malformations.";
RL Am. J. Hum. Genet. 76:42-51(2005).
RN [9]
RP INTERACTION WITH STK26, FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=17360971; DOI=10.1091/mbc.e06-07-0608;
RA Ma X., Zhao H., Shan J., Long F., Chen Y., Chen Y., Zhang Y., Han X.,
RA Ma D.;
RT "PDCD10 interacts with Ste20-related kinase MST4 to promote cell growth and
RT transformation via modulation of the ERK pathway.";
RL Mol. Biol. Cell 18:1965-1978(2007).
RN [10]
RP INTERACTION WITH CCM2; STK25 AND STK26, AND IDENTIFICATION IN A COMPLEX
RP WITH KRIT1 AND CCM2.
RX PubMed=19370760; DOI=10.1002/humu.20996;
RA Voss K., Stahl S., Hogan B.M., Reinders J., Schleider E.,
RA Schulte-Merker S., Felbor U.;
RT "Functional analyses of human and zebrafish 18-amino acid in-frame deletion
RT pave the way for domain mapping of the cerebral cavernous malformation 3
RT protein.";
RL Hum. Mutat. 30:1003-1011(2009).
RN [11]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-179, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [12]
RP FUNCTION, INTERACTION WITH GOLGA2; STK24; STK25 AND STK26, AND SUBCELLULAR
RP LOCATION.
RX PubMed=20332113; DOI=10.1242/jcs.061341;
RA Fidalgo M., Fraile M., Pires A., Force T., Pombo C., Zalvide J.;
RT "CCM3/PDCD10 stabilizes GCKIII proteins to promote Golgi assembly and cell
RT orientation.";
RL J. Cell Sci. 123:1274-1284(2010).
RN [13]
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 [14]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [15]
RP FUNCTION, AND INTERACTION WITH RIPOR1; STK24 AND STK26.
RX PubMed=27807006; DOI=10.1242/jcs.198614;
RA Mardakheh F.K., Self A., Marshall C.J.;
RT "RHO binding to FAM65A regulates Golgi reorientation during cell
RT migration.";
RL J. Cell Sci. 129:4466-4479(2016).
RN [16]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-186, 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).
RN [17]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS), SUBUNIT, INTERACTION WITH CCM2 AND
RP PXN, SUBCELLULAR LOCATION, AND MUTAGENESIS OF LYS-132; ALA-135; LYS-139;
RP LYS-172; SER-175 AND LYS-179.
RX PubMed=20489202; DOI=10.1074/jbc.m110.128470;
RA Li X., Zhang R., Zhang H., He Y., Ji W., Min W., Boggon T.J.;
RT "Crystal structure of CCM3, a cerebral cavernous malformation protein
RT critical for vascular integrity.";
RL J. Biol. Chem. 285:24099-24107(2010).
CC -!- FUNCTION: Promotes cell proliferation. Modulates apoptotic pathways.
CC Increases mitogen-activated protein kinase activity and STK26 activity
CC (PubMed:27807006). Important for cell migration, and for normal
CC structure and assembly of the Golgi complex (PubMed:27807006).
CC Important for KDR/VEGFR2 signaling. Increases the stability of
CC KDR/VEGFR2 and prevents its breakdown. Required for normal
CC cardiovascular development. Required for normal angiogenesis,
CC vasculogenesis and hematopoiesis during embryonic development (By
CC similarity). {ECO:0000250|UniProtKB:Q8VE70,
CC ECO:0000269|PubMed:15543491, ECO:0000269|PubMed:17360971,
CC ECO:0000269|PubMed:20332113, ECO:0000269|PubMed:27807006}.
CC -!- SUBUNIT: Homodimer (PubMed:20489202). Interacts (via C-terminus) with
CC CCM2 (PubMed:17360971, PubMed:20489202). Interacts (via C-terminus)
CC with PXN (PubMed:20489202). Interacts (via N-terminus) with STK25
CC (PubMed:17360971, PubMed:20332113). Interacts (via N-terminus) with
CC STK26 (PubMed:17360971, PubMed:20332113, PubMed:27807006). Interacts
CC (via N-terminus) with STK24 (PubMed:20332113, PubMed:27807006).
