Reviewed, UniProtKB/Swiss-Prot Q09161 (NCBP1_HUMAN)

Names and origin

Protein names

Recommended name:
    Nuclear cap-binding protein subunit 1
Alternative name(s):
    80 kDa nuclear cap-binding protein
      Short name=NCBP 80 kDa subunit
      Short name=CBP80

Gene names

Name:	NCBP1
Synonyms:	CBP80, NCBP

Organism

Homo sapiens (Human) [Complete proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	790 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Component of the cap-binding complex (CBC), which binds co-transcriptionally to the 5' cap of pre-mRNAs and is involved in various processes such as pre-mRNA splicing, translation regulation, nonsense-mediated mRNA decay, RNA-mediated gene silencing (RNAi) by microRNAs (miRNAs) and mRNA export. The CBC complex is involved in mRNA export from the nucleus via its interaction with THOC4/ALY, leading to the recruitment of the mRNA export machinery to the 5' end of mRNA and to mRNA export in a 5' to 3' direction through the nuclear pore. The CBC complex is also involved in mediating U snRNA and intronless mRNAs export from the nucleus. The CBC complex is essential for a pioneer round of mRNA translation, before steady state translation when the CBC complex is replaced by cytoplasmic cap-binding protein eIF4E. The pioneer round of mRNA translation mediated by the CBC complex plays a central role in nonsense-mediated mRNA decay (NMD), NMD only taking place in mRNAs bound to the CBC complex, but not on eIF4E-bound mRNAs. The CBC complex enhances NMD in mRNAs containing at least one exon-junction complex (EJC) via its interaction with UPF1, promoting the interaction between UPF1 and UPF2. The CBC complex is also involved in 'failsafe' NMD, which is independent of the EJC complex, while it does not participate in Staufen-mediated mRNA decay (SMD). During cell proliferation, the CBC complex is also involved in microRNAs (miRNAs) biogenesis via its interaction with SRRT/ARS2 and is required for miRNA-mediated RNA interference. The CBC complex also acts as a negative regulator of PARN, thereby acting as an inhibitor of mRNA deadenylation. In the CBC complex, NCBP1/CBP80 does not bind directly capped RNAs (m7GpppG-capped RNA) but is required to stabilize the movement of the N-terminal loop of NCBP2/CBP20 and lock the CBC into a high affinity cap-binding state with the cap structure. Ref.1 Ref.7 Ref.10 Ref.13 Ref.14 Ref.15 Ref.17 Ref.18 Ref.20 Ref.21 Ref.24 Ref.25
Subunit structure	Component of the nuclear cap-binding complex (CBC), a heterodimer composed of NCBP1/CBP80 and NCBP2/CBP20 that interacts with m7GpppG-capped RNA. Found in a U snRNA export complex with RNUXA/PHAX, NCBP1/CBP80, NCBP2/CBP20, RAN, XPO1 and m7G-capped RNA. Interaction with RNUXA/PHAX By similarity. Heterodimer with NCBP2. Identified in a mRNP granule complex, at least composed of ACTB, ACTN4, DHX9, ERG, HNRNPA1, HNRNPA2B1, HNRNPAB, HNRNPD, HNRNPL, HNRNPR, HNRNPU, HSPA1, HSPA8, IGF2BP1, ILF2, ILF3, NCBP1, NCL, PABPC1, PABPC4, PABPN1, RPLP0, RPS3, RPS3A, RPS4X, RPS8, RPS9, SYNCRIP, TROVE2, YBX1 and untranslated mRNAs. Is part of the exon junction complex (EJC) containing NCBP1, NCBP2, RNPS1, RBM8A, SRRM1, NXF1, UPF3B, UPF2, THOC4 and/or REFBP2. Interacts with SRRT/ARS2, EIF4G2, IGF2BP1, HNRNPF, HNRNPH1, KIAA0427/CTIF, PARN, RNASEN, UPF1 and THOC4. May interact with EIF4G1; the interaction is however controversial since it is reported by Ref.11, Ref.13 and Ref.14, but is not observed by Ref.25. Ref.13 Ref.14 Ref.15 Ref.17 Ref.18 Ref.25 Ref.8 Ref.11 Ref.12 Ref.19
Subcellular location	Nucleus. Cytoplasm. Note: Localized in cytoplasmic mRNP granules containing untranslated mRNAs. Ref.25 Ref.19
Sequence similarities	Belongs to the NCBP1 family. Contains 1 MIF4G domain.
Sequence caution	The sequence CAI12863.1 differs from that shown. Reason: Erroneous gene model prediction.

