Q15366 (PCBP2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Poly(rC)-binding protein 2

Alternative name(s):
Alpha-CP2
Heterogeneous nuclear ribonucleoprotein E2
Short name=hnRNP E2

Gene names

Name:

PCBP2

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

General annotation (Comments)

Function	Single-stranded nucleic acid binding protein that binds preferentially to oligo dC. Major cellular poly(rC)-binding protein. Binds also poly(rU). Negatively regulates cellular antiviral responses mediated by MAVS signaling. It acts as an adapter between MAVS and the E3 ubiquitin ligase ITCH, therefore triggering MAVS ubiquitinationa and degradation. Ref.14
Subunit structure	Identified in a mRNP complex, at least composed of DHX9, DDX3X, ELAVL1, HNRNPU, IGF2BP1, ILF3, PABPC1, PCBP2, PTBP2, STAU1, STAU2, SYNCRIP and YBX1. Interacts with IFIH1 and RNF135. Interacts with MAVS (via C-terminus) and ITCH (via WW domains). Ref.14 Ref.15
Subcellular location	Nucleus. Cytoplasm. Note: Loosely bound in the nucleus. May shuttle between the nucleus and the cytoplasm. Ref.15
Tissue specificity	Detected in all tissues examined.
Domain	The KH domains mediates poly(C) binding.
Post-translational modification	Phosphorylated. The non-phosphorylated form(s) exhibited the strongest poly(rC)-binding activity.
Sequence similarities	Contains 3 KH domains.
Sequence caution	The sequence BAD92062.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Ontologies

Keywords
Biological process	Antiviral defense Immunity Innate immunity
Cellular component	Cytoplasm Nucleus
Coding sequence diversity	Alternative splicing
Domain	Repeat
Ligand	DNA-binding RNA-binding
Molecular function	Ribonucleoprotein
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	defense response to virus Inferred from electronic annotation. Source: UniProtKB-KW innate immune response Traceable author statement. Source: Reactome mRNA splicing, via spliceosome Traceable author statement. Source: Reactome negative regulation of defense response to virus Inferred from mutant phenotype Ref.14. Source: UniProtKB negative regulation of type I interferon production Traceable author statement. Source: Reactome proteasomal ubiquitin-dependent protein catabolic process Inferred from mutant phenotype Ref.14. Source: UniProtKB
Cellular_component	cytosol Traceable author statement. Source: Reactome nucleoplasm Traceable author statement. Source: Reactome ribonucleoprotein complex Inferred from electronic annotation. Source: UniProtKB-KW
Molecular_function	DNA binding Inferred from electronic annotation. Source: UniProtKB-KW RNA binding Inferred from direct assay Ref.1. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
PCBP1	Q15365	2	EBI-945799,EBI-946095

Alternative products

This entry describes 6 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q15366-1)

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: Q15366-2)

The sequence of this isoform differs from the canonical sequence as follows:
     279-279: W → WA

Note: No experimental confirmation available.

Isoform 3 (identifier: Q15366-3)

The sequence of this isoform differs from the canonical sequence as follows:
     169-172: Missing.
     279-279: W → WA

Isoform 4 (identifier: Q15366-4)

The sequence of this isoform differs from the canonical sequence as follows:
     169-172: Missing.
     198-228: Missing.
     279-279: W → WA

Note: No experimental confirmation available.

Isoform 5 (identifier: Q15366-5)

The sequence of this isoform differs from the canonical sequence as follows:
     198-228: Missing.
     279-279: W → WA

Note: No experimental confirmation available.

Isoform 6 (identifier: Q15366-6)

The sequence of this isoform differs from the canonical sequence as follows:
     169-172: Missing.

Note: No experimental confirmation available.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 365

365

Poly(rC)-binding protein 2

PRO_0000050090

Regions

Domain

13 – 75

63

KH 1

Domain

97 – 162

66

KH 2

Domain

287 – 351

65

KH 3

Amino acid modifications

Modified residue

173

1

Phosphoserine Ref.17 Ref.19

Modified residue

189

1

Phosphoserine Ref.16 Ref.17

Modified residue

272

1

Phosphoserine Ref.12

Modified residue

364

1

Phosphoserine Ref.17 Ref.19

Modified residue

365

1

Phosphoserine Ref.19

Natural variations

Alternative sequence

169 – 172

4

Missing in isoform 3, isoform 4 and isoform 6.

