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P31942 (HNRH3_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 146. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | 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 ribonucleoprotein H3

Short name=hnRNP H3
Alternative name(s):
Heterogeneous nuclear ribonucleoprotein 2H9
Short name=hnRNP 2H9
Gene names
Name:HNRNPH3
Synonyms:HNRPH3
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length346 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Involved in the splicing process and participates in early heat shock-induced splicing arrest. Due to their great structural variations the different isoforms may possess different functions in the splicing reaction.

Subcellular location

Nucleus Ref.1.

Sequence similarities

Contains 2 RRM (RNA recognition motif) domains.

Alternative products

This entry describes 6 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P31942-1)

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 2 (identifier: P31942-2)

Also known as: 2H9A;

The sequence of this isoform differs from the canonical sequence as follows:
     132-146: Missing.
Isoform 3 (identifier: P31942-3)

Also known as: 2H9B;

The sequence of this isoform differs from the canonical sequence as follows:
     1-49: Missing.
Isoform 4 (identifier: P31942-4)

Also known as: 2H9C;

The sequence of this isoform differs from the canonical sequence as follows:
     1-131: Missing.
Isoform 5 (identifier: P31942-5)

Also known as: 2H9D;

The sequence of this isoform differs from the canonical sequence as follows:
     1-131: Missing.
     259-276: QHRYIELFLNSTPGGGSG → RKWCLWHTILFPKREFIK
     277-346: Missing.
Isoform 6 (identifier: P31942-6)

Also known as: 2H9E;

The sequence of this isoform differs from the canonical sequence as follows:
     1-137: Missing.
     138-145: RGGDGYDG → MCFSLNYT
     259-276: QHRYIELFLNSTPGGGSG → RKWCLWHTILFPKREFIK
     277-346: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 346346Heterogeneous nuclear ribonucleoprotein H3
PRO_0000081861

Regions

Domain16 – 9378RRM 1
Domain195 – 27076RRM 2
Compositional bias108 – 344237Gly-rich

Amino acid modifications

Modified residue11N-acetylmethionine Ref.7
Modified residue1211Asymmetric dimethylarginine Ref.10
Modified residue2161Phosphoserine Ref.12 Ref.13 Ref.14 Ref.15 Ref.16 Ref.17 Ref.19
Modified residue2871Omega-N-methylarginine Ref.7
Modified residue2981Phosphoserine Ref.16 Ref.17 Ref.19
Modified residue3141Phosphothreonine Ref.16

Natural variations

Alternative sequence1 – 137137Missing in isoform 6.
VSP_005841
Alternative sequence1 – 131131Missing in isoform 4 and isoform 5.
VSP_005839
Alternative sequence1 – 4949Missing in isoform 3.
VSP_005838
Alternative sequence132 – 14615Missing in isoform 2.
VSP_005840
Alternative sequence138 – 1458RGGDGYDG → MCFSLNYT in isoform 6.
VSP_005842
Alternative sequence259 – 27618QHRYI…GGGSG → RKWCLWHTILFPKREFIK in isoform 5 and isoform 6.
VSP_005843
Alternative sequence277 – 34670Missing in isoform 5 and isoform 6.
VSP_005844
Natural variant1631N → S.
Corresponds to variant rs2273903 [ dbSNP | Ensembl ].
VAR_020333
Natural variant2841G → A.
Corresponds to variant rs16925347 [ dbSNP | Ensembl ].
VAR_052226

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified September 19, 2002. Version 2.
Checksum: F7D14C2947930E9E

FASTA34636,926
        10         20         30         40         50         60 
MDWVMKHNGP NDASDGTVRL RGLPFGCSKE EIVQFFQGLE IVPNGITLTM DYQGRSTGEA 

        70         80         90        100        110        120 
FVQFASKEIA ENALGKHKER IGHRYIEIFR SSRSEIKGFY DPPRRLLGQR PGPYDRPIGG 

       130        140        150        160        170        180 
RGGYYGAGRG SMYDRMRRGG DGYDGGYGGF DDYGGYNNYG YGNDGFDDRM RDGRGMGGHG 

       190        200        210        220        230        240 
YGGAGDASSG FHGGHFVHMR GLPFRATEND IANFFSPLNP IRVHIDIGAD GRATGEADVE 

       250        260        270        280        290        300 
FVTHEDAVAA MSKDKNNMQH RYIELFLNST PGGGSGMGGS GMGGYGRDGM DNQGGYGSVG 

       310        320        330        340 
RMGMGNNYSG GYGTPDGLGG YGRGGGGSGG YYGQGGMSGG GWRGMY 

« Hide

Isoform 2 (2H9A) [UniParc].

