P07910 (HNRPC_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Heterogeneous nuclear ribonucleoproteins C1/C2
Short name=hnRNP C1/C2

Gene names

Name:	HNRNPC
Synonyms:	HNRPC

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	306 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Binds pre-mRNA and nucleates the assembly of 40S hnRNP particles. Single HNRNPC tetramers bind 230-240 nucleotides. Trimers of HNRNPC tetramers bind 700 nucleotides. May play a role in the early steps of spliceosome assembly and pre-mRNA splicing. Interacts with poly-U tracts in the 3'-UTR or 5'-UTR of mRNA and modulates the stability and the level of translation of bound mRNA molecules. Ref.10 Ref.11 Ref.14 Ref.16
Subunit structure	Tetramer composed of 3 copies of isoform C1 and 1 copy of isoform C2. Assembly of 3 tetramers with bound pre-mRNA gives rise to a 19S complex that interacts with HNRNPA2B1 tetramers. Component of the 40S hnRNP particle. Identified in the spliceosome C complex. Interacts with IGF2BP1. Ref.10 Ref.12 Ref.20 Ref.31 Ref.33
Subcellular location	Nucleus. Note: Component of ribonucleosomes.
Post-translational modification	Phosphorylated on Ser-260 and Ser-299 in resting cells. Phosphorylated on Ser-253 and on 1 serine residue in the poly-Ser stretch at position 238 in response to hydrogen peroxide. Ref.13 Sumoylated. Sumoylation reduces affinity for mRNA. Ref.15
Sequence similarities	Belongs to the RRM HNRPC family. RALY subfamily. Contains 1 RRM (RNA recognition motif) domain.
Sequence caution	The sequence BAD92764.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Ontologies

Keywords
Biological process	mRNA processing mRNA splicing
Cellular component	Nucleus Spliceosome
Coding sequence diversity	Alternative splicing Polymorphism
Ligand	RNA-binding
Molecular function	Ribonucleoprotein
PTM	Acetylation Isopeptide bond Phosphoprotein Ubl conjugation
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	mRNA splicing, via spliceosome Inferred by curator Ref.12. Source: UniProtKB
Cellular_component	catalytic step 2 spliceosome Inferred from direct assay Ref.12. Source: UniProtKB nucleoplasm Traceable author statement. Source: Reactome
Molecular_function	RNA binding Non-traceable author statement PubMed 9731529. Source: HGNC nucleotide binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
itself		2	EBI-357966,EBI-357966

Alternative products

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

Isoform C2 (identifier: P07910-1)

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 C1 (identifier: P07910-2)

The sequence of this isoform differs from the canonical sequence as follows:
     108-120: Missing.

Note: Contains a phosphoserine at position 107. Contains a phosphoserine at position 108.

Isoform 3 (identifier: P07910-3)

The sequence of this isoform differs from the canonical sequence as follows:
     39-119: KYGKIVGCSV...EHPSPSPLLS → N

Isoform 4 (identifier: P07910-4)

The sequence of this isoform differs from the canonical sequence as follows:
     108-120: Missing.
     153-195: Missing.

Note: Contains a phosphoserine at position 107. Contains a phosphoserine at position 108.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed Ref.7

Chain

2 – 306

305

Heterogeneous nuclear ribonucleoproteins C1/C2

PRO_0000081844

Regions

Domain

16 – 87

72

RRM

Motif

155 – 161

7

Nuclear localization signal Potential

Compositional bias

181 – 303

123

Asp/Glu-rich (acidic)