Ontologies

Keywords
Biological process	Nonsense-mediated mRNA decay RNA-mediated gene silencing Translation regulation Transport mRNA capping mRNA processing mRNA splicing mRNA transport
Cellular component	Cytoplasm Nucleus
Domain	Coiled coil
PTM	Acetylation Phosphoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing
Gene Ontology (GO)
Biological process	gene silencing by RNA Inferred from electronic annotation. Source: UniProtKB-KW mRNA capping Ref.30 Inferred from direct assay. Source: UniProtKB mRNA cleavage Inferred from direct assay. Source: UniProtKB mRNA export from nucleus Ref.17 Inferred from mutant phenotype. Source: UniProtKB nuclear-transcribed mRNA catabolic process, nonsense-mediated decay Ref.10 Ref.20 Ref.21 Inferred from direct assay. Source: UniProtKB positive regulation of mRNA 3'-end processing Inferred from direct assay. Source: UniProtKB regulation of translational initiation Ref.10 Inferred from direct assay. Source: UniProtKB spliceosomal snRNP assembly Inferred from Experiment. Source: Reactome
Cellular component	cytosol Inferred from Experiment. Source: Reactome mRNA cap binding complex Ref.7 Ref.30 Inferred from direct assay. Source: UniProtKB nucleoplasm Ref.2 Inferred from Experiment. Source: Reactome ribonucleoprotein complex Ref.19 Inferred from direct assay. Source: UniProtKB
Molecular function	RNA cap binding Ref.1 Traceable author statement. Source: ProtInc protein binding Ref.8 Ref.14 Ref.17 Ref.19 Ref.25 Ref.29 Inferred from physical interaction. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
EIF4G3	O43432	1	EBI-464743,EBI-464766
NCBP2	P52298	2	EBI-464743,EBI-464729
POLDIP3	Q9BY77	1	EBI-464743,EBI-1776152
RPS6	P62753	2	EBI-464743,EBI-356625

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 790

790

Nuclear cap-binding protein subunit 1

PRO_0000089364

Regions

Domain

28 – 240

213

MIF4G

Coiled coil

643 – 713

71

Potential

Motif

3 – 20

18

Nuclear localization signal Potential

Amino acid modifications

Modified residue

7

1

Phosphoserine; by RPS6KB1 Ref.9

Modified residue

21

1

Phosphothreonine; by RPS6KB1 Ref.9 Ref.22

Modified residue

22

1

Phosphoserine; by RPS6KB1 Ref.9 Ref.22 Ref.26

Modified residue

204

1

N6-acetyllysine Ref.27

Modified residue

674

1

Phosphoserine Ref.16

Modified residue

698

1

N6-acetyllysine Ref.27

Experimental info

Mutagenesis

7

1

S → A: Reduced phosphorylation by RPS6KB1. Abolishes phosphorylation by RPS6KB1; when associated with 21-A-A-22. Ref.9

Mutagenesis

17 – 18

2

KR → AA: Abolishes nuclear localization and phosphorylation by RPS6KB1.

Mutagenesis

21 – 22

2

TS → A: Reduced phosphorylation by RPS6KB1. Abolishes phosphorylation by RPS6KB1; when associated with A-7.

Sequence conflict

80

1

P → S in BAG35665. Ref.3

Sequence conflict

159

1

E → D in BAD92470. Ref.4

Sequence conflict

674

1

S → G in BAG35665. Ref.3

Secondary structure

1

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790

Helix Strand Turn

Details...

