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Programmed cell death protein 10 (Cerebral cavernous malformations 3 protein) (TF-1 cell apoptosis-related protein 15)

 PDC10_HUMAN             Reviewed;         212 AA.
Q9BUL8; A8K515; D3DNN5; O14811;
11-OCT-2005, integrated into UniProtKB/Swiss-Prot.
01-JUN-2001, sequence version 1.
25-OCT-2017, entry version 138.
RecName: Full=Programmed cell death protein 10;
AltName: Full=Cerebral cavernous malformations 3 protein;
AltName: Full=TF-1 cell apoptosis-related protein 15;
Name=PDCD10; Synonyms=CCM3, TFAR15;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT ALA-102.
Wang Y.G., Liu H.T., Ma D.L., Zhang Y.M.;
"cDNA cloning and expression of an apoptosis-related gene, human TFAR-
15 gene.";
Sci. China, Ser. C, Life Sci. 42:323-329(1999).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
"Cloning of human full open reading frames in Gateway(TM) system entry
vector (pDONR201).";
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16641997; DOI=10.1038/nature04728;
Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R.,
Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R.,
Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V.,
Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R.,
Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Morgan M.B.,
Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Wei S.,
Wheeler D.A., Wright M.W., Worley K.C., Yuan Y., Zhang Z., Adams C.Q.,
Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z.,
Clendenning J., Clerc-Blankenburg K.P., Chen R., Chen Z., Davis C.,
Delgado O., Dinh H.H., Dong W., Draper H., Ernst S., Fu G.,
Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., Hao B.,
Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., Jackson L.R.,
Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., Liu J.,
Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Palmeiri A.,
Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B.,
Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H.,
Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J.,
Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J.,
Zhang X., Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H.,
Reinhardt R., Naylor S.L., Yang H., Olson M., Weinstock G.,
Gibbs R.A.;
"The DNA sequence, annotation and analysis of human chromosome 3.";
Nature 440:1194-1198(2006).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Skin, and Urinary bladder;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[7]
PROTEIN SEQUENCE OF 36-45 AND 117-124, AND IDENTIFICATION BY MASS
SPECTROMETRY.
TISSUE=Platelet;
Bienvenut W.V., Claeys D.;
Submitted (NOV-2005) to UniProtKB.
[8]
FUNCTION, TISSUE SPECIFICITY, AND INVOLVEMENT IN CCM3.
PubMed=15543491; DOI=10.1086/426952;
Bergametti F., Denier C., Labauge P., Arnoult M., Boetto S.,
Clanet M., Coubes P., Echenne B., Ibrahim R., Irthum B., Jacquet G.,
Lonjon M., Moreau J.J., Neau J.P., Parker F., Tremoulet M.,
Tournier-Lasserve E.;
"Mutations within the programmed cell death 10 gene cause cerebral
cavernous malformations.";
Am. J. Hum. Genet. 76:42-51(2005).
[9]
INTERACTION WITH STK26, FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=17360971; DOI=10.1091/mbc.E06-07-0608;
Ma X., Zhao H., Shan J., Long F., Chen Y., Chen Y., Zhang Y., Han X.,
Ma D.;
"PDCD10 interacts with Ste20-related kinase MST4 to promote cell
growth and transformation via modulation of the ERK pathway.";
Mol. Biol. Cell 18:1965-1978(2007).
[10]
INTERACTION WITH CCM2; STK25 AND STK26, AND IDENTIFICATION IN A
COMPLEX WITH KRIT1 AND CCM2.
PubMed=19370760; DOI=10.1002/humu.20996;
Voss K., Stahl S., Hogan B.M., Reinders J., Schleider E.,
Schulte-Merker S., Felbor U.;
"Functional analyses of human and zebrafish 18-amino acid in-frame
deletion pave the way for domain mapping of the cerebral cavernous
malformation 3 protein.";
Hum. Mutat. 30:1003-1011(2009).
[11]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-179, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19608861; DOI=10.1126/science.1175371;
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
Walther T.C., Olsen J.V., Mann M.;
"Lysine acetylation targets protein complexes and co-regulates major
cellular functions.";
Science 325:834-840(2009).
[12]
FUNCTION, INTERACTION WITH GOLGA2; STK24; STK25 AND STK26, AND
SUBCELLULAR LOCATION.
