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O75689

- ADAP1_HUMAN

UniProt

O75689 - ADAP1_HUMAN

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Protein

Arf-GAP with dual PH domain-containing protein 1

Gene

ADAP1

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

Functioni

GTPase-activating protein for the ADP ribosylation factor family (Probable). Binds phosphatidylinositol 3,4,5-trisphosphate (PtdInsP3) and inositol 1,3,4,5-tetrakisphosphate (InsP4).1 Publication1 PublicationCurated

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri21 – 4424C4-typePROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

  1. ARF GTPase activator activity Source: UniProtKB
  2. inositol 1,3,4,5 tetrakisphosphate binding Source: UniProtKB
  3. phosphatidylinositol-3,4,5-trisphosphate binding Source: Ensembl
  4. zinc ion binding Source: InterPro

GO - Biological processi

  1. cell surface receptor signaling pathway Source: ProtInc
  2. positive regulation of GTPase activity Source: GOC
  3. regulation of ARF GTPase activity Source: InterPro
  4. regulation of GTPase activity Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

GTPase activation

Keywords - Ligandi

Metal-binding, Zinc

Names & Taxonomyi

Protein namesi
Recommended name:
Arf-GAP with dual PH domain-containing protein 1
Alternative name(s):
Centaurin-alpha-1
Short name:
Cnt-a1
Putative MAPK-activating protein PM25
Gene namesi
Name:ADAP1
Synonyms:CENTA1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 7

Organism-specific databases

HGNCiHGNC:16486. ADAP1.

Subcellular locationi

Nucleus. Cytoplasm
Note: Recruited to the plasma membrane upon epidermal growth factor-dependent activation of phosphatidylinositol 4,5-diphosphate (PtdInsP2) 3-kinase.

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB
  2. nucleus Source: UniProtKB
  3. plasma membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi21 – 211C → A: Loss of GTPase-activating activity. 1 Publication
Mutagenesisi24 – 241C → A: Loss of GTPase-activating activity. 1 Publication
Mutagenesisi149 – 1491R → C: 40-45% reduction in PtdInsP2 3-kinase dependent membrane localization. Almost complete loss of PtdInsP2 3-kinase dependent membrane localization; when associated with C-273. 2 Publications
Mutagenesisi273 – 2731R → C: 70% reduction in PtdInsP2 3-kinase dependent membrane localization. Almost complete loss of PtdInsP2 3-kinase dependent membrane localization; when associated with C-149. 2 Publications

Organism-specific databases

PharmGKBiPA26404.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 374374Arf-GAP with dual PH domain-containing protein 1PRO_0000074205Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei87 – 871Phosphoserine; by PKC1 Publication
Modified residuei272 – 2721N6-acetyllysine1 Publication
Modified residuei276 – 2761Phosphothreonine; by PKC1 Publication

Post-translational modificationi

Phosphorylated by PRKCA, PRKCI, PRKCZ and PRKD1 in vitro.1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiO75689.
PaxDbiO75689.
PRIDEiO75689.

PTM databases

PhosphoSiteiO75689.

Expressioni

Tissue specificityi

Expressed at highest levels in brain and at lower levels in peripheral blood leukocytes.1 Publication

Gene expression databases

BgeeiO75689.
CleanExiHS_ADAP1.
ExpressionAtlasiO75689. baseline.
GenevestigatoriO75689.

Organism-specific databases

HPAiHPA007033.
HPA012049.

Interactioni

Subunit structurei

Interacts with PRKCA, PRKCI and PRKCZ. Interacts with the N-terminal region of PRKD1.1 Publication

Protein-protein interaction databases

BioGridi116222. 14 interactions.
DIPiDIP-41731N.
IntActiO75689. 5 interactions.
MINTiMINT-193767.
STRINGi9606.ENSP00000265846.

