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Q6P2E9

- EDC4_HUMAN

UniProt

Q6P2E9 - EDC4_HUMAN

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Protein

Enhancer of mRNA-decapping protein 4

Gene

EDC4

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

Functioni

In the process of mRNA degradation, seems to play a role in mRNA decapping. Component of a complex containing DCP2 and DCP1A which functions in decapping of ARE-containing mRNAs. Promotes complex formation between DCP1A and DCP2. Enhances the catalytic activity of DCP2 (in vitro).1 Publication

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. RNA metabolic process Source: Reactome
Complete GO annotation...

Enzyme and pathway databases

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

Names & Taxonomyi

Protein namesi
Recommended name:
Enhancer of mRNA-decapping protein 4
Alternative name(s):
Autoantigen Ge-1
Autoantigen RCD-8
Human enhancer of decapping large subunit
Short name:
Hedls
Gene namesi
Name:EDC4
Synonyms:HEDLS
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 16

Organism-specific databases

HGNCiHGNC:17157. EDC4.

Subcellular locationi

GO - Cellular componenti

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

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA145148958.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 14011400Enhancer of mRNA-decapping protein 4PRO_0000278962Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine1 Publication
Modified residuei125 – 1251N6-acetyllysine1 Publication
Modified residuei693 – 6931Phosphothreonine2 Publications
Modified residuei723 – 7231Phosphoserine1 Publication
Modified residuei725 – 7251Phosphoserine1 Publication
Modified residuei729 – 7291Phosphoserine4 Publications
Modified residuei741 – 7411Phosphoserine2 Publications
Modified residuei821 – 8211Phosphothreonine1 Publication
Modified residuei844 – 8441Phosphoserine2 Publications
Modified residuei871 – 8711Phosphoserine2 Publications
Modified residuei875 – 8751Phosphoserine1 Publication
Modified residuei879 – 8791Phosphoserine3 Publications
Modified residuei887 – 8871PhosphoserineBy similarity
Modified residuei892 – 8921Phosphoserine1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ6P2E9.
PaxDbiQ6P2E9.
PRIDEiQ6P2E9.

PTM databases

PhosphoSiteiQ6P2E9.

Miscellaneous databases

PMAP-CutDBQ6P2E9.

Expressioni

Gene expression databases

BgeeiQ6P2E9.
CleanExiHS_EDC4.
ExpressionAtlasiQ6P2E9. baseline.
GenevestigatoriQ6P2E9.

Organism-specific databases

HPAiHPA041164.

Interactioni

Subunit structurei

Part of a decapping complex consisting of DCP1A, DCP2, EDC3, EDC4 and probably DDX6. Part of a complex consisting of DCP1A, EDC3, EDC4 and DDX6. Part of a complex consisting of DCP1B, EDC3, EDC4 and DDX6. Interacts with DCP2. Interacts with RC3H1 (By similarity).By similarity

Binary interactionsi

WithEntry#Exp.IntActNotes
COASYQ130573EBI-1006038,EBI-745967
DCP2Q8IU604EBI-1006038,EBI-521577
EIF2AK2P195252EBI-1006038,EBI-640775

Protein-protein interaction databases

BioGridi117171. 42 interactions.
DIPiDIP-31192N.
IntActiQ6P2E9. 23 interactions.
MINTiMINT-5005241.
STRINGi9606.ENSP00000351811.

Structurei

3D structure databases

ProteinModelPortaliQ6P2E9.
SMRiQ6P2E9. Positions 1268-1397.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati174 – 21441WD 1Add
BLAST
Repeati230 – 27748WD 2Add
BLAST
Repeati295 – 33440WD 3Add
BLAST
Repeati342 – 39352WD 4Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni913 – 93422Sufficient for nuclear localizationAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili954 – 102572Sequence AnalysisAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi602 – 67675Ser-richAdd
BLAST

Sequence similaritiesi

Belongs to the WD repeat EDC4 family.Curated
Contains 4 WD repeats.PROSITE-ProRule annotation

Keywords - Domaini

Coiled coil, Repeat, WD repeat

Phylogenomic databases

eggNOGiNOG270061.
GeneTreeiENSGT00510000047791.
HOVERGENiHBG053855.
InParanoidiQ6P2E9.
KOiK12616.
OMAiESPRNGL.
OrthoDBiEOG72JWFV.
PhylomeDBiQ6P2E9.
TreeFamiTF350715.

