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Q9Z204 (HNRPC_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 127. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·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
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length313 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 By similarity.

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 By similarity.

Subcellular location

Nucleus By similarity. Note: Component of ribonucleosomes By similarity.

Post-translational modification

Phosphorylated on Ser-268 and Ser-306 in resting cells By similarity.

Sumoylated. Sumoylation reduces affinity for mRNA By similarity.

Sequence similarities

Belongs to the RRM HNRPC family. RALY subfamily.

Contains 1 RRM (RNA recognition motif) domain.

Alternative products

This entry describes 5 isoforms produced by alternative splicing. [Align] [Select]
Isoform C2 (identifier: Q9Z204-1)

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: Q9Z204-2)

The sequence of this isoform differs from the canonical sequence as follows:
     108-120: Missing.
Isoform 3 (identifier: Q9Z204-3)

The sequence of this isoform differs from the canonical sequence as follows:
     108-120: Missing.
     227-233: Missing.
Isoform 4 (identifier: Q9Z204-4)

The sequence of this isoform differs from the canonical sequence as follows:
     108-120: Missing.
     227-234: Missing.
Isoform 5 (identifier: Q9Z204-5)

The sequence of this isoform differs from the canonical sequence as follows:
     227-233: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 313312Heterogeneous nuclear ribonucleoproteins C1/C2
PRO_0000081845

Regions

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

Amino acid modifications

Modified residue21N-acetylalanine By similarity
Modified residue1131Phosphoserine By similarity
Modified residue1151Phosphoserine By similarity
Modified residue1621Phosphoserine By similarity
Modified residue1661Phosphoserine By similarity
Modified residue1761N6-acetyllysine Ref.8
Modified residue2311Phosphoserine Ref.6
Modified residue2411Phosphoserine Ref.7
Modified residue2491Phosphoserine By similarity
Modified residue2611Phosphoserine By similarity
Modified residue2681Phosphoserine Ref.5 Ref.7
Modified residue3061Phosphoserine By similarity
Modified residue3131Phosphoserine By similarity
Cross-link258Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) By similarity

Natural variations

Alternative sequence108 – 12013Missing in isoform C1, isoform 3 and isoform 4.
VSP_005832
Alternative sequence227 – 2348Missing in isoform 4.
VSP_019227
Alternative sequence227 – 2337Missing in isoform 3 and isoform 5.
VSP_005833

Experimental info

Sequence conflict461C → R in AAH04706. Ref.3

Sequences

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

Last modified May 1, 1999. Version 1.
Checksum: 4AB834051E3E301B

FASTA31334,385
        10         20         30         40         50         60 
MASNVTNKTD PRSMNSRVFI GNLNTLVVKK SDVEAIFSKY GKIVGCSVHK GFAFVQYVNE 

        70         80         90        100        110        120 
RNARAAVAGE DGRMIAGQVL DINLAAEPKV NRGKAGVKRS AAEMYGSVPE HPSPSPLLSS 

       130        140        150        160        170        180 
SFDLDYDFQR DYYDRMYSYP ARVPPPPPIA RAVVPSKRQR VSGNTSRRGK SGFNSKSGQR 

       190        200        210        220        230        240 
GSSSKSGKLK GDDLQAIKKE LTQIKQKVDS LLESLEKIEK EQSKQADLSF SSPVEMKNEK 

       250        260        270        280        290        300 
SEEEQSSASV KKDETNVKME SEAGADDSAE EGDLLDDDDN EDRGDDQLEL KDDEKEPEEG 

       310 
EDDRDSANGE DDS 

« Hide

Isoform C1 [UniParc].

Checksum: 5D602FF5656B750B
Show »

FASTA30033,056
Isoform 3 [UniParc].

Checksum: 7AC110DB06014FEC
Show »

FASTA29332,323
Isoform 4 [UniParc].

Checksum: 84A26D34AABD5806
Show »

FASTA29232,223
Isoform 5 [UniParc].

