Q6P2E9 (EDC4_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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 names

Name:	EDC4
Synonyms:	HEDLS

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	1401 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	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). Ref.7
Subunit structure	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. Ref.7
Subcellular location	Cytoplasm › P-body. Nucleus Ref.1 Ref.6 Ref.7.
Sequence similarities	Belongs to the WD repeat EDC4 family. Contains 4 WD repeats.
Sequence caution	The sequence AAA21833.1 differs from that shown. Reason: Frameshift at position 1189. The sequence AAB51444.1 differs from that shown. Reason: Erroneous initiation. The sequence AAH53598.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
Cellular component	Cytoplasm Nucleus
Coding sequence diversity	Alternative splicing
Domain	Coiled coil Repeat WD repeat
PTM	Acetylation Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	exonucleolytic nuclear-transcribed mRNA catabolic process involved in deadenylation-dependent decay Traceable author statement. Source: Reactome gene expression Traceable author statement. Source: Reactome
Cellular_component	cytoplasmic mRNA processing body Inferred from direct assay PubMed 20826699. Source: MGI cytosol Traceable author statement. Source: Reactome nucleus Inferred from direct assay Ref.1. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
DCP2	Q8IU60	4	EBI-1006038,EBI-521577
EIF2AK2	P19525	2	EBI-1006038,EBI-640775

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q6P2E9-1)

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.

Isoform 2 (identifier: Q6P2E9-2)