VSP_043161

Alternative sequence

198 – 228

31

Missing in isoform 4 and isoform 5.

VSP_043362

Alternative sequence

279

1

W → WA in isoform 2, isoform 3, isoform 4 and isoform 5.

VSP_042833

Secondary structure

1

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365

Helix Strand Turn

Details...

Beta strand

14 – 21

8

Helix

22 – 29

8

Helix

31 – 33

3

Helix

34 – 43

10

Beta strand

46 – 49

4

Beta strand

55 – 63

9

Helix

65 – 80

16

Beta strand

89 – 91

3

Beta strand

97 – 105

9

Helix

106 – 113

8

Helix

115 – 117

3

Helix

118 – 127

10

Beta strand

128 – 131

4

Beta strand

143 – 150

8

Helix

152 – 168

17

Beta strand

288 – 295

8

Helix

296 – 303

8

Helix

305 – 307

3

Helix

308 – 317

10

Beta strand

320 – 323

4

Beta strand

331 – 339

9

Helix

341 – 355

15

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified November 1, 1996. Version 1. Checksum: 43F035D76FDC2C63	FASTA	365	38,580
	10 20 30 40 50 60 MDTGVIEGGL NVTLTIRLLM HGKEVGSIIG KKGESVKKMR EESGARINIS EGNCPERIIT 70 80 90 100 110 120 LAGPTNAIFK AFAMIIDKLE EDISSSMTNS TAASRPPVTL RLVVPASQCG SLIGKGGCKI 130 140 150 160 170 180 KEIRESTGAQ VQVAGDMLPN STERAITIAG IPQSIIECVK QICVVMLETL SQSPPKGVTI 190 200 210 220 230 240 PYRPKPSSSP VIFAGGQDRY STGSDSASFP HTTPSMCLNP DLEGPPLEAY TIQGQYAIPQ 250 260 270 280 290 300 PDLTKLHQLA MQQSHFPMTH GNTGFSGIES SSPEVKGYWG LDASAQTTSH ELTIPNDLIG 310 320 330 340 350 360 CIIGRQGAKI NEIRQMSGAQ IKIANPVEGS TDRQVTITGS AASISLAQYL INVRLSSETG GMGSS
	Isoform 2 [UniParc]. Checksum: 3464C973504D90DE	FASTA	366	38,651
	10 20 30 40 50 60 MDTGVIEGGL NVTLTIRLLM HGKEVGSIIG KKGESVKKMR EESGARINIS EGNCPERIIT 70 80 90 100 110 120 LAGPTNAIFK AFAMIIDKLE EDISSSMTNS TAASRPPVTL RLVVPASQCG SLIGKGGCKI 130 140 150 160 170 180 KEIRESTGAQ VQVAGDMLPN STERAITIAG IPQSIIECVK QICVVMLETL SQSPPKGVTI 190 200 210 220 230 240 PYRPKPSSSP VIFAGGQDRY STGSDSASFP HTTPSMCLNP DLEGPPLEAY TIQGQYAIPQ 250 260 270 280 290 300 PDLTKLHQLA MQQSHFPMTH GNTGFSGIES SSPEVKGYWA GLDASAQTTS HELTIPNDLI 310 320 330 340 350 360 GCIIGRQGAK INEIRQMSGA QIKIANPVEG STDRQVTITG SAASISLAQY LINVRLSSET GGMGSS
	Isoform 3 [UniParc]. Checksum: 70C8AF710E3BF3C0	FASTA	362	38,222
	10 20 30 40 50 60 MDTGVIEGGL NVTLTIRLLM HGKEVGSIIG KKGESVKKMR EESGARINIS EGNCPERIIT 70 80 90 100 110 120 LAGPTNAIFK AFAMIIDKLE EDISSSMTNS TAASRPPVTL RLVVPASQCG SLIGKGGCKI 130 140 150 160 170 180 KEIRESTGAQ VQVAGDMLPN STERAITIAG IPQSIIECVK QICVVMLESP PKGVTIPYRP 190 200 210 220 230 240 KPSSSPVIFA GGQDRYSTGS DSASFPHTTP SMCLNPDLEG PPLEAYTIQG QYAIPQPDLT 250 260 270 280 290 300 KLHQLAMQQS HFPMTHGNTG FSGIESSSPE VKGYWAGLDA SAQTTSHELT IPNDLIGCII 310 320 330 340 350 360 GRQGAKINEI RQMSGAQIKI ANPVEGSTDR QVTITGSAAS ISLAQYLINV RLSSETGGMG SS
	Isoform 4 [UniParc]. Checksum: E831D4BF718C26E3	FASTA	331	34,917
	10 20 30 40 50 60 MDTGVIEGGL NVTLTIRLLM HGKEVGSIIG KKGESVKKMR EESGARINIS EGNCPERIIT 70 80 90 100 110 120 LAGPTNAIFK AFAMIIDKLE EDISSSMTNS TAASRPPVTL RLVVPASQCG SLIGKGGCKI 130 140 150 160 170 180 KEIRESTGAQ VQVAGDMLPN STERAITIAG IPQSIIECVK QICVVMLESP PKGVTIPYRP 190 200 210 220 230 240 KPSSSPVIFA GGQAYTIQGQ YAIPQPDLTK LHQLAMQQSH FPMTHGNTGF SGIESSSPEV 250 260 270 280 290 300 KGYWAGLDAS AQTTSHELTI PNDLIGCIIG RQGAKINEIR QMSGAQIKIA NPVEGSTDRQ 310 320 330 VTITGSAASI SLAQYLINVR LSSETGGMGS S
	Isoform 5 [UniParc]. Checksum: BD1A8AA65EABF0BF	FASTA	335	35,347
	10 20 30 40 50 60 MDTGVIEGGL NVTLTIRLLM HGKEVGSIIG KKGESVKKMR EESGARINIS EGNCPERIIT 70 80 90 100 110 120 LAGPTNAIFK AFAMIIDKLE EDISSSMTNS TAASRPPVTL RLVVPASQCG SLIGKGGCKI 130 140 150 160 170 180 KEIRESTGAQ VQVAGDMLPN STERAITIAG IPQSIIECVK QICVVMLETL SQSPPKGVTI 190 200 210 220 230 240 PYRPKPSSSP VIFAGGQAYT IQGQYAIPQP DLTKLHQLAM QQSHFPMTHG NTGFSGIESS 250 260 270 280 290 300 SPEVKGYWAG LDASAQTTSH ELTIPNDLIG CIIGRQGAKI NEIRQMSGAQ IKIANPVEGS 310 320 330 TDRQVTITGS AASISLAQYL INVRLSSETG GMGSS
	Isoform 6 [UniParc]. Checksum: 4F96378919BF3215	FASTA	361	38,151
	10 20 30 40 50 60 MDTGVIEGGL NVTLTIRLLM HGKEVGSIIG KKGESVKKMR EESGARINIS EGNCPERIIT 70 80 90 100 110 120 LAGPTNAIFK AFAMIIDKLE EDISSSMTNS TAASRPPVTL RLVVPASQCG SLIGKGGCKI 130 140 150 160 170 180 KEIRESTGAQ VQVAGDMLPN STERAITIAG IPQSIIECVK QICVVMLESP PKGVTIPYRP 190 200 210 220 230 240 KPSSSPVIFA GGQDRYSTGS DSASFPHTTP SMCLNPDLEG PPLEAYTIQG QYAIPQPDLT 250 260 270 280 290 300 KLHQLAMQQS HFPMTHGNTG FSGIESSSPE VKGYWGLDAS AQTTSHELTI PNDLIGCIIG 310 320 330 340 350 360 RQGAKINEIR QMSGAQIKIA NPVEGSTDRQ VTITGSAASI SLAQYLINVR LSSETGGMGS S

