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Q7L2J0

- MEPCE_HUMAN

UniProt

Q7L2J0 - MEPCE_HUMAN

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Protein

7SK snRNA methylphosphate capping enzyme

Gene

MEPCE

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

Functioni

S-adenosyl-L-methionine-dependent methyltransferase that adds a methylphosphate cap at the 5'-end of 7SK snRNA, leading to stabilize it.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei581 – 5811S-adenosyl-L-methionine; via carbonyl oxygen

GO - Molecular functioni

  1. poly(A) RNA binding Source: UniProtKB
  2. RNA methyltransferase activity Source: UniProtKB
  3. S-adenosylmethionine-dependent methyltransferase activity Source: UniProtKB

GO - Biological processi

  1. negative regulation of chromatin binding Source: Ensembl
  2. negative regulation of transcription from RNA polymerase II promoter Source: Ensembl
  3. positive regulation of G1/S transition of mitotic cell cycle Source: Ensembl
  4. RNA methylation Source: UniProtKB
  5. snRNA metabolic process Source: UniProtKB
  6. snRNA modification Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Methyltransferase, Transferase

Keywords - Ligandi

S-adenosyl-L-methionine

Names & Taxonomyi

Protein namesi
Recommended name:
7SK snRNA methylphosphate capping enzyme (EC:2.1.1.-)
Short name:
MePCE
Alternative name(s):
Bicoid-interacting protein 3 homolog
Short name:
Bin3 homolog
Gene namesi
Name:MEPCE
Synonyms:BCDIN3
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 7

Organism-specific databases

HGNCiHGNC:20247. MEPCE.

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA162395768.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 6896897SK snRNA methylphosphate capping enzymePRO_0000289262Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionine1 Publication
Modified residuei57 – 571Phosphoserine1 Publication
Modified residuei60 – 601Phosphoserine2 Publications
Modified residuei69 – 691Phosphoserine4 Publications
Modified residuei101 – 1011Phosphoserine1 Publication
Modified residuei152 – 1521Phosphoserine1 Publication
Modified residuei175 – 1751Phosphoserine3 Publications
Modified residuei179 – 1791Phosphoserine1 Publication
Modified residuei213 – 2131Phosphothreonine4 Publications
Modified residuei216 – 2161Phosphoserine2 Publications
Modified residuei217 – 2171Phosphoserine3 Publications
Modified residuei254 – 2541Phosphoserine4 Publications
Modified residuei330 – 3301Phosphoserine1 Publication
Modified residuei390 – 3901Phosphoserine1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ7L2J0.
PaxDbiQ7L2J0.
PeptideAtlasiQ7L2J0.
PRIDEiQ7L2J0.

PTM databases

PhosphoSiteiQ7L2J0.

Expressioni

Tissue specificityi

Expressed in chronic myeloid leukemia cells, adrenal gland, brain, cerebellum, kidney, lung, mammary gland and testis. Weakly or not expressed in other tissues.1 Publication

Gene expression databases

BgeeiQ7L2J0.
CleanExiHS_MEPCE.
GenevestigatoriQ7L2J0.

Organism-specific databases

HPAiCAB026384.
HPA042912.
HPA051587.

Interactioni

Subunit structurei

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.2 Publications

Protein-protein interaction databases

BioGridi121122. 182 interactions.
IntActiQ7L2J0. 8 interactions.
STRINGi9606.ENSP00000308546.

Structurei

Secondary structure

1
689
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi432 – 4354
Helixi439 – 4413
Turni442 – 4443
Beta strandi445 – 4517
Helixi456 – 4649
Beta strandi468 – 4758
Helixi477 – 4859
Turni549 – 5524
Beta strandi553 – 5575
Helixi565 – 5684
Beta strandi575 – 5828
Helixi584 – 60623
Beta strandi607 – 61610
Helixi620 – 6245
Turni625 – 6284
Helixi631 – 6399
Helixi644 – 6463
Helixi647 – 6515
Turni654 – 6563
Beta strandi660 – 6645
Beta strandi678 – 6825

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3G07X-ray2.65A/B/C/D/E/F400-689[»]
ProteinModelPortaliQ7L2J0.
SMRiQ7L2J0. Positions 431-685.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ7L2J0.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini431 – 686256Bin3-type SAMPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni451 – 4533S-adenosyl-L-methionine binding
Regioni474 – 4752S-adenosyl-L-methionine binding
Regioni559 – 5602S-adenosyl-L-methionine binding

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi25 – 161137Gly-richAdd
BLAST

Sequence similaritiesi

Belongs to the methyltransferase superfamily.Curated
Contains 1 Bin3-type SAM domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiNOG322893.
GeneTreeiENSGT00390000015611.
HOGENOMiHOG000113562.
HOVERGENiHBG099856.
InParanoidiQ7L2J0.
KOiK15190.
OMAiHRGQNRD.
OrthoDBiEOG78M02C.
PhylomeDBiQ7L2J0.
TreeFamiTF324061.

Family and domain databases

Gene3Di3.40.50.150. 2 hits.
InterProiIPR010675. Bin3.
IPR024160. BIN3_SAM-bd_dom.
IPR029063. SAM-dependent_MTases-like.
[Graphical view]
PfamiPF06859. Bin3. 1 hit.
[Graphical view]
SUPFAMiSSF53335. SSF53335. 2 hits.
PROSITEiPS51515. BIN3_SAM. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q7L2J0-1) [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
MIEMAAEKEP FLVPAPPPPL KDESGGGGGP TVPPHQEAAS GELRGGTERG
60 70 80 90 100
PGRCAPSAGS PAAAVGRESP GAAATSSSGP QAQQHRGGGP QAQSHGEARL
110 120 130 140 150
SDPPGRAAPP DVGEERRGGG GTELGPPAPP RPRNGYQPHR PPGGGGGKRR
160 170 180 190 200
NSCNVGGGGG GFKHPAFKRR RRVNSDCDSV LPSNFLLGGN IFDPLNLNSL
210 220 230 240 250
LDEEVSRTLN AETPKSSPLP AKGRDPVEIL IPKDITDPLS LNTCTDEGHV
260 270 280 290 300
VLASPLKTGR KRHRHRGQHH QQQQAAGGSE SHPVPPTAPL TPLLHGEGAS
310 320 330 340 350
QQPRHRGQNR DAPQPYELNT AINCRDEVVS PLPSALQGPS GSLSAPPAAS
360 370 380 390 400
VISAPPSSSS RHRKRRRTSS KSEAGARGGG QGSKEKGRGS WGGRHHHHHP
410 420 430 440 450
LPAAGFKKQQ RKFQYGNYCK YYGYRNPSCE DGRLRVLKPE WFRGRDVLDL
460 470 480 490 500
GCNVGHLTLS IACKWGPSRM VGLDIDSRLI HSARQNIRHY LSEELRLPPQ
510 520 530 540 550
TLEGDPGAEG EEGTTTVRKR SCFPASLTAS RGPIAAPQVP LDGADTSVFP
560 570 580 590 600
NNVVFVTGNY VLDRDDLVEA QTPEYDVVLC LSLTKWVHLN WGDEGLKRMF
610 620 630 640 650
RRIYRHLRPG GILVLEPQPW SSYGKRKTLT ETIYKNYYRI QLKPEQFSSY
660 670 680
LTSPDVGFSS YELVATPHNT SKGFQRPVYL FHKARSPSH
Length:689
Mass (Da):74,355
Last modified:July 5, 2004 - v1
Checksum:iCBB1D6BF144C923A
GO
Isoform 2 (identifier: Q7L2J0-2) [UniParc]FASTAAdd to Basket

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

Note: No experimental confirmation available.

Show »
Length:220
Mass (Da):24,950
Checksum:i799B7EB8BDF56524
GO

Sequence cautioni

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.

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti661 – 6611Y → N in BAG51598. (PubMed:14702039)Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 469469Missing in isoform 2. 1 PublicationVSP_044512Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSiCCDS55136.1. [Q7L2J0-2]
CCDS5693.1. [Q7L2J0-1]
RefSeqiNP_001181919.1. NM_001194990.1. [Q7L2J0-2]
NP_001181920.1. NM_001194991.1. [Q7L2J0-2]
NP_001181921.1. NM_001194992.1. [Q7L2J0-2]
NP_062552.2. NM_019606.5. [Q7L2J0-1]
UniGeneiHs.178011.

