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Q9NPI6

- DCP1A_HUMAN

UniProt

Q9NPI6 - DCP1A_HUMAN

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Protein

mRNA-decapping enzyme 1A

Gene

DCP1A

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

Functioni

Necessary for the degradation of mRNAs, both in normal mRNA turnover and in nonsense-mediated mRNA decay. Removes the 7-methyl guanine cap structure from mRNA molecules, yielding a 5'-phosphorylated mRNA fragment and 7m-GDP. Contributes to the transactivation of target genes after stimulation by TGFB1.2 Publications

GO - Molecular functioni

  1. hydrolase activity Source: UniProtKB-KW
  2. identical protein binding Source: IntAct

GO - Biological processi

  1. exonucleolytic nuclear-transcribed mRNA catabolic process involved in deadenylation-dependent decay Source: Reactome
  2. gene expression Source: Reactome
  3. mRNA metabolic process Source: Reactome
  4. nuclear-transcribed mRNA catabolic process, deadenylation-dependent decay Source: Reactome
  5. nuclear-transcribed mRNA catabolic process, nonsense-mediated decay Source: UniProtKB-KW
  6. RNA metabolic process Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Nonsense-mediated mRNA decay

Enzyme and pathway databases

ReactomeiREACT_20518. mRNA decay by 5' to 3' exoribonuclease.
REACT_24915. Butyrate Response Factor 1 (BRF1) destabilizes mRNA.
REACT_25064. Tristetraprolin (TTP) destabilizes mRNA.

Protein family/group databases

TCDBi3.A.18.1.1. the nuclear mrna exporter (mrna-e) family.

Names & Taxonomyi

Protein namesi
Recommended name:
mRNA-decapping enzyme 1A (EC:3.-.-.-)
Alternative name(s):
Smad4-interacting transcriptional co-activator
Transcription factor SMIF
Gene namesi
Name:DCP1A
Synonyms:SMIF
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Unplaced

Organism-specific databases

HGNCiHGNC:18714. DCP1A.

Subcellular locationi

CytoplasmP-body. Nucleus
Note: Co-localizes with NANOS3 in the processing bodies (By similarity). Predominantly cytoplasmic, in processing bodies (PB). Nuclear, after TGFB1 treatment. Translocation to the nucleus depends on interaction with SMAD4.By similarity

GO - Cellular componenti

  1. cytoplasmic mRNA processing body Source: UniProtKB
  2. cytosol Source: Reactome
  3. membrane Source: UniProtKB
  4. nucleus Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi20 – 201D → A: Lowers decapping activity. 1 Publication
Mutagenesisi59 – 591R → A: Lowers decapping activity. 1 Publication

Organism-specific databases

PharmGKBiPA134931379.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 582582mRNA-decapping enzyme 1APRO_0000189632Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei142 – 1421Phosphoserine1 Publication
Modified residuei180 – 1801Phosphoserine1 Publication
Modified residuei315 – 3151Phosphoserine6 Publications
Modified residuei319 – 3191Phosphoserine3 Publications
Modified residuei334 – 3341Phosphoserine2 Publications
Modified residuei353 – 3531Phosphoserine4 Publications
Modified residuei401 – 4011Phosphothreonine1 Publication
Modified residuei422 – 4221Phosphoserine1 Publication
Modified residuei522 – 5221Phosphoserine2 Publications
Modified residuei523 – 5231Phosphoserine2 Publications
Modified residuei525 – 5251Phosphoserine2 Publications
Modified residuei531 – 5311Phosphothreonine3 Publications

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ9NPI6.
PaxDbiQ9NPI6.
PRIDEiQ9NPI6.

PTM databases

PhosphoSiteiQ9NPI6.

Expressioni

Tissue specificityi

Detected in heart, brain, placenta, lung, skeletal muscle, liver, kidney and pancreas.1 Publication

Gene expression databases

CleanExiHS_DCP1A.
GenevestigatoriQ9NPI6.

Organism-specific databases

HPAiHPA013202.

Interactioni

Subunit structurei

Forms a complex with EDC3, DCP2, DDX6 and EDC4/HEDLS, within this complex directly interacts with EDC3. Binds DCP1B, UPF1 and SMAD4. Part of a cytoplasmic complex containing proteins involved in mRNA decay, including XRN1 and LSM1. Interacts with PNRC2. Interacts with DDX17 in an RNA-independent manner. Interacts with ZC3HAV1.6 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
itself4EBI-374238,EBI-374238
BAG4O954293EBI-374238,EBI-2949658
DCP2Q8IU607EBI-374238,EBI-521577
DDX6P261965EBI-374238,EBI-351257
UPF1Q9290013EBI-374238,EBI-373471
ZFP36P266512EBI-374238,EBI-374248

Protein-protein interaction databases

BioGridi120914. 26 interactions.
DIPiDIP-31292N.
IntActiQ9NPI6. 16 interactions.
MINTiMINT-5005647.
STRINGi9606.ENSP00000294241.