PubMed=20332113; DOI=10.1242/jcs.061341;
Fidalgo M., Fraile M., Pires A., Force T., Pombo C., Zalvide J.;
"CCM3/PDCD10 stabilizes GCKIII proteins to promote Golgi assembly and
cell orientation.";
J. Cell Sci. 123:1274-1284(2010).
[13]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[14]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25944712; DOI=10.1002/pmic.201400617;
Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M.,
Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
"N-terminome analysis of the human mitochondrial proteome.";
Proteomics 15:2519-2524(2015).
[15]
FUNCTION, AND INTERACTION WITH RIPOR1; STK24 AND STK26.
PubMed=27807006; DOI=10.1242/jcs.198614;
Mardakheh F.K., Self A., Marshall C.J.;
"RHO binding to FAM65A regulates Golgi reorientation during cell
migration.";
J. Cell Sci. 129:4466-4479(2016).
[16]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-186, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=28112733; DOI=10.1038/nsmb.3366;
Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
Nielsen M.L.;
"Site-specific mapping of the human SUMO proteome reveals co-
modification with phosphorylation.";
Nat. Struct. Mol. Biol. 24:325-336(2017).
[17]
X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS), SUBUNIT, INTERACTION WITH CCM2
AND PXN, SUBCELLULAR LOCATION, AND MUTAGENESIS OF LYS-132; ALA-135;
LYS-139; LYS-172; SER-175 AND LYS-179.
PubMed=20489202; DOI=10.1074/jbc.M110.128470;
Li X., Zhang R., Zhang H., He Y., Ji W., Min W., Boggon T.J.;
"Crystal structure of CCM3, a cerebral cavernous malformation protein
critical for vascular integrity.";
J. Biol. Chem. 285:24099-24107(2010).
-!- FUNCTION: Promotes cell proliferation. Modulates apoptotic
pathways. Increases mitogen-activated protein kinase activity and
STK26 activity (PubMed:27807006). Important for cell migration,
and for normal structure and assembly of the Golgi complex
(PubMed:27807006). Important for KDR/VEGFR2 signaling. Increases
the stability of KDR/VEGFR2 and prevents its breakdown. Required
for normal cardiovascular development. Required for normal
angiogenesis, vasculogenesis and hematopoiesis during embryonic
development (By similarity). {ECO:0000250|UniProtKB:Q8VE70,
ECO:0000269|PubMed:15543491, ECO:0000269|PubMed:17360971,
ECO:0000269|PubMed:20332113, ECO:0000269|PubMed:27807006}.
-!- SUBUNIT: Homodimer (PubMed:20489202). Interacts (via C-terminus)
with CCM2 (PubMed:17360971, PubMed:20489202). Interacts (via C-
terminus) with PXN (PubMed:20489202). Interacts (via N-terminus)
with STK25 (PubMed:17360971, PubMed:20332113). Interacts (via N-
terminus) with STK26 (PubMed:17360971, PubMed:20332113,
PubMed:27807006). Interacts (via N-terminus) with STK24
(PubMed:20332113, PubMed:27807006). Interacts with GOLGA2
(PubMed:20332113). Identified in a complex with KRIT1 and CCM2.
Interacts with KDR/VEGFR2. Interaction with KDR/VEGFR2 is enhanced
by stimulation with VEGFA (By similarity). Interacts with RIPOR1
(via C-terminus); this interaction is required for the association
of RIPOR1 with either STK24 and STK26 kinases and occurs in a Rho-
independent manner (PubMed:27807006). {ECO:0000250,
ECO:0000269|PubMed:17360971, ECO:0000269|PubMed:20332113,
ECO:0000269|PubMed:20489202, ECO:0000269|PubMed:27807006}.