Helix

30 – 37

8

Helix

46 – 78

33

Helix

80 – 82

3

Helix

83 – 96

14

Helix

98 – 117

20

Helix

121 – 136

16

Helix

142 – 153

12

Helix

154 – 157

4

Helix

163 – 174

12

Helix

177 – 205

29

Helix

211 – 214

4

Beta strand

216 – 218

3

Helix

228 – 241

14

Turn

242 – 244

3

Helix

252 – 256

5

Helix

257 – 261

5

Helix

294 – 296

3

Helix

309 – 325

17

Helix

329 – 337

9

Helix

347 – 359

13

Helix

369 – 382

14

Turn

384 – 386

3

Helix

387 – 400

14

Helix

401 – 404

4

Helix

407 – 422

16

Turn

423 – 426

4

Helix

430 – 436

7

Helix

444 – 458

15

Helix

462 – 468

7

Helix

471 – 476

6

Beta strand

488 – 490

3

Beta strand

493 – 495

3

Helix

498 – 509

12

Helix

514 – 520

7

Helix

521 – 523

3

Helix

541 – 551

11

Helix

553 – 555

3

Helix

559 – 568

10

Helix

570 – 576

7

Helix

580 – 594

15

Helix

598 – 610

13

Helix

616 – 624

9

Helix

626 – 628

3

Helix

635 – 650

16

Turn

652 – 701

50

Helix

703 – 730

28

Helix

738 – 753

16

Helix

755 – 758

4

Helix

759 – 761

3

Helix

762 – 768

7

Helix

776 – 787

12

Sequences

	Sequence		Length	Mass (Da)
	Q09161-1 [UniParc]. Last modified October 1, 1996. Version 1. Checksum: F10DE7B9D16FDA0B	FASTA	790	91,839
	10 20 30 40 50 60 MSRRRHSDEN DGGQPHKRRK TSDANETEDH LESLICKVGE KSACSLESNL EGLAGVLEAD 70 80 90 100 110 120 LPNYKSKILR LLCTVARLLP EKLTIYTTLV GLLNARNYNF GGEFVEAMIR QLKESLKANN 130 140 150 160 170 180 YNEAVYLVRF LSDLVNCHVI AAPSMVAMFE NFVSVTQEED VPQVRRDWYV YAFLSSLPWV 190 200 210 220 230 240 GKELYEKKDA EMDRIFANTE SYLKRRQKTH VPMLQVWTAD KPHPQEEYLD CLWAQIQKLK 250 260 270 280 290 300 KDRWQERHIL RPYLAFDSIL CEALQHNLPP FTPPPHTEDS VYPMPRVIFR MFDYTDDPEG 310 320 330 340 350 360 PVMPGSHSVE RFVIEENLHC IIKSHWKERK TCAAQLVSYP GKNKIPLNYH IVEVIFAELF 370 380 390 400 410 420 QLPAPPHIDV MYTTLLIELC KLQPGSLPQV LAQATEMLYM RLDTMNTTCV DRFINWFSHH 430 440 450 460 470 480 LSNFQFRWSW EDWSDCLSQD PESPKPKFVR EVLEKCMRLS YHQRILDIVP PTFSALCPAN 490 500 510 520 530 540 PTCIYKYGDE SSNSLPGHSV ALCLAVAFKS KATNDEIFSI LKDVPNPNQD DDDDEGFSFN 550 560 570 580 590 600 PLKIEVFVQT LLHLAAKSFS HSFSALAKFH EVFKTLAESD EGKLHVLRVM FEVWRNHPQM 610 620 630 640 650 660 IAVLVDKMIR TQIVDCAAVA NWIFSSELSR DFTRLFVWEI LHSTIRKMNK HVLKIQKELE 670 680 690 700 710 720 EAKEKLARQH KRRSDDDDRS SDRKDGVLEE QIERLQEKVE SAQSEQKNLF LVIFQRFIMI 730 740 750 760 770 780 LTEHLVRCET DGTSVLTPWY KNCIERLQQI FLQHHQIIQQ YMVTLENLLF TAELDPHILA 790 VFQQFCALQA