Amino acid modifications

Modified residue

2

1

N-acetylalanine Ref.7

Modified residue

109

1

Phosphothreonine Ref.25

Modified residue

113

1

Phosphoserine Ref.23 Ref.25

Modified residue

115

1

Phosphoserine Ref.25

Modified residue

162

1

Phosphoserine Ref.17 Ref.28

Modified residue

166

1

Phosphoserine Ref.28

Modified residue

233

1

Phosphoserine Ref.17 Ref.23 Ref.24 Ref.25 Ref.26 Ref.28

Modified residue

241

1

Phosphoserine Ref.23 Ref.28

Modified residue

253

1

Phosphoserine Ref.13 Ref.17 Ref.22 Ref.24 Ref.25 Ref.28

Modified residue

260

1

Phosphoserine Ref.13 Ref.17 Ref.19 Ref.22 Ref.24 Ref.25 Ref.26 Ref.28

Modified residue

299

1

Phosphoserine Ref.13 Ref.18 Ref.21 Ref.24 Ref.26 Ref.28

Modified residue

306

1

Phosphoserine Ref.24 Ref.28

Cross-link

250

Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) Ref.15

Natural variations

Alternative sequence

39 – 119

81

KYGKI…SPLLS → N in isoform 3.

VSP_019225

Alternative sequence

108 – 120

13

Missing in isoform C1 and isoform 4.

VSP_005831

Alternative sequence

153 – 195

43

Missing in isoform 4.

VSP_019226

Natural variant

167

1

R → Q.
Corresponds to variant rs3272 [ dbSNP | Ensembl ].

VAR_052224

Experimental info

Mutagenesis

197

1

K → R: No effect on sumoylation. Ref.15

Mutagenesis

250

1

K → R: Loss of sumoylation. Ref.15

Sequence conflict

110

1

E → G in AAH08423. Ref.6

Sequence conflict

217

1

I → M Ref.1

Sequence conflict

217

1

I → M Ref.2

Sequence conflict

224

1

Q → R in AAH08364. Ref.6

Sequence conflict

244

1

K → R in AAH08364. Ref.6

Sequence conflict

254

1

E → G in AAH07052. Ref.6

Sequence conflict

303 – 306

4

EDDS → G Ref.1

Sequence conflict

303 – 306

4

EDDS → G Ref.2

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

306

Helix Strand Turn

Details...