Checksum: A3BA8D0F5FC07369
Show »

FASTA33135,239
Isoform 3 (2H9B) [UniParc].

Checksum: AAE63A29063E5153
Show »

FASTA29731,525
Isoform 4 (2H9C) [UniParc].

Checksum: 969F8FE2710D2646
Show »

FASTA21522,322
Isoform 5 (2H9D) [UniParc].

Checksum: 286234CBE7C9C996
Show »

FASTA14516,084
Isoform 6 (2H9E) [UniParc].

Checksum: F1E137E637675D93
Show »

FASTA13915,413

References

« Hide 'large scale' references
[1]"Cloning of human 2H9 heterogeneous nuclear ribonucleoproteins. Relation with splicing and early heat shock-induced splicing arrest."
Mahe D., Mahl P., Gattoni R., Fischer N., Mattei M.-G., Stevenin J., Fuchs J.-P.
J. Biol. Chem. 272:1827-1836(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SUBCELLULAR LOCATION.
[2]"The hnRNP 2H9 gene, which is involved in the splicing reaction, is a multiply spliced gene."
Honore B.
Biochim. Biophys. Acta 1492:108-119(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORMS 1; 2; 3; 4; 5 AND 6).
[3]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 4).
Tissue: Brain and Placenta.
[4]"The full-ORF clone resource of the German cDNA consortium."
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I.
BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
Tissue: Uterus.
[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 (JUL-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] (ISOFORM 2).
Tissue: Ovary and Skin.
[7]Bienvenut W.V., Lilla S., von Kriegsheim A., Lempens A., Kolch W.
Submitted (DEC-2008) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 1-6; 56-76; 85-90; 98-104; 175-200; 223-253 AND 262-323, ACETYLATION AT MET-1, METHYLATION AT ARG-287, IDENTIFICATION BY MASS SPECTROMETRY.
Tissue: Ovarian carcinoma.
[8]Lubec G., Vishwanath V., Chen W.-Q., Sun Y.
Submitted (DEC-2008) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 56-67; 206-222; 233-253 AND 262-287, IDENTIFICATION BY MASS SPECTROMETRY.
Tissue: Brain, Cajal-Retzius cell and Fetal brain cortex.
[9]"Microsequences of 145 proteins recorded in the two-dimensional gel protein database of normal human epidermal keratinocytes."
Rasmussen H.H., van Damme J., Puype M., Gesser B., Celis J.E., Vandekerckhove J.
Electrophoresis 13:960-969(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 94-104 AND 288-298.
Tissue: Keratinocyte.
[10]"A post-translational modification of nuclear proteins, N(G),N(G)-dimethyl-Arg, found in a natural HLA class I peptide ligand."
Yague J., Vazquez J., Lopez de Castro J.A.
Protein Sci. 9:2210-2217(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 116-127, METHYLATION AT ARG-121.
[11]"Immunoaffinity profiling of tyrosine phosphorylation in cancer cells."
Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H., Zha X.-M., Polakiewicz R.D., Comb M.J.
Nat. Biotechnol. 23:94-101(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[12]"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-216, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[13]"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-216, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[14]"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-216, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[15]"Large-scale proteomics analysis of the human kinome."
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G., Mann M., Daub H.
Mol. Cell. Proteomics 8:1751-1764(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-216, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[16]"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 SER-216; SER-298 AND THR-314, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[17]"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-216 AND SER-298, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[18]"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].
[19]"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-216 AND SER-298, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L32610 mRNA. Translation: AAD45179.1.
AF132360 Genomic DNA. Translation: AAF68843.1.
AF132360 Genomic DNA. Translation: AAF68844.1.
AF132360 Genomic DNA. Translation: AAF68845.1.
AF132360 Genomic DNA. Translation: AAF68846.1.
AF132360 Genomic DNA. Translation: AAF68847.1.
AF132360 Genomic DNA. Translation: AAF68848.1.
AF132361 mRNA. Translation: AAF68849.1.
AF132362 mRNA. Translation: AAF68850.1.
AF132363 mRNA. Translation: AAF68851.1.
AF132364 mRNA. Translation: AAF68852.1.
AK091411 mRNA. Translation: BAG52353.1.
AK291547 mRNA. Translation: BAF84236.1.
AL117395 mRNA. Translation: CAB55897.1.
CH471083 Genomic DNA. Translation: EAW54281.1.
CH471083 Genomic DNA. Translation: EAW54282.1.
BC004511 mRNA. Translation: AAH04511.2.
BC039824 mRNA. Translation: AAH39824.1.
CCDSCCDS7278.1. [P31942-1]
CCDS7279.1. [P31942-2]
PIRT17207.
RefSeqNP_036339.1. NM_012207.2. [P31942-1]
NP_067676.2. NM_021644.3. [P31942-2]
XP_005269805.1. XM_005269748.2. [P31942-1]
XP_005269806.1. XM_005269749.2. [P31942-2]
XP_005269808.1. XM_005269751.2. [P31942-4]
XP_005269809.1. XM_005269752.2. [P31942-4]
XP_006717879.1. XM_006717816.1. [P31942-1]
XP_006717880.1. XM_006717817.1. [P31942-2]
UniGeneHs.643472.