Structurei

Secondary structure

1
374
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi3 – 1210Combined sources
Helixi16 – 183Combined sources
Turni22 – 243Combined sources
Beta strandi31 – 333Combined sources
Turni34 – 374Combined sources
Beta strandi38 – 403Combined sources
Helixi42 – 498Combined sources
Turni52 – 543Combined sources
Beta strandi57 – 593Combined sources
Turni60 – 623Combined sources
Helixi67 – 759Combined sources
Helixi78 – 858Combined sources
Turni86 – 883Combined sources
Helixi102 – 11312Combined sources
Turni117 – 1193Combined sources
Helixi121 – 1244Combined sources
Helixi125 – 1284Combined sources
Beta strandi129 – 13911Combined sources
Beta strandi141 – 1433Combined sources
Beta strandi146 – 1549Combined sources
Turni155 – 1584Combined sources
Beta strandi159 – 1635Combined sources
Beta strandi165 – 1673Combined sources
Beta strandi172 – 1765Combined sources
Helixi177 – 1793Combined sources
Beta strandi180 – 1845Combined sources
Helixi186 – 1894Combined sources
Beta strandi195 – 2017Combined sources
Beta strandi204 – 2118Combined sources
Helixi215 – 23622Combined sources
Beta strandi237 – 2404Combined sources
Helixi242 – 2454Combined sources
Helixi246 – 2483Combined sources
Beta strandi254 – 2618Combined sources
Beta strandi271 – 2788Combined sources
Beta strandi281 – 2877Combined sources
Beta strandi294 – 2985Combined sources
Helixi302 – 3043Combined sources
Beta strandi307 – 3115Combined sources
Beta strandi323 – 3286Combined sources
Beta strandi333 – 3408Combined sources
Helixi341 – 35616Combined sources
Helixi363 – 3697Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3FEHX-ray1.90A3-370[»]
3FM8X-ray2.30C/D1-374[»]
3LJUX-ray1.70X3-370[»]
3MDBX-ray2.95C/D1-374[»]
ProteinModelPortaliO75689.
SMRiO75689. Positions 2-370.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO75689.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini7 – 126120Arf-GAPPROSITE-ProRule annotationAdd
BLAST
Domaini129 – 230102PH 1PROSITE-ProRule annotationAdd
BLAST
Domaini252 – 356105PH 2PROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 1 Arf-GAP domain.PROSITE-ProRule annotation
Contains 2 PH domains.PROSITE-ProRule annotation

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri21 – 4424C4-typePROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

Repeat, Zinc-finger

Phylogenomic databases

eggNOGiCOG5347.
GeneTreeiENSGT00530000062917.
HOGENOMiHOG000006719.
HOVERGENiHBG050888.
InParanoidiO75689.
OrthoDBiEOG71K62W.
PhylomeDBiO75689.
TreeFamiTF324540.

Family and domain databases

Gene3Di2.30.29.30. 2 hits.
InterProiIPR001164. ArfGAP.
IPR001849. PH_domain.
IPR011993. PH_like_dom.
[Graphical view]
PfamiPF01412. ArfGap. 1 hit.
[Graphical view]
PRINTSiPR00405. REVINTRACTNG.
SMARTiSM00105. ArfGap. 1 hit.
SM00233. PH. 2 hits.
[Graphical view]
PROSITEiPS50115. ARFGAP. 1 hit.
PS50003. PH_DOMAIN. 2 hits.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: O75689-1) [UniParc]FASTAAdd to Basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MAKERRRAVL ELLQRPGNAR CADCGAPDPD WASYTLGVFI CLSCSGIHRN
60 70 80 90 100
IPQVSKVKSV RLDAWEEAQV EFMASHGNDA ARARFESKVP SFYYRPTPSD
110 120 130 140 150
CQLLREQWIR AKYERQEFIY PEKQEPYSAG YREGFLWKRG RDNGQFLSRK
160 170 180 190 200
FVLTEREGAL KYFNRNDAKE PKAVMKIEHL NATFQPAKIG HPHGLQVTYL
210 220 230 240 250
KDNSTRNIFI YHEDGKEIVD WFNALRAARF HYLQVAFPGA GDADLVPKLS
260 270 280 290 300
RNYLKEGYME KTGPKQTEGF RKRWFTMDDR RLMYFKDPLD AFARGEVFIG
310 320 330 340 350
SKESGYTVLH GFPPSTQGHH WPHGITIVTP DRKFLFACET ESDQREWVAA
360 370
FQKAVDRPML PQEYAVEAHF KHKP
Length:374
Mass (Da):43,395
Last modified:November 25, 2008 - v2
Checksum:i38547281FB09D9B9
GO
Isoform 2 (identifier: O75689-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-27: MAKERRRAVLELLQRPGNARCADCGAP → MFQFVFSRVYCINPARRKWKEFEKMLGCAEEGHASLGR