-!- INTERACTION:
Q96BA2:-; NbExp=5; IntAct=EBI-740195, EBI-10282278;
Q8IY42:C4orf19; NbExp=5; IntAct=EBI-740195, EBI-10216552;
Q9BSQ5:CCM2; NbExp=5; IntAct=EBI-740195, EBI-1573056;
Q499L9:MST4; NbExp=5; IntAct=EBI-740195, EBI-6137569;
Q12923:PTPN13; NbExp=3; IntAct=EBI-740195, EBI-355227;
Q9Y6E0:STK24; NbExp=9; IntAct=EBI-740195, EBI-740175;
Q9Y6E0-2:STK24; NbExp=5; IntAct=EBI-740195, EBI-10299018;
O00506:STK25; NbExp=23; IntAct=EBI-740195, EBI-618295;
Q9P289:STK26; NbExp=9; IntAct=EBI-740195, EBI-618239;
Q9P289-1:STK26; NbExp=10; IntAct=EBI-740195, EBI-15996971;
O43815:STRN; NbExp=4; IntAct=EBI-740195, EBI-1046642;
-!- SUBCELLULAR LOCATION: Cytoplasm. Golgi apparatus membrane;
Peripheral membrane protein; Cytoplasmic side. Cell membrane;
Peripheral membrane protein; Cytoplasmic side. Note=Partially co-
localizes with endogenous PXN at the leading edges of migrating
cells.
-!- TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:15543491}.
-!- DISEASE: Cerebral cavernous malformations 3 (CCM3) [MIM:603285]: A
congenital vascular anomaly of the central nervous system that can
result in hemorrhagic stroke, seizures, recurrent headaches, and
focal neurologic deficits. The lesions are characterized by
grossly enlarged blood vessels consisting of a single layer of
endothelium and without any intervening neural tissue, ranging in
diameter from a few millimeters to several centimeters.
{ECO:0000269|PubMed:15543491}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- SIMILARITY: Belongs to the PDCD10 family. {ECO:0000305}.
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EMBL; AF022385; AAB72225.1; -; mRNA.
EMBL; CR457107; CAG33388.1; -; mRNA.
EMBL; AK291130; BAF83819.1; -; mRNA.
EMBL; AC079822; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471052; EAW78574.1; -; Genomic_DNA.
EMBL; CH471052; EAW78575.1; -; Genomic_DNA.
EMBL; CH471052; EAW78576.1; -; Genomic_DNA.
EMBL; CH471052; EAW78577.1; -; Genomic_DNA.
EMBL; CH471052; EAW78578.1; -; Genomic_DNA.
EMBL; CH471052; EAW78580.1; -; Genomic_DNA.
EMBL; CH471052; EAW78581.1; -; Genomic_DNA.
EMBL; BC002506; AAH02506.1; -; mRNA.
EMBL; BC016353; AAH16353.1; -; mRNA.
CCDS; CCDS3202.1; -.
RefSeq; NP_009148.2; NM_007217.3.
RefSeq; NP_665858.1; NM_145859.1.
RefSeq; NP_665859.1; NM_145860.1.
RefSeq; XP_005247143.1; XM_005247086.4.
RefSeq; XP_005247144.1; XM_005247087.4.
RefSeq; XP_005247145.1; XM_005247088.3.
RefSeq; XP_006713548.1; XM_006713485.3.
RefSeq; XP_011510670.1; XM_011512368.2.
RefSeq; XP_011510671.1; XM_011512369.2.
RefSeq; XP_016861133.1; XM_017005644.1.
UniGene; Hs.478150; -.
PDB; 3AJM; X-ray; 2.30 A; A/B=8-212.
PDB; 3L8I; X-ray; 2.50 A; A/B/C/D=1-212.
PDB; 3L8J; X-ray; 3.05 A; A=14-212.
PDB; 3RQE; X-ray; 2.80 A; A/B/C/D=1-212.
PDB; 3RQF; X-ray; 2.70 A; A/B/C/D=1-212.
PDB; 3RQG; X-ray; 2.50 A; A/B/C/D=1-212.
PDB; 3W8H; X-ray; 2.43 A; A=8-212.
PDB; 3W8I; X-ray; 2.40 A; A=8-212.
PDB; 4GEH; X-ray; 1.95 A; A/C=9-212.
PDB; 4TVQ; X-ray; 2.80 A; A/B/C/D=1-212.
PDBsum; 3AJM; -.
PDBsum; 3L8I; -.
PDBsum; 3L8J; -.
PDBsum; 3RQE; -.
PDBsum; 3RQF; -.
PDBsum; 3RQG; -.
PDBsum; 3W8H; -.
