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Protein

mRNA-decapping enzyme 1B

Gene

DCP1B

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

Functioni

May play a role in the degradation of mRNAs, both in normal mRNA turnover and in nonsense-mediated mRNA decay. May remove the 7-methyl guanine cap structure from mRNA molecules, yielding a 5'-phosphorylated mRNA fragment and 7m-GDP (By similarity).By similarity

GO - Molecular functioni

  1. enzyme regulator activity Source: GO_Central
  2. hydrolase activity Source: UniProtKB-KW
  3. mRNA binding Source: GO_Central
  4. RNA 7-methylguanosine cap binding Source: GO_Central

GO - Biological processi

  1. deadenylation-dependent decapping of nuclear-transcribed mRNA Source: GO_Central
  2. deadenylation-independent decapping of nuclear-transcribed mRNA Source: GO_Central
  3. exonucleolytic nuclear-transcribed mRNA catabolic process involved in deadenylation-dependent decay Source: Reactome
  4. gene expression Source: Reactome
  5. nuclear-transcribed mRNA catabolic process, deadenylation-dependent decay Source: Reactome
  6. nuclear-transcribed mRNA catabolic process, nonsense-mediated decay Source: UniProtKB-KW
  7. regulation of catalytic activity Source: GOC
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.

Names & Taxonomyi

Protein namesi
Recommended name:
mRNA-decapping enzyme 1B (EC:3.-.-.-)
Gene namesi
Name:DCP1B
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 12

Organism-specific databases

HGNCiHGNC:24451. DCP1B.

Subcellular locationi

Cytoplasm 1 Publication. Nucleus By similarity

GO - Cellular componenti

  1. cytoplasm Source: HPA
  2. cytoplasmic mRNA processing body Source: GO_Central
  3. cytosol Source: Reactome
  4. intracellular membrane-bounded organelle Source: HPA
  5. membrane Source: UniProtKB
  6. nucleus Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA134889143.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed3 Publications
Chaini2 – 617616mRNA-decapping enzyme 1BPRO_0000402799Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine3 Publications
Modified residuei191 – 1911Phosphotyrosine1 Publication
Modified residuei336 – 3361Phosphoserine1 Publication
Modified residuei448 – 4481Phosphoserine1 Publication
Modified residuei511 – 5111Phosphoserine1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ8IZD4.
PaxDbiQ8IZD4.
PRIDEiQ8IZD4.

PTM databases

PhosphoSiteiQ8IZD4.

Expressioni

Gene expression databases

BgeeiQ8IZD4.
CleanExiHS_DCP1B.
ExpressionAtlasiQ8IZD4. baseline and differential.
GenevestigatoriQ8IZD4.

Organism-specific databases

HPAiHPA039709.

Interactioni

Subunit structurei

Binds DCP1A. Part of a complex containing enzymes involved in mRNA decay, including DCP2, LSM1, LSM3 and CNOT6.

Binary interactionsi

WithEntry#Exp.IntActNotes
DCP2Q8IU603EBI-521595,EBI-521577
EDC3Q96F863EBI-521595,EBI-997311

Protein-protein interaction databases

BioGridi128216. 22 interactions.
DIPiDIP-31289N.
IntActiQ8IZD4. 13 interactions.
MINTiMINT-1190113.
STRINGi9606.ENSP00000280665.

Structurei

3D structure databases

ProteinModelPortaliQ8IZD4.
SMRiQ8IZD4. Positions 13-134, 573-606.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi252 – 26110Poly-Gln

Sequence similaritiesi

Belongs to the DCP1 family.Curated

Phylogenomic databases

eggNOGiNOG314415.
GeneTreeiENSGT00390000014855.
HOGENOMiHOG000090228.
HOVERGENiHBG103159.
InParanoidiQ8IZD4.
KOiK12611.
OMAiDEYTKCK.
OrthoDBiEOG75QR3K.
PhylomeDBiQ8IZD4.
TreeFamiTF320504.