Beta strand

18 – 23

6

Turn

25 – 27

3

Helix

30 – 35

6

Beta strand

43 – 49

7

Beta strand

51 – 59

9

Helix

60 – 68

9

Turn

69 – 72

4

Beta strand

81 – 84

4

Helix

194 – 216

23

Sequences

	Sequence		Length	Mass (Da)
	Isoform C2 [UniParc]. Last modified June 13, 2006. Version 4. Checksum: 17BBC78690C69C5C	FASTA	306	33,670
	10 20 30 40 50 60 MASNVTNKTD PRSMNSRVFI GNLNTLVVKK SDVEAIFSKY GKIVGCSVHK GFAFVQYVNE 70 80 90 100 110 120 RNARAAVAGE DGRMIAGQVL DINLAAEPKV NRGKAGVKRS AAEMYGSVTE HPSPSPLLSS 130 140 150 160 170 180 SFDLDYDFQR DYYDRMYSYP ARVPPPPPIA RAVVPSKRQR VSGNTSRRGK SGFNSKSGQR 190 200 210 220 230 240 GSSKSGKLKG DDLQAIKKEL TQIKQKVDSL LENLEKIEKE QSKQAVEMKN DKSEEEQSSS 250 260 270 280 290 300 SVKKDETNVK MESEGGADDS AEEGDLLDDD DNEDRGDDQL ELIKDDEKEA EEGEDDRDSA NGEDDS
	Isoform C1 [UniParc]. Checksum: B90DDFD06A77FEE8	FASTA	293	32,338
	10 20 30 40 50 60 MASNVTNKTD PRSMNSRVFI GNLNTLVVKK SDVEAIFSKY GKIVGCSVHK GFAFVQYVNE 70 80 90 100 110 120 RNARAAVAGE DGRMIAGQVL DINLAAEPKV NRGKAGVKRS AAEMYGSSFD LDYDFQRDYY 130 140 150 160 170 180 DRMYSYPARV PPPPPIARAV VPSKRQRVSG NTSRRGKSGF NSKSGQRGSS KSGKLKGDDL 190 200 210 220 230 240 QAIKKELTQI KQKVDSLLEN LEKIEKEQSK QAVEMKNDKS EEEQSSSSVK KDETNVKMES 250 260 270 280 290 EGGADDSAEE GDLLDDDDNE DRGDDQLELI KDDEKEAEEG EDDRDSANGE DDS
	Isoform 3 [UniParc]. Checksum: BE6EC8C7A9FD7114	FASTA	226	25,230
	10 20 30 40 50 60 MASNVTNKTD PRSMNSRVFI GNLNTLVVKK SDVEAIFSNS SFDLDYDFQR DYYDRMYSYP 70 80 90 100 110 120 ARVPPPPPIA RAVVPSKRQR VSGNTSRRGK SGFNSKSGQR GSSKSGKLKG DDLQAIKKEL 130 140 150 160 170 180 TQIKQKVDSL LENLEKIEKE QSKQAVEMKN DKSEEEQSSS SVKKDETNVK MESEGGADDS 190 200 210 220 AEEGDLLDDD DNEDRGDDQL ELIKDDEKEA EEGEDDRDSA NGEDDS
	Isoform 4 [UniParc]. Checksum: 543388C3EC431836	FASTA	250	27,822
	10 20 30 40 50 60 MASNVTNKTD PRSMNSRVFI GNLNTLVVKK SDVEAIFSKY GKIVGCSVHK GFAFVQYVNE 70 80 90 100 110 120 RNARAAVAGE DGRMIAGQVL DINLAAEPKV NRGKAGVKRS AAEMYGSSFD LDYDFQRDYY 130 140 150 160 170 180 DRMYSYPARV PPPPPIARAI KKELTQIKQK VDSLLENLEK IEKEQSKQAV EMKNDKSEEE 190 200 210 220 230 240 QSSSSVKKDE TNVKMESEGG ADDSAEEGDL LDDDDNEDRG DDQLELIKDD EKEAEEGEDD 250 RDSANGEDDS