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"A nuclear cap binding protein complex involved in pre-mRNA splicing." Izaurralde E., Lewis J., McGuigan C., Jankowska E., Darzynkiewicz E., Mattaj I.W. Cell 78:657-668(1994) [PubMed: 8069914] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 119-128; 513-522 AND 687-693, FUNCTION IN MRNA SPLICING.
[2]	"Cloning of a complementary DNA encoding an 80 kilodalton nuclear cap binding protein." Kataoka N., Ohno M., Kangawa K., Tokoro Y., Shimura Y. Nucleic Acids Res. 22:3861-3865(1994) [PubMed: 7937105] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE.
[3]	"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: 14702039] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Testis.
[4]	Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S., Ohara O., Nagase T., Kikuno R.F. Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Brain.
[5]	"DNA sequence and analysis of human chromosome 9." Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S., Bagguley C.L. , Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A., Frankland J.A., French L., Fricker D.G., Garner P., Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S., Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E., Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D., Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E., Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K., Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M., Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J., Dunham I. Nature 429:369-374(2004) [PubMed: 15164053] [Abstract] 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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Placenta.
[7]	"A cap-binding protein complex mediating U snRNA export." Izaurralde E., Lewis J., Gamberi C., Jarmolowski A., McGuigan C., Mattaj A.W. Nature 376:709-712(1995) [PubMed: 7651522] [Abstract] Cited for: FUNCTION.
[8]	"Interaction between the human nuclear cap-binding protein complex and hnRNP F." Gamberi C., Izaurralde E., Beisel C., Mattaj I.W. Mol. Cell. Biol. 17:2587-2597(1997) [PubMed: 9111328] [Abstract] Cited for: INTERACTION WITH HNRNPF AND HNRNPH1.
[9]	"Cdc42 stimulates RNA splicing via the S6 kinase and a novel S6 kinase target, the nuclear cap-binding complex." Wilson K.F., Wu W.J., Cerione R.A. J. Biol. Chem. 275:37307-37310(2000) [PubMed: 10973943] [Abstract] Cited for: PHOSPHORYLATION AT SER-7; THR-21 AND SER-22, MUTAGENESIS OF SER-7; 17-LYS-ARG-18 AND 21-THR-SER-22.
[10]	"Evidence for a pioneer round of mRNA translation: mRNAs subject to nonsense-mediated decay in mammalian cells are bound by CBP80 and CBP20." Ishigaki Y., Li X., Serin G., Maquat L.E. Cell 106:607-617(2001) [PubMed: 11551508] [Abstract] Cited for: FUNCTION IN PIONEER ROUND OF MRNA TRANSLATION.
[11]	"Interaction of eukaryotic translation initiation factor 4G with the nuclear cap-binding complex provides a link between nuclear and cytoplasmic functions of the m(7) guanosine cap." McKendrick L., Thompson E., Ferreira J., Morley S.J., Lewis J.D. Mol. Cell. Biol. 21:3632-3641(2001) [PubMed: 11340157] [Abstract] Cited for: INTERACTION WITH EIF4G1.
[12]	"The exon junction complex is detected on CBP80-bound but not eIF4E-bound mRNA in mammalian cells: dynamics of mRNP remodeling." Lejeune F., Ishigaki Y., Li X., Maquat L.E. EMBO J. 21:3536-3545(2002) [PubMed: 12093754] [Abstract] Cited for: INTERACTION WITH THE EXON JUNCTION COMPLEX.
[13]	"The pioneer translation initiation complex is functionally distinct from but structurally overlaps with the steady-state translation initiation complex." Chiu S.-Y., Lejeune F., Ranganathan A.C., Maquat L.E. Genes Dev. 18:745-754(2004) [PubMed: 15059963] [Abstract] Cited for: FUNCTION IN PIONEER ROUND OF MRNA TRANSLATION, INTERACTION WITH EIF4G1.
[14]	"eIF4G is required for the pioneer round of translation in mammalian cells." Lejeune F., Ranganathan A.C., Maquat L.E. Nat. Struct. Mol. Biol. 11:992-1000(2004) [PubMed: 15361857] [Abstract] Cited for: FUNCTION IN PIONEER ROUND OF MRNA TRANSLATION, INTERACTION WITH EIF4G1 AND EIF4G2.