CC Interacts with GOLGA2 (PubMed:20332113). Identified in a complex with
CC KRIT1 and CCM2. Interacts with KDR/VEGFR2. Interaction with KDR/VEGFR2
CC is enhanced by stimulation with VEGFA (By similarity). Interacts with
CC RIPOR1 (via C-terminus); this interaction is required for the
CC association of RIPOR1 with either STK24 and STK26 kinases and occurs in
CC a Rho-independent manner (PubMed:27807006). {ECO:0000250,
CC ECO:0000269|PubMed:17360971, ECO:0000269|PubMed:20332113,
CC ECO:0000269|PubMed:20489202, ECO:0000269|PubMed:27807006}.
CC -!- INTERACTION:
CC Q9BUL8; Q8IY42: C4orf19; NbExp=8; IntAct=EBI-740195, EBI-10216552;
CC Q9BUL8; Q9BSQ5: CCM2; NbExp=5; IntAct=EBI-740195, EBI-1573056;
CC Q9BUL8; Q9BPY3: FAM118B; NbExp=3; IntAct=EBI-740195, EBI-726822;
CC Q9BUL8; Q9Y285: FARSA; NbExp=3; IntAct=EBI-740195, EBI-725361;
CC Q9BUL8; O94915-2: FRYL; NbExp=3; IntAct=EBI-740195, EBI-12023420;
CC Q9BUL8; Q9UPX6: MINAR1; NbExp=3; IntAct=EBI-740195, EBI-11977115;
CC Q9BUL8; Q499L9: MST4; NbExp=5; IntAct=EBI-740195, EBI-6137569;
CC Q9BUL8; Q5SXH7-1: PLEKHS1; NbExp=3; IntAct=EBI-740195, EBI-26412802;
CC Q9BUL8; Q86WR7-2: PROSER2; NbExp=3; IntAct=EBI-740195, EBI-13089670;
CC Q9BUL8; Q12923: PTPN13; NbExp=3; IntAct=EBI-740195, EBI-355227;
CC Q9BUL8; Q9Y6E0: STK24; NbExp=11; IntAct=EBI-740195, EBI-740175;
CC Q9BUL8; Q9Y6E0-2: STK24; NbExp=9; IntAct=EBI-740195, EBI-10299018;
CC Q9BUL8; O00506: STK25; NbExp=30; IntAct=EBI-740195, EBI-618295;
CC Q9BUL8; Q9P289: STK26; NbExp=8; IntAct=EBI-740195, EBI-618239;
CC Q9BUL8; Q9P289-1: STK26; NbExp=10; IntAct=EBI-740195, EBI-15996971;
CC Q9BUL8; O43815: STRN; NbExp=5; IntAct=EBI-740195, EBI-1046642;
CC Q9BUL8; O43815-2: STRN; NbExp=3; IntAct=EBI-740195, EBI-1266294;
CC Q9BUL8; Q96BA2; NbExp=5; IntAct=EBI-740195, EBI-10282278;
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Golgi apparatus membrane; Peripheral
CC membrane protein; Cytoplasmic side. Cell membrane; Peripheral membrane
CC protein; Cytoplasmic side. Note=Partially co-localizes with endogenous
CC PXN at the leading edges of migrating cells.
CC -!- TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:15543491}.
CC -!- DISEASE: Cerebral cavernous malformations 3 (CCM3) [MIM:603285]: A form
CC of cerebral cavernous malformations, a congenital vascular anomaly of
CC the central nervous system that can result in hemorrhagic stroke,
CC seizures, recurrent headaches, and focal neurologic deficits. The
CC lesions are characterized by grossly enlarged blood vessels consisting
CC of a single layer of endothelium and without any intervening neural
CC tissue, ranging in diameter from a few millimeters to several
CC centimeters. CCM3 inheritance is autosomal dominant.
CC {ECO:0000269|PubMed:15543491}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the PDCD10 family. {ECO:0000305}.
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DR EMBL; AF022385; AAB72225.1; -; mRNA.
DR EMBL; CR457107; CAG33388.1; -; mRNA.
DR EMBL; AK291130; BAF83819.1; -; mRNA.
DR EMBL; AC079822; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471052; EAW78574.1; -; Genomic_DNA.
DR EMBL; CH471052; EAW78575.1; -; Genomic_DNA.
DR EMBL; CH471052; EAW78576.1; -; Genomic_DNA.
DR EMBL; CH471052; EAW78577.1; -; Genomic_DNA.
DR EMBL; CH471052; EAW78578.1; -; Genomic_DNA.