3D structure databases

ProteinModelPortalP31942.
SMRP31942. Positions 10-97, 194-270.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid109430. 79 interactions.
IntActP31942. 45 interactions.
MINTMINT-5004191.

PTM databases

PhosphoSiteP31942.

Polymorphism databases

DMDM23503095.

Proteomic databases

MaxQBP31942.
PaxDbP31942.
PRIDEP31942.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000265866; ENSP00000265866; ENSG00000096746. [P31942-1]
ENST00000354695; ENSP00000346726; ENSG00000096746. [P31942-2]
GeneID3189.
KEGGhsa:3189.
UCSCuc001jnw.4. human. [P31942-1]
uc001jnx.4. human. [P31942-2]

Organism-specific databases

CTD3189.
GeneCardsGC10P070090.
HGNCHGNC:5043. HNRNPH3.
HPAHPA038264.
MIM602324. gene.
neXtProtNX_P31942.
PharmGKBPA162391325.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG262593.
HOVERGENHBG055557.
InParanoidP31942.
KOK12898.
OMAPYDRPLG.
OrthoDBEOG7BS4BZ.
PhylomeDBP31942.
TreeFamTF316157.

Gene expression databases

ArrayExpressP31942.
BgeeP31942.
CleanExHS_HNRNPH3.
GenevestigatorP31942.

Family and domain databases

Gene3D3.30.70.330. 2 hits.
InterProIPR012677. Nucleotide-bd_a/b_plait.
IPR000504. RRM_dom.
[Graphical view]
SMARTSM00360. RRM. 2 hits.
[Graphical view]
PROSITEPS50102. RRM. 2 hits.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSHNRNPH3. human.
GeneWikiHNRPH3.
GenomeRNAi3189.
NextBio12680.
PROP31942.
SOURCESearch...

Entry information

Entry nameHNRH3_HUMAN
AccessionPrimary (citable) accession number: P31942
Secondary accession number(s): A8K682 expand/collapse secondary AC list , B3KRE1, Q9BSX1, Q9NP53, Q9NP96, Q9NPA7, Q9NPI4, Q9UFU4, Q9Y4J5
Entry history
Integrated into UniProtKB/Swiss-Prot: July 1, 1993
Last sequence update: September 19, 2002
Last modified: July 9, 2014
This is version 146 of the entry and version 2 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

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 10

Human chromosome 10: entries, gene names and cross-references to MIM