Structurei

Secondary structure

582
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi1 – 1919
Beta strandi23 – 3917
Turni40 – 434
Beta strandi44 – 6320
Beta strandi65 – 717
Beta strandi78 – 814
Beta strandi87 – 915
Beta strandi94 – 985
Beta strandi104 – 1118
Helixi112 – 12615
Helixi539 – 55719
Helixi559 – 57113

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2WX3X-ray2.31A/B/C539-582[»]
4B6HX-ray2.60A/B1-130[»]
ProteinModelPortaliQ9NPI6.
SMRiQ9NPI6. Positions 1-129, 539-582.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9NPI6.

Family & Domainsi

Sequence similaritiesi

Belongs to the DCP1 family.Curated

Phylogenomic databases

eggNOGiNOG314415.
GeneTreeiENSGT00390000014855.
HOVERGENiHBG051320.
InParanoidiQ9NPI6.
KOiK12610.
PhylomeDBiQ9NPI6.

Family and domain databases

Gene3Di2.30.29.30. 1 hit.
InterProiIPR010334. DCP1.
IPR011993. PH_like_dom.
[Graphical view]
PANTHERiPTHR16290. PTHR16290. 1 hit.
PfamiPF06058. DCP1. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9NPI6-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MEALSRAGQE MSLAALKQHD PYITSIADLT GQVALYTFCP KANQWEKTDI
60 70 80 90 100
EGTLFVYRRS ASPYHGFTIV NRLNMHNLVE PVNKDLEFQL HEPFLLYRNA
110 120 130 140 150
SLSIYSIWFY DKNDCHRIAK LMADVVEEET RRSQQAARDK QSPSQANGCS
160 170 180 190 200
DHRPIDILEM LSRAKDEYER NQMGDSNISS PGLQPSTQLS NLGSTETLEE
210 220 230 240 250
MPSGSQDKSA PSGHKHLTVE ELFGTSLPKE QPAVVGLDSE EMERLPGDAS
260 270 280 290 300
QKEPNSFLPF PFEQLGGAPQ SETLGVPSAA HHSVQPEITT PVLITPASIT
310 320 330 340 350
QSNEKHAPTY TIPLSPVLSP TLPAEAPTAQ VPPSLPRNST MMQAVKTTPR
360 370 380 390 400
QRSPLLNQPV PELSHASLIA NQSPFRAPLN VTNTAGTSLP SVDLLQKLRL
410 420 430 440 450
TPQHDQIQTQ PLGKGAMVAS FSPAAGQLAT PESFIEPPSK TAAARVAASA
460 470 480 490 500
SLSNMVLAPL QSMQQNQDPE VFVQPKVLSS AIQVAGAPLV TATTTAVSSV
510 520 530 540 550
LLAPSVFQQT VTRSSDLERK ASSPSPLTIG TPESQRKPSI ILSKSQLQDT
560 570 580
LIHLIKNDSS FLSTLHEVYL QVLTKNKDNH NL
Length:582
Mass (Da):63,309
Last modified:May 18, 2010 - v2
Checksum:iD218180ABA7FD768
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti483 – 4831Q → P in AAN62763. (PubMed:12417715)Curated
Sequence conflicti483 – 4831Q → P in CAB77023. (PubMed:11836524)Curated
Sequence conflicti483 – 4831Q → P in BAA92008. (PubMed:14702039)Curated
Sequence conflicti483 – 4831Q → P in AAH07439. (PubMed:15489334)Curated

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AY146651 mRNA. Translation: AAN62763.1.
AJ275986 mRNA. Translation: CAB77023.1.
AK001969 mRNA. Translation: BAA92008.1.
AC097015 Genomic DNA. No translation available.
AC112218 Genomic DNA. No translation available.
BC007439 mRNA. Translation: AAH07439.1.
RefSeqiNP_001277134.1. NM_001290205.1.
NP_001277135.1. NM_001290206.1.
NP_060873.4. NM_018403.6.
UniGeneiHs.476353.

Genome annotation databases

EnsembliENST00000610213; ENSP00000476386; ENSG00000272886.
GeneIDi55802.
KEGGihsa:55802.
UCSCiuc021wzi.1. human.

Polymorphism databases

DMDMi296434475.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AY146651 mRNA. Translation: AAN62763.1 .
AJ275986 mRNA. Translation: CAB77023.1 .
AK001969 mRNA. Translation: BAA92008.1 .
AC097015 Genomic DNA. No translation available.
AC112218 Genomic DNA. No translation available.
BC007439 mRNA. Translation: AAH07439.1 .
RefSeqi NP_001277134.1. NM_001290205.1.
NP_001277135.1. NM_001290206.1.
NP_060873.4. NM_018403.6.
UniGenei Hs.476353.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2WX3 X-ray 2.31 A/B/C 539-582 [» ]
4B6H X-ray 2.60 A/B 1-130 [» ]
ProteinModelPortali Q9NPI6.
SMRi Q9NPI6. Positions 1-129, 539-582.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 120914. 26 interactions.
DIPi DIP-31292N.
IntActi Q9NPI6. 16 interactions.
MINTi MINT-5005647.
STRINGi 9606.ENSP00000294241.