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

Note: No experimental confirmation available.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 1401	1401	Enhancer of mRNA-decapping protein 4		PRO_0000278962
Regions
	Repeat	174 – 214	41	WD 1
	Repeat	230 – 277	48	WD 2
	Repeat	295 – 334	40	WD 3
	Repeat	342 – 393	52	WD 4
	Region	913 – 934	22	Sufficient for nuclear localization
	Coiled coil	954 – 1025	72	Potential
	Compositional bias	602 – 676	75	Ser-rich
Amino acid modifications
	Modified residue	125	1	N6-acetyllysine Ref.18
	Modified residue	693	1	Phosphothreonine Ref.10 Ref.17
	Modified residue	723	1	Phosphoserine Ref.15
	Modified residue	725	1	Phosphoserine Ref.15
	Modified residue	729	1	Phosphoserine Ref.12 Ref.14 Ref.16 Ref.17
	Modified residue	741	1	Phosphoserine Ref.11 Ref.17
	Modified residue	821	1	Phosphothreonine Ref.15
	Modified residue	844	1	Phosphoserine Ref.9 Ref.15
	Modified residue	871	1	Phosphoserine Ref.14 Ref.15
	Modified residue	875	1	Phosphoserine Ref.17
	Modified residue	879	1	Phosphoserine Ref.15 Ref.16 Ref.17
	Modified residue	887	1	Phosphoserine By similarity
	Modified residue	892	1	Phosphoserine Ref.17
Natural variations
	Alternative sequence	1 – 381	381	Missing in isoform 2.		VSP_023412
Experimental info
	Sequence conflict	271 – 272	2	ML → IV in AAA21833. Ref.1
	Sequence conflict	621	1	S → N in AAB51444. Ref.6
	Sequence conflict	1018 – 1019	2	QL → HW in AAA21833. Ref.1
	Sequence conflict	1160 – 1161	2	KA → NG in AAA21833. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified July 5, 2004. Version 1. Checksum: 0790BB8ADF488356	FASTA	1,401	151,661
	10 20 30 40 50 60 MASCASIDIE DATQHLRDIL KLDRPAGGPS AESPRPSSAY NGDLNGLLVP DPLCSGDSTS 70 80 90 100 110 120 ANKTGLRTMP PINLQEKQVI CLSGDDSSTC IGILAKEVEI VASSDSSISS KARGSNKVKI 130 140 150 160 170 180 QPVAKYDWEQ KYYYGNLIAV SNSFLAYAIR AANNGSAMVR VISVSTSERT LLKGFTGSVA 190 200 210 220 230 240 DLAFAHLNSP QLACLDEAGN LFVWRLALVN GKIQEEILVH IRQPEGTPLN HFRRIIWCPF 250 260 270 280 290 300 IPEESEDCCE ESSPTVALLH EDRAEVWDLD MLRSSHSTWP VDVSQIKQGF IVVKGHSTCL 310 320 330 340 350 360 SEGALSPDGT VLATASHDGY VKFWQIYIEG QDEPRCLHEW KPHDGRPLSC LLFCDNHKKQ 370 380 390 400 410 420 DPDVPFWRFL ITGADQNREL KMWCTVSWTC LQTIRFSPDI FSSVSVPPSL KVCLDLSAEY 430 440 450 460 470 480 LILSDVQRKV LYVMELLQNQ EEGHACFSSI SEFLLTHPVL SFGIQVVSRC RLRHTEVLPA 490 500 510 520 530 540 EEENDSLGAD GTHGAGAMES AAGVLIKLFC VHTKALQDVQ IRFQPQLNPD VVAPLPTHTA 550 560 570 580 590 600 HEDFTFGESR PELGSEGLGS AAHGSQPDLR RIVELPAPAD FLSLSSETKP KLMTPDAFMT 610 620 630 640 650 660 PSASLQQITA SPSSSSSGSS SSSSSSSSSL TAVSAMSSTS AVDPSLTRPP EELTLSPKLQ 670 680 690 700 710 720 LDGSLTMSSS GSLQASPRGL LPGLLPAPAD KLTPKGPGQV PTATSALSLE LQEVEPLGLP 730 740 750 760 770 780 QASPSRTRSP DVISSASTAL SQDIPEIASE ALSRGFGSSA PEGLEPDSMA SAASALHLLS 790 800 810 820 830 840 PRPRPGPELG PQLGLDGGPG DGDRHNTPSL LEAALTQEAS TPDSQVWPTA PDITRETCST 850 860 870 880 890 900 LAESPRNGLQ EKHKSLAFHR PPYHLLQQRD SQDASAEQSD HDDEVASLAS ASGGFGTKVP 910 920 930 940 950 960 APRLPAKDWK TKGSPRTSPK LKRKSKKDDG DAAMGSRLTE HQVAEPPEDW PALIWQQQRE 970 980 990 1000 1010 1020 LAELRHSQEE LLQRLCTQLE GLQSTVTGHV ERALETRHEQ EQRRLERALA EGQQRGGQLQ 1030 1040 1050 1060 1070 1080 EQLTQQLSQA LSSAVAGRLE RSIRDEIKKT VPPCVSRSLE PMAGQLSNSV ATKLTAVEGS 1090 1100 1110 1120 1130 1140 MKENISKLLK SKNLTDAIAR AAADTLQGPM QAAYREAFQS VVLPAFEKSC QAMFQQINDS 1150 1160 1170 1180 1190 1200 FRLGTQEYLQ QLESHMKSRK AREQEAREPV LAQLRGLVST LQSATEQMAA TVAGSVRAEV 1210 1220 1230 1240 1250 1260 QHQLHVAVGS LQESILAQVQ RIVKGEVSVA LKEQQAAVTS SIMQAMRSAA GTPVPSAHLD 1270 1280 1290 1300 1310 1320 CQAQQAHILQ LLQQGHLNQA FQQALTAADL NLVLYVCETV DPAQVFGQPP CPLSQPVLLS 1330 1340 1350 1360 1370 1380 LIQQLASDLG TRTDLKLSYL EEAVMHLDHS DPITRDHMGS VMAQVRQKLF QFLQAEPHNS 1390 1400 LGKAARRLSL MLHGLVTPSL P
	Isoform 2 [UniParc]. Checksum: 45357808C08C8555	FASTA	1,020	109,728
	10 20 30 40 50 60 MWCTVSWTCL QTIRFSPDIF SSVSVPPSLK VCLDLSAEYL ILSDVQRKVL YVMELLQNQE 70 80 90 100 110 120 EGHACFSSIS EFLLTHPVLS FGIQVVSRCR LRHTEVLPAE EENDSLGADG THGAGAMESA 130 140 150 160 170 180 AGVLIKLFCV HTKALQDVQI RFQPQLNPDV VAPLPTHTAH EDFTFGESRP ELGSEGLGSA 190 200 210 220 230 240 AHGSQPDLRR IVELPAPADF LSLSSETKPK LMTPDAFMTP SASLQQITAS PSSSSSGSSS 250 260 270 280 290 300 SSSSSSSSLT AVSAMSSTSA VDPSLTRPPE ELTLSPKLQL DGSLTMSSSG SLQASPRGLL 310 320 330 340 350 360 PGLLPAPADK LTPKGPGQVP TATSALSLEL QEVEPLGLPQ ASPSRTRSPD VISSASTALS 370 380 390 400 410 420 QDIPEIASEA LSRGFGSSAP EGLEPDSMAS AASALHLLSP RPRPGPELGP QLGLDGGPGD 430 440 450 460 470 480 GDRHNTPSLL EAALTQEAST PDSQVWPTAP DITRETCSTL AESPRNGLQE KHKSLAFHRP 490 500 510 520 530 540 PYHLLQQRDS QDASAEQSDH DDEVASLASA SGGFGTKVPA PRLPAKDWKT KGSPRTSPKL 550 560 570 580 590 600 KRKSKKDDGD AAMGSRLTEH QVAEPPEDWP ALIWQQQREL AELRHSQEEL LQRLCTQLEG 610 620 630 640 650 660 LQSTVTGHVE RALETRHEQE QRRLERALAE GQQRGGQLQE QLTQQLSQAL SSAVAGRLER 670 680 690 700 710 720 SIRDEIKKTV PPCVSRSLEP MAGQLSNSVA TKLTAVEGSM KENISKLLKS KNLTDAIARA 730 740 750 760 770 780 AADTLQGPMQ AAYREAFQSV VLPAFEKSCQ AMFQQINDSF RLGTQEYLQQ LESHMKSRKA 790 800 810 820 830 840 REQEAREPVL AQLRGLVSTL QSATEQMAAT VAGSVRAEVQ HQLHVAVGSL QESILAQVQR 850 860 870 880 890 900 IVKGEVSVAL KEQQAAVTSS IMQAMRSAAG TPVPSAHLDC QAQQAHILQL LQQGHLNQAF 910 920 930 940 950 960 QQALTAADLN LVLYVCETVD PAQVFGQPPC PLSQPVLLSL IQQLASDLGT RTDLKLSYLE 970 980 990 1000 1010 1020 EAVMHLDHSD PITRDHMGSV MAQVRQKLFQ FLQAEPHNSL GKAARRLSLM LHGLVTPSLP