Genome annotation databases

EnsembliENST00000310512; ENSP00000308546; ENSG00000146834. [Q7L2J0-1]
ENST00000414441; ENSP00000400875; ENSG00000146834. [Q7L2J0-2]
GeneIDi56257.
KEGGihsa:56257.
UCSCiuc003uuv.3. human. [Q7L2J0-2]
uc003uuw.3. human. [Q7L2J0-1]

Polymorphism databases

DMDMi74758999.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSi CCDS55136.1. [Q7L2J0-2 ]
CCDS5693.1. [Q7L2J0-1 ]
RefSeqi NP_001181919.1. NM_001194990.1. [Q7L2J0-2 ]
NP_001181920.1. NM_001194991.1. [Q7L2J0-2 ]
NP_001181921.1. NM_001194992.1. [Q7L2J0-2 ]
NP_062552.2. NM_019606.5. [Q7L2J0-1 ]
UniGenei Hs.178011.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
3G07 X-ray 2.65 A/B/C/D/E/F 400-689 [» ]
ProteinModelPortali Q7L2J0.
SMRi Q7L2J0. Positions 431-685.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 121122. 182 interactions.
IntActi Q7L2J0. 8 interactions.
STRINGi 9606.ENSP00000308546.

PTM databases

PhosphoSitei Q7L2J0.

Polymorphism databases

DMDMi 74758999.

Proteomic databases

MaxQBi Q7L2J0.
PaxDbi Q7L2J0.
PeptideAtlasi Q7L2J0.
PRIDEi Q7L2J0.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000310512 ; ENSP00000308546 ; ENSG00000146834 . [Q7L2J0-1 ]
ENST00000414441 ; ENSP00000400875 ; ENSG00000146834 . [Q7L2J0-2 ]
GeneIDi 56257.
KEGGi hsa:56257.
UCSCi uc003uuv.3. human. [Q7L2J0-2 ]
uc003uuw.3. human. [Q7L2J0-1 ]

Organism-specific databases

CTDi 56257.
GeneCardsi GC07P100026.
HGNCi HGNC:20247. MEPCE.
HPAi CAB026384.
HPA042912.
HPA051587.
MIMi 611478. gene.
neXtProti NX_Q7L2J0.
PharmGKBi PA162395768.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG322893.
GeneTreei ENSGT00390000015611.
HOGENOMi HOG000113562.
HOVERGENi HBG099856.
InParanoidi Q7L2J0.
KOi K15190.
OMAi HRGQNRD.
OrthoDBi EOG78M02C.
PhylomeDBi Q7L2J0.
TreeFami TF324061.

Miscellaneous databases

ChiTaRSi MEPCE. human.
EvolutionaryTracei Q7L2J0.
GenomeRNAii 56257.
NextBioi 61905.
PROi Q7L2J0.
SOURCEi Search...

Gene expression databases

Bgeei Q7L2J0.
CleanExi HS_MEPCE.
Genevestigatori Q7L2J0.

Family and domain databases

Gene3Di 3.40.50.150. 2 hits.
InterProi IPR010675. Bin3.
IPR024160. BIN3_SAM-bd_dom.
IPR029063. SAM-dependent_MTases-like.
[Graphical view ]
Pfami PF06859. Bin3. 1 hit.
[Graphical view ]
SUPFAMi SSF53335. SSF53335. 2 hits.
PROSITEi PS51515. BIN3_SAM. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  12. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-60; SER-69; THR-213; SER-216; SER-217 AND SER-254, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  13. "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 MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  14. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-254, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  15. "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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  16. "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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  17. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  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 THR-213, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  19. "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.

Entry informationi

Entry nameiMEPCE_HUMAN
AccessioniPrimary (citable) accession number: Q7L2J0
Secondary accession number(s): B3KP86, D6W5V7, Q9NPD4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 29, 2007
Last sequence update: July 5, 2004
Last modified: October 29, 2014
This is version 113 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

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 7
    Human chromosome 7: 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