Show »
Length:385
Mass (Da):44,936
Checksum:i67ACBB2A85819D46
GO
Isoform 3 (identifier: O75689-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-72: Missing.

Show »
Length:302
Mass (Da):35,353
Checksum:i8197A42910488E1E
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti215 – 2151G → R in BAG52556. (PubMed:14702039)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti241 – 2411G → S.4 Publications
Corresponds to variant rs10256887 [ dbSNP | Ensembl ].
VAR_047470

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 7272Missing in isoform 3. 1 PublicationVSP_054793Add
BLAST
Alternative sequencei1 – 2727MAKER…DCGAP → MFQFVFSRVYCINPARRKWK EFEKMLGCAEEGHASLGR in isoform 2. 1 PublicationVSP_054794Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ006422 mRNA. Translation: CAA07024.1.
AF082324 mRNA. Translation: AAD11414.1.
AB097049 mRNA. Translation: BAC77402.1.
AK300999 mRNA. Translation: BAG62618.1.
AC073957 Genomic DNA. No translation available.
AK092471 mRNA. Translation: BAG52556.1.
CH236965 Genomic DNA. Translation: EAL23709.1.
CH471144 Genomic DNA. Translation: EAW87183.1.
CH471144 Genomic DNA. Translation: EAW87184.1.
BC033747 mRNA. Translation: AAH33747.1.
CCDSiCCDS5318.1. [O75689-1]
CCDS64576.1. [O75689-3]
CCDS64577.1. [O75689-2]
PIRiJC7091.
RefSeqiNP_001271237.1. NM_001284308.1.
NP_001271238.1. NM_001284309.1.
NP_001271239.1. NM_001284310.1.
NP_001271240.1. NM_001284311.1.
NP_006860.1. NM_006869.3.
UniGeneiHs.602573.

Genome annotation databases

EnsembliENST00000265846; ENSP00000265846; ENSG00000105963. [O75689-1]
ENST00000449296; ENSP00000407267; ENSG00000105963. [O75689-3]
ENST00000539900; ENSP00000442682; ENSG00000105963. [O75689-2]
ENST00000611167; ENSP00000481154; ENSG00000105963. [O75689-3]
GeneIDi11033.
KEGGihsa:11033.
UCSCiuc003sjm.4. human. [O75689-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ006422 mRNA. Translation: CAA07024.1 .
AF082324 mRNA. Translation: AAD11414.1 .
AB097049 mRNA. Translation: BAC77402.1 .
AK300999 mRNA. Translation: BAG62618.1 .
AC073957 Genomic DNA. No translation available.
AK092471 mRNA. Translation: BAG52556.1 .
CH236965 Genomic DNA. Translation: EAL23709.1 .
CH471144 Genomic DNA. Translation: EAW87183.1 .
CH471144 Genomic DNA. Translation: EAW87184.1 .
BC033747 mRNA. Translation: AAH33747.1 .
CCDSi CCDS5318.1. [O75689-1 ]
CCDS64576.1. [O75689-3 ]
CCDS64577.1. [O75689-2 ]
PIRi JC7091.
RefSeqi NP_001271237.1. NM_001284308.1.
NP_001271238.1. NM_001284309.1.
NP_001271239.1. NM_001284310.1.
NP_001271240.1. NM_001284311.1.
NP_006860.1. NM_006869.3.
UniGenei Hs.602573.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
3FEH X-ray 1.90 A 3-370 [» ]
3FM8 X-ray 2.30 C/D 1-374 [» ]
3LJU X-ray 1.70 X 3-370 [» ]
3MDB X-ray 2.95 C/D 1-374 [» ]
ProteinModelPortali O75689.
SMRi O75689. Positions 2-370.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 116222. 14 interactions.
DIPi DIP-41731N.
IntActi O75689. 5 interactions.
MINTi MINT-193767.
STRINGi 9606.ENSP00000265846.

