O60942 (MCE1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
mRNA-capping enzyme

Alternative name(s):
HCAP1
HCE

Including the following 2 domains:

1. Polynucleotide 5'-triphosphatase
   EC=3.1.3.33
   Alternative name(s):
   mRNA 5'-triphosphatase
   Short name=TPase
2. mRNA guanylyltransferase
   EC=2.7.7.50
   Alternative name(s):
   GTP--RNA guanylyltransferase
   Short name=GTase

Gene names

Name:	RNGTT
Synonyms:	CAP1A

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

General annotation (Comments)

Function	Bifunctional mRNA-capping enzyme exhibiting RNA 5'-triphosphatase activity in the N-terminal part and mRNA guanylyltransferase activity in the C-terminal part. Catalyzes the first two steps of cap formation: by removing the gamma-phosphate from the 5'-triphosphate end of nascent mRNA to yield a diphosphate end, and by transferring the gmp moiety of GTP to the 5'-diphosphate terminus.
Catalytic activity	A 5'-phosphopolynucleotide + H2O = a polynucleotide + phosphate. GTP + (5')pp-Pur-mRNA = diphosphate + G(5')ppp-Pur-mRNA.
Subunit structure	Interacts with SUPT5H and RNMT. Interacts with HIV-1 Tat. Ref.7 Ref.8 Ref.9
Subcellular location	Nucleus By similarity.
Tissue specificity	Isoform 1 and isoform 4 (at a lesser extent) are expressed in cerebrum, cerebellum, thyroid, lung, heart, liver, kidney, spleen, large intestine, testis, skin and muscle.
Miscellaneous	Isoform 2 to isoform 4 lack mRNA 5'-guanylyltransferase activity due to disruptions of the GTase domain.
Sequence similarities	In the N-terminal section; belongs to the non-receptor class of the protein-tyrosine phosphatase family. In the C-terminal section; belongs to the eukaryotic GTase family.

Ontologies

Keywords
Biological process	Host-virus interaction mRNA capping mRNA processing
Cellular component	Nucleus
Coding sequence diversity	Alternative splicing Polymorphism
Ligand	GTP-binding Nucleotide-binding
Molecular function	Hydrolase Nucleotidyltransferase Transferase
Technical term	3D-structure Complete proteome Multifunctional enzyme Reference proteome
Gene Ontology (GO)
Biological_process	7-methylguanosine mRNA capping Traceable author statement. Source: Reactome peptidyl-tyrosine dephosphorylation Inferred from electronic annotation. Source: GOC transcription from RNA polymerase II promoter Traceable author statement. Source: Reactome viral reproduction Traceable author statement. Source: Reactome virus-host interaction Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	nucleoplasm Traceable author statement. Source: Reactome
Molecular_function	GTP binding Inferred from electronic annotation. Source: UniProtKB-KW mRNA guanylyltransferase activity Traceable author statement Ref.3. Source: ProtInc polynucleotide 5'-phosphatase activity Inferred from electronic annotation. Source: EC protein tyrosine phosphatase activity Inferred from electronic annotation. Source: InterPro protein tyrosine/serine/threonine phosphatase activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Alternative products

This entry describes 4 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: O60942-1)

Also known as: HCE1; HCAP1A;

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: O60942-2)

Also known as: HCE1A;

The sequence of this isoform differs from the canonical sequence as follows:
     424-446: Missing.

Isoform 3 (identifier: O60942-3)

Also known as: HCE1B;

The sequence of this isoform differs from the canonical sequence as follows:
     424-446: Missing.
     481-597: Missing.

Isoform 4 (identifier: O60942-4)

Also known as: HCAP1B;

The sequence of this isoform differs from the canonical sequence as follows:
     504-597: TKELKQYDNK...PPPKRPRPLT → CLFIFSVLFL...KISCSSTLGG

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 597

597

mRNA-capping enzyme

PRO_0000210108

Regions

Region

1 – 212

212

TPase

Region

229 – 597

369

GTase

Compositional bias

195 – 205

11

Asp/Glu-rich

Sites

Active site

126

1

For RNA 5'-triphosphatase activity By similarity

Active site

294

1

N6-GMP-lysine intermediate

Natural variations

Alternative sequence

424 – 446

23

Missing in isoform 2 and isoform 3.

VSP_003202

Alternative sequence

481 – 597

117

Missing in isoform 3.

VSP_003203

Alternative sequence

504 – 597

94

TKELK…PRPLT → CLFIFSVLFLDVLLSGIHQN LANNNQHIKISCSSTLGG in isoform 4.

VSP_003204

Natural variant

594

1

R → H. Ref.6
Corresponds to variant rs17856595 [ dbSNP | Ensembl ].

VAR_046481

Experimental info

Mutagenesis

294

1

K → A: Loss of GTase activity.

Mutagenesis

299

1

R → A: Loss of GTase activity.

Mutagenesis

345

1

E → A: Loss of GTase activity.

Mutagenesis

458

1

K → A: Loss of GTase activity.

Mutagenesis

460

1

K → A: Loss of GTase activity.

Sequence conflict

30

1

M → I in AAB91559. Ref.1

Sequence conflict

212

1

P → T in AAH19954. Ref.6

Sequence conflict

484

1

Q → P in AAB91559. Ref.1

Secondary structure

1

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597

Helix Strand Turn

Details...

Turn

21 – 23

3

Beta strand

24 – 27

4

Helix

33 – 38

6

Helix

41 – 43

3

Helix

47 – 57

11

Beta strand

60 – 66

7

Helix

77 – 80

4

Turn

81 – 83

3

Beta strand

85 – 88

4

Helix

100 – 110

11

Beta strand

120 – 125

6

Beta strand

127 – 130

4

Helix

131 – 143

13

Helix

149 – 159

11

Helix

167 – 177

11

Helix

180 – 182

3

Beta strand

232 – 235

4

Beta strand

241 – 243

3

Helix

247 – 261

15

Beta strand

265 – 267

3

Beta strand

270 – 275

6

Turn

278 – 280

3

Helix

281 – 285

5

Beta strand

289 – 295

7

Beta strand

298 – 304

7

Beta strand

306 – 308

3

Beta strand

310 – 314

5

Beta strand

319 – 324

6

Beta strand

339 – 351

13

Beta strand

354 – 367

14

Helix

372 – 374

3

Helix

377 – 387

11

Helix

389 – 394

6

Turn

395 – 397

3

Beta strand

398 – 401

4

Turn

403 – 405

3

Beta strand

406 – 412

7

Helix

418 – 424

7

Beta strand

437 – 446

10

Beta strand

451 – 459

9

Helix

462 – 464

3

Beta strand

466 – 476

11

Beta strand

484 – 490

7

Beta strand

498 – 501

4

Helix

507 – 509

3

Beta strand

512 – 520

9

Beta strand

523 – 529

7

Helix

539 – 550

12

Helix

555 – 563

9

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 (HCE1) (HCAP1A) [UniParc]. Last modified August 1, 1998. Version 1. Checksum: 51CEEC1B190603DE	FASTA	597	68,557
	10 20 30 40 50 60 MAHNKIPPRW LNCPRRGQPV AGRFLPLKTM LGPRYDSQVA EENRFHPSML SNYLKSLKVK 70 80 90 100 110 120 MGLLVDLTNT SRFYDRNDIE KEGIKYIKLQ CKGHGECPTT ENTETFIRLC ERFNERNPPE 130 140 150 160 170 180 LIGVHCTHGF NRTGFLICAF LVEKMDWSIE AAVATFAQAR PPGIYKGDYL KELFRRYGDI 190 200 210 220 230 240 EEAPPPPLLP DWCFEDDEDE DEDEDGKKES EPGSSASFGK RRKERLKLGA IFLEGVTVKG 250 260 270 280 290 300 VTQVTTQPKL GEVQQKCHQF CGWEGSGFPG AQPVSMDKQN IKLLDLKPYK VSWKADGTRY 310 320 330 340 350 360 MMLIDGTNEV FMIDRDNSVF HVSNLEFPFR KDLRMHLSNT LLDGEMIIDR VNGQAVPRYL 370 380 390 400 410 420 IYDIIKFNSQ PVGDCDFNVR LQCIEREIIS PRHEKMKTGL IDKTQEPFSV RNKPFFDICT 430 440 450 460 470 480 SRKLLEGNFA KEVSHEMDGL IFQPTGKYKP GRCDDILKWK PPSLNSVDFR LKITRMGGEG 490 500 510 520 530 540 LLPQNVGLLY VGGYERPFAQ IKVTKELKQY DNKIIECKFE NNSWVFMRQR TDKSFPNAYN 550 560 570 580 590 TAMAVCNSIS NPVTKEMLFE FIDRCTAASQ GQKRKHHLDP DTELMPPPPP KRPRPLT