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Primary structures of the heterogeneous nuclear ribonucleoprotein A2, B1, and C2 proteins: a diversity of RNA binding proteins is generated by small peptide inserts." Burd C.G., Swanson M.S., Goerlach M., Dreyfuss G. Proc. Natl. Acad. Sci. U.S.A. 86:9788-9792(1989) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM C2).
[2]	"Primary structure of human nuclear ribonucleoprotein particle C proteins: conservation of sequence and domain structures in heterogeneous nuclear RNA, mRNA, and pre-rRNA-binding proteins." Swanson M.S., Nakagawa T.Y., Levan K., Dreyfuss G. Mol. Cell. Biol. 7:1731-1739(1987) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM C1).
[3]	"Full-length cDNA libraries and normalization." Li W.B., Gruber C., Jessee J., Polayes D. Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS C1 AND 3). Tissue: Neuroblastoma and Placenta.
[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] (ISOFORM C2). Tissue: Brain.
[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] (ISOFORMS C1; C2 AND 4). Tissue: Bone marrow, Brain, Chondrosarcoma, Eye and Placenta.
[7]	Bienvenut W.V., Matallanas D., Cooper W.N., Calvo F., Kolch W. Submitted (FEB-2008) to UniProtKB Cited for: PROTEIN SEQUENCE OF 2-12; 18-39; 43-61; 74-89; 143-151; 188-198 AND 205-216, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, MASS SPECTROMETRY. Tissue: Cervix carcinoma and Mammary carcinoma.
[8]	Lubec G., Vishwanath V., Chen W.-Q., Sun Y. Submitted (DEC-2008) to UniProtKB Cited for: PROTEIN SEQUENCE OF 18-39; 51-61; 74-89 AND 207-216, MASS SPECTROMETRY. Tissue: Brain, Cajal-Retzius cell and Fetal brain cortex.
[9]	"Primary structure differences between proteins C1 and C2 of HeLa 40S nuclear ribonucleoprotein particles." Merrill B.M., Barnett S.F., Lestourgeon W.M., Williams K.R. Nucleic Acids Res. 17:8441-8449(1989) [PubMed] [Europe PMC] [Abstract] Cited for: PARTIAL PROTEIN SEQUENCE, ALTERNATIVE SPLICING, CHARACTERIZATION.
[10]	"The C-protein tetramer binds 230 to 240 nucleotides of pre-mRNA and nucleates the assembly of 40S heterogeneous nuclear ribonucleoprotein particles." Huang M., Rech J.E., Northington S.J., Flicker P.F., Mayeda A., Krainer A.R., LeStourgeon W.M. Mol. Cell. Biol. 14:518-533(1994) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, SUBUNIT.
[11]	"A T to G mutation in the polypyrimidine tract of the second intron of the human beta-globin gene reduces in vitro splicing efficiency: evidence for an increased hnRNP C interaction." Sebillon P., Beldjord C., Kaplan J.-C., Brody E., Marie J. Nucleic Acids Res. 23:3419-3425(1995) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[12]	"Purification and characterization of native spliceosomes suitable for three-dimensional structural analysis." Jurica M.S., Licklider L.J., Gygi S.P., Grigorieff N., Moore M.J. RNA 8:426-439(2002) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN THE SPLICEOSOMAL C COMPLEX.
[13]	"Basal and hydrogen peroxide stimulated sites of phosphorylation in heterogeneous nuclear ribonucleoprotein C1/C2." Stone J.R., Maki J.L., Collins T. Biochemistry 42:1301-1308(2003) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION AT SER-253; SER-260 AND SER-299, MASS SPECTROMETRY.
[14]	"Heterogeneous nuclear ribonucleoprotein C modulates translation of c-myc mRNA in a cell cycle phase-dependent manner." Kim J.H., Paek K.Y., Choi K., Kim T.-D., Hahm B., Kim K.-T., Jang S.K. Mol. Cell. Biol. 23:708-720(2003) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[15]	"SUMO modification of heterogeneous nuclear ribonucleoproteins." Vassileva M.T., Matunis M.J. Mol. Cell. Biol. 24:3623-3632(2004) [PubMed] [Europe PMC] [Abstract] Cited for: MUTAGENESIS OF LYS-197 AND LYS-250, SUMOYLATION AT LYS-250.
[16]	"Regulation of urokinase receptor mRNA stability by hnRNP C in lung epithelial cells." Shetty S. Mol. Cell. Biochem. 272:107-118(2005) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[17]	"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks." Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M. Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-162; SER-233; SER-253 AND SER-260, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[18]	"Phosphoproteomic analysis of the human pituitary." Beranova-Giorgianni S., Zhao Y., Desiderio D.M., Giorgianni F. Pituitary 9:109-120(2006) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-299, MASS SPECTROMETRY. Tissue: Pituitary.
[19]	"Quantitative phosphoproteome profiling of Wnt3a-mediated signaling network: indicating the involvement of ribonucleoside-diphosphate reductase M2 subunit phosphorylation at residue serine 20 in canonical Wnt signal transduction." Tang L.-Y., Deng N., Wang L.-S., Dai J., Wang Z.-L., Jiang X.-S., Li S.-J., Li L., Sheng Q.-H., Wu D.-Q., Li L., Zeng R. Mol. Cell. Proteomics 6:1952-1967(2007) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-260, MASS SPECTROMETRY. Tissue: Embryonic kidney.
[20]	"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] [Europe PMC] [Abstract] Cited for: INTERACTION WITH IGF2BP1.
[21]	"Phosphorylation analysis of primary human T lymphocytes using sequential IMAC and titanium oxide enrichment." Carrascal M., Ovelleiro D., Casas V., Gay M., Abian J. J. Proteome Res. 7:5167-5176(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-299, MASS SPECTROMETRY. Tissue: T-cell.
[22]	"Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle." Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M. Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-253 AND SER-260, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[23]	"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-113; SER-233 AND SER-241, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-107 AND SER-108 (ISOFORMS 4 AND C1), MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[24]	"Large-scale phosphoproteome analysis of human liver tissue by enrichment and fractionation of phosphopeptides with strong anion exchange chromatography." Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D., Zou H., Gu J. Proteomics 8:1346-1361(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-233; SER-253; SER-260; SER-299 AND SER-306, MASS SPECTROMETRY. Tissue: Liver.
[25]	"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions." Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K. Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-109; SER-113; SER-115; SER-233; SER-253 AND SER-260, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[26]	"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-233; SER-260 AND SER-299, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[27]	"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].
[28]	"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-162; SER-166; SER-233; SER-241; SER-253; SER-260; SER-299 AND SER-306, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-107 (ISOFORMS 4 AND C1), MASS SPECTROMETRY.
[29]	"1H, 13C, and 15N NMR assignments and global folding pattern of the RNA-binding domain of the human hnRNP C proteins." Witteking M., Goerlach M., Friedrichs M., Dreyfuss G., Mueller L. Biochemistry 31:6254-6265(1992) [PubMed] [Europe PMC] [Abstract] Cited for: STRUCTURE BY NMR OF 1-94.
[30]	"Interaction of the RNA-binding domain of the hnRNP C proteins with RNA." Goerlach M., Witteking M., Beckman R.A., Mueller L., Dreyfuss G. EMBO J. 11:3289-3295(1992) [PubMed] [Europe PMC] [Abstract] Cited for: STRUCTURE BY NMR OF 1-94.
[31]	"An antiparallel four-helix bundle orients the high-affinity RNA binding sites in hnRNP C: a mechanism for RNA chaperonin activity." Shahied L., Braswell E.H., LeStourgeon W.M., Krezel A.M. J. Mol. Biol. 305:817-828(2001) [PubMed] [Europe PMC] [Abstract] Cited for: STRUCTURE BY NMR OF 193-220, SUBUNIT.
[32]	"Solution structure of RRM domain in HNRPC protein." RIKEN structural genomics initiative (RSGI) Submitted (NOV-2004) to the PDB data bank Cited for: STRUCTURE BY NMR OF 8-92.
[33]	"Solution structure of the symmetric coiled coil tetramer formed by the oligomerization domain of hnRNP C: implications for biological function." Whitson S.R., LeStourgeon W.M., Krezel A.M. J. Mol. Biol. 350:319-337(2005) [PubMed] [Europe PMC] [Abstract] Cited for: STRUCTURE BY NMR OF 193-220, SUBUNIT.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