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases 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: MASS SPECTROMETRY, INTERACTION WITH DCP1A; DCP1B; DCP2; DDX6 AND EDC3, SUBCELLULAR LOCATION, FUNCTION.
[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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[11]	"ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage." Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J. Science 316:1160-1166(2007) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-741, MASS SPECTROMETRY. 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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[15]	"A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-723; SER-725; THR-821; SER-844; SER-871 AND SER-879, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[16]	"Large-scale proteomics analysis of the human kinome." Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G., Mann M., Daub H. Mol. Cell. Proteomics 8:1751-1764(2009) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-729 AND SER-879, MASS SPECTROMETRY.
[17]	"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, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[18]	"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, MASS SPECTROMETRY.
[19]	"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.
[20]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[21]	"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].
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	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.
IPI	IPI00376317. IPI00641449.
PIR	I52882.
RefSeq	NP_055144.3. NM_014329.4.
UniGene	Hs.75682.
3D structure databases
ProteinModelPortal	Q6P2E9.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-31192N.
IntAct	Q6P2E9. 20 interactions.
STRING	9606.ENSP00000351811.
PTM databases
PhosphoSite	Q6P2E9.
Polymorphism databases
DMDM	74758241.
Proteomic databases
PaxDb	Q6P2E9.
PRIDE	Q6P2E9.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000358933; ENSP00000351811; ENSG00000038358.
GeneID	23644.
KEGG	hsa:23644.
UCSC	uc002eur.3. human.
Organism-specific databases
CTD	23644.
GeneCards	GC16P067906.
HGNC	HGNC:17157. EDC4.
HPA	HPA041164.
MIM	606030. gene.
neXtProt	NX_Q6P2E9.
PharmGKB	PA145148958.
GenAtlas	Search...
Phylogenomic databases
eggNOG	NOG270061.
HOVERGEN	HBG053855.
InParanoid	Q6P2E9.
KO	K12616.
OMA	ESPRNGL.
OrthoDB	EOG42JNQK.
PhylomeDB	Q6P2E9.
Enzyme and pathway databases
Reactome	REACT_21257. Metabolism of RNA. REACT_71. Gene Expression.
Gene expression databases
ArrayExpress	Q6P2E9.
Bgee	Q6P2E9.
CleanEx	HS_EDC4.
Genevestigator	Q6P2E9.
Family and domain databases
Gene3D	2.130.10.10. 1 hit.
InterPro	IPR015943. WD40/YVTN_repeat-like_dom. IPR001680. WD40_repeat. IPR017986. WD40_repeat_dom. [Graphical view]
SMART	SM00320. WD40. 3 hits. [Graphical view]
SUPFAM	SSF50978. WD40_like. 1 hit.
PROSITE	PS00678. WD_REPEATS_1. False negative. PS50082. WD_REPEATS_2. 1 hit. PS50294. WD_REPEATS_REGION. 1 hit. [Graphical view]
ProtoNet	Search...
Other
GenomeRNAi	23644.
NextBio	46453.
PMAP-CutDB	Q6P2E9.
SOURCE	Search...

Entry information

Entry name

EDC4_HUMAN

Accession

Primary (citable) accession number: Q6P2E9
Secondary accession number(s): A6NGM1 , A8K4T4, Q13025, Q13826, Q6ZR12, Q7Z6H7

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 6, 2007
Last sequence update:	July 5, 2004
Last modified:	May 1, 2013
This is version 100 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.