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Protein

Heterogeneous nuclear ribonucleoprotein C

Gene

Hnrnpc

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Binds pre-mRNA and nucleates the assembly of 40S hnRNP particles. Specifically recognizes and binds N6-methyladenosine (m6A)-containing RNAs, a modification present at internal sites of mRNAs that affects mRNA splicing, processing and stability. M6A alters the local structure in mRNAs and long non-coding RNAs (lncRNAs) via a mechanism named 'm6A-switch' to facilitate binding of HNRNPC, leading to regulation of mRNA splicing. 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.By similarity

GO - Molecular functioni

  • deaminase binding Source: RGD
  • enzyme inhibitor activity Source: RGD
  • mRNA binding Source: RGD
  • N6-methyladenosine-containing RNA binding Source: UniProtKB
  • nucleotide binding Source: InterPro
  • protein domain specific binding Source: RGD
  • ribonucleoprotein complex binding Source: RGD

GO - Biological processi

  • mRNA splicing, via spliceosome Source: UniProtKB
  • negative regulation of catalytic activity Source: GOC
  • negative regulation of mRNA modification Source: RGD
Complete GO annotation...

Keywords - Molecular functioni

Ribonucleoprotein

Keywords - Biological processi

mRNA processing, mRNA splicing

Keywords - Ligandi

RNA-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Heterogeneous nuclear ribonucleoprotein CCurated
Short name:
hnRNP C
Alternative name(s):
hnRNP core protein C
Gene namesi
Name:HnrnpcImported
Synonyms:Hnrpc
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi1309982. Hnrnpc.

Subcellular locationi

  • Nucleus By similarity

  • Note: Component of ribonucleosomes.By similarity

GO - Cellular componenti

  • nucleoplasmic periphery of the nuclear pore complex Source: RGD
  • nucleus Source: RGD
  • spliceosomal complex Source: HGNC
Complete GO annotation...

Keywords - Cellular componenti

Nucleus, Spliceosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedBy similarity
Chaini2 – 298297Heterogeneous nuclear ribonucleoprotein CPRO_0000432125Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanineBy similarity
Cross-linki50 – 50Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Cross-linki89 – 89Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Cross-linki94 – 94Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Modified residuei108 – 1081PhosphoserineBy similarity
Modified residuei149 – 1491PhosphoserineBy similarity
Modified residuei153 – 1531PhosphoserineBy similarity
Modified residuei163 – 1631N6-acetyllysine; alternateBy similarity
Cross-linki163 – 163Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateBy similarity
Cross-linki209 – 209Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Modified residuei214 – 2141PhosphoserineCombined sources
Modified residuei216 – 2161PhosphoserineBy similarity
Modified residuei217 – 2171PhosphoserineCombined sources
Cross-linki222 – 222Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Cross-linki225 – 225Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Modified residuei226 – 2261PhosphoserineCombined sources
Modified residuei231 – 2311PhosphoserineCombined sources
Modified residuei232 – 2321PhosphoserineBy similarity
Modified residuei234 – 2341PhosphoserineCombined sources
Cross-linki236 – 236Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Cross-linki237 – 237Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Cross-linki243 – 243Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)By similarity
Modified residuei246 – 2461PhosphoserineCombined sources
Modified residuei253 – 2531PhosphoserineCombined sources
Modified residuei291 – 2911PhosphoserineCombined sources
Modified residuei298 – 2981PhosphoserineBy similarity

Post-translational modificationi

Phosphorylated on Ser-253 and Ser-291 in resting cells.By similarity
Sumoylated. Sumoylation reduces affinity for mRNA.By similarity

Keywords - PTMi

Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

PaxDbiG3V9R8.
PRIDEiG3V9R8.

PTM databases

iPTMnetiG3V9R8.

Expressioni

Gene expression databases

GenevisibleiG3V9R8. RN.

Interactioni

Subunit structurei

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.By similarity

GO - Molecular functioni

  • deaminase binding Source: RGD
  • protein domain specific binding Source: RGD

Protein-protein interaction databases

IntActiG3V9R8. 1 interaction.
MINTiMINT-7138494.
STRINGi10116.ENSRNOP00000057257.

Structurei

3D structure databases

ProteinModelPortaliG3V9R8.
SMRiG3V9R8. Positions 2-92, 179-206.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini16 – 8772RRMPROSITE-ProRule annotationAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili176 – 21136Sequence analysisAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi142 – 1487Nuclear localization signalSequence analysis

Sequence similaritiesi

Belongs to the RRM HNRPC family. RALY subfamily.Curated
Contains 1 RRM (RNA recognition motif) domain.PROSITE-ProRule annotation

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiKOG0118. Eukaryota.
COG0724. LUCA.
HOGENOMiHOG000231958.
HOVERGENiHBG002302.
OMAiSPVEMKN.
OrthoDBiEOG7KWSK9.
PhylomeDBiG3V9R8.
TreeFamiTF330974.