Protein family/group databases

TCDBi 3.A.18.1.1. the nuclear mrna exporter (mrna-e) family.

PTM databases

PhosphoSitei Q9NPI6.

Polymorphism databases

DMDMi 296434475.

Proteomic databases

MaxQBi Q9NPI6.
PaxDbi Q9NPI6.
PRIDEi Q9NPI6.

Protocols and materials databases

DNASUi 55802.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000610213 ; ENSP00000476386 ; ENSG00000272886 .
GeneIDi 55802.
KEGGi hsa:55802.
UCSCi uc021wzi.1. human.

Organism-specific databases

CTDi 55802.
GeneCardsi GC03M053319.
HGNCi HGNC:18714. DCP1A.
HPAi HPA013202.
MIMi 607010. gene.
neXtProti NX_Q9NPI6.
PharmGKBi PA134931379.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG314415.
GeneTreei ENSGT00390000014855.
HOVERGENi HBG051320.
InParanoidi Q9NPI6.
KOi K12610.
PhylomeDBi Q9NPI6.

Enzyme and pathway databases

Reactomei REACT_20518. mRNA decay by 5' to 3' exoribonuclease.
REACT_24915. Butyrate Response Factor 1 (BRF1) destabilizes mRNA.
REACT_25064. Tristetraprolin (TTP) destabilizes mRNA.

Miscellaneous databases

ChiTaRSi DCP1A. human.
EvolutionaryTracei Q9NPI6.
GeneWikii DCP1A.
GenomeRNAii 55802.
NextBioi 60947.
PROi Q9NPI6.
SOURCEi Search...

Gene expression databases

CleanExi HS_DCP1A.
Genevestigatori Q9NPI6.

Family and domain databases

Gene3Di 2.30.29.30. 1 hit.
InterProi IPR010334. DCP1.
IPR011993. PH_like_dom.
[Graphical view ]
PANTHERi PTHR16290. PTHR16290. 1 hit.
Pfami PF06058. DCP1. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Identification of a human decapping complex associated with hUpf proteins in nonsense-mediated decay."
    Lykke-Andersen J.
    Mol. Cell. Biol. 22:8114-8121(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, MUTAGENESIS OF ASP-20 AND ARG-59, INTERACTION WITH DCP1B AND DCP2, SUBCELLULAR LOCATION.
  2. "SMIF, a Smad4-interacting protein that functions as a co-activator in TGFbeta signalling."
    Bai R.-Y., Koester C., Ouyang T., Hahn S.A., Hammerschmidt M., Peschel C., Duyster J.
    Nat. Cell Biol. 4:181-190(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INTERACTION WITH SMAD4, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
    Tissue: Pancreas.
  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(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Placenta.
  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(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "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].
    Tissue: Muscle.
  6. "The human LSm1-7 proteins colocalize with the mRNA-degrading enzymes Dcp1/2 and Xrnl in distinct cytoplasmic foci."
    Ingelfinger D., Arndt-Jovin D.J., Luehrmann R., Achsel T.
    RNA 8:1489-1501(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, INTERACTION WITH A COMPLEX CONTAINING ENZYMES INVOLVED IN MRNA DECAY.
  7. "Multiple processing body factors and the ARE binding protein TTP activate mRNA decapping."
    Fenger-Groen M., Fillman C., Norrild B., Lykke-Andersen J.
    Mol. Cell 20:905-915(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH EDC3; DCP2; EDC4 AND DDX6, SUBCELLULAR LOCATION.
  8. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
    Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
    Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-353, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  9. "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis."
    Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III
    J. Proteome Res. 7:1346-1351(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-315; SER-334 AND THR-531, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  10. "Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
    Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
    Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-315 AND SER-353, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  11. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-142; SER-315; SER-319; SER-334; SER-353; THR-401; SER-522; SER-523; SER-525 AND THR-531, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  12. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
    Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
    Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  13. "Human proline-rich nuclear receptor coregulatory protein 2 mediates an interaction between mRNA surveillance machinery and decapping complex."
    Cho H., Kim K.M., Kim Y.K.
    Mol. Cell 33:75-86(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH PNRC2.
  14. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
    Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
    Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-180; SER-315; SER-319; SER-522; SER-523; SER-525 AND THR-531, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  15. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
    Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-315; SER-319; SER-353 AND SER-422, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  16. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  17. "Zinc-finger antiviral protein inhibits HIV-1 infection by selectively targeting multiply spliced viral mRNAs for degradation."
    Zhu Y., Chen G., Lv F., Wang X., Ji X., Xu Y., Sun J., Wu L., Zheng Y.T., Gao G.
    Proc. Natl. Acad. Sci. U.S.A. 108:15834-15839(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH ZC3HAV1 AND DDX17.
  18. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
    Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
    Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-315, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiDCP1A_HUMAN
AccessioniPrimary (citable) accession number: Q9NPI6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 1, 2005
Last sequence update: May 18, 2010
Last modified: October 29, 2014
This is version 114 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 3
    Human chromosome 3: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3