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Characterisation of two major cellular poly(rC)-binding human proteins, each containing three K-homologous (KH) domains." Leffers H., Dejgaard K., Celis J.E. Eur. J. Biochem. 230:447-453(1995) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[2]	"Homo sapiens mRNA." Sugiyama A., Inoue H., Oka M. Submitted (AUG-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4).
[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] (ISOFORM 3). Tissue: Synovium.
[4]	"Homo sapiens protein coding cDNA." 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] (ISOFORM 6). Tissue: Brain.
[5]	"The finished DNA sequence of human chromosome 12." Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R. , Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K., Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D., Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J., Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A., Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M., Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I., Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A., Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G., Gibbs R.A. Nature 440:346-351(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]	Mural R.J., Istrail S., Sutton 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 (JUL-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] (ISOFORMS 1; 3 AND 5). Tissue: Eye, Lung and Mammary gland.
[8]	Lubec G., Chen W.-Q., Sun Y. Submitted (DEC-2008) to UniProtKB Cited for: PROTEIN SEQUENCE OF 47-70; 102-115; 145-160 AND 323-354, MASS SPECTROMETRY. Tissue: Fetal brain cortex.
[9]	"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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Tissue: Cervix carcinoma.
[10]	"Improved titanium dioxide enrichment of phosphopeptides from HeLa cells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra." Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D. J. Proteome Res. 6:4150-4162(2007) [PubMed] [Europe PMC] [Abstract] Cited for: 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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. 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-272, 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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[14]	"PCBP2 mediates degradation of the adaptor MAVS via the HECT ubiquitin ligase AIP4." You F., Sun H., Zhou X., Sun W., Liang S., Zhai Z., Jiang Z. Nat. Immunol. 10:1300-1308(2009) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, INTERACTION WITH IFIH1; RNF135; MAVS AND ITCH.
[15]	"Control of c-myc mRNA stability by IGF2BP1-associated cytoplasmic RNPs." Weidensdorfer D., Stoehr N., Baude A., Lederer M., Koehn M., Schierhorn A., Buchmeier S., Wahle E., Huettelmaiery S. RNA 15:104-115(2009) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION IN A MRNP COMPLEX, SUBCELLULAR LOCATION, IDENTIFICATION BY MASS SPECTROMETRY.
[16]	"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 SER-189, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[17]	"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-173; SER-189 AND SER-364, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[18]	"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].
[19]	"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 SER-173; SER-364 AND SER-365, MASS SPECTROMETRY.
[20]	"Crystal structure of the first KH domain of human poly(C)-binding protein-2 in complex with a C-rich strand of human telomeric DNA at 1.7 A." Du Z., Lee J.K., Tjhen R., Li S., Pan H., Stroud R.M., James T.L. J. Biol. Chem. 280:38823-38830(2005) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 11-82 IN COMPLEX WITH DNA.
[21]	"Crystal structure of the third KH domain of human poly(C)-binding protein-2 in complex with a C-rich strand of human telomeric DNA at 1.6 A resolution." Fenn S., Du Z., Lee J.K., Tjhen R., Stroud R.M., James T.L. Nucleic Acids Res. 35:2651-2660(2007) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF 285-359 IN COMPLEX WITH DNA.
[22]	"X-ray crystallographic and NMR studies of protein-protein and protein-nucleic acid interactions involving the KH domains from human poly(C)-binding protein-2." Du Z., Lee J.K., Fenn S., Tjhen R., Stroud R.M., James T.L. RNA 13:1043-1051(2007) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.12 ANGSTROMS) OF 11-82 IN COMPLEX WITH DNA.
[23]	"Structure of a construct of a human poly(C)-binding protein containing the first and second KH domains reveals insights into its regulatory mechanisms." Du Z., Fenn S., Tjhen R., James T.L. J. Biol. Chem. 283:28757-28766(2008) [PubMed] [Europe PMC] [Abstract] Cited for: STRUCTURE BY NMR OF 11-169.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

X78136 mRNA. Translation: CAA55015.1.
AB188306 mRNA. Translation: BAD36897.1.
AK292141 mRNA. Translation: BAF84830.1.
AB208825 mRNA. Translation: BAD92062.1. Different initiation.
AC023509 Genomic DNA. No translation available.
AC068889 Genomic DNA. No translation available.
CH471054 Genomic DNA. Translation: EAW96706.1.
CH471054 Genomic DNA. Translation: EAW96707.1.
CH471054 Genomic DNA. Translation: EAW96709.1.
BC001155 mRNA. Translation: AAH01155.1.
BC071942 mRNA. Translation: AAH71942.1.
BC107688 mRNA. Translation: AAI07689.1.