Checksum: 7AD8B459F9A7FF9B
Show »

FASTA30633,651

References

« Hide 'large scale' references
[1]"hnRNP C is required for postimplantation mouse development but is dispensable for cell viability."
Williamson D.J., Banik-Maiti S., DeGregori J., Ruley H.E.
Mol. Cell. Biol. 20:4094-4105(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM C2).
[2]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS C1; C2; 3 AND 5).
Strain: C57BL/6J and NOD.
Tissue: Colon, Embryo and Thymus.
[3]"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 AND 4).
Strain: FVB/N.
Tissue: Mammary gland.
[4]Lubec G., Yang J.W., Zigmond M.
Submitted (JUL-2007) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 51-61.
Tissue: Brain.
[5]"Phosphoproteomic analysis of the developing mouse brain."
Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.
Mol. Cell. Proteomics 3:1093-1101(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-268, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Embryonic brain.
[6]"Large-scale phosphorylation analysis of mouse liver."
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-231, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Liver.
[7]"The phagosomal proteome in interferon-gamma-activated macrophages."
Trost M., English L., Lemieux S., Courcelles M., Desjardins M., Thibault P.
Immunity 30:143-154(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-241 AND SER-268, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[8]"SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-176, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Embryonic fibroblast.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF095257 mRNA. Translation: AAD03717.1.
AF095258 Genomic DNA. Translation: AAD19892.1.
AK011336 mRNA. Translation: BAB27553.1.
AK012633 mRNA. Translation: BAB28370.1.
AK019958 mRNA. Translation: BAB31934.1.
AK088245 mRNA. Translation: BAC40233.1.
AK088678 mRNA. Translation: BAC40499.1.
AK089061 mRNA. Translation: BAC40728.1.
AK166590 mRNA. Translation: BAE38877.1.
AK168802 mRNA. Translation: BAE40632.1.
BC004706 mRNA. Translation: AAH04706.1.
BC095922 mRNA. Translation: AAH95922.1.
RefSeqNP_001164452.1. NM_001170981.1.
NP_001164453.1. NM_001170982.1.
NP_001164454.1. NM_001170983.1.
NP_001164455.1. NM_001170984.1.
NP_058580.1. NM_016884.3.
XP_006518634.1. XM_006518571.1.
XP_006518635.1. XM_006518572.1.
XP_006518636.1. XM_006518573.1.
XP_006518637.1. XM_006518574.1.
XP_006518639.1. XM_006518576.1.
XP_006518640.1. XM_006518577.1.
XP_006518641.1. XM_006518578.1.
XP_006518642.1. XM_006518579.1.
XP_006518643.1. XM_006518580.1.
XP_006518644.1. XM_006518581.1.
UniGeneMm.427321.
Mm.473169.

3D structure databases

ProteinModelPortalQ9Z204.
SMRQ9Z204. Positions 2-92, 194-221.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid200356. 2 interactions.
DIPDIP-59747N.
IntActQ9Z204. 1 interaction.
MINTMINT-1864181.

PTM databases

PhosphoSiteQ9Z204.

Proteomic databases

PaxDbQ9Z204.
PRIDEQ9Z204.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000111610; ENSMUSP00000107237; ENSMUSG00000060373. [Q9Z204-1]
ENSMUST00000164655; ENSMUSP00000133052; ENSMUSG00000060373. [Q9Z204-1]
GeneID15381.
KEGGmmu:15381.
UCSCuc007tob.2. mouse. [Q9Z204-1]
uc007toc.2. mouse. [Q9Z204-4]
uc007tod.2. mouse. [Q9Z204-2]
uc007toe.2. mouse. [Q9Z204-3]
uc007tof.2. mouse. [Q9Z204-5]

Organism-specific databases

CTD3183.
MGIMGI:107795. Hnrnpc.

Phylogenomic databases

eggNOGNOG311712.
GeneTreeENSGT00390000006718.
HOVERGENHBG002302.
KOK12884.
OMAFSSPVEM.
OrthoDBEOG7KWSK9.
PhylomeDBQ9Z204.
TreeFamTF330974.

Gene expression databases

BgeeQ9Z204.
CleanExMM_HNRNPC.
GenevestigatorQ9Z204.

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. mouse.
NextBio288046.
PROQ9Z204.
SOURCESearch...

Entry information

Entry nameHNRPC_MOUSE
AccessionPrimary (citable) accession number: Q9Z204
Secondary accession number(s): Q3TLB5 expand/collapse secondary AC list , Q501Q3, Q8C2G5, Q99KE2, Q9CQT3, Q9CY83
Entry history
Integrated into UniProtKB/Swiss-Prot: May 2, 2002
Last sequence update: May 1, 1999
Last modified: April 16, 2014
This is version 127 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot