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Protein

Programmed cell death protein 10

Gene

PDCD10

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Promotes cell proliferation. Modulates apoptotic pathways. Increases mitogen-activated protein kinase activity and STK26 activity. Important for cell migration, and for normal structure and assembly of the Golgi complex. 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).By similarity

GO - Molecular functioni

  1. protein homodimerization activity Source: UniProtKB
  2. protein kinase binding Source: UniProtKB
  3. protein N-terminus binding Source: UniProtKB

GO - Biological processi

  1. angiogenesis Source: UniProtKB-KW
  2. establishment of Golgi localization Source: UniProtKB
  3. Golgi reassembly Source: UniProtKB
  4. intrinsic apoptotic signaling pathway in response to hydrogen peroxide Source: UniProtKB
  5. negative regulation of apoptotic process Source: UniProtKB
  6. negative regulation of blood vessel endothelial cell proliferation involved in sprouting angiogenesis Source: UniProtKB
  7. negative regulation of cell migration involved in sprouting angiogenesis Source: UniProtKB
  8. negative regulation of gene expression Source: UniProtKB
  9. positive regulation of cell migration Source: UniProtKB
  10. positive regulation of cell proliferation Source: UniProtKB
  11. positive regulation of gene expression Source: UniProtKB
  12. positive regulation of MAP kinase activity Source: UniProtKB
  13. positive regulation of Notch signaling pathway Source: UniProtKB
  14. positive regulation of peptidyl-serine phosphorylation Source: UniProtKB
  15. positive regulation of protein serine/threonine kinase activity Source: UniProtKB
  16. positive regulation of stress-activated MAPK cascade Source: UniProtKB
  17. protein stabilization Source: UniProtKB
  18. response to hydrogen peroxide Source: UniProtKB
  19. wound healing, spreading of cells Source: UniProtKB
Complete GO annotation...

Keywords - Biological processi

Angiogenesis, Apoptosis

Names & Taxonomyi

Protein namesi
Recommended name:
Programmed cell death protein 10
Alternative name(s):
Cerebral cavernous malformations 3 protein
TF-1 cell apoptosis-related protein 15
Gene namesi
Name:PDCD10
Synonyms:CCM3, TFAR15
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 3

Organism-specific databases

HGNCiHGNC:8761. PDCD10.

Subcellular locationi

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.

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB
  2. cytosol Source: UniProtKB
  3. extracellular vesicular exosome Source: UniProtKB
  4. Golgi apparatus Source: UniProtKB
  5. Golgi membrane Source: UniProtKB-SubCell
  6. plasma membrane Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Golgi apparatus, Membrane

Pathology & Biotechi

Involvement in diseasei

Cerebral cavernous malformations 3 (CCM3)1 Publication

The disease is caused by mutations affecting the gene represented in this entry.

Disease descriptionA 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.

See also OMIM:603285

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi132 – 1321K → D: Loss of interaction with CCM2 and PXN; when associated with D-139; D-172 and D-179. 1 Publication
Mutagenesisi135 – 1351A → D: Loss of interaction with CCM2. 1 Publication
Mutagenesisi139 – 1391K → D: Loss of interaction with CCM2 and PXN; when associated with D-132; D-172 and D-179. 1 Publication
Mutagenesisi172 – 1721K → D: Loss of interaction with CCM2 and PXN; when associated with D-132; D-139 and D-179. 1 Publication
Mutagenesisi175 – 1751S → D: Loss of interaction with CCM2. 1 Publication
Mutagenesisi179 – 1791K → D: Loss of interaction with CCM2 and PXN; when associated with D-132; D-139 and D-172. 1 Publication

Organism-specific databases

MIMi603285. phenotype.
Orphaneti221061. Hereditary cerebral cavernous malformation.
PharmGKBiPA33111.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 212212Programmed cell death protein 10PRO_0000187562Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei179 – 1791N6-acetyllysine1 Publication

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiQ9BUL8.
PaxDbiQ9BUL8.
PRIDEiQ9BUL8.

2D gel databases

OGPiQ9BUL8.

PTM databases

PhosphoSiteiQ9BUL8.