IPI

IPI00012066.
IPI00216689.
IPI00470509.
IPI00791223.
IPI00796337.

PIR

S42471. S65679.

RefSeq

NP_001092090.1. NM_001098620.2.
NP_001122383.1. NM_001128911.1.
NP_001122384.1. NM_001128912.1.
NP_001122385.1. NM_001128913.1.
NP_001122386.1. NM_001128914.1.
NP_005007.2. NM_005016.5.
NP_114366.1. NM_031989.4.

UniGene

Hs.546271.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2AXY	X-ray	1.70	A/B/C/D	11-82	[»]
2JZX	NMR	-	A	11-169	[»]
2P2R	X-ray	1.60	A	285-359	[»]
2PQU	X-ray	2.12	A/B/C/D	11-82	[»]
2PY9	X-ray	2.56	A/B/C/D	11-82	[»]

ProteinModelPortal

Q15366.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-58934N.

IntAct

Q15366. 13 interactions.

MINT

MINT-96192.

STRING

9606.ENSP00000352438.

PTM databases

PhosphoSite

Q15366.

Polymorphism databases

DMDM

6707736.

Proteomic databases

PaxDb

Q15366.

PeptideAtlas

Q15366.

PRIDE

Q15366.

Protocols and materials databases

DNASU

5094.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000359282; ENSP00000352228; ENSG00000197111.
ENST00000359462; ENSP00000352438; ENSG00000197111.
ENST00000439930; ENSP00000408949; ENSG00000197111.
ENST00000447282; ENSP00000394116; ENSG00000197111.
ENST00000546463; ENSP00000448762; ENSG00000197111.
ENST00000548933; ENSP00000449062; ENSG00000197111.
ENST00000552296; ENSP00000448927; ENSG00000197111.

GeneID

5094.

KEGG

hsa:5094.

UCSC

uc001sdl.4. human.

Organism-specific databases

CTD

5094.

GeneCards

GC12P053844.

HGNC

HGNC:8648. PCBP2.

HPA

HPA038356.

MIM

601210. gene.

neXtProt

NX_Q15366.

PharmGKB

PA32987.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG315872.

HOGENOM

HOG000182823.

HOVERGEN

HBG053520.

InParanoid

Q15366.

KO

K13162.

OMA

CVVMLEL.

Enzyme and pathway databases

Reactome

REACT_1675. mRNA Processing.
REACT_6900. Immune System.
REACT_71. Gene Expression.

Gene expression databases

ArrayExpress

Q15366.

Bgee

Q15366.

CleanEx

HS_PCBP2.

Genevestigator

Q15366.

GermOnline

ENSG00000197111. Homo sapiens.

Family and domain databases

InterPro

IPR004087. KH_dom.
IPR004088. KH_dom_type_1.
[Graphical view]

Pfam

PF00013. KH_1. 3 hits.
[Graphical view]

SMART

SM00322. KH. 3 hits.
[Graphical view]

PROSITE

PS50084. KH_TYPE_1. 3 hits.
[Graphical view]

ProtoNet

Search...

Other

ChiTaRS

PCBP2. human.

EvolutionaryTrace

Q15366.

GenomeRNAi

5094.

NextBio

19648.

SOURCE

Search...

Entry information

Entry name

PCBP2_HUMAN

Accession

Primary (citable) accession number: Q15366
Secondary accession number(s): A8K7X6 , F8VYL7, I6L8F9, Q32Q82, Q59HD4, Q68Y55, Q6IPF4, Q6PKG5

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 30, 2000
Last sequence update:	November 1, 1996
Last modified:	May 1, 2013
This is version 131 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.