	Isoform 2 (HCE1A) [UniParc]. Checksum: CFE64E51F6F88232	FASTA	574	66,042
	10 20 30 40 50 60 MAHNKIPPRW LNCPRRGQPV AGRFLPLKTM LGPRYDSQVA EENRFHPSML SNYLKSLKVK 70 80 90 100 110 120 MGLLVDLTNT SRFYDRNDIE KEGIKYIKLQ CKGHGECPTT ENTETFIRLC ERFNERNPPE 130 140 150 160 170 180 LIGVHCTHGF NRTGFLICAF LVEKMDWSIE AAVATFAQAR PPGIYKGDYL KELFRRYGDI 190 200 210 220 230 240 EEAPPPPLLP DWCFEDDEDE DEDEDGKKES EPGSSASFGK RRKERLKLGA IFLEGVTVKG 250 260 270 280 290 300 VTQVTTQPKL GEVQQKCHQF CGWEGSGFPG AQPVSMDKQN IKLLDLKPYK VSWKADGTRY 310 320 330 340 350 360 MMLIDGTNEV FMIDRDNSVF HVSNLEFPFR KDLRMHLSNT LLDGEMIIDR VNGQAVPRYL 370 380 390 400 410 420 IYDIIKFNSQ PVGDCDFNVR LQCIEREIIS PRHEKMKTGL IDKTQEPFSV RNKPFFDICT 430 440 450 460 470 480 SRKKYKPGRC DDILKWKPPS LNSVDFRLKI TRMGGEGLLP QNVGLLYVGG YERPFAQIKV 490 500 510 520 530 540 TKELKQYDNK IIECKFENNS WVFMRQRTDK SFPNAYNTAM AVCNSISNPV TKEMLFEFID 550 560 570 RCTAASQGQK RKHHLDPDTE LMPPPPPKRP RPLT
	Isoform 3 (HCE1B) [UniParc]. Checksum: 4F3B52CA4F6CC56B	FASTA	457	52,533
	10 20 30 40 50 60 MAHNKIPPRW LNCPRRGQPV AGRFLPLKTM LGPRYDSQVA EENRFHPSML SNYLKSLKVK 70 80 90 100 110 120 MGLLVDLTNT SRFYDRNDIE KEGIKYIKLQ CKGHGECPTT ENTETFIRLC ERFNERNPPE 130 140 150 160 170 180 LIGVHCTHGF NRTGFLICAF LVEKMDWSIE AAVATFAQAR PPGIYKGDYL KELFRRYGDI 190 200 210 220 230 240 EEAPPPPLLP DWCFEDDEDE DEDEDGKKES EPGSSASFGK RRKERLKLGA IFLEGVTVKG 250 260 270 280 290 300 VTQVTTQPKL GEVQQKCHQF CGWEGSGFPG AQPVSMDKQN IKLLDLKPYK VSWKADGTRY 310 320 330 340 350 360 MMLIDGTNEV FMIDRDNSVF HVSNLEFPFR KDLRMHLSNT LLDGEMIIDR VNGQAVPRYL 370 380 390 400 410 420 IYDIIKFNSQ PVGDCDFNVR LQCIEREIIS PRHEKMKTGL IDKTQEPFSV RNKPFFDICT 430 440 450 SRKKYKPGRC DDILKWKPPS LNSVDFRLKI TRMGGEG
	Isoform 4 (HCAP1B) [UniParc]. Checksum: DF795898785EC2D4	FASTA	541	61,705
	10 20 30 40 50 60 MAHNKIPPRW LNCPRRGQPV AGRFLPLKTM LGPRYDSQVA EENRFHPSML SNYLKSLKVK 70 80 90 100 110 120 MGLLVDLTNT SRFYDRNDIE KEGIKYIKLQ CKGHGECPTT ENTETFIRLC ERFNERNPPE 130 140 150 160 170 180 LIGVHCTHGF NRTGFLICAF LVEKMDWSIE AAVATFAQAR PPGIYKGDYL KELFRRYGDI 190 200 210 220 230 240 EEAPPPPLLP DWCFEDDEDE DEDEDGKKES EPGSSASFGK RRKERLKLGA IFLEGVTVKG 250 260 270 280 290 300 VTQVTTQPKL GEVQQKCHQF CGWEGSGFPG AQPVSMDKQN IKLLDLKPYK VSWKADGTRY 310 320 330 340 350 360 MMLIDGTNEV FMIDRDNSVF HVSNLEFPFR KDLRMHLSNT LLDGEMIIDR VNGQAVPRYL 370 380 390 400 410 420 IYDIIKFNSQ PVGDCDFNVR LQCIEREIIS PRHEKMKTGL IDKTQEPFSV RNKPFFDICT 430 440 450 460 470 480 SRKLLEGNFA KEVSHEMDGL IFQPTGKYKP GRCDDILKWK PPSLNSVDFR LKITRMGGEG 490 500 510 520 530 540 LLPQNVGLLY VGGYERPFAQ IKVCLFIFSV LFLDVLLSGI HQNLANNNQH IKISCSSTLG G

