Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

P07910 (HNRPC_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 184. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Heterogeneous nuclear ribonucleoproteins C1/C2

Short name=hnRNP C1/C2
Gene names
Name:HNRNPC
Synonyms:HNRPC
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length306 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence 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.33 Ref.35

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 processmRNA processing
mRNA splicing
   Cellular componentNucleus
Spliceosome
   Coding sequence diversityAlternative splicing
Polymorphism
   LigandRNA-binding
   Molecular functionRibonucleoprotein
   PTMAcetylation
Isopeptide bond
Phosphoprotein
Ubl conjugation
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_process3'-UTR-mediated mRNA stabilization

Inferred from mutant phenotype Ref.16. Source: UniProt

ATP-dependent chromatin remodeling

Inferred from direct assay PubMed 16217013. Source: UniProt

RNA splicing

Traceable author statement. Source: Reactome

gene expression

Traceable author statement. Source: Reactome

mRNA splicing, via spliceosome

Inferred by curator Ref.12. Source: UniProtKB

osteoblast differentiation

Inferred from direct assay PubMed 16210410. Source: UniProt

   Cellular_componentcatalytic step 2 spliceosome

Inferred from direct assay Ref.12. Source: UniProtKB

cytosol

Inferred from direct assay Ref.16. Source: UniProt

extracellular vesicular exosome

Inferred from direct assay PubMed 20458337PubMed 23376485. Source: UniProt

membrane

Inferred from direct assay PubMed 16210410. Source: UniProt

nuclear chromatin

Inferred from direct assay PubMed 16217013. Source: UniProt

nucleoplasm

Traceable author statement. Source: Reactome

nucleus

Inferred from direct assay PubMed 21630459PubMed 22720776. Source: UniProt

protein complex

Inferred from direct assay PubMed 16217013. Source: UniProt

spliceosomal complex

Inferred from direct assay PubMed 9731529. Source: HGNC

   Molecular_functionRNA binding

Non-traceable author statement PubMed 9731529. Source: HGNC

RNA polymerase II core promoter proximal region sequence-specific DNA binding

Inferred from direct assay PubMed 16217013. Source: UniProt

RNA polymerase II distal enhancer sequence-specific DNA binding

Inferred from direct assay PubMed 16217013. Source: UniProt

identical protein binding

Inferred from physical interaction PubMed 16189514PubMed 21516116PubMed 22365833. Source: IntAct

mRNA 3'-UTR binding

Inferred from direct assay Ref.16. Source: UniProt

nucleosomal DNA binding

Inferred from direct assay PubMed 16217013. Source: UniProt

nucleotide binding

Inferred from electronic annotation. Source: InterPro

poly(A) RNA binding

Inferred from direct assay PubMed 22658674PubMed 22681889. Source: UniProtKB

poly(U) RNA binding

Inferred from direct assay Ref.16. Source: UniProt

protein binding

Inferred from physical interaction Ref.20. Source: UniProtKB

Complete GO annotation...

Binary interactions

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 keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.7
Chain2 – 306305Heterogeneous nuclear ribonucleoproteins C1/C2
PRO_0000081844

Regions

Domain16 – 8772RRM
Motif155 – 1617Nuclear localization signal Potential
Compositional bias181 – 303123Asp/Glu-rich (acidic)

Amino acid modifications

Modified residue21N-acetylalanine Ref.7 Ref.30
Modified residue1091Phosphothreonine Ref.26
Modified residue1131Phosphoserine Ref.23 Ref.26
Modified residue1151Phosphoserine Ref.26
Modified residue1621Phosphoserine Ref.17 Ref.29
Modified residue1661Phosphoserine Ref.29
Modified residue1761N6-acetyllysine By similarity
Modified residue2331Phosphoserine Ref.17 Ref.23 Ref.24 Ref.26 Ref.27 Ref.29
Modified residue2411Phosphoserine Ref.23 Ref.29
Modified residue2531Phosphoserine Ref.13 Ref.17 Ref.22 Ref.24 Ref.26 Ref.29
Modified residue2601Phosphoserine Ref.13 Ref.17 Ref.19 Ref.22 Ref.24 Ref.26 Ref.27 Ref.29
Modified residue2991Phosphoserine Ref.13 Ref.18 Ref.21 Ref.24 Ref.27 Ref.29
Modified residue3061Phosphoserine Ref.24 Ref.29
Cross-link250Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) Ref.15

Natural variations

Alternative sequence39 – 11981KYGKI…SPLLS → N in isoform 3.
VSP_019225
Alternative sequence108 – 12013Missing in isoform C1 and isoform 4.
VSP_005831
Alternative sequence153 – 19543Missing in isoform 4.
VSP_019226
Natural variant1671R → Q.
Corresponds to variant rs3272 [ dbSNP | Ensembl ].
VAR_052224

Experimental info

Mutagenesis1971K → R: No effect on sumoylation. Ref.15
Mutagenesis2501K → R: Loss of sumoylation. Ref.15
Sequence conflict1101E → G in AAH08423. Ref.6
Sequence conflict2171I → M Ref.1
Sequence conflict2171I → M Ref.2
Sequence conflict2241Q → R in AAH08364. Ref.6
Sequence conflict2441K → R in AAH08364. Ref.6
Sequence conflict2541E → G in AAH07052. Ref.6
Sequence conflict303 – 3064EDDS → G Ref.1
Sequence conflict303 – 3064EDDS → G Ref.2

Secondary structure

................. 306
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform C2 [UniParc].

