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P07910

- HNRPC_HUMAN

UniProt

P07910 - HNRPC_HUMAN

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Protein

Heterogeneous nuclear ribonucleoproteins C1/C2

Gene

HNRNPC

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

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.4 Publications

GO - Molecular functioni

  1. identical protein binding Source: IntAct
  2. mRNA 3'-UTR binding Source: UniProt
  3. nucleosomal DNA binding Source: UniProt
  4. nucleotide binding Source: InterPro
  5. poly(A) RNA binding Source: UniProtKB
  6. poly(U) RNA binding Source: UniProt
  7. RNA binding Source: HGNC
  8. RNA polymerase II core promoter proximal region sequence-specific DNA binding Source: UniProt
  9. RNA polymerase II distal enhancer sequence-specific DNA binding Source: UniProt

GO - Biological processi

  1. 3'-UTR-mediated mRNA stabilization Source: UniProt
  2. ATP-dependent chromatin remodeling Source: UniProt
  3. gene expression Source: Reactome
  4. mRNA splicing, via spliceosome Source: UniProtKB
  5. osteoblast differentiation Source: UniProt
  6. RNA splicing Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Ribonucleoprotein

Keywords - Biological processi

mRNA processing, mRNA splicing

Keywords - Ligandi

RNA-binding

Enzyme and pathway databases

ReactomeiREACT_125. Processing of Capped Intron-Containing Pre-mRNA.
REACT_467. mRNA Splicing - Major Pathway.

Names & Taxonomyi

Protein namesi
Recommended name:
Heterogeneous nuclear ribonucleoproteins C1/C2
Short name:
hnRNP C1/C2
Gene namesi
Name:HNRNPC
Synonyms:HNRPC
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 14

Organism-specific databases

HGNCiHGNC:5035. HNRNPC.

Subcellular locationi

Nucleus
Note: Component of ribonucleosomes.

GO - Cellular componenti

  1. catalytic step 2 spliceosome Source: UniProtKB
  2. cytosol Source: UniProt
  3. extracellular vesicular exosome Source: UniProt
  4. membrane Source: UniProt
  5. nuclear chromatin Source: UniProt
  6. nucleoplasm Source: Reactome
  7. nucleus Source: UniProt
  8. protein complex Source: UniProt
  9. spliceosomal complex Source: HGNC
Complete GO annotation...

Keywords - Cellular componenti

Nucleus, Spliceosome

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi197 – 1971K → R: No effect on sumoylation. 1 Publication
Mutagenesisi250 – 2501K → R: Loss of sumoylation. 1 Publication

Organism-specific databases

PharmGKBiPA162391217.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed2 Publications
Chaini2 – 306305Heterogeneous nuclear ribonucleoproteins C1/C2PRO_0000081844Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine2 Publications
Modified residuei109 – 1091Phosphothreonine1 Publication
Modified residuei113 – 1131Phosphoserine2 Publications
Modified residuei115 – 1151Phosphoserine1 Publication
Modified residuei162 – 1621Phosphoserine2 Publications
Modified residuei166 – 1661Phosphoserine1 Publication
Modified residuei176 – 1761N6-acetyllysineBy similarity
Modified residuei233 – 2331Phosphoserine6 Publications
Modified residuei241 – 2411Phosphoserine2 Publications
Cross-linki250 – 250Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)
Modified residuei253 – 2531Phosphoserine6 Publications
Modified residuei260 – 2601Phosphoserine8 Publications
Modified residuei299 – 2991Phosphoserine6 Publications
Modified residuei306 – 3061Phosphoserine2 Publications

Post-translational modificationi

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.11 Publications
Sumoylated. Sumoylation reduces affinity for mRNA.1 Publication

Keywords - PTMi

Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiP07910.
PaxDbiP07910.
PRIDEiP07910.

2D gel databases

SWISS-2DPAGEP07910.

PTM databases

PhosphoSiteiP07910.

Expressioni

Gene expression databases

BgeeiP07910.
ExpressionAtlasiP07910. baseline and differential.
GenevestigatoriP07910.

Organism-specific databases

HPAiCAB005223.
HPA051075.

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 IGF2BP1.5 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
itself4EBI-357966,EBI-357966
SRPK2P783622EBI-357966,EBI-593303
YWHAZP631042EBI-357966,EBI-347088

Protein-protein interaction databases

BioGridi109424. 144 interactions.
DIPiDIP-29854N.
IntActiP07910. 71 interactions.
MINTiMINT-4999718.

Structurei

Secondary structure

1
306
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi18 – 236Combined sources
Turni25 – 273Combined sources
Helixi30 – 356Combined sources
Beta strandi43 – 497Combined sources
Beta strandi51 – 599Combined sources
Helixi60 – 689Combined sources
Turni69 – 724Combined sources
Beta strandi81 – 844Combined sources
Helixi194 – 21623Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1TXPNMR-A/B/C/D194-220[»]
1WF2NMR-A8-92[»]
3LN4X-ray1.30C102-117[»]
ProteinModelPortaliP07910.
SMRiP07910. Positions 2-92.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP07910.

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 coili190 – 23849Sequence AnalysisAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi155 – 1617Nuclear localization signalSequence Analysis

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi181 – 303123Asp/Glu-rich (acidic)Add
BLAST

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

eggNOGiNOG311712.
GeneTreeiENSGT00390000006718.
HOVERGENiHBG002302.
InParanoidiP07910.
KOiK12884.
OMAiFSSPVEM.
OrthoDBiEOG7KWSK9.
PhylomeDBiP07910.
TreeFamiTF330974.

Family and domain databases

Gene3Di3.30.70.330. 1 hit.
InterProiIPR017347. hnRNP_C_Raly.
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]
PROSITEiPS50102. RRM. 1 hit.
[Graphical view]

Sequences (4)i

Sequence statusi: Complete.

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

This entry describes 4 isoformsi produced by alternative splicing. Align

Isoform C2 (identifier: P07910-1) [UniParc]FASTAAdd to Basket

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.

« 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
AAEMYGSVTE HPSPSPLLSS SFDLDYDFQR DYYDRMYSYP ARVPPPPPIA
160 170 180 190 200
RAVVPSKRQR VSGNTSRRGK SGFNSKSGQR GSSKSGKLKG DDLQAIKKEL
210 220 230 240 250
TQIKQKVDSL LENLEKIEKE QSKQAVEMKN DKSEEEQSSS SVKKDETNVK
260 270 280 290 300
MESEGGADDS AEEGDLLDDD DNEDRGDDQL ELIKDDEKEA EEGEDDRDSA

NGEDDS
Length:306
Mass (Da):33,670
Last modified:June 13, 2006 - v4
Checksum:i17BBC78690C69C5C
GO
Isoform C1 (identifier: P07910-2) [UniParc]FASTAAdd to Basket

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.

Show »
Length:293
Mass (Da):32,338
Checksum:iB90DDFD06A77FEE8
GO
Isoform 3 (identifier: P07910-3) [UniParc]FASTAAdd to Basket

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

Show »
Length:226
Mass (Da):25,230
Checksum:iBE6EC8C7A9FD7114
GO
Isoform 4 (identifier: P07910-4) [UniParc]FASTAAdd to Basket

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.

Show »
Length:250
Mass (Da):27,822
Checksum:i543388C3EC431836
GO

Sequence cautioni

The sequence BAD92764.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti110 – 1101E → G in AAH08423. (PubMed:15489334)Curated
Sequence conflicti217 – 2171I → M(PubMed:2557628)Curated
Sequence conflicti217 – 2171I → M(PubMed:3110598)Curated
Sequence conflicti224 – 2241Q → R in AAH08364. (PubMed:15489334)Curated
Sequence conflicti244 – 2441K → R in AAH08364. (PubMed:15489334)Curated
Sequence conflicti254 – 2541E → G in AAH07052. (PubMed:15489334)Curated
Sequence conflicti303 – 3064EDDS → G(PubMed:2557628)Curated
Sequence conflicti303 – 3064EDDS → G(PubMed:3110598)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti167 – 1671R → Q.
Corresponds to variant rs3272 [ dbSNP | Ensembl ].
VAR_052224

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei39 – 11981KYGKI…SPLLS → N in isoform 3. 1 PublicationVSP_019225Add
BLAST
Alternative sequencei108 – 12013Missing in isoform C1 and isoform 4. 3 PublicationsVSP_005831Add
BLAST
Alternative sequencei153 – 19543Missing in isoform 4. 1 PublicationVSP_019226Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS41915.1. [P07910-1]
CCDS45079.1. [P07910-2]
PIRiA26885.
C34504.
RefSeqiNP_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]
UniGeneiHs.508848.
Hs.675546.

Genome annotation databases

EnsembliENST00000420743; ENSP00000404848; ENSG00000092199. [P07910-1]
ENST00000430246; ENSP00000442816; 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]
GeneIDi3183.
KEGGihsa:3183.
UCSCiuc001vzw.3. human. [P07910-2]
uc001vzy.3. human. [P07910-1]
uc001wac.3. human. [P07910-4]
uc001wad.3. human. [P07910-3]

Polymorphism databases

DMDMi108935845.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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 .
CCDSi CCDS41915.1. [P07910-1 ]
CCDS45079.1. [P07910-2 ]
PIRi A26885.
C34504.
RefSeqi NP_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 ]
UniGenei Hs.508848.
Hs.675546.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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 [» ]
ProteinModelPortali P07910.
SMRi P07910. Positions 2-92.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 109424. 144 interactions.
DIPi DIP-29854N.
IntActi P07910. 71 interactions.
MINTi MINT-4999718.

Chemistry

ChEMBLi CHEMBL2216742.

PTM databases

PhosphoSitei P07910.

Polymorphism databases

DMDMi 108935845.

2D gel databases

SWISS-2DPAGE P07910.

Proteomic databases

MaxQBi P07910.
PaxDbi P07910.
PRIDEi P07910.

Protocols and materials databases

DNASUi 3183.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000420743 ; ENSP00000404848 ; ENSG00000092199 . [P07910-1 ]
ENST00000430246 ; ENSP00000442816 ; 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 ]
GeneIDi 3183.
KEGGi hsa:3183.
UCSCi uc001vzw.3. human. [P07910-2 ]
uc001vzy.3. human. [P07910-1 ]
uc001wac.3. human. [P07910-4 ]
uc001wad.3. human. [P07910-3 ]

Organism-specific databases

CTDi 3183.
GeneCardsi GC14M021677.
HGNCi HGNC:5035. HNRNPC.
HPAi CAB005223.
HPA051075.
MIMi 164020. gene.
neXtProti NX_P07910.
PharmGKBi PA162391217.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG311712.
GeneTreei ENSGT00390000006718.
HOVERGENi HBG002302.
InParanoidi P07910.
KOi K12884.
OMAi FSSPVEM.
OrthoDBi EOG7KWSK9.
PhylomeDBi P07910.
TreeFami TF330974.

Enzyme and pathway databases

Reactomei REACT_125. Processing of Capped Intron-Containing Pre-mRNA.
REACT_467. mRNA Splicing - Major Pathway.

Miscellaneous databases

ChiTaRSi HNRNPC. human.
EvolutionaryTracei P07910.
GeneWikii HNRNPC.
GenomeRNAii 3183.
NextBioi 12634.
PROi P07910.
SOURCEi Search...

Gene expression databases

Bgeei P07910.
ExpressionAtlasi P07910. baseline and differential.
Genevestigatori P07910.

Family and domain databases

Gene3Di 3.30.70.330. 1 hit.
InterProi IPR017347. hnRNP_C_Raly.
IPR012677. Nucleotide-bd_a/b_plait.
IPR000504. RRM_dom.
[Graphical view ]
Pfami PF00076. RRM_1. 1 hit.
[Graphical view ]
PIRSFi PIRSF037992. hnRNP-C_Raly. 1 hit.
SMARTi SM00360. RRM. 1 hit.
[Graphical view ]
PROSITEi PS50102. RRM. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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. 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. 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. 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. 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. 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. 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.

Entry informationi

Entry nameiHNRPC_HUMAN
AccessioniPrimary (citable) accession number: P07910
Secondary accession number(s): D3DS19
, D3DS22, P22628, Q53EX2, Q59FD3, Q5FWE8, Q86SF8, Q86U45, Q96HK7, Q96HM4, Q96IY5, Q9BTS3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1988
Last sequence update: June 13, 2006
Last modified: November 26, 2014
This is version 188 of the entry and version 4 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 14
    Human chromosome 14: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

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