Family and domain databases

Gene3Di2.130.10.10. 1 hit.
InterProiIPR015943. WD40/YVTN_repeat-like_dom.
IPR001680. WD40_repeat.
IPR017986. WD40_repeat_dom.
[Graphical view]
SMARTiSM00320. WD40. 3 hits.
[Graphical view]
SUPFAMiSSF50978. SSF50978. 1 hit.
PROSITEiPS50082. WD_REPEATS_2. 1 hit.
PS50294. WD_REPEATS_REGION. 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. Align

Isoform 1 (identifier: Q6P2E9-1) [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
MASCASIDIE DATQHLRDIL KLDRPAGGPS AESPRPSSAY NGDLNGLLVP
60 70 80 90 100
DPLCSGDSTS ANKTGLRTMP PINLQEKQVI CLSGDDSSTC IGILAKEVEI
110 120 130 140 150
VASSDSSISS KARGSNKVKI QPVAKYDWEQ KYYYGNLIAV SNSFLAYAIR
160 170 180 190 200
AANNGSAMVR VISVSTSERT LLKGFTGSVA DLAFAHLNSP QLACLDEAGN
210 220 230 240 250
LFVWRLALVN GKIQEEILVH IRQPEGTPLN HFRRIIWCPF IPEESEDCCE
260 270 280 290 300
ESSPTVALLH EDRAEVWDLD MLRSSHSTWP VDVSQIKQGF IVVKGHSTCL
310 320 330 340 350
SEGALSPDGT VLATASHDGY VKFWQIYIEG QDEPRCLHEW KPHDGRPLSC
360 370 380 390 400
LLFCDNHKKQ DPDVPFWRFL ITGADQNREL KMWCTVSWTC LQTIRFSPDI
410 420 430 440 450
FSSVSVPPSL KVCLDLSAEY LILSDVQRKV LYVMELLQNQ EEGHACFSSI
460 470 480 490 500
SEFLLTHPVL SFGIQVVSRC RLRHTEVLPA EEENDSLGAD GTHGAGAMES
510 520 530 540 550
AAGVLIKLFC VHTKALQDVQ IRFQPQLNPD VVAPLPTHTA HEDFTFGESR
560 570 580 590 600
PELGSEGLGS AAHGSQPDLR RIVELPAPAD FLSLSSETKP KLMTPDAFMT
610 620 630 640 650
PSASLQQITA SPSSSSSGSS SSSSSSSSSL TAVSAMSSTS AVDPSLTRPP
660 670 680 690 700
EELTLSPKLQ LDGSLTMSSS GSLQASPRGL LPGLLPAPAD KLTPKGPGQV
710 720 730 740 750
PTATSALSLE LQEVEPLGLP QASPSRTRSP DVISSASTAL SQDIPEIASE
760 770 780 790 800
ALSRGFGSSA PEGLEPDSMA SAASALHLLS PRPRPGPELG PQLGLDGGPG
810 820 830 840 850
DGDRHNTPSL LEAALTQEAS TPDSQVWPTA PDITRETCST LAESPRNGLQ
860 870 880 890 900
EKHKSLAFHR PPYHLLQQRD SQDASAEQSD HDDEVASLAS ASGGFGTKVP
910 920 930 940 950
APRLPAKDWK TKGSPRTSPK LKRKSKKDDG DAAMGSRLTE HQVAEPPEDW
960 970 980 990 1000
PALIWQQQRE LAELRHSQEE LLQRLCTQLE GLQSTVTGHV ERALETRHEQ
1010 1020 1030 1040 1050
EQRRLERALA EGQQRGGQLQ EQLTQQLSQA LSSAVAGRLE RSIRDEIKKT
1060 1070 1080 1090 1100
VPPCVSRSLE PMAGQLSNSV ATKLTAVEGS MKENISKLLK SKNLTDAIAR
1110 1120 1130 1140 1150
AAADTLQGPM QAAYREAFQS VVLPAFEKSC QAMFQQINDS FRLGTQEYLQ
1160 1170 1180 1190 1200
QLESHMKSRK AREQEAREPV LAQLRGLVST LQSATEQMAA TVAGSVRAEV
1210 1220 1230 1240 1250
QHQLHVAVGS LQESILAQVQ RIVKGEVSVA LKEQQAAVTS SIMQAMRSAA
1260 1270 1280 1290 1300
GTPVPSAHLD CQAQQAHILQ LLQQGHLNQA FQQALTAADL NLVLYVCETV
1310 1320 1330 1340 1350
DPAQVFGQPP CPLSQPVLLS LIQQLASDLG TRTDLKLSYL EEAVMHLDHS
1360 1370 1380 1390 1400
DPITRDHMGS VMAQVRQKLF QFLQAEPHNS LGKAARRLSL MLHGLVTPSL