PDBsum; 3W8I; -.
PDBsum; 4GEH; -.
PDBsum; 4TVQ; -.
ProteinModelPortal; Q9BUL8; -.
SMR; Q9BUL8; -.
BioGrid; 116400; 60.
DIP; DIP-40607N; -.
IntAct; Q9BUL8; 36.
MINT; MINT-5003501; -.
STRING; 9606.ENSP00000376506; -.
iPTMnet; Q9BUL8; -.
PhosphoSitePlus; Q9BUL8; -.
BioMuta; PDCD10; -.
DMDM; 74733232; -.
OGP; Q9BUL8; -.
EPD; Q9BUL8; -.
MaxQB; Q9BUL8; -.
PaxDb; Q9BUL8; -.
PeptideAtlas; Q9BUL8; -.
PRIDE; Q9BUL8; -.
TopDownProteomics; Q9BUL8; -.
DNASU; 11235; -.
Ensembl; ENST00000392750; ENSP00000376506; ENSG00000114209.
Ensembl; ENST00000461494; ENSP00000420021; ENSG00000114209.
Ensembl; ENST00000470131; ENSP00000417202; ENSG00000114209.
Ensembl; ENST00000473645; ENSP00000418317; ENSG00000114209.
Ensembl; ENST00000497056; ENSP00000420553; ENSG00000114209.
GeneID; 11235; -.
KEGG; hsa:11235; -.
UCSC; uc003fex.5; human.
CTD; 11235; -.
DisGeNET; 11235; -.
EuPathDB; HostDB:ENSG00000114209.14; -.
GeneCards; PDCD10; -.
GeneReviews; PDCD10; -.
HGNC; HGNC:8761; PDCD10.
HPA; HPA027095; -.
MalaCards; PDCD10; -.
MIM; 603285; phenotype.
MIM; 609118; gene.
neXtProt; NX_Q9BUL8; -.
OpenTargets; ENSG00000114209; -.
Orphanet; 221061; Hereditary cerebral cavernous malformation.
PharmGKB; PA33111; -.
eggNOG; KOG4025; Eukaryota.
eggNOG; ENOG410XTA6; LUCA.
GeneTree; ENSGT00390000017913; -.
HOGENOM; HOG000007888; -.
HOVERGEN; HBG052811; -.
InParanoid; Q9BUL8; -.
KO; K18269; -.
OMA; TMGDETP; -.
OrthoDB; EOG091G0JQQ; -.
PhylomeDB; Q9BUL8; -.
TreeFam; TF105802; -.
SIGNOR; Q9BUL8; -.
ChiTaRS; PDCD10; human.
EvolutionaryTrace; Q9BUL8; -.
GeneWiki; PDCD10; -.
GenomeRNAi; 11235; -.
PRO; PR:Q9BUL8; -.
Proteomes; UP000005640; Chromosome 3.
Bgee; ENSG00000114209; -.
CleanEx; HS_PDCD10; -.
ExpressionAtlas; Q9BUL8; baseline and differential.
Genevisible; Q9BUL8; HS.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0005829; C:cytosol; IDA:UniProtKB.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:0005794; C:Golgi apparatus; IDA:UniProtKB.
GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
GO; GO:0042803; F:protein homodimerization activity; IPI:UniProtKB.
GO; GO:0019901; F:protein kinase binding; IPI:UniProtKB.
GO; GO:0047485; F:protein N-terminus binding; IPI:UniProtKB.
GO; GO:0001525; P:angiogenesis; IEA:UniProtKB-KW.
GO; GO:1990830; P:cellular response to leukemia inhibitory factor; IEA:Ensembl.
GO; GO:0051683; P:establishment of Golgi localization; IMP:UniProtKB.
GO; GO:0090168; P:Golgi reassembly; IMP:UniProtKB.
GO; GO:0036481; P:intrinsic apoptotic signaling pathway in response to hydrogen peroxide; IGI:UniProtKB.
GO; GO:0043066; P:negative regulation of apoptotic process; IDA:UniProtKB.
GO; GO:1903588; P:negative regulation of blood vessel endothelial cell proliferation involved in sprouting angiogenesis; IMP:UniProtKB.