PTM databases

PhosphoSitei O75689.

Proteomic databases

MaxQBi O75689.
PaxDbi O75689.
PRIDEi O75689.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000265846 ; ENSP00000265846 ; ENSG00000105963 . [O75689-1 ]
ENST00000449296 ; ENSP00000407267 ; ENSG00000105963 . [O75689-3 ]
ENST00000539900 ; ENSP00000442682 ; ENSG00000105963 . [O75689-2 ]
ENST00000611167 ; ENSP00000481154 ; ENSG00000105963 . [O75689-3 ]
GeneIDi 11033.
KEGGi hsa:11033.
UCSCi uc003sjm.4. human. [O75689-1 ]

Organism-specific databases

CTDi 11033.
GeneCardsi GC07M000938.
HGNCi HGNC:16486. ADAP1.
HPAi HPA007033.
HPA012049.
MIMi 608114. gene.
neXtProti NX_O75689.
PharmGKBi PA26404.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG5347.
GeneTreei ENSGT00530000062917.
HOGENOMi HOG000006719.
HOVERGENi HBG050888.
InParanoidi O75689.
OrthoDBi EOG71K62W.
PhylomeDBi O75689.
TreeFami TF324540.

Miscellaneous databases

ChiTaRSi ADAP1. human.
EvolutionaryTracei O75689.
GeneWikii Centaurin,_alpha_1.
GenomeRNAii 11033.
NextBioi 35469618.
PROi O75689.
SOURCEi Search...

Gene expression databases

Bgeei O75689.
CleanExi HS_ADAP1.
ExpressionAtlasi O75689. baseline.
Genevestigatori O75689.