P
Length:1,401
Mass (Da):151,661
Last modified:July 5, 2004 - v1
Checksum:i0790BB8ADF488356
GO
Isoform 2 (identifier: Q6P2E9-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-381: Missing.

Note: No experimental confirmation available.

Show »
Length:1,020
Mass (Da):109,728
Checksum:i45357808C08C8555
GO

Sequence cautioni

The sequence AAA21833.1 differs from that shown. Reason: Frameshift at position 1189. Curated
The sequence AAB51444.1 differs from that shown. Reason: Erroneous initiation. Curated
The sequence AAH53598.1 differs from that shown. Reason: Erroneous initiation. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti271 – 2722ML → IV in AAA21833. (PubMed:7520377)Curated
Sequence conflicti621 – 6211S → N in AAB51444. (PubMed:9067524)Curated
Sequence conflicti1018 – 10192QL → HW in AAA21833. (PubMed:7520377)Curated
Sequence conflicti1160 – 11612KA → NG in AAA21833. (PubMed:7520377)Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 381381Missing in isoform 2. 1 PublicationVSP_023412Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L26339 mRNA. Translation: AAA21833.1. Frameshift.
AK128582 mRNA. No translation available.
AK291049 mRNA. Translation: BAF83738.1.
AC040162 Genomic DNA. No translation available.
CH471092 Genomic DNA. Translation: EAW83183.1.
BC043616 mRNA. Translation: AAH43616.1.
BC053598 mRNA. Translation: AAH53598.1. Different initiation.
BC064567 mRNA. Translation: AAH64567.1.
U17474 mRNA. Translation: AAB51444.1. Different initiation.
CCDSiCCDS10849.1. [Q6P2E9-1]
PIRiI52882.
RefSeqiNP_055144.3. NM_014329.4. [Q6P2E9-1]
UniGeneiHs.75682.

Genome annotation databases

EnsembliENST00000358933; ENSP00000351811; ENSG00000038358. [Q6P2E9-1]
GeneIDi23644.
KEGGihsa:23644.
UCSCiuc002eur.3. human. [Q6P2E9-1]

Polymorphism databases

DMDMi74758241.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L26339 mRNA. Translation: AAA21833.1 . Frameshift.
AK128582 mRNA. No translation available.
AK291049 mRNA. Translation: BAF83738.1 .
AC040162 Genomic DNA. No translation available.
CH471092 Genomic DNA. Translation: EAW83183.1 .
BC043616 mRNA. Translation: AAH43616.1 .
BC053598 mRNA. Translation: AAH53598.1 . Different initiation.
BC064567 mRNA. Translation: AAH64567.1 .
U17474 mRNA. Translation: AAB51444.1 . Different initiation.
CCDSi CCDS10849.1. [Q6P2E9-1 ]
PIRi I52882.
RefSeqi NP_055144.3. NM_014329.4. [Q6P2E9-1 ]
UniGenei Hs.75682.

3D structure databases

ProteinModelPortali Q6P2E9.
SMRi Q6P2E9. Positions 1268-1397.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 117171. 42 interactions.
DIPi DIP-31192N.
IntActi Q6P2E9. 23 interactions.
MINTi MINT-5005241.
STRINGi 9606.ENSP00000351811.

PTM databases

PhosphoSitei Q6P2E9.

Polymorphism databases

DMDMi 74758241.