GO; GO:0090051; P:negative regulation of cell migration involved in sprouting angiogenesis; IMP:UniProtKB.
GO; GO:0010629; P:negative regulation of gene expression; IMP:UniProtKB.
GO; GO:0030335; P:positive regulation of cell migration; IDA:UniProtKB.
GO; GO:0008284; P:positive regulation of cell proliferation; IDA:UniProtKB.
GO; GO:0010628; P:positive regulation of gene expression; IMP:UniProtKB.
GO; GO:0090316; P:positive regulation of intracellular protein transport; IMP:UniProtKB.
GO; GO:0043406; P:positive regulation of MAP kinase activity; IDA:UniProtKB.
GO; GO:0045747; P:positive regulation of Notch signaling pathway; IMP:UniProtKB.
GO; GO:0033138; P:positive regulation of peptidyl-serine phosphorylation; IMP:UniProtKB.
GO; GO:0071902; P:positive regulation of protein serine/threonine kinase activity; IMP:UniProtKB.
GO; GO:0032874; P:positive regulation of stress-activated MAPK cascade; IDA:UniProtKB.
GO; GO:0050821; P:protein stabilization; IMP:UniProtKB.
GO; GO:0042542; P:response to hydrogen peroxide; IDA:UniProtKB.
GO; GO:0044319; P:wound healing, spreading of cells; IMP:UniProtKB.
InterPro; IPR009652; PDCD10.
PANTHER; PTHR13250; PTHR13250; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Angiogenesis; Apoptosis; Cell membrane;
Complete proteome; Cytoplasm; Direct protein sequencing;
Golgi apparatus; Isopeptide bond; Membrane; Polymorphism;
Reference proteome; Ubl conjugation.
CHAIN 1 212 Programmed cell death protein 10.
/FTId=PRO_0000187562.
MOD_RES 179 179 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
CROSSLNK 186 186 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
VARIANT 102 102 D -> A (in dbSNP:rs1129087).
{ECO:0000269|Ref.1}.
/FTId=VAR_023578.
MUTAGEN 132 132 K->D: Loss of interaction with CCM2 and
PXN; when associated with D-139; D-172
and D-179. {ECO:0000269|PubMed:20489202}.
MUTAGEN 135 135 A->D: Loss of interaction with CCM2.
{ECO:0000269|PubMed:20489202}.
MUTAGEN 139 139 K->D: Loss of interaction with CCM2 and
PXN; when associated with D-132; D-172
and D-179. {ECO:0000269|PubMed:20489202}.
MUTAGEN 172 172 K->D: Loss of interaction with CCM2 and
PXN; when associated with D-132; D-139
and D-179. {ECO:0000269|PubMed:20489202}.
MUTAGEN 175 175 S->D: Loss of interaction with CCM2.
{ECO:0000269|PubMed:20489202}.
MUTAGEN 179 179 K->D: Loss of interaction with CCM2 and
PXN; when associated with D-132; D-139
and D-172. {ECO:0000269|PubMed:20489202}.
HELIX 5 9 {ECO:0000244|PDB:3L8I}.
HELIX 11 14 {ECO:0000244|PDB:3L8I}.
HELIX 17 19 {ECO:0000244|PDB:4GEH}.
HELIX 20 24 {ECO:0000244|PDB:4GEH}.
HELIX 26 34 {ECO:0000244|PDB:4GEH}.
HELIX 38 54 {ECO:0000244|PDB:4GEH}.
HELIX 58 69 {ECO:0000244|PDB:4GEH}.
HELIX 76 82 {ECO:0000244|PDB:4GEH}.
TURN 83 85 {ECO:0000244|PDB:4GEH}.
HELIX 88 91 {ECO:0000244|PDB:4GEH}.
HELIX 98 115 {ECO:0000244|PDB:4GEH}.
HELIX 117 120 {ECO:0000244|PDB:4GEH}.
STRAND 121 123 {ECO:0000244|PDB:4TVQ}.
HELIX 124 151 {ECO:0000244|PDB:4GEH}.
TURN 152 156 {ECO:0000244|PDB:4GEH}.
HELIX 157 184 {ECO:0000244|PDB:4GEH}.
HELIX 187 208 {ECO:0000244|PDB:4GEH}.
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


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