Q7L2J0 (MEPCE_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
7SK snRNA methylphosphate capping enzyme
Short name=MePCE
EC=2.1.1.-

Alternative name(s):
Bicoid-interacting protein 3 homolog
Short name=Bin3 homolog

Gene names

Name:	MEPCE
Synonyms:	BCDIN3

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	689 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	S-adenosyl-L-methionine-dependent methyltransferase that adds a methylphosphate cap at the 5'-end of 7SK snRNA, leading to stabilize it. Ref.9
Subunit structure	Component of the 7SK snRNP complex at least composed of P-TEFb (composed of CDK9 and CCNT1/cyclin-T1), HEXIM1, HEXIM2, MEPCE/BCDIN3, SART3 proteins and 7SK and U6 snRNAs. Ref.9
Tissue specificity	Expressed in chronic myeloid leukemia cells, adrenal gland, brain, cerebellum, kidney, lung, mammary gland and testis. Weakly or not expressed in other tissues. Ref.5
Sequence similarities	Belongs to the methyltransferase superfamily. Contains 1 Bin3-type SAM domain.
Sequence caution	The sequence AAF74767.1 differs from that shown. Reason: Erroneous initiation. The sequence AAH16396.1 differs from that shown. Reason: Erroneous initiation. The sequence BAA91040.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
Coding sequence diversity	Alternative splicing
Ligand	S-adenosyl-L-methionine
Molecular function	Methyltransferase Transferase
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	snRNA modification Inferred from direct assay Ref.9. Source: UniProtKB
Molecular_function	RNA methyltransferase activity Inferred from direct assay Ref.9. Source: UniProtKB S-adenosylmethionine-dependent methyltransferase activity Inferred from direct assay Ref.9. Source: UniProtKB
Complete GO annotation...

Alternative products

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

Isoform 1 (identifier: Q7L2J0-1)

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: Q7L2J0-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-469: Missing.

Note: No experimental confirmation available.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 689

689

7SK snRNA methylphosphate capping enzyme

PRO_0000289262

Regions

Domain

431 – 686

256

Bin3-type SAM

Region

451 – 453

3

S-adenosyl-L-methionine binding

Region

474 – 475

2

S-adenosyl-L-methionine binding

Region

559 – 560

2

S-adenosyl-L-methionine binding

Compositional bias

25 – 161

137

Gly-rich

Sites

Binding site

581

1

S-adenosyl-L-methionine; via carbonyl oxygen

Amino acid modifications

Modified residue

57

1

Phosphoserine Ref.11

Modified residue

60

1

Phosphoserine Ref.11 Ref.12

Modified residue

69

1

Phosphoserine Ref.7 Ref.11 Ref.12 Ref.15

Modified residue

101

1

Phosphoserine Ref.15

Modified residue

152

1

Phosphoserine Ref.11

Modified residue

175

1

Phosphoserine Ref.7 Ref.10 Ref.11

Modified residue

179

1

Phosphoserine Ref.10

Modified residue

213

1

Phosphothreonine Ref.12 Ref.14 Ref.15 Ref.17

Modified residue

216

1

Phosphoserine Ref.12 Ref.15

Modified residue

217

1

Phosphoserine Ref.8 Ref.12 Ref.15

Modified residue

254

1

Phosphoserine Ref.11 Ref.12 Ref.13 Ref.15

Modified residue

330

1

Phosphoserine Ref.11

Modified residue

390

1

Phosphoserine Ref.15

Natural variations

Alternative sequence

1 – 469

469

Missing in isoform 2.

VSP_044512

Experimental info

Sequence conflict

661

1

Y → N in BAG51598. Ref.1

Secondary structure

1

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689

Helix Strand Turn

Details...