DR EMBL; CH471052; EAW78580.1; -; Genomic_DNA.
DR EMBL; CH471052; EAW78581.1; -; Genomic_DNA.
DR EMBL; BC002506; AAH02506.1; -; mRNA.
DR EMBL; BC016353; AAH16353.1; -; mRNA.
DR CCDS; CCDS3202.1; -.
DR RefSeq; NP_009148.2; NM_007217.3.
DR RefSeq; NP_665858.1; NM_145859.1.
DR RefSeq; NP_665859.1; NM_145860.1.
DR RefSeq; XP_005247143.1; XM_005247086.4.
DR RefSeq; XP_005247144.1; XM_005247087.4.
DR RefSeq; XP_005247145.1; XM_005247088.3.
DR RefSeq; XP_006713548.1; XM_006713485.3.
DR RefSeq; XP_011510670.1; XM_011512368.2.
DR RefSeq; XP_011510671.1; XM_011512369.2.
DR RefSeq; XP_016861133.1; XM_017005644.1.
DR PDB; 3AJM; X-ray; 2.30 A; A/B=8-212.
DR PDB; 3L8I; X-ray; 2.50 A; A/B/C/D=1-212.
DR PDB; 3L8J; X-ray; 3.05 A; A=14-212.
DR PDB; 3RQE; X-ray; 2.80 A; A/B/C/D=1-212.
DR PDB; 3RQF; X-ray; 2.70 A; A/B/C/D=1-212.
DR PDB; 3RQG; X-ray; 2.50 A; A/B/C/D=1-212.
DR PDB; 3W8H; X-ray; 2.43 A; A=8-212.
DR PDB; 3W8I; X-ray; 2.40 A; A=8-212.
DR PDB; 4GEH; X-ray; 1.95 A; A/C=9-212.
DR PDB; 4TVQ; X-ray; 2.80 A; A/B/C/D=1-212.
DR PDBsum; 3AJM; -.
DR PDBsum; 3L8I; -.
DR PDBsum; 3L8J; -.
DR PDBsum; 3RQE; -.
DR PDBsum; 3RQF; -.
DR PDBsum; 3RQG; -.
DR PDBsum; 3W8H; -.
DR PDBsum; 3W8I; -.
DR PDBsum; 4GEH; -.
DR PDBsum; 4TVQ; -.
DR AlphaFoldDB; Q9BUL8; -.
DR SMR; Q9BUL8; -.
DR BioGRID; 116400; 102.
DR ComplexPortal; CPX-984; CCM endothelial permeability complex.
DR DIP; DIP-40607N; -.
DR IntAct; Q9BUL8; 48.
DR MINT; Q9BUL8; -.
DR STRING; 9606.ENSP00000376506; -.
DR iPTMnet; Q9BUL8; -.
DR MetOSite; Q9BUL8; -.
DR PhosphoSitePlus; Q9BUL8; -.
DR BioMuta; PDCD10; -.
DR DMDM; 74733232; -.
DR OGP; Q9BUL8; -.
DR EPD; Q9BUL8; -.
DR jPOST; Q9BUL8; -.
DR MassIVE; Q9BUL8; -.
DR MaxQB; Q9BUL8; -.
DR PaxDb; Q9BUL8; -.
DR PeptideAtlas; Q9BUL8; -.
DR PRIDE; Q9BUL8; -.
DR ProteomicsDB; 79108; -.
DR TopDownProteomics; Q9BUL8; -.
DR Antibodypedia; 18593; 278 antibodies from 31 providers.
DR DNASU; 11235; -.
DR Ensembl; ENST00000392750.7; ENSP00000376506.2; ENSG00000114209.15.
DR Ensembl; ENST00000461494.5; ENSP00000420021.1; ENSG00000114209.15.
DR Ensembl; ENST00000470131.5; ENSP00000417202.1; ENSG00000114209.15.
DR Ensembl; ENST00000473645.6; ENSP00000418317.2; ENSG00000114209.15.
DR Ensembl; ENST00000497056.6; ENSP00000420553.2; ENSG00000114209.15.
DR GeneID; 11235; -.
DR KEGG; hsa:11235; -.
DR MANE-Select; ENST00000392750.7; ENSP00000376506.2; NM_007217.4; NP_009148.2.
DR UCSC; uc003fex.5; human.
DR CTD; 11235; -.
DR DisGeNET; 11235; -.