[15]	"CBP80 promotes interaction of Upf1 with Upf2 during nonsense-mediated mRNA decay in mammalian cells." Hosoda N., Kim Y.K., Lejeune F., Maquat L.E. Nat. Struct. Mol. Biol. 12:893-901(2005) [PubMed: 16186820] [Abstract] Cited for: FUNCTION IN NONSENSE-MEDIATED MRNA DECAY, INTERACTION WITH UPF1.
[16]	"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: 17081983] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-674, MASS SPECTROMETRY. Tissue: Epithelium.
[17]	"Human mRNA export machinery recruited to the 5' end of mRNA." Cheng H., Dufu K., Lee C.-S., Hsu J.L., Dias A., Reed R. Cell 127:1389-1400(2006) [PubMed: 17190602] [Abstract] Cited for: FUNCTION IN MRNA EXPORT, INTERACTION WITH THOC4.
[18]	"Inhibition of mRNA deadenylation by the nuclear cap binding complex (CBC)." Balatsos N.A.A., Nilsson P., Mazza C., Cusack S., Virtanen A. J. Biol. Chem. 281:4517-4522(2006) [PubMed: 16317009] [Abstract] Cited for: FUNCTION IN MRNA DEADENYLATION, INTERACTION WITH PARN.
[19]	"Molecular composition of IMP1 ribonucleoprotein granules." Joeson L., Vikesaa J., Krogh A., Nielsen L.K., Hansen T., Borup R., Johnsen A.H., Christiansen J., Nielsen F.C. Mol. Cell. Proteomics 6:798-811(2007) [PubMed: 17289661] [Abstract] Cited for: IDENTIFICATION IN A MRNP GRANULE COMPLEX, INTERACTION WITH IGF2BP1, IDENTIFICATION BY MASS SPECTROMETRY, SUBCELLULAR LOCATION.
[20]	"Failsafe nonsense-mediated mRNA decay does not detectably target eIF4E-bound mRNA." Matsuda D., Hosoda N., Kim Y.K., Maquat L.E. Nat. Struct. Mol. Biol. 14:974-979(2007) [PubMed: 17873884] [Abstract] Cited for: FUNCTION IN NONSENSE-MEDIATED MRNA DECAY.
[21]	"NMD resulting from encephalomyocarditis virus IRES-directed translation initiation seems to be restricted to CBP80/20-bound mRNA." Woeller C.F., Gaspari M., Isken O., Maquat L.E. EMBO Rep. 9:446-451(2008) [PubMed: 18369367] [Abstract] Cited for: FUNCTION IN NONSENSE-MEDIATED MRNA DECAY.
[22]	"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: 18669648] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-21 AND SER-22, MASS SPECTROMETRY.
[23]	Colinge J., Superti-Furga G., Bennett K.L. Submitted (OCT-2008) to UniProtKB Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[24]	"Ars2 links the nuclear cap-binding complex to RNA interference and cell proliferation." Gruber J.J., Zatechka D.S., Sabin L.R., Yong J., Lum J.J., Kong M., Zong W.-X., Zhang Z., Lau C.-K., Rawlings J., Cherry S., Ihle J.N., Dreyfuss G., Thompson C.B. Cell 138:328-339(2009) [PubMed: 19632182] [Abstract] Cited for: FUNCTION IN MIRNAS BIOGENESIS.
[25]	"A new MIF4G domain-containing protein, CTIF, directs nuclear cap-binding protein CBP80/20-dependent translation." Kim K.M., Cho H., Choi K., Kim J., Kim B.-W., Ko Y.-G., Jang S.K., Kim Y.K. Genes Dev. 23:2033-2045(2009) [PubMed: 19648179] [Abstract] Cited for: FUNCTION IN PIONEER ROUND OF MRNA TRANSLATION, INTERACTION WITH KIAA0427, SUBCELLULAR LOCATION.
[26]	"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: 19690332] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-22, MASS SPECTROMETRY. Tissue: T-cell.
[27]	"Lysine acetylation targets protein complexes and co-regulates major cellular functions." Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T., Olsen J.V., Mann M. Science 325:834-840(2009) [PubMed: 19608861] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-204 AND LYS-698, MASS SPECTROMETRY.
[28]	"Crystal structure of the human nuclear cap binding complex." Mazza C., Ohno M., Segref A., Mattaj I.W., Cusack S. Mol. Cell 8:383-396(2001) [PubMed: 11545740] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 20-790 IN COMPLEX WITH NCBP2.
[29]	"Large-scale induced fit recognition of an m(7)GpppG cap analogue by the human nuclear cap-binding complex." Mazza C., Segref A., Mattaj I.W., Cusack S. EMBO J. 21:5548-5557(2002) [PubMed: 12374755] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS) OF 20-790 IN COMPLEX WITH NCBP2.
[30]	"Structural basis of m7GpppG binding to the nuclear cap-binding protein complex." Calero G., Wilson K.F., Ly T., Rios-Steiner J.L., Clardy J.C., Cerione R.A. Nat. Struct. Biol. 9:912-917(2002) [PubMed: 12434151] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.11 ANGSTROMS) IN COMPLEX WITH NCBP2.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