Helix

432 – 435

4

Helix

439 – 441

3

Turn

442 – 444

3

Beta strand

445 – 451

7

Helix

456 – 464

9

Beta strand

468 – 475

8

Helix

477 – 485

9

Turn

549 – 552

4

Beta strand

553 – 557

5

Helix

565 – 568

4

Beta strand

575 – 582

8

Helix

584 – 606

23

Beta strand

607 – 616

10

Helix

620 – 624

5

Turn

625 – 628

4

Helix

631 – 639

9

Helix

644 – 646

3

Helix

647 – 651

5

Turn

654 – 656

3

Beta strand

660 – 664

5

Beta strand

678 – 682

5

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified July 5, 2004. Version 1. Checksum: CBB1D6BF144C923A	FASTA	689	74,355
	10 20 30 40 50 60 MIEMAAEKEP FLVPAPPPPL KDESGGGGGP TVPPHQEAAS GELRGGTERG PGRCAPSAGS 70 80 90 100 110 120 PAAAVGRESP GAAATSSSGP QAQQHRGGGP QAQSHGEARL SDPPGRAAPP DVGEERRGGG 130 140 150 160 170 180 GTELGPPAPP RPRNGYQPHR PPGGGGGKRR NSCNVGGGGG GFKHPAFKRR RRVNSDCDSV 190 200 210 220 230 240 LPSNFLLGGN IFDPLNLNSL LDEEVSRTLN AETPKSSPLP AKGRDPVEIL IPKDITDPLS 250 260 270 280 290 300 LNTCTDEGHV VLASPLKTGR KRHRHRGQHH QQQQAAGGSE SHPVPPTAPL TPLLHGEGAS 310 320 330 340 350 360 QQPRHRGQNR DAPQPYELNT AINCRDEVVS PLPSALQGPS GSLSAPPAAS VISAPPSSSS 370 380 390 400 410 420 RHRKRRRTSS KSEAGARGGG QGSKEKGRGS WGGRHHHHHP LPAAGFKKQQ RKFQYGNYCK 430 440 450 460 470 480 YYGYRNPSCE DGRLRVLKPE WFRGRDVLDL GCNVGHLTLS IACKWGPSRM VGLDIDSRLI 490 500 510 520 530 540 HSARQNIRHY LSEELRLPPQ TLEGDPGAEG EEGTTTVRKR SCFPASLTAS RGPIAAPQVP 550 560 570 580 590 600 LDGADTSVFP NNVVFVTGNY VLDRDDLVEA QTPEYDVVLC LSLTKWVHLN WGDEGLKRMF 610 620 630 640 650 660 RRIYRHLRPG GILVLEPQPW SSYGKRKTLT ETIYKNYYRI QLKPEQFSSY LTSPDVGFSS 670 680 YELVATPHNT SKGFQRPVYL FHKARSPSH
	Isoform 2 [UniParc]. Checksum: 799B7EB8BDF56524	FASTA	220	24,950
	10 20 30 40 50 60 MVGLDIDSRL IHSARQNIRH YLSEELRLPP QTLEGDPGAE GEEGTTTVRK RSCFPASLTA 70 80 90 100 110 120 SRGPIAAPQV PLDGADTSVF PNNVVFVTGN YVLDRDDLVE AQTPEYDVVL CLSLTKWVHL 130 140 150 160 170 180 NWGDEGLKRM FRRIYRHLRP GGILVLEPQP WSSYGKRKTL TETIYKNYYR IQLKPEQFSS 190 200 210 220 YLTSPDVGFS SYELVATPHN TSKGFQRPVY LFHKARSPSH