Expressioni

Tissue specificityi

Ubiquitous.1 Publication

Gene expression databases

BgeeiQ9BUL8.
CleanExiHS_PDCD10.
ExpressionAtlasiQ9BUL8. baseline and differential.
GenevestigatoriQ9BUL8.

Organism-specific databases

HPAiHPA027095.

Interactioni

Subunit structurei

Homodimer. Interacts (via C-terminus) with CCM2 and PXN. Interacts (via N-terminus) with STK24, STK25 and STK26. Interacts with GOLGA2. Identified in a complex with CCM1 and CCM2. Interacts with KDR/VEGFR2. Interaction with KDR/VEGFR2 is enhanced by stimulation with VEGFA (By similarity).By similarity

Binary interactionsi

WithEntry#Exp.IntActNotes
CCM2Q9BSQ55EBI-740195,EBI-1573056
PTPN13Q129233EBI-740195,EBI-355227
STK24Q9Y6E07EBI-740195,EBI-740175
STK25O005069EBI-740195,EBI-618295
STRNO438153EBI-740195,EBI-1046642

Protein-protein interaction databases

BioGridi116400. 48 interactions.
DIPiDIP-40607N.
IntActiQ9BUL8. 25 interactions.
MINTiMINT-5003501.
STRINGi9606.ENSP00000338141.

Structurei

Secondary structure

1
212
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi17 – 193Combined sources
Helixi20 – 245Combined sources
Helixi26 – 349Combined sources
Helixi38 – 5417Combined sources
Helixi58 – 6912Combined sources
Helixi76 – 827Combined sources
Turni83 – 853Combined sources
Helixi88 – 914Combined sources
Helixi98 – 11518Combined sources
Helixi117 – 1204Combined sources
Beta strandi121 – 1233Combined sources
Helixi124 – 15128Combined sources
Turni152 – 1565Combined sources
Helixi157 – 18428Combined sources
Helixi187 – 20822Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3AJMX-ray2.30A/B8-212[»]
3L8IX-ray2.50A/B/C/D1-212[»]
3L8JX-ray3.05A14-212[»]
3RQEX-ray2.80A/B/C/D1-212[»]
3RQFX-ray2.70A/B/C/D1-212[»]
3RQGX-ray2.50A/B/C/D1-212[»]
3W8HX-ray2.43A8-212[»]
3W8IX-ray2.40A8-212[»]
4GEHX-ray1.95A/C9-212[»]
ProteinModelPortaliQ9BUL8.
SMRiQ9BUL8. Positions 11-211.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9BUL8.

Family & Domainsi

Sequence similaritiesi

Belongs to the PDCD10 family.Curated

Phylogenomic databases

eggNOGiNOG275788.
GeneTreeiENSGT00390000017913.
HOGENOMiHOG000007888.
HOVERGENiHBG052811.
InParanoidiQ9BUL8.
KOiK18269.
OMAiKREFVKY.
OrthoDBiEOG7ZPNM3.
PhylomeDBiQ9BUL8.
TreeFamiTF105802.

Family and domain databases

InterProiIPR009652. DUF1241.
[Graphical view]
PANTHERiPTHR13250. PTHR13250. 1 hit.
PfamiPF06840. DUF1241. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9BUL8-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRMTMEEMKN EAETTSMVSM PLYAVMYPVF NELERVNLSA AQTLRAAFIK
60 70 80 90 100
AEKENPGLTQ DIIMKILEKK SVEVNFTESL LRMAADDVEE YMIERPEPEF
110 120 130 140 150
QDLNEKARAL KQILSKIPDE INDRVRFLQT IKDIASAIKE LLDTVNNVFK
160 170 180 190 200
KYQYQNRRAL EHQKKEFVKY SKSFSDTLKT YFKDGKAINV FVSANRLIHQ
210
TNLILQTFKT VA
Length:212
Mass (Da):24,702
Last modified:June 1, 2001 - v1
Checksum:i5AA613F71FAAEF56
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti102 – 1021D → A.1 Publication
Corresponds to variant rs1129087 [ dbSNP | Ensembl ].
VAR_023578

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF022385 mRNA. Translation: AAB72225.1.
CR457107 mRNA. Translation: CAG33388.1.
AK291130 mRNA. Translation: BAF83819.1.
AC079822 Genomic DNA. No translation available.
CH471052 Genomic DNA. Translation: EAW78574.1.
CH471052 Genomic DNA. Translation: EAW78575.1.
CH471052 Genomic DNA. Translation: EAW78576.1.
CH471052 Genomic DNA. Translation: EAW78577.1.
CH471052 Genomic DNA. Translation: EAW78578.1.
CH471052 Genomic DNA. Translation: EAW78580.1.
CH471052 Genomic DNA. Translation: EAW78581.1.
BC002506 mRNA. Translation: AAH02506.1.
BC016353 mRNA. Translation: AAH16353.1.
CCDSiCCDS3202.1.
RefSeqiNP_009148.2. NM_007217.3.
NP_665858.1. NM_145859.1.
NP_665859.1. NM_145860.1.
XP_005247143.1. XM_005247086.2.
XP_005247144.1. XM_005247087.2.
XP_005247145.1. XM_005247088.2.
XP_006713548.1. XM_006713485.1.
UniGeneiHs.478150.

Genome annotation databases

EnsembliENST00000392750; ENSP00000376506; ENSG00000114209.
ENST00000461494; ENSP00000420021; ENSG00000114209.
ENST00000470131; ENSP00000417202; ENSG00000114209.
ENST00000473645; ENSP00000418317; ENSG00000114209.
ENST00000497056; ENSP00000420553; ENSG00000114209.
GeneIDi11235.
KEGGihsa:11235.
UCSCiuc003fex.3. human.

Polymorphism databases

DMDMi74733232.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF022385 mRNA. Translation: AAB72225.1.
CR457107 mRNA. Translation: CAG33388.1.
AK291130 mRNA. Translation: BAF83819.1.
AC079822 Genomic DNA. No translation available.
CH471052 Genomic DNA. Translation: EAW78574.1.
CH471052 Genomic DNA. Translation: EAW78575.1.
CH471052 Genomic DNA. Translation: EAW78576.1.
CH471052 Genomic DNA. Translation: EAW78577.1.
CH471052 Genomic DNA. Translation: EAW78578.1.
CH471052 Genomic DNA. Translation: EAW78580.1.
CH471052 Genomic DNA. Translation: EAW78581.1.
BC002506 mRNA. Translation: AAH02506.1.
BC016353 mRNA. Translation: AAH16353.1.
CCDSiCCDS3202.1.
RefSeqiNP_009148.2. NM_007217.3.
NP_665858.1. NM_145859.1.
NP_665859.1. NM_145860.1.
XP_005247143.1. XM_005247086.2.
XP_005247144.1. XM_005247087.2.
XP_005247145.1. XM_005247088.2.
XP_006713548.1. XM_006713485.1.
UniGeneiHs.478150.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3AJMX-ray2.30A/B8-212[»]
3L8IX-ray2.50A/B/C/D1-212[»]
3L8JX-ray3.05A14-212[»]
3RQEX-ray2.80A/B/C/D1-212[»]
3RQFX-ray2.70A/B/C/D1-212[»]
3RQGX-ray2.50A/B/C/D1-212[»]
3W8HX-ray2.43A8-212[»]
3W8IX-ray2.40A8-212[»]
4GEHX-ray1.95A/C9-212[»]
ProteinModelPortaliQ9BUL8.
SMRiQ9BUL8. Positions 11-211.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi116400. 48 interactions.
DIPiDIP-40607N.
IntActiQ9BUL8. 25 interactions.
MINTiMINT-5003501.
STRINGi9606.ENSP00000338141.

PTM databases

PhosphoSiteiQ9BUL8.

Polymorphism databases

DMDMi74733232.

2D gel databases

OGPiQ9BUL8.

Proteomic databases

MaxQBiQ9BUL8.
PaxDbiQ9BUL8.
PRIDEiQ9BUL8.

Protocols and materials databases

DNASUi11235.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000392750; ENSP00000376506; ENSG00000114209.
ENST00000461494; ENSP00000420021; ENSG00000114209.
ENST00000470131; ENSP00000417202; ENSG00000114209.
ENST00000473645; ENSP00000418317; ENSG00000114209.
ENST00000497056; ENSP00000420553; ENSG00000114209.
GeneIDi11235.
KEGGihsa:11235.
UCSCiuc003fex.3. human.