X80030 mRNA. Translation: CAA56334.1.
D32002 mRNA. Translation: BAA06769.1.
AK312807 mRNA. Translation: BAG35665.1.
AB209233 mRNA. Translation: BAD92470.1. Different initiation.
AL445531, AL162385 Genomic DNA. Translation: CAI15431.1.
AL162385, AL445531 Genomic DNA. Translation: CAI12861.1.
AL162385 Genomic DNA. Translation: CAI12863.1. Sequence problems.
BC001450 mRNA. Translation: AAH01450.1.

IPI

IPI00019380.

PIR

S50082.

RefSeq

NP_002477.1.

UniGene

Hs.595669
Hs.686479

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1H2T	X-ray	2.15	C	20-790	[»]
1H2U	X-ray	2.40	A/B	20-790	[»]
1H2V	X-ray	2.00	C	20-790	[»]
1H6K	X-ray	2.00	A/B/C	20-790	[»]
1N52	X-ray	2.11	A	1-790	[»]
1N54	X-ray	2.72	A	1-790	[»]
3FEX	X-ray	3.55	A	1-790	[»]
3FEY	X-ray	2.20	A	1-790	[»]

DisProt

DP00392.

ModBase

Search...

Protein-protein interaction databases

IntAct

Q09161. 14 interactions.

STRING

Q09161.

PTM databases

PhosphoSite

Q09161.

Proteomic databases

PeptideAtlas

Q09161.

PRIDE

Q09161.

Genome annotation databases

Ensembl

ENST00000375130; ENSP00000364272; ENSG00000136937; Homo sapiens. [Genome view]
ENST00000375132; ENSP00000364274; ENSG00000136937; Homo sapiens. [Genome view]
ENST00000375147; ENSP00000364289; ENSG00000136937; Homo sapiens. [Genome view]

GeneID

4686.

KEGG

hsa:4686.

UCSC

uc004axq.1. human.

Organism-specific databases

CTD

4686.

GeneCards

GC09P099435.

H-InvDB

HIX0008214.

HGNC

HGNC:7658. NCBP1.

MIM

600469. gene.

PharmGKB

PA31461.

GenAtlas

Search...

Phylogenomic databases

eggNOG

prNOG15959.

HOGENOM

HBG378185.

HOVERGEN

Q09161.

InParanoid

Q09161.

OMA

FTAELDH.

OrthoDB

EOG95B41X.

PhylomeDB

Q09161.

Enzyme and pathway databases

Reactome

REACT_11052. Metabolism of non-coding RNA.
REACT_125. Processing of Capped Intron-Containing Pre-mRNA.
REACT_1675. mRNA Processing.
REACT_1788. Transcription.
REACT_6167. Influenza Infection.
REACT_6185. HIV Infection.
REACT_71. Gene Expression.

Gene expression databases

ArrayExpress

Q09161.

Bgee

Q09161.

CleanEx

HS_NCBP1.

Genevestigator

Q09161.

GermOnline

ENSG00000136937. Homo sapiens.

Family and domain databases

InterPro

IPR016024. ARM-type_fold.
IPR016021. MIF4-like_typ_1/2/3.
IPR015172. MIF4G-like_typ-1.
IPR015174. MIF4G-like_typ-2.
IPR003890. MIF4G-like_typ-3.
[Graphical view]

Gene3D

G3DSA:1.25.40.180. MIF4-like_typ_1/2/3. 3 hits.

Pfam

PF02854. MIF4G. 1 hit.
PF09088. MIF4G_like. 1 hit.
PF09090. MIF4G_like_2. 1 hit.
[Graphical view]

SMART

SM00543. MIF4G. 1 hit.
[Graphical view]

ProtoNet

Search...

Other Resources

NextBio

18072.

SOURCE

Search...

Entry information

Entry name

NCBP1_HUMAN

Accession

Primary (citable) accession number: Q09161
Secondary accession number(s): B2R718 , Q59G76, Q5T1V0, Q5T7X2

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1996
Last sequence update:	October 1, 1996
Last modified:	February 9, 2010
This is version 101 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

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.