Proteomic databases

MaxQBi Q6P2E9.
PaxDbi Q6P2E9.
PRIDEi Q6P2E9.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000358933 ; ENSP00000351811 ; ENSG00000038358 . [Q6P2E9-1 ]
GeneIDi 23644.
KEGGi hsa:23644.
UCSCi uc002eur.3. human. [Q6P2E9-1 ]

Organism-specific databases

CTDi 23644.
GeneCardsi GC16P067906.
HGNCi HGNC:17157. EDC4.
HPAi HPA041164.
MIMi 606030. gene.
neXtProti NX_Q6P2E9.
PharmGKBi PA145148958.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG270061.
GeneTreei ENSGT00510000047791.
HOVERGENi HBG053855.
InParanoidi Q6P2E9.
KOi K12616.
OMAi ESPRNGL.
OrthoDBi EOG72JWFV.
PhylomeDBi Q6P2E9.
TreeFami TF350715.

Enzyme and pathway databases

Reactomei REACT_20518. mRNA decay by 5' to 3' exoribonuclease.

Miscellaneous databases

ChiTaRSi EDC4. human.
GenomeRNAii 23644.
NextBioi 46453.
PMAP-CutDB Q6P2E9.
PROi Q6P2E9.
SOURCEi Search...

Gene expression databases

Bgeei Q6P2E9.
CleanExi HS_EDC4.
ExpressionAtlasi Q6P2E9. baseline.
Genevestigatori Q6P2E9.

Family and domain databases

Gene3Di 2.130.10.10. 1 hit.
InterProi IPR015943. WD40/YVTN_repeat-like_dom.
IPR001680. WD40_repeat.
IPR017986. WD40_repeat_dom.
[Graphical view ]
SMARTi SM00320. WD40. 3 hits.
[Graphical view ]
SUPFAMi SSF50978. SSF50978. 1 hit.
PROSITEi PS50082. WD_REPEATS_2. 1 hit.
PS50294. WD_REPEATS_REGION. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "The immunoreactive region in a novel autoantigen contains a nuclear localization sequence."
    Bloch D.B., Rabkina D., Quertermous T., Bloch K.D.
    Clin. Immunol. Immunopathol. 72:380-389(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SUBCELLULAR LOCATION.
  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(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
    Tissue: Trachea.
  3. "The sequence and analysis of duplication-rich human chromosome 16."
    Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G., Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E., Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J.
    , Buckingham J.M., Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C., Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M., Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M., Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E., Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H., Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y., Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J., Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D., Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S., Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A., Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M., Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H., Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A., Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J., DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J., Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M., Myers R.M., Rubin E.M., Pennacchio L.A.
    Nature 432:988-994(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. 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] (ISOFORM 1).
    Tissue: Duodenum, Skin and Testis.
  6. "Cytoplasmic detection of a novel protein containing a nuclear localization sequence by human autoantibodies."
    Garcia-Lozano J.R., Gonzalez-Escribano M.F., Wichmann I., Nunez-Roldan A.
    Clin. Exp. Immunol. 107:501-506(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 421-1401 (ISOFORMS 1/2), SUBCELLULAR LOCATION.
  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 DCP1A; DCP1B; DCP2; DDX6 AND EDC3, SUBCELLULAR LOCATION, FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY.
  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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  9. "A probability-based approach for high-throughput protein phosphorylation analysis and site localization."
    Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.
    Nat. Biotechnol. 24:1285-1292(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-844, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  10. "Improved titanium dioxide enrichment of phosphopeptides from HeLa cells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra."
    Yu L.R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.
    J. Proteome Res. 6:4150-4162(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-693, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  11. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-741, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic kidney.
  12. "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-729, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  13. "Phosphorylation analysis of primary human T lymphocytes using sequential IMAC and titanium oxide enrichment."
    Carrascal M., Ovelleiro D., Casas V., Gay M., Abian J.
    J. Proteome Res. 7:5167-5176(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: T-cell.
  14. "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-729 AND SER-871, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  15. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-723; SER-725; THR-821; SER-844; SER-871 AND SER-879, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  16. "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: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
  17. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-729 AND SER-879, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  18. "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 THR-693; SER-729; SER-741; SER-875; SER-879 AND SER-892, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  19. "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-125, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  20. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  21. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  22. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiEDC4_HUMAN
AccessioniPrimary (citable) accession number: Q6P2E9
Secondary accession number(s): A6NGM1
, A8K4T4, Q13025, Q13826, Q6ZR12, Q7Z6H7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 6, 2007
Last sequence update: July 5, 2004
Last modified: November 26, 2014
This is version 116 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

Complete proteome, Reference proteome

Documents

  1. Human chromosome 16
    Human chromosome 16: 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. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3