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]

Sequences (2)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q8IZD4-1) [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
MAAVAAGGLV GKGRDISLAA LQRHDPYINR IVDVASQVAL YTFGHRANEW
60 70 80 90 100
EKTDVEGTLF VYTRSASPKH GFTIMNRLSM ENRTEPITKD LDFQLQDPFL
110 120 130 140 150
LYRNARLSIY GIWFYDKEEC QRIAELMKNL TQYEQLKAHQ GTGAGISPVI
160 170 180 190 200
LNSGEGKEVD ILRMLIKAKD EYTKCKTCSE PKKITSSSAI YDNPNLIKPI
210 220 230 240 250
PVKPSENQQQ RIPQPNQTLD PEPQHLSLTA LFGKQDKATC QETVEPPQTL
260 270 280 290 300
HQQQQQQQQQ QEKLPIRQGV VRSLSYEEPR RHSPPIEKQL CPAIQKLMVR
310 320 330 340 350
SADLHPLSEL PENRPCENGS THSAGEFFTG PVQPGSPHNI GTSRGVQNAS
360 370 380 390 400
RTQNLFEKLQ STPGAANKCD PSTPAPASSA ALNRSRAPTS VTPVAPGKGL
410 420 430 440 450
AQPPQAYFNG SLPPQTVGHQ AHGREQSTLP RQTLPISGSQ TGSSGVISPQ
460 470 480 490 500
ELLKKLQIVQ QEQQLHASNR PALAAKFPVL AQSSGTGKPL ESWINKTPNT
510 520 530 540 550
EQQTPLFQVI SPQRIPATAA PSLLMSPMVF AQPTSVPPKE RESGLLPVGG
560 570 580 590 600
QEPPAAATSL LLPIQSPEPS VITSSPLTKL QLQEALLYLI QNDDNFLNII
610
YEAYLFSMTQ AAMKKTM
Length:617
Mass (Da):67,723
Last modified:January 11, 2011 - v2
Checksum:i00B9D9592BAC3B64
GO
Isoform 2 (identifier: Q8IZD4-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-107: MAAVAAGGLV...PFLLYRNARL → MQIKV

Note: No experimental confirmation available.

Show »
Length:515
Mass (Da):56,273
Checksum:i200E0AAD38984003
GO

Sequence cautioni

The sequence AAH15368.2 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti251 – 2511H → HQ in AAN62764 (PubMed:12417715).Curated
Sequence conflicti251 – 2511H → HQ in BAB71118 (PubMed:14702039).Curated
Sequence conflicti251 – 2511H → HQ in AAH15368 (PubMed:15489334).Curated
Sequence conflicti251 – 2511H → HQ in AAH43437 (PubMed:15489334).Curated
Sequence conflicti426 – 4261Q → R in BAB71118 (PubMed:14702039).Curated
Sequence conflicti435 – 4351P → A in AAH43437 (PubMed:15489334).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti195 – 1951N → D.
Corresponds to variant rs12423058 [ dbSNP | Ensembl ].
VAR_047395
Natural varianti216 – 2161N → S.
Corresponds to variant rs34730825 [ dbSNP | Ensembl ].
VAR_047396
Natural varianti301 – 3011S → T.
Corresponds to variant rs2470449 [ dbSNP | Ensembl ].
VAR_047397
Natural varianti344 – 3441R → H.
Corresponds to variant rs715146 [ dbSNP | Ensembl ].
VAR_047398

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 107107MAAVA…RNARL → MQIKV in isoform 2. 1 PublicationVSP_056044Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY146652 mRNA. Translation: AAN62764.1.
AK056200 mRNA. Translation: BAB71118.1.
AK299203 mRNA. Translation: BAG61243.1.
AC005342 Genomic DNA. No translation available.
BC015368 mRNA. Translation: AAH15368.2. Different initiation.
BC043437 mRNA. Translation: AAH43437.1.
CCDSiCCDS31727.1. [Q8IZD4-1]
RefSeqiNP_689853.3. NM_152640.3. [Q8IZD4-1]
XP_006719034.1. XM_006718971.1. [Q8IZD4-1]
XP_006719035.1. XM_006718972.1. [Q8IZD4-2]
UniGeneiHs.130934.