DR GeneCards; PDCD10; -.
DR GeneReviews; PDCD10; -.
DR HGNC; HGNC:8761; PDCD10.
DR HPA; ENSG00000114209; Low tissue specificity.
DR MalaCards; PDCD10; -.
DR MIM; 603285; phenotype.
DR MIM; 609118; gene.
DR neXtProt; NX_Q9BUL8; -.
DR OpenTargets; ENSG00000114209; -.
DR Orphanet; 221061; Familial cerebral cavernous malformation.
DR PharmGKB; PA33111; -.
DR VEuPathDB; HostDB:ENSG00000114209; -.
DR eggNOG; KOG4025; Eukaryota.
DR GeneTree; ENSGT00390000017913; -.
DR InParanoid; Q9BUL8; -.
DR OMA; HVVLFPI; -.
DR OrthoDB; 1507394at2759; -.
DR PhylomeDB; Q9BUL8; -.
DR TreeFam; TF105802; -.
DR PathwayCommons; Q9BUL8; -.
DR SignaLink; Q9BUL8; -.
DR SIGNOR; Q9BUL8; -.
DR BioGRID-ORCS; 11235; 69 hits in 1090 CRISPR screens.
DR ChiTaRS; PDCD10; human.
DR EvolutionaryTrace; Q9BUL8; -.
DR GeneWiki; PDCD10; -.
DR GenomeRNAi; 11235; -.
DR Pharos; Q9BUL8; Tbio.
DR PRO; PR:Q9BUL8; -.
DR Proteomes; UP000005640; Chromosome 3.
DR RNAct; Q9BUL8; protein.
DR Bgee; ENSG00000114209; Expressed in jejunal mucosa and 212 other tissues.
DR ExpressionAtlas; Q9BUL8; baseline and differential.
DR Genevisible; Q9BUL8; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0090443; C:FAR/SIN/STRIPAK complex; IBA:GO_Central.
DR GO; GO:0005794; C:Golgi apparatus; IDA:UniProtKB.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0042803; F:protein homodimerization activity; IPI:UniProtKB.
DR GO; GO:0019901; F:protein kinase binding; IPI:UniProtKB.
DR GO; GO:0047485; F:protein N-terminus binding; IPI:UniProtKB.
DR GO; GO:0001525; P:angiogenesis; IEA:UniProtKB-KW.
DR GO; GO:1990830; P:cellular response to leukemia inhibitory factor; IEA:Ensembl.
DR GO; GO:0003158; P:endothelium development; IC:ComplexPortal.
DR GO; GO:0051683; P:establishment of Golgi localization; IMP:UniProtKB.
DR GO; GO:0090168; P:Golgi reassembly; IMP:UniProtKB.
DR GO; GO:0036481; P:intrinsic apoptotic signaling pathway in response to hydrogen peroxide; IGI:UniProtKB.
DR GO; GO:0043066; P:negative regulation of apoptotic process; IDA:UniProtKB.
DR GO; GO:1903588; P:negative regulation of blood vessel endothelial cell proliferation involved in sprouting angiogenesis; IMP:UniProtKB.
DR GO; GO:0090051; P:negative regulation of cell migration involved in sprouting angiogenesis; IMP:UniProtKB.
DR GO; GO:0010629; P:negative regulation of gene expression; IMP:UniProtKB.
DR GO; GO:0030335; P:positive regulation of cell migration; IDA:UniProtKB.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; IDA:UniProtKB.
DR GO; GO:0010628; P:positive regulation of gene expression; IMP:UniProtKB.
DR GO; GO:0090316; P:positive regulation of intracellular protein transport; IMP:UniProtKB.
DR GO; GO:0043406; P:positive regulation of MAP kinase activity; IDA:UniProtKB.
DR GO; GO:0045747; P:positive regulation of Notch signaling pathway; IMP:UniProtKB.
DR GO; GO:0033138; P:positive regulation of peptidyl-serine phosphorylation; IMP:UniProtKB.
DR GO; GO:0071902; P:positive regulation of protein serine/threonine kinase activity; IMP:UniProtKB.
DR GO; GO:0032874; P:positive regulation of stress-activated MAPK cascade; IDA:UniProtKB.
DR GO; GO:0050821; P:protein stabilization; IMP:UniProtKB.
DR GO; GO:0045765; P:regulation of angiogenesis; IC:ComplexPortal.