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Mammalian capping enzyme complements mutant Saccharomyces cerevisiae lacking mRNA guanylyltransferase and selectively binds the elongating form of RNA polymerase II." Yue Z., Maldonado E., Pillutla R., Cho H., Reinberg D., Shatkin A.J. Proc. Natl. Acad. Sci. U.S.A. 94:12898-12903(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[2]	"Isolation and characterization of a human cDNA for mRNA 5'-capping enzyme." Yamada-Okabe T., Doi R., Shimmi O., Arisawa M., Yamada-Okabe H. Nucleic Acids Res. 26:1700-1706(1998) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2 AND 3), MUTAGENESIS.
[3]	"Cloning and characterization of two human cDNAs encoding the mRNA capping enzyme." Tsukamoto T., Shibagaki Y., Murakoshi T., Suzuki M., Nakamura A., Gotoh H., Mizumoto K. Biochem. Biophys. Res. Commun. 243:101-108(1998) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 4). Tissue: Colon adenocarcinoma.
[4]	"The DNA sequence and analysis of human chromosome 6." Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D. , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S. Nature 425:805-811(2003) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]	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 (SEP-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]	"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], VARIANT HIS-594. Tissue: Skin.
[7]	"Recombinant human mRNA cap methyltransferase binds capping enzyme/RNA polymerase IIo complexes." Pillutla R.C., Yue Z., Maldonado E., Shatkin A.J. J. Biol. Chem. 273:21443-21446(1998) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH RNMT.
[8]	"Transcription elongation factor hSPT5 stimulates mRNA capping." Wen Y., Shatkin A.J. Genes Dev. 13:1774-1779(1999) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH SUPT5H.
[9]	"HIV-1 Tat protein interacts with mammalian capping enzyme and stimulates capping of TAR RNA." Chiu Y.-L., Coronel E., Ho C.K., Shuman S., Rana T.M. J. Biol. Chem. 276:12959-12966(2001) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH HIV-1 TAT.
[10]	"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].
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AF025654 mRNA. Translation: AAB91559.1.
AB009022 mRNA. Translation: BAA25894.1.
AB009023 mRNA. Translation: BAA25895.1.
AB009024 mRNA. Translation: BAA25896.1.
AB012142 mRNA. Translation: BAA25198.1.
AB012143 mRNA. Translation: BAA25199.1.
AL079342 , AL096868, AL133408, AL445530 Genomic DNA. Translation: CAI22537.1.
AL096868 , AL079342, AL133408, AL445530 Genomic DNA. Translation: CAI21547.1.
AL133408 , AL079342, AL096868, AL445530 Genomic DNA. Translation: CAI21542.1.
AL445530 , AL079342, AL096868, AL133408 Genomic DNA. Translation: CAI22048.1.
CH471051 Genomic DNA. Translation: EAW48566.1.
CH471051 Genomic DNA. Translation: EAW48567.1.
CH471051 Genomic DNA. Translation: EAW48569.1.
CH471051 Genomic DNA. Translation: EAW48570.1.
BC019954 mRNA. Translation: AAH19954.1.