Organism-specific databases

CTDi11235.
GeneCardsiGC03M167381.
GeneReviewsiPDCD10.
HGNCiHGNC:8761. PDCD10.
HPAiHPA027095.
MIMi603285. phenotype.
609118. gene.
neXtProtiNX_Q9BUL8.
Orphaneti221061. Hereditary cerebral cavernous malformation.
PharmGKBiPA33111.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG275788.
GeneTreeiENSGT00390000017913.
HOGENOMiHOG000007888.
HOVERGENiHBG052811.
InParanoidiQ9BUL8.
KOiK18269.
OMAiKREFVKY.
OrthoDBiEOG7ZPNM3.
PhylomeDBiQ9BUL8.
TreeFamiTF105802.

Miscellaneous databases

ChiTaRSiPDCD10. human.
EvolutionaryTraceiQ9BUL8.
GeneWikiiPDCD10.
GenomeRNAii11235.
NextBioi42758.
PROiQ9BUL8.
SOURCEiSearch...

Gene expression databases

BgeeiQ9BUL8.
CleanExiHS_PDCD10.
ExpressionAtlasiQ9BUL8. baseline and differential.
GenevestigatoriQ9BUL8.

Family and domain databases

InterProiIPR009652. DUF1241.
[Graphical view]
PANTHERiPTHR13250. PTHR13250. 1 hit.
PfamiPF06840. DUF1241. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "cDNA cloning and expression of an apoptosis-related gene, human TFAR-15 gene."
    Wang Y.G., Liu H.T., Ma D.L., Zhang Y.M.
    Sci. China, Ser. C, Life Sci. 42:323-329(1998)
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT ALA-102.
  2. "Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
    Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
    Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  3. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    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.
    Nat. Genet. 36:40-45(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  4. "The DNA sequence, annotation and analysis of human chromosome 3."
    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.
    Nature 440:1194-1198(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Skin and Urinary bladder.
  7. Bienvenut W.V., Claeys D.
    Submitted (OCT-2005) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 36-45 AND 117-124, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Platelet.
  8. Cited for: FUNCTION, TISSUE SPECIFICITY, INVOLVEMENT IN CCM3.
  9. "PDCD10 interacts with Ste20-related kinase MST4 to promote cell growth and transformation via modulation of the ERK pathway."
    Ma X., Zhao H., Shan J., Long F., Chen Y., Chen Y., Zhang Y., Han X., Ma D.
    Mol. Biol. Cell 18:1965-1978(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH STK26, FUNCTION, SUBCELLULAR LOCATION.
  10. "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."
    Voss K., Stahl S., Hogan B.M., Reinders J., Schleider E., Schulte-Merker S., Felbor U.
    Hum. Mutat. 30:1003-1011(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH CCM2; STK25 AND STK26, IDENTIFICATION IN A COMPLEX WITH CCM1 AND CCM2.
  11. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
    Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
    Science 325:834-840(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-179, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  12. "CCM3/PDCD10 stabilizes GCKIII proteins to promote Golgi assembly and cell orientation."
    Fidalgo M., Fraile M., Pires A., Force T., Pombo C., Zalvide J.
    J. Cell Sci. 123:1274-1284(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH GOLGA2; STK24; STK25 AND STK26, SUBCELLULAR LOCATION.
  13. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  14. "Crystal structure of CCM3, a cerebral cavernous malformation protein critical for vascular integrity."
    Li X., Zhang R., Zhang H., He Y., Ji W., Min W., Boggon T.J.
    J. Biol. Chem. 285:24099-24107(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS), SUBUNIT, INTERACTION WITH CCM2 AND PXN, SUBCELLULAR LOCATION, MUTAGENESIS OF LYS-132; ALA-135; LYS-139; LYS-172; SER-175 AND LYS-179.

Entry informationi

Entry nameiPDC10_HUMAN
AccessioniPrimary (citable) accession number: Q9BUL8
Secondary accession number(s): A8K515, D3DNN5, O14811
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 11, 2005
Last sequence update: June 1, 2001
Last modified: March 4, 2015
This is version 114 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 3
    Human chromosome 3: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.