P52298 (NCBP2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Nuclear cap-binding protein subunit 2

Alternative name(s):
20 kDa nuclear cap-binding protein
Cell proliferation-inducing gene 55 protein
NCBP 20 kDa subunit
Short name=CBP20
NCBP-interacting protein 1
Short name=NIP1

Gene names

Name:	NCBP2
Synonyms:	CBP20
ORF Names:	PIG55

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	156 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 ALYREF/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, thereby being 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, NCBP2/CBP20 recognizes and binds capped RNAs (m7GpppG-capped RNA) but requires NCBP1/CBP80 to stabilize the movement of its N-terminal loop and lock the CBC into a high affinity cap-binding state with the cap structure. Ref.10 Ref.12 Ref.13 Ref.14 Ref.15 Ref.17 Ref.18
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. Is part of the exon junction complex (EJC) containing NCBP1, NCBP2, RNPS1, RBM8A, SRRM1, NXF1, UPF3B, UPF2, ALYREF/THOC4 and/or REFBP2. Interacts with EIF4G1, HNRNPF, HNRNPH1 and ALYREF/THOC4/ALY. Ref.9 Ref.11 Ref.12 Ref.14
Subcellular location	Nucleus. Cytoplasm Ref.8.
Sequence similarities	Belongs to the RRM NCBP2 family. Contains 1 RRM (RNA recognition motif) domain.

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
Coding sequence diversity	Alternative splicing
Ligand	RNA-binding
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	7-methylguanosine mRNA capping Inferred from direct assay Ref.23. Source: UniProtKB gene silencing by RNA Inferred from electronic annotation. Source: UniProtKB-KW histone mRNA metabolic process Traceable author statement. Source: Reactome mRNA 3'-end processing Traceable author statement. Source: Reactome mRNA cis splicing, via spliceosome Inferred from direct assay PubMed 18426921. Source: UniProtKB mRNA export from nucleus Traceable author statement. Source: Reactome ncRNA metabolic process Traceable author statement. Source: Reactome nuclear-transcribed mRNA catabolic process, nonsense-mediated decay Inferred from direct assay Ref.10. Source: UniProtKB positive regulation of RNA export from nucleus Inferred from sequence or structural similarity. Source: UniProtKB positive regulation of viral transcription Traceable author statement. Source: Reactome regulation of translational initiation Inferred from direct assay Ref.10. Source: UniProtKB snRNA export from nucleus Inferred from sequence or structural similarity. Source: UniProtKB spliceosomal snRNP assembly Traceable author statement. Source: Reactome termination of RNA polymerase II transcription Traceable author statement. Source: Reactome transcription elongation from RNA polymerase II promoter Traceable author statement. Source: Reactome viral reproduction Traceable author statement. Source: Reactome
Cellular_component	cytosol Traceable author statement. Source: Reactome mRNA cap binding complex Inferred from direct assay Ref.23Ref.1PubMed 9342333. Source: UniProtKB nuclear cap binding complex Inferred from electronic annotation. Source: InterPro nucleoplasm Inferred from direct assay Ref.8. Source: UniProtKB
Molecular_function	RNA 7-methylguanosine cap binding Inferred from direct assay Ref.23PubMed 18426921. Source: UniProtKB nucleotide binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
NCBP1	Q09161	5	EBI-464729,EBI-464743

Alternative products

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

Isoform 1 (identifier: P52298-1)

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: P52298-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-26: MSGGLLKALRSDSYVELSQYRDQHFR → MVLRKLYA

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 156

156

Nuclear cap-binding protein subunit 2

PRO_0000081499

Regions

Domain

40 – 118

79

RRM

Region

112 – 116

5

mRNA cap-binding

Region

123 – 127

5

mRNA cap-binding

Region

133 – 134

2

mRNA cap-binding

Sites

Binding site

20

1

mRNA cap

Binding site

43

1

mRNA cap

Amino acid modifications

Modified residue

13

1

Phosphoserine By similarity

Modified residue

18

1

Phosphoserine Ref.16

Natural variations

Alternative sequence

1 – 26

26

MSGGL…DQHFR → MVLRKLYA in isoform 2.

VSP_038125

Experimental info

Mutagenesis

20

1

Y → A: Abolishes mRNA cap-binding. Ref.22

Mutagenesis

20

1

Y → F: Strongly impairs mRNA cap-binding. Ref.22

Mutagenesis

25

1

F → A: Does not affect mRNA cap-binding. Ref.21

Mutagenesis

43

1

Y → A: Abolishes mRNA cap-binding. Ref.21 Ref.22

Mutagenesis

43

1

Y → F: Does not affect mRNA cap-binding. Ref.21 Ref.22

Mutagenesis

46

1

N → A: Does not affect mRNA cap-binding. Ref.21

Mutagenesis

83

1

F → A: Abolishes mRNA cap-binding. Ref.21

Mutagenesis

85

1

F → A: Impairs mRNA cap-binding.