IPI

IPI00000104.
IPI00219610.
IPI00219611.
IPI00219612.

PIR

JC5936.
JC5937.

RefSeq

NP_003791.3. NM_003800.3.

UniGene

Hs.567378.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2C46	X-ray	1.60	A/B/C/D	1-219	[»]
3S24	X-ray	3.01	A/B/C/D/E/F/G	229-567	[»]

ProteinModelPortal

O60942.

ModBase

Search...

Protein-protein interaction databases

IntAct

O60942. 1 interaction.

STRING

9606.ENSP00000358497.

PTM databases

PhosphoSite

O60942.

Proteomic databases

PaxDb

O60942.

PRIDE

O60942.

Protocols and materials databases

DNASU

8732.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000265607; ENSP00000265607; ENSG00000111880.
ENST00000369485; ENSP00000358497; ENSG00000111880.

GeneID

8732.

KEGG

hsa:8732.

UCSC

uc003pmr.2. human.
uc003pms.2. human.

Organism-specific databases

CTD

8732.

GeneCards

GC06M089376.

HGNC

HGNC:10073. RNGTT.

HPA

HPA003750.

MIM

603512. gene.

neXtProt

NX_O60942.

PharmGKB

PA34446.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG5226.

HOVERGEN

HBG006332.

InParanoid

O60942.

KO

K13917.

OMA

FFDIHAS.

OrthoDB

EOG4NP733.

PhylomeDB

O60942.

Enzyme and pathway databases

BRENDA

2.7.7.50. 2681.

Reactome

REACT_116125. Disease.
REACT_1675. mRNA Processing.
REACT_1788. Transcription.
REACT_71. Gene Expression.

Gene expression databases

ArrayExpress

O60942.

Bgee

O60942.

CleanEx

HS_RNGTT.

Genevestigator

O60942.

GermOnline

ENSG00000111880. Homo sapiens.

Family and domain databases

Gene3D

2.40.50.140. 1 hit.

InterPro

IPR000340. Dual-sp_phosphatase_cat-dom.
IPR017074. mRNA_cap_enz_bifunc.
IPR001339. mRNA_cap_enzyme.
IPR013846. mRNA_cap_enzyme_C.
IPR012340. NA-bd_OB-fold.
IPR000387. Tyr/Dual-sp_Pase.
IPR016130. Tyr_Pase_AS.
[Graphical view]

Pfam

PF00782. DSPc. 1 hit.
PF03919. mRNA_cap_C. 1 hit.
PF01331. mRNA_cap_enzyme. 1 hit.
[Graphical view]

PIRSF

PIRSF036958. mRNA_capping_HCE. 1 hit.

SUPFAM

SSF50249. Nucleic_acid_OB. 1 hit.

PROSITE

PS00383. TYR_PHOSPHATASE_1. 1 hit.
PS50056. TYR_PHOSPHATASE_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

ChiTaRS

RNGTT. human.

EvolutionaryTrace

O60942.

GenomeRNAi

8732.

NextBio

32757.

SOURCE

Search...

Entry information

Entry name

MCE1_HUMAN

Accession

Primary (citable) accession number: O60942
Secondary accession number(s): E1P513 , E1P514, O43483, O60257, O60351, Q5TCW8, Q8WUM8

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 30, 2000
Last sequence update:	August 1, 1998
Last modified:	May 1, 2013
This is version 129 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.