Family and domain databases

Gene3Di3.30.70.330. 1 hit.
InterProiIPR017347. hnRNP_C.
IPR012677. Nucleotide-bd_a/b_plait.
IPR000504. RRM_dom.
[Graphical view]
PfamiPF00076. RRM_1. 1 hit.
[Graphical view]
PIRSFiPIRSF037992. hnRNP-C_Raly. 1 hit.
SMARTiSM00360. RRM. 1 hit.
[Graphical view]
SUPFAMiSSF54928. SSF54928. 1 hit.
PROSITEiPS50102. RRM. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

G3V9R8-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MASNVTNKTD PRSMNSRVFI GNLNTLVVKK SDVEAIFSKY GKIVGCSVHK
60 70 80 90 100
GFAFVQYVNE RNARAAVAGE DGRMIAGQVL DINLAAEPKV NRGKAGVKRS
110 120 130 140 150
AAEMYGSSFD LDYDFQRDYY DRMYSYPARV PPPPPIARAV VPSKRQRVSG
160 170 180 190 200
NTSRRGKSGF NSKSGQRGSS SKSVKGDDLQ AIKKELTQIK QKVDSLLESL
210 220 230 240 250
EKIEKEQSKQ ADLSFSSPVE MKNEKSEEEQ SSASVKKDET NVKMESEAGA
260 270 280 290
DDSAEEGDLL DDDDNEDRGD DQLELKDDEK EPEEGEDDRD SANGEDDS
Length:298
Mass (Da):32,857
Last modified:April 3, 2013 - v2
Checksum:iF4D2F4A6E3F85479
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AABR06080380 Genomic DNA. No translation available.
AABR06080381 Genomic DNA. No translation available.
AABR06080382 Genomic DNA. No translation available.
AABR06080383 Genomic DNA. No translation available.
AABR06080384 Genomic DNA. No translation available.
AABR06082837 Genomic DNA. No translation available.
AABR06082838 Genomic DNA. No translation available.
AABR06082839 Genomic DNA. No translation available.
BC097346 mRNA. Translation: AAH97346.1.
UniGeneiRn.101929.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AABR06080380 Genomic DNA. No translation available.
AABR06080381 Genomic DNA. No translation available.
AABR06080382 Genomic DNA. No translation available.
AABR06080383 Genomic DNA. No translation available.
AABR06080384 Genomic DNA. No translation available.
AABR06082837 Genomic DNA. No translation available.
AABR06082838 Genomic DNA. No translation available.
AABR06082839 Genomic DNA. No translation available.
BC097346 mRNA. Translation: AAH97346.1.
UniGeneiRn.101929.

3D structure databases

ProteinModelPortaliG3V9R8.
SMRiG3V9R8. Positions 2-92, 179-206.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiG3V9R8. 1 interaction.
MINTiMINT-7138494.
STRINGi10116.ENSRNOP00000057257.

PTM databases

iPTMnetiG3V9R8.

Proteomic databases

PaxDbiG3V9R8.
PRIDEiG3V9R8.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Organism-specific databases

RGDi1309982. Hnrnpc.

Phylogenomic databases

eggNOGiKOG0118. Eukaryota.
COG0724. LUCA.
HOGENOMiHOG000231958.
HOVERGENiHBG002302.
OMAiSPVEMKN.
OrthoDBiEOG7KWSK9.
PhylomeDBiG3V9R8.
TreeFamiTF330974.

Miscellaneous databases

PROiG3V9R8.

Gene expression databases

GenevisibleiG3V9R8. RN.

Family and domain databases

Gene3Di3.30.70.330. 1 hit.
InterProiIPR017347. hnRNP_C.
IPR012677. Nucleotide-bd_a/b_plait.
IPR000504. RRM_dom.
[Graphical view]
PfamiPF00076. RRM_1. 1 hit.
[Graphical view]
PIRSFiPIRSF037992. hnRNP-C_Raly. 1 hit.
SMARTiSM00360. RRM. 1 hit.
[Graphical view]
SUPFAMiSSF54928. SSF54928. 1 hit.
PROSITEiPS50102. RRM. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Genome sequence of the Brown Norway rat yields insights into mammalian evolution."
    Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J., Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G., Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G., Morgan M.
    , Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G., Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S., Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T., Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D., Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L., Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D., Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M., Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C., Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J., Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H., Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X., Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q., Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P., Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A., Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C., Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J., Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J., Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F., Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A., Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A., Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J., Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E., Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M., Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C., Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L., Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W., Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y., Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V., Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M., Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S., Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B., Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R., Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J., Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D., Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S., Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S., Mockrin S., Collins F.S.
    Nature 428:493-521(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Brown Norway.
  2. "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].
    Tissue: Placenta.
  3. "Quantitative phosphoproteomics of vasopressin-sensitive renal cells: regulation of aquaporin-2 phosphorylation at two sites."
    Hoffert J.D., Pisitkun T., Wang G., Shen R.-F., Knepper M.A.
    Proc. Natl. Acad. Sci. U.S.A. 103:7159-7164(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-234, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  4. "Quantitative maps of protein phosphorylation sites across 14 different rat organs and tissues."
    Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C., Olsen J.V.
    Nat. Commun. 3:876-876(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-214; SER-217; SER-226; SER-231; SER-246; SER-253 AND SER-291, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiHNRPC_RAT
AccessioniPrimary (citable) accession number: G3V9R8
Secondary accession number(s): D4ACR0, Q4V8K6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 4, 2015
Last sequence update: April 3, 2013
Last modified: June 8, 2016
This is version 45 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.