Mutagenesis

112

1

R → A or T: Does not affect mRNA cap-binding. Ref.22

Mutagenesis

114

1

D → A: Does not affect mRNA cap-binding. Ref.21

Mutagenesis

116

1

D → A: Abolishes mRNA cap-binding. Ref.21

Mutagenesis

119

1

F → A: Does not affect mRNA cap-binding. Ref.21

Mutagenesis

138

1

Y → A: Does not affect mRNA cap-binding. Ref.22

Sequence conflict

97

1

A → S in BAA09599. Ref.2

Secondary structure

1

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156

Helix Strand Turn

Details...

Helix

7 – 10

4

Helix

13 – 15

3

Beta strand

23 – 27

5

Turn

34 – 38

5

Beta strand

41 – 46

6

Helix

53 – 60

8

Helix

61 – 63

3

Beta strand

66 – 73

8

Turn

75 – 77

3

Beta strand

80 – 90

11

Helix

91 – 100

10

Turn

101 – 103

3

Beta strand

104 – 106

3

Beta strand

112 – 117

6

Turn

121 – 124

4

Helix

134 – 137

4

Helix

144 – 146

3

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified October 1, 1996. Version 1. Checksum: B6C94F3182A2CC3D	FASTA	156	18,001
	10 20 30 40 50 60 MSGGLLKALR SDSYVELSQY RDQHFRGDNE EQEKLLKKSC TLYVGNLSFY TTEEQIYELF 70 80 90 100 110 120 SKSGDIKKII MGLDKMKKTA CGFCFVEYYS RADAENAMRY INGTRLDDRI IRTDWDAGFK 130 140 150 EGRQYGRGRS GGQVRDEYRQ DYDAGRGGYG KLAQNQ
	Isoform 2 [UniParc]. Checksum: D2475AF0597FDC0F	FASTA	138	15,937
	10 20 30 40 50 60 MVLRKLYAGD NEEQEKLLKK SCTLYVGNLS FYTTEEQIYE LFSKSGDIKK IIMGLDKMKK 70 80 90 100 110 120 TACGFCFVEY YSRADAENAM RYINGTRLDD RIIRTDWDAG FKEGRQYGRG RSGGQVRDEY 130 RQDYDAGRGG YGKLAQNQ

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PROTEIN SEQUENCE OF 9-25 AND 113-145.
[2]	"Identification of the factors that interact with NCBP, an 80 kDa nuclear cap binding protein." Kataoka N., Ohno M., Moda I., Shimura Y. Nucleic Acids Res. 23:3638-3641(1995) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). Tissue: Cervix carcinoma.
[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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2). Tissue: Brain.
[4]	"Identification of a human cell proliferation gene." Kim J.W. Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
[5]	"Cloning of human full-length CDSs in BD Creator(TM) system donor vector." Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A. Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[6]	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].
[7]	"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: Cervix.
[8]	"A nuclear cap-binding complex binds Balbiani ring pre-mRNA cotranscriptionally and accompanies the ribonucleoprotein particle during nuclear export." Visa N., Izaurralde E., Ferreira J., Daneholt B., Mattaj I.W. J. Cell Biol. 133:5-14(1996) [PubMed] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION.
[9]	"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] [Europe PMC] [Abstract] Cited for: INTERACTION WITH HNRNPF AND HNRNPH1.
[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] [Europe PMC] [Abstract] Cited for: FUNCTION IN PIONEER ROUND OF MRNA TRANSLATION.
[11]	"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] [Europe PMC] [Abstract] Cited for: INTERACTION WITH THE EXON JUNCTION COMPLEX.
[12]	"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] [Europe PMC] [Abstract] Cited for: FUNCTION IN PIONEER ROUND OF MRNA TRANSLATION, INTERACTION WITH EIF4G1.
[13]	"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] [Europe PMC] [Abstract] Cited for: FUNCTION IN MRNA EXPORT.
[14]	"The interaction between cap-binding complex and RNA export factor is required for intronless mRNA export." Nojima T., Hirose T., Kimura H., Hagiwara M. J. Biol. Chem. 282:15645-15651(2007) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION IN MRNA EXPORT, INTERACTION WITH ALYREF/THOC4.
[15]	"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] [Europe PMC] [Abstract] Cited for: FUNCTION IN NONSENSE-MEDIATED MRNA DECAY.
[16]	"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-18, MASS SPECTROMETRY. Tissue: Embryonic kidney.
[17]	"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] [Europe PMC] [Abstract] Cited for: FUNCTION IN NONSENSE-MEDIATED MRNA DECAY.
[18]	"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] [Europe PMC] [Abstract] Cited for: FUNCTION IN MIRNAS BIOGENESIS.
[19]	"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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Tissue: Leukemic T-cell.
[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]	"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] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 20-790 IN COMPLEX WITH NCBP1, RNA-BINDING, MUTAGENESIS OF PHE-25; TYR-43; ASN-46; PHE-83; ASP-114; ASP-116 AND PHE-119.
[22]	"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] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS) OF 20-790 IN COMPLEX WITH NCBP1 AND MRNA CAP, RNA-BINDING, MUTAGENESIS OF TYR-20; TYR-43; ARG-112 AND TYR-138.
[23]	"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] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.11 ANGSTROMS) IN COMPLEX WITH NCBP1 AND MRNA CAP, RNA-BINDING.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