DR GO; GO:1903358; P:regulation of Golgi organization; IBA:GO_Central.
DR GO; GO:0042542; P:response to hydrogen peroxide; IDA:UniProtKB.
DR GO; GO:0044319; P:wound healing, spreading of cells; IMP:UniProtKB.
DR Gene3D; 1.10.12.70; -; 1.
DR InterPro; IPR046409; PDC10_dimerisation_sf.
DR InterPro; IPR009652; PDCD10.
DR PANTHER; PTHR13250; PTHR13250; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Angiogenesis; Apoptosis; Cell membrane;
KW Cytoplasm; Direct protein sequencing; Golgi apparatus; Isopeptide bond;
KW Membrane; Reference proteome; Ubl conjugation.
FT CHAIN 1..212
FT /note="Programmed cell death protein 10"
FT /id="PRO_0000187562"
FT MOD_RES 179
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT CROSSLNK 186
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VARIANT 102
FT /note="D -> A (in dbSNP:rs1129087)"
FT /evidence="ECO:0000269|Ref.1"
FT /id="VAR_023578"
FT MUTAGEN 132
FT /note="K->D: Loss of interaction with CCM2 and PXN; when
FT associated with D-139; D-172 and D-179."
FT /evidence="ECO:0000269|PubMed:20489202"
FT MUTAGEN 135
FT /note="A->D: Loss of interaction with CCM2."
FT /evidence="ECO:0000269|PubMed:20489202"
FT MUTAGEN 139
FT /note="K->D: Loss of interaction with CCM2 and PXN; when
FT associated with D-132; D-172 and D-179."
FT /evidence="ECO:0000269|PubMed:20489202"
FT MUTAGEN 172
FT /note="K->D: Loss of interaction with CCM2 and PXN; when
FT associated with D-132; D-139 and D-179."
FT /evidence="ECO:0000269|PubMed:20489202"
FT MUTAGEN 175
FT /note="S->D: Loss of interaction with CCM2."
FT /evidence="ECO:0000269|PubMed:20489202"
FT MUTAGEN 179
FT /note="K->D: Loss of interaction with CCM2 and PXN; when
FT associated with D-132; D-139 and D-172."
FT /evidence="ECO:0000269|PubMed:20489202"
FT HELIX 5..9
FT /evidence="ECO:0007829|PDB:3L8I"
FT HELIX 11..14
FT /evidence="ECO:0007829|PDB:3L8I"
FT HELIX 17..19
FT /evidence="ECO:0007829|PDB:4GEH"
FT HELIX 20..24
FT /evidence="ECO:0007829|PDB:4GEH"
FT HELIX 26..34
FT /evidence="ECO:0007829|PDB:4GEH"
FT HELIX 38..54
FT /evidence="ECO:0007829|PDB:4GEH"
FT HELIX 58..69
FT /evidence="ECO:0007829|PDB:4GEH"
FT HELIX 76..82
FT /evidence="ECO:0007829|PDB:4GEH"
FT TURN 83..85
FT /evidence="ECO:0007829|PDB:4GEH"
FT HELIX 88..91
FT /evidence="ECO:0007829|PDB:4GEH"
FT HELIX 98..115
FT /evidence="ECO:0007829|PDB:4GEH"
FT HELIX 117..120
FT /evidence="ECO:0007829|PDB:4GEH"
FT STRAND 121..123
FT /evidence="ECO:0007829|PDB:4TVQ"
FT HELIX 124..151
FT /evidence="ECO:0007829|PDB:4GEH"
FT TURN 152..156
FT /evidence="ECO:0007829|PDB:4GEH"
FT HELIX 157..184
FT /evidence="ECO:0007829|PDB:4GEH"
FT HELIX 187..208
FT /evidence="ECO:0007829|PDB:4GEH"
SQ SEQUENCE 212 AA; 24702 MW; 5AA613F71FAAEF56 CRC64;
MRMTMEEMKN EAETTSMVSM PLYAVMYPVF NELERVNLSA AQTLRAAFIK AEKENPGLTQ
DIIMKILEKK SVEVNFTESL LRMAADDVEE YMIERPEPEF QDLNEKARAL KQILSKIPDE
INDRVRFLQT IKDIASAIKE LLDTVNNVFK KYQYQNRRAL EHQKKEFVKY SKSFSDTLKT
YFKDGKAINV FVSANRLIHQ TNLILQTFKT VA