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"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] (ISOFORM 2), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 320-689 (ISOFORM 1). Tissue: Colon mucosa.
[2]	"The DNA sequence of human chromosome 7." Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H., Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A., Delehaunty K.D., Miner T.L. , Nash W.E., Cordes M., Du H., Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C., Latreille P., Miller N., Johnson D., Murray J., Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E., Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H., Wilson R.K. Nature 424:157-164(2003) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]	"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].
[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(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). Tissue: Brain.
[5]	"Identification and characterization of a novel gene encoding a SEREX antigen in chronic myeloid leukaemia." Rogers S.A., Bowen D.J., Ling M., Thomson P., Wang Z., Lim S.H. Br. J. Haematol. 119:112-114(2002) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 73-689, TISSUE SPECIFICITY.
[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(2005) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[7]	"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-69 AND SER-175, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[8]	"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-217, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[9]	"Systematic analysis of the protein interaction network for the human transcription machinery reveals the identity of the 7SK capping enzyme." Jeronimo C., Forget D., Bouchard A., Li Q., Chua G., Poitras C., Therien C., Bergeron D., Bourassa S., Greenblatt J., Chabot B., Poirier G.G., Hughes T.R., Blanchette M., Price D.H., Coulombe B. Mol. Cell 27:262-274(2007) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, IDENTIFICATION IN THE 7SK SNRNP COMPLEX, CATALYTIC ACTIVITY.
[10]	"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-175 AND SER-179, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[11]	"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-57; SER-60; SER-69; SER-152; SER-175; SER-254 AND SER-330, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[12]	"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-60; SER-69; THR-213; SER-216; SER-217 AND SER-254, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[13]	"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-254, MASS SPECTROMETRY.
[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 THR-213, MASS SPECTROMETRY. 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-69; SER-101; THR-213; SER-216; SER-217; SER-254 AND SER-390, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[16]	"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].
[17]	"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 THR-213, MASS SPECTROMETRY.
[18]	"Methyltransferase domain of human bicoid-interacting protein 3 homolog (drosophila)." Structural genomics consortium (SGC) Submitted (MAY-2009) to the PDB data bank Cited for: X-RAY CRYSTALLOGRAPHY (2.65 ANGSTROMS) OF 400-689 IN COMPLEX WITH SUBSTRATE.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AK055964 mRNA. Translation: BAG51598.1.
AC092849 Genomic DNA. No translation available.
CH471091 Genomic DNA. Translation: EAW76534.1.
CH471091 Genomic DNA. Translation: EAW76535.1.
CH471091 Genomic DNA. Translation: EAW76536.1.
CH236956 Genomic DNA. Translation: EAL23834.1.
BC000556 mRNA. Translation: AAH00556.2.
BC016396 mRNA. Translation: AAH16396.1. Different initiation.
BC018935 mRNA. Translation: AAH18935.2.
AF264752 Genomic DNA. Translation: AAF74767.1. Different initiation.
AK000264 mRNA. Translation: BAA91040.1. Different initiation.

IPI

IPI00021320.

RefSeq

NP_001181919.1. NM_001194990.1.
NP_001181920.1. NM_001194991.1.
NP_001181921.1. NM_001194992.1.
NP_062552.2. NM_019606.5.

UniGene

Hs.178011.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
3G07	X-ray	2.65	A/B/C/D/E/F	400-689	[»]

ProteinModelPortal

Q7L2J0.

ModBase

Search...

Protein-protein interaction databases

IntAct

Q7L2J0. 7 interactions.

STRING

9606.ENSP00000308546.

PTM databases

PhosphoSite

Q7L2J0.

Polymorphism databases

DMDM

74758999.

Proteomic databases

PaxDb

Q7L2J0.

PeptideAtlas

Q7L2J0.

PRIDE

Q7L2J0.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000310512; ENSP00000308546; ENSG00000146834.
ENST00000414441; ENSP00000400875; ENSG00000146834.
ENST00000425355; ENSP00000400045; ENSG00000146834.

GeneID

56257.

KEGG

hsa:56257.

UCSC

uc003uuw.3. human.

Organism-specific databases

CTD

56257.

GeneCards

GC07P100026.

HGNC

HGNC:20247. MEPCE.

HPA

CAB026384.

MIM

611478. gene.

neXtProt

NX_Q7L2J0.

PharmGKB

PA162395768.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG322893.

HOGENOM

HOG000113562.

HOVERGEN

HBG099856.

InParanoid

Q7L2J0.

KO

K15190.

OMA

EKEPFLV.

OrthoDB

EOG4GHZPB.

PhylomeDB

Q7L2J0.

Gene expression databases

ArrayExpress

Q7L2J0.

Bgee

Q7L2J0.

CleanEx

HS_MEPCE.

Genevestigator

Q7L2J0.

Family and domain databases

InterPro

IPR010675. Bin3.
IPR024160. BIN3_SAM-bd_dom.
[Graphical view]

Pfam

PF06859. Bin3. 1 hit.
[Graphical view]

PROSITE

PS51515. BIN3_SAM. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

ChiTaRS

MEPCE. human.

EvolutionaryTrace

Q7L2J0.

GenomeRNAi

56257.

NextBio

61905.

SOURCE

Search...

Entry information

Entry name

MEPCE_HUMAN

Accession

Primary (citable) accession number: Q7L2J0
Secondary accession number(s): B3KP86, D6W5V7, Q9NPD4

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 29, 2007
Last sequence update:	July 5, 2004
Last modified:	May 1, 2013
This is version 98 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.