M29063 mRNA. Translation: AAA36576.1.
M16342 mRNA. Translation: AAA52680.1.
BX161480 mRNA. Translation: CAD61934.1.
BX247961 mRNA. Translation: CAD62300.1.
BX247992 mRNA. Translation: CAD62326.1.
AB209527 mRNA. Translation: BAD92764.1. Different initiation.
AK223517 mRNA. Translation: BAD97237.1.
CH471078 Genomic DNA. Translation: EAW66392.1.
CH471078 Genomic DNA. Translation: EAW66393.1.
CH471078 Genomic DNA. Translation: EAW66394.1.
CH471078 Genomic DNA. Translation: EAW66395.1.
CH471078 Genomic DNA. Translation: EAW66396.1.
CH471078 Genomic DNA. Translation: EAW66399.1.
CH471078 Genomic DNA. Translation: EAW66400.1.
BC003394 mRNA. Translation: AAH03394.1.
BC007052 mRNA. Translation: AAH07052.1.
BC008364 mRNA. Translation: AAH08364.1.
BC008423 mRNA. Translation: AAH08423.1.
BC066932 mRNA. Translation: AAH66932.1.
BC089438 mRNA. Translation: AAH89438.1.
BC108658 mRNA. Translation: AAI08659.1.
BC103758 mRNA. Translation: AAI03759.1.