Family and domain databases

Gene3Di 2.30.29.30. 2 hits.
InterProi IPR001164. ArfGAP.
IPR001849. PH_domain.
IPR011993. PH_like_dom.
[Graphical view ]
Pfami PF01412. ArfGap. 1 hit.
[Graphical view ]
PRINTSi PR00405. REVINTRACTNG.
SMARTi SM00105. ArfGap. 1 hit.
SM00233. PH. 2 hits.
[Graphical view ]
PROSITEi PS50115. ARFGAP. 1 hit.
PS50003. PH_DOMAIN. 2 hits.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Molecular cloning and functional characterization of a human homologue of centaurin-alpha."
    Venkateswarlu K., Cullen P.J.
    Biochem. Biophys. Res. Commun. 262:237-244(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, MUTAGENESIS OF ARG-149 AND ARG-273.
    Tissue: Blood1 Publication.
  2. "Identification of centaurin-alpha1 as a potential in vivo phosphatidylinositol 3,4,5-trisphosphate-binding protein that is functionally homologous to the yeast ADP-ribosylation factor (ARF) GTPase-activating protein, Gcs1."
    Venkateswarlu K., Oatey P.B., Tavare J.M., Jackson T.R., Cullen P.J.
    Biochem. J. 340:359-363(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, SUBCELLULAR LOCATION, MUTAGENESIS OF CYS-21; CYS-24; ARG-149 AND ARG-273, VARIANT SER-241.
    Tissue: Peripheral bloodImported.
  3. "Molecular identification of a high-affinity Ins(1,3,4,5)tetrakisphosphate/phosphatidylinositol(3,4, 5)trisphosphate binding protein from human brain, p42IP4."
    Horstmeyer A., Reiser G.
    Submitted (AUG-1998) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT SER-241.
    Tissue: BrainImported.
  4. "Large-scale identification and characterization of human genes that activate NF-kappaB and MAPK signaling pathways."
    Matsuda A., Suzuki Y., Honda G., Muramatsu S., Matsuzaki O., Nagano Y., Doi T., Shimotohno K., Harada T., Nishida E., Hayashi H., Sugano S.
    Oncogene 22:3307-3318(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), VARIANT SER-241.
    Tissue: Lung fibroblast.
  5. "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(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3).
    Tissue: Small intestine.
  6. "Human chromosome 7: DNA sequence and biology."
    Scherer S.W., Cheung J., MacDonald J.R., Osborne L.R., Nakabayashi K., Herbrick J.-A., Carson A.R., Parker-Katiraee L., Skaug J., Khaja R., Zhang J., Hudek A.K., Li M., Haddad M., Duggan G.E., Fernandez B.A., Kanematsu E., Gentles S.
    , Christopoulos C.C., Choufani S., Kwasnicka D., Zheng X.H., Lai Z., Nusskern D.R., Zhang Q., Gu Z., Lu F., Zeesman S., Nowaczyk M.J., Teshima I., Chitayat D., Shuman C., Weksberg R., Zackai E.H., Grebe T.A., Cox S.R., Kirkpatrick S.J., Rahman N., Friedman J.M., Heng H.H.Q., Pelicci P.G., Lo-Coco F., Belloni E., Shaffer L.G., Pober B., Morton C.C., Gusella J.F., Bruns G.A.P., Korf B.R., Quade B.J., Ligon A.H., Ferguson H., Higgins A.W., Leach N.T., Herrick S.R., Lemyre E., Farra C.G., Kim H.-G., Summers A.M., Gripp K.W., Roberts W., Szatmari P., Winsor E.J.T., Grzeschik K.-H., Teebi A., Minassian B.A., Kere J., Armengol L., Pujana M.A., Estivill X., Wilson M.D., Koop B.F., Tosi S., Moore G.E., Boright A.P., Zlotorynski E., Kerem B., Kroisel P.M., Petek E., Oscier D.G., Mould S.J., Doehner H., Doehner K., Rommens J.M., Vincent J.B., Venter J.C., Li P.W., Mural R.J., Adams M.D., Tsui L.-C.
    Science 300:767-772(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  7. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  8. "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(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), VARIANT SER-241.
    Tissue: BrainImported.
  9. "Centaurin-alpha(1) associates with and is phosphorylated by isoforms of protein kinase C."
    Zemlickova E., Dubois T., Kerai P., Clokie S., Cronshaw A.D., Wakefield R.I.D., Johannes F.-J., Aitken A.
    Biochem. Biophys. Res. Commun. 307:459-465(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH PRKCA; PRKCI; PRKCZ AND PRKD1, PHOSPHORYLATION AT SER-87 AND THR-276.
  10. "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(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-272, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  11. "Crystal structure of full length centaurin alpha-1."
    Structural genomics consortium (SGC)
    Submitted (DEC-2008) to the PDB data bank
    Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 3-370.

Entry informationi

Entry nameiADAP1_HUMAN
AccessioniPrimary (citable) accession number: O75689
Secondary accession number(s): A4D2Q2
, B3KRZ4, B4DVA6, F6XZ68, H7C2Q4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 5, 2005
Last sequence update: November 25, 2008
Last modified: November 26, 2014
This is version 124 of the entry and version 2 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, Reference proteome

Documents

  1. Human chromosome 7
    Human chromosome 7: 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