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 24-JAN-2024, entry version 173. 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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; 111. DR ComplexPortal; CPX-984; CCM endothelial permeability complex. DR DIP; DIP-40607N; -. DR IntAct; Q9BUL8; 49. 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; 9606-ENSP00000376506; -. DR PeptideAtlas; Q9BUL8; -. DR ProteomicsDB; 79108; -. DR Pumba; Q9BUL8; -. DR TopDownProteomics; Q9BUL8; -. DR Antibodypedia; 18593; 301 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 AGR; HGNC:8761; -. 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; 3801237at2759; -. DR PhylomeDB; Q9BUL8; -. DR TreeFam; TF105802; -. DR PathwayCommons; Q9BUL8; -. DR SignaLink; Q9BUL8; -. DR SIGNOR; Q9BUL8; -. DR BioGRID-ORCS; 11235; 82 hits in 1176 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 214 other cell types or tissues. DR ExpressionAtlas; Q9BUL8; baseline and differential. 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; IBA:GO_Central. 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; NAS: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; NAS:ComplexPortal. DR GO; GO:1903358; P:regulation of Golgi organization; IBA:GO_Central. DR GO; GO:0031098; P:stress-activated protein kinase signaling cascade; IMP:UniProtKB. DR GO; GO:0044319; P:wound healing, spreading of cells; IMP:UniProtKB. DR Gene3D; 1.10.12.70; -; 1. DR Gene3D; 1.20.120.330; Nucleotidyltransferases domain 2; 1. DR InterPro; IPR046409; PDC10_dimerisation_sf. DR InterPro; IPR009652; PDCD10. DR InterPro; IPR048288; PDCD10_N. DR PANTHER; PTHR13250:SF1; PROGRAMMED CELL DEATH PROTEIN 10; 1. DR PANTHER; PTHR13250; TF-1 CELL APOPTOSIS RELATED PROTEIN-15; 1. DR Pfam; PF06840; PDC10_C; 1. DR Pfam; PF20929; PDCD10_N; 1. DR Genevisible; Q9BUL8; HS. 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 //