Last modified June 13, 2006. Version 4.
Checksum: 17BBC78690C69C5C

FASTA30633,670
        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 

« Hide

Isoform C1 [UniParc].

Checksum: B90DDFD06A77FEE8
Show »

FASTA29332,338
Isoform 3 [UniParc].

Checksum: BE6EC8C7A9FD7114
Show »

FASTA22625,230
Isoform 4 [UniParc].

Checksum: 543388C3EC431836
Show »

FASTA25027,822

References

« Hide '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. expand/collapse author list , 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, IDENTIFICATION BY 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, IDENTIFICATION BY 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, IDENTIFICATION BY 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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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), IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Liver.
[25]"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[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] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-109; SER-113; SER-115; SER-233; SER-253 AND SER-260, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[27]"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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[28]"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].
[29]"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), IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[30]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[31]"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.
[32]"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.
[33]"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.
[34]"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.
[35]"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.
CCDSCCDS41915.1. [P07910-1]
CCDS45079.1. [P07910-2]
PIRA26885.
C34504.
RefSeqNP_001070910.1. NM_001077442.1. [P07910-1]
NP_001070911.1. NM_001077443.1. [P07910-2]
NP_004491.2. NM_004500.3. [P07910-2]
NP_112604.2. NM_031314.2. [P07910-1]
XP_006720188.1. XM_006720125.1. [P07910-2]
XP_006720189.1. XM_006720126.1. [P07910-2]
UniGeneHs.508848.
Hs.675546.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1TXPNMR-A/B/C/D194-220[»]
1WF2NMR-A8-92[»]
3LN4X-ray1.30C102-117[»]
ProteinModelPortalP07910.
SMRP07910. Positions 2-92.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid109424. 133 interactions.
DIPDIP-29854N.
IntActP07910. 70 interactions.
MINTMINT-4999718.

Chemistry

ChEMBLCHEMBL2216742.

PTM databases

PhosphoSiteP07910.

Polymorphism databases

DMDM108935845.

2D gel databases

SWISS-2DPAGEP07910.

Proteomic databases

MaxQBP07910.
PaxDbP07910.
PRIDEP07910.

Protocols and materials databases

DNASU3183.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000320084; ENSP00000319690; ENSG00000092199. [P07910-1]
ENST00000420743; ENSP00000404848; ENSG00000092199. [P07910-1]
ENST00000430246; ENSP00000442816; ENSG00000092199. [P07910-2]
ENST00000449098; ENSP00000404559; ENSG00000092199. [P07910-2]
ENST00000553300; ENSP00000450544; ENSG00000092199. [P07910-2]
ENST00000554455; ENSP00000451291; ENSG00000092199. [P07910-1]
ENST00000554969; ENSP00000450725; ENSG00000092199. [P07910-2]
ENST00000555883; ENSP00000450629; ENSG00000092199. [P07910-4]
ENST00000556628; ENSP00000451652; ENSG00000092199. [P07910-3]
ENST00000556897; ENSP00000451176; ENSG00000092199. [P07910-2]
ENST00000557201; ENSP00000452276; ENSG00000092199. [P07910-1]
GeneID3183.
KEGGhsa:3183.
UCSCuc001vzw.3. human. [P07910-2]
uc001vzy.3. human. [P07910-1]
uc001wac.3. human. [P07910-4]
uc001wad.3. human. [P07910-3]

Organism-specific databases

CTD3183.
GeneCardsGC14M021677.
HGNCHGNC:5035. HNRNPC.
HPACAB005223.
HPA051075.
MIM164020. gene.
neXtProtNX_P07910.
PharmGKBPA162391217.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG311712.
HOVERGENHBG002302.
InParanoidP07910.
KOK12884.
OMAFSSPVEM.
OrthoDBEOG7KWSK9.
PhylomeDBP07910.
TreeFamTF330974.

Enzyme and pathway databases

ReactomeREACT_71. Gene Expression.

Gene expression databases

ArrayExpressP07910.
BgeeP07910.
GenevestigatorP07910.

Family and domain databases

Gene3D3.30.70.330. 1 hit.
InterProIPR017347. hnRNP_C_Raly.
IPR012677. Nucleotide-bd_a/b_plait.
IPR000504. RRM_dom.
[Graphical view]
PfamPF00076. RRM_1. 1 hit.
[Graphical view]
PIRSFPIRSF037992. hnRNP-C_Raly. 1 hit.
SMARTSM00360. RRM. 1 hit.
[Graphical view]
PROSITEPS50102. RRM. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSHNRNPC. human.
EvolutionaryTraceP07910.
GeneWikiHNRNPC.
GenomeRNAi3183.
NextBio12634.
PROP07910.
SOURCESearch...

Entry information

Entry nameHNRPC_HUMAN
AccessionPrimary (citable) accession number: P07910
Secondary accession number(s): D3DS19 expand/collapse secondary AC list , 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: July 9, 2014
This is version 184 of the entry and version 4 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 14

Human chromosome 14: entries, gene names and cross-references to MIM