Genome annotation databases

EnsembliENST00000280665; ENSP00000280665; ENSG00000151065. [Q8IZD4-1]
GeneIDi196513.
KEGGihsa:196513.
UCSCiuc001qjx.1. human. [Q8IZD4-1]

Polymorphism databases

DMDMi317373353.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY146652 mRNA. Translation: AAN62764.1.
AK056200 mRNA. Translation: BAB71118.1.
AK299203 mRNA. Translation: BAG61243.1.
AC005342 Genomic DNA. No translation available.
BC015368 mRNA. Translation: AAH15368.2. Different initiation.
BC043437 mRNA. Translation: AAH43437.1.
CCDSiCCDS31727.1. [Q8IZD4-1]
RefSeqiNP_689853.3. NM_152640.3. [Q8IZD4-1]
XP_006719034.1. XM_006718971.1. [Q8IZD4-1]
XP_006719035.1. XM_006718972.1. [Q8IZD4-2]
UniGeneiHs.130934.

3D structure databases

ProteinModelPortaliQ8IZD4.
SMRiQ8IZD4. Positions 13-134, 573-606.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi128216. 22 interactions.
DIPiDIP-31289N.
IntActiQ8IZD4. 13 interactions.
MINTiMINT-1190113.
STRINGi9606.ENSP00000280665.

PTM databases

PhosphoSiteiQ8IZD4.

Polymorphism databases

DMDMi317373353.

Proteomic databases

MaxQBiQ8IZD4.
PaxDbiQ8IZD4.
PRIDEiQ8IZD4.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000280665; ENSP00000280665; ENSG00000151065. [Q8IZD4-1]
GeneIDi196513.
KEGGihsa:196513.
UCSCiuc001qjx.1. human. [Q8IZD4-1]

Organism-specific databases

CTDi196513.
GeneCardsiGC12M002055.
H-InvDBHIX0201841.
HGNCiHGNC:24451. DCP1B.
HPAiHPA039709.
MIMi609843. gene.
neXtProtiNX_Q8IZD4.
PharmGKBiPA134889143.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG314415.
GeneTreeiENSGT00390000014855.
HOGENOMiHOG000090228.
HOVERGENiHBG103159.
InParanoidiQ8IZD4.
KOiK12611.
OMAiDEYTKCK.
OrthoDBiEOG75QR3K.
PhylomeDBiQ8IZD4.
TreeFamiTF320504.

Enzyme and pathway databases

ReactomeiREACT_20518. mRNA decay by 5' to 3' exoribonuclease.

Miscellaneous databases

ChiTaRSiDCP1B. human.
GeneWikiiDCP1B.
GenomeRNAii196513.
NextBioi35474354.
PROiQ8IZD4.
SOURCEiSearch...

Gene expression databases

BgeeiQ8IZD4.
CleanExiHS_DCP1B.
ExpressionAtlasiQ8IZD4. baseline and differential.
GenevestigatoriQ8IZD4.

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]
ProtoNetiSearch...

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(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), INTERACTION WITH DCP1A.
  2. "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] (ISOFORMS 1 AND 2).
    Tissue: Teratocarcinoma.
  3. "The finished DNA sequence of human chromosome 12."
    Scherer S.E., Muzny D.M., 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., Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K., Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D., Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J., Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A., Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M., Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I., Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A., Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G., Gibbs R.A.
    Nature 440:346-351(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. "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] (ISOFORM 1).
    Tissue: Testis and Uterus.
  5. "Cytoplasmic foci are sites of mRNA decay in human cells."
    Cougot N., Babajko S., Seraphin B.
    J. Cell Biol. 165:31-40(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, INTERACTION WITH DCP1A.
  6. "Immunoaffinity profiling of tyrosine phosphorylation in cancer cells."
    Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H., Zha X.-M., Polakiewicz R.D., Comb M.J.
    Nat. Biotechnol. 23:94-101(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-191, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  7. "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(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
  8. "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(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-448 AND SER-511, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  9. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  10. "Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
    Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
    Mol. Cell. Proteomics 11:M111.015131-M111.015131(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
  11. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
  12. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-336, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.

Entry informationi

Entry nameiDCP1B_HUMAN
AccessioniPrimary (citable) accession number: Q8IZD4
Secondary accession number(s): B4DRD1
, Q86XH9, Q96BP8, Q96MZ8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 1, 2005
Last sequence update: January 11, 2011
Last modified: March 4, 2015
This is version 108 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

Complete proteome, Reference proteome

Documents

  1. Human chromosome 12
    Human chromosome 12: 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. 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.