IPI

IPI00216592.
IPI00477313.
IPI00759596.
IPI00759822.

PIR

A26885.
C34504.

RefSeq

NP_001070910.1. NM_001077442.1.
NP_001070911.1. NM_001077443.1.
NP_004491.2. NM_004500.3.
NP_112604.2. NM_031314.2.

UniGene

Hs.508848.
Hs.708738.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1TXP	NMR	-	A/B/C/D	194-220	[»]
1WF2	NMR	-	A	8-92	[»]
3LN4	X-ray	1.30	C	102-117	[»]

ProteinModelPortal

P07910.

SMR

P07910. Positions 2-92, 193-220.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-29854N.

IntAct

P07910. 51 interactions.

MINT

MINT-4999718.

PTM databases

PhosphoSite

P07910.

Polymorphism databases

DMDM

108935845.

2D gel databases

SWISS-2DPAGE

P07910.

Proteomic databases

PaxDb

P07910.

PRIDE

P07910.

Protocols and materials databases

DNASU

3183.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000320084; ENSP00000319690; ENSG00000092199.
ENST00000420743; ENSP00000404848; ENSG00000092199.
ENST00000430246; ENSP00000442816; ENSG00000092199.
ENST00000449098; ENSP00000404559; ENSG00000092199.
ENST00000553300; ENSP00000450544; ENSG00000092199.
ENST00000554455; ENSP00000451291; ENSG00000092199.
ENST00000554969; ENSP00000450725; ENSG00000092199.
ENST00000555883; ENSP00000450629; ENSG00000092199.
ENST00000556628; ENSP00000451652; ENSG00000092199.
ENST00000556897; ENSP00000451176; ENSG00000092199.
ENST00000557201; ENSP00000452276; ENSG00000092199.

GeneID

3183.

KEGG

hsa:3183.

UCSC

uc001vzw.3. human.
uc001vzy.3. human.
uc001wac.3. human.
uc001wad.3. human.

Organism-specific databases

CTD

3183.

GeneCards

GC14M021677.

HGNC

HGNC:5035. HNRNPC.

HPA

CAB005223.

MIM

164020. gene.

neXtProt

NX_P07910.

PharmGKB

PA162391217.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG311712.

HOVERGEN

HBG002302.

InParanoid

P07910.

KO

K12884.

OMA

FSSPVEM.

OrthoDB

EOG45490H.

Enzyme and pathway databases

Pathway_Interaction_DB

telomerasepathway. Regulation of Telomerase.

Reactome

REACT_1675. mRNA Processing.
REACT_71. Gene Expression.

Gene expression databases

ArrayExpress

P07910.

Bgee

P07910.

Genevestigator

P07910.

GermOnline

ENSG00000092199. Homo sapiens.

Family and domain databases

Gene3D

3.30.70.330. 1 hit.

InterPro

IPR017347. hnRNP_C_Raly.
IPR012677. Nucleotide-bd_a/b_plait.
IPR000504. RRM_dom.
[Graphical view]

Pfam

PF00076. RRM_1. 1 hit.
[Graphical view]

PIRSF

PIRSF037992. hnRNP-C_Raly. 1 hit.

SMART

SM00360. RRM. 1 hit.
[Graphical view]

PROSITE

PS50102. RRM. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

ChiTaRS

HNRNPC. human.

EvolutionaryTrace

P07910.

GenomeRNAi

3183.

NextBio

12634.

SOURCE

Search...

Entry information

Entry name

HNRPC_HUMAN

Accession

Primary (citable) accession number: P07910
Secondary accession number(s): D3DS19 , D3DS22, P22628, Q53EX2, Q59FD3, Q5FWE8, Q86SF8, Q86U45, Q96HK7, Q96HM4, Q96IY5, Q9BTS3

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 1, 1988
Last sequence update:	June 13, 2006
Last modified:	May 1, 2013
This is version 170 of the entry and version 4 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.