X84157 mRNA. Translation: CAA58962.1.
D59253 mRNA. Translation: BAA09599.1.
AK297506 mRNA. Translation: BAG59919.1.
AK315903 mRNA. Translation: BAH14274.1.
AK316601 mRNA. Translation: BAG38188.1.
AY644767 mRNA. Translation: AAV85455.1.
BT006842 mRNA. Translation: AAP35488.1.
CH471191 Genomic DNA. Translation: EAW53624.1.
BC001255 mRNA. Translation: AAH01255.1.

IPI

IPI00183500.
IPI00927860.

PIR

I37222.
S60109.

RefSeq

NP_001036005.1. NM_001042540.1.
NP_031388.2. NM_007362.3.

UniGene

Hs.591671.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1H2T	X-ray	2.15	Z	1-156	[»]
1H2U	X-ray	2.40	X/Y	1-156	[»]
1H2V	X-ray	2.00	Z	1-156	[»]
1H6K	X-ray	2.00	X/Y/Z	22-120	[»]
1N52	X-ray	2.11	B	1-156	[»]
1N54	X-ray	2.72	B	1-156	[»]
3FEX	X-ray	3.55	B	1-156	[»]
3FEY	X-ray	2.20	B	1-156	[»]

DisProt

DP00393.

ProteinModelPortal

P52298.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-33246N.

IntAct

P52298. 7 interactions.

MINT

MINT-248711.

STRING

9606.ENSP00000326806.

PTM databases

PhosphoSite

P52298.

Polymorphism databases

DMDM

1705651.

Proteomic databases

PaxDb

P52298.

PRIDE

P52298.

Protocols and materials databases

DNASU

22916.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000321256; ENSP00000326806; ENSG00000114503.
ENST00000452404; ENSP00000412785; ENSG00000114503.

GeneID

22916.

KEGG

hsa:22916.

UCSC

uc003fxb.1. human.
uc011btz.1. human.

Organism-specific databases

CTD

22916.

GeneCards

GC03M196662.

HGNC

HGNC:7659. NCBP2.

HPA

HPA044850.

MIM

605133. gene.

neXtProt

NX_P52298.

PharmGKB

PA31462.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG0724.

HOGENOM

HOG000217589.

HOVERGEN

HBG052581.

InParanoid

P52298.

KO

K12883.

OMA

RQDYDPA.

PhylomeDB

P52298.

Enzyme and pathway databases

Reactome

REACT_116125. Disease.
REACT_1675. mRNA Processing.
REACT_1788. Transcription.
REACT_21257. Metabolism of RNA.
REACT_71. Gene Expression.
REACT_78. Post-Elongation Processing of the Transcript.

Gene expression databases

ArrayExpress

P52298.

Bgee

P52298.

CleanEx

HS_NCBP2.

Genevestigator

P52298.

GermOnline

ENSG00000114503. Homo sapiens.

Family and domain databases

Gene3D

3.30.70.330. 1 hit.

InterPro

IPR027157. NCBP2.
IPR012677. Nucleotide-bd_a/b_plait.
IPR000504. RRM_dom.
[Graphical view]

PANTHER

PTHR18847. PTHR18847. 1 hit.

Pfam

PF00076. RRM_1. 1 hit.
[Graphical view]

SMART

SM00360. RRM. 1 hit.
[Graphical view]

PROSITE

PS50102. RRM. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

ChiTaRS

NCBP2. human.

EvolutionaryTrace

P52298.

GenomeRNAi

22916.

NextBio

43603.

SOURCE

Search...

Entry information

Entry name

NCBP2_HUMAN

Accession

Primary (citable) accession number: P52298
Secondary accession number(s): B2RE91 , B4DMK7, Q14924, Q2TS50

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1996
Last sequence update:	October 1, 1996
Last modified:	May 1, 2013
This is version 139 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.