P70333 (HNRH2_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Heterogeneous nuclear ribonucleoprotein H2
Short name=hnRNP H2

Alternative name(s):
Heterogeneous nuclear ribonucleoprotein H'
Short name=hnRNP H'

Gene names

Name:	Hnrnph2
Synonyms:	Hnrph2

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	449 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	This protein is a component of the heterogeneous nuclear ribonucleoprotein (hnRNP) complexes which provide the substrate for the processing events that pre-mRNAs undergo before becoming functional, translatable mRNAs in the cytoplasm. Binds poly(RG) By similarity.
Subunit structure	Interacts with TXNL4/DIM1 By similarity.
Subcellular location	Nucleus › nucleoplasm By similarity.
Sequence similarities	Contains 3 RRM (RNA recognition motif) domains.

Ontologies

Keywords
Cellular component	Nucleus
Domain	Repeat
Ligand	RNA-binding
Molecular function	Ribonucleoprotein
PTM	Acetylation Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Cellular_component	nucleoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell ribonucleoprotein complex Inferred from sequence orthology PubMed 18809582. Source: MGI
Molecular_function	RNA binding Inferred from electronic annotation. Source: UniProtKB-KW nucleotide binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 449	449	Heterogeneous nuclear ribonucleoprotein H2		PRO_0000081860
Regions
	Domain	11 – 90	80	RRM 1
	Domain	111 – 188	78	RRM 2
	Repeat	234 – 249	16	1-1
	Domain	289 – 364	76	RRM 3
	Repeat	354 – 372	19	2-1
	Repeat	374 – 392	19	2-2
	Repeat	418 – 433	16	1-2
	Region	234 – 433	200	2 X 16 AA Gly-rich approximate repeats
	Region	354 – 392	39	2 X 19 AA perfect repeats
Amino acid modifications
	Modified residue	1	1	N-acetylmethionine By similarity
	Modified residue	104	1	Phosphoserine Ref.4 Ref.5 Ref.6 Ref.7 Ref.8
	Modified residue	107	1	Phosphothreonine Ref.7
	Modified residue	310	1	Phosphoserine By similarity

Sequences

	Sequence		Length	Mass (Da)
	P70333 [UniParc]. Last modified February 1, 1997. Version 1. Checksum: 2ED0A7A87A7EDF5E	FASTA	449	49,280
	10 20 30 40 50 60 MMLSTEGREG FVVKVRGLPW SCSAEEVMRF FSDCKIQNGT SGVRFIYTRE GRPSGEAFVE 70 80 90 100 110 120 LESEDEVKLA LKKDRETMGH RYVEVFKSNS VEMDWVLKHT GPNSPDTAND GFVRLRGLPF 130 140 150 160 170 180 GCSKEEIVQF FSGLEIVPNG MTLPVDFQGR STGEAFVQFA SQEIAEKALK KHKERIGHRY 190 200 210 220 230 240 IEIFKSSRAE VRTHYDPPRK LMTMQRPGPY DRPGAGRGYN SIGRGAGFER MRRGAYGGGY 250 260 270 280 290 300 GGYDDYGGYN DGYGFGSDRF GRDLNYCFSG MSDHRYGDGG SSFQSTTGHC VHMRGLPYRA 310 320 330 340 350 360 TENDIYNFFS PLNPMRVHIE IGPDGRVTGE ADVEFATHED AVAAMAKDKA NMQHRYVELF 370 380 390 400 410 420 LNSTAGTSGG AYDHSYVELF LNSTAGASGG AYGSQMMGGM GLSNQSSYGG PASQQLSGGY 430 440 GGGYGGQSSM SGYDQVLQEN SSDYQSNLA

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Sixty-nine kilobases of contiguous human genomic sequence containing the alpha-galactosidase A and Bruton's tyrosine kinase loci." Oeltjen J.C., Liu X., Lu J., Allen R.C., Muzny D.M., Belmont J.W., Gibbs R.A. Mamm. Genome 6:334-338(1995) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: C129.
[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. , 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]. Strain: BALB/c and C57BL/6J. Tissue: Kidney and Spinal cord.
[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]. Tissue: Mammary gland.
[4]	"Identification of phosphoproteins and their phosphorylation sites in the WEHI-231 B lymphoma cell line." Shu H., Chen S., Bi Q., Mumby M., Brekken D.L. Mol. Cell. Proteomics 3:279-286(2004) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-104, MASS SPECTROMETRY. Tissue: B-cell lymphoma.
[5]	"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-104, MASS SPECTROMETRY. Tissue: Liver.
[6]	"Specific phosphopeptide enrichment with immobilized titanium ion affinity chromatography adsorbent for phosphoproteome analysis." Zhou H., Ye M., Dong J., Han G., Jiang X., Wu R., Zou H. J. Proteome Res. 7:3957-3967(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-104, MASS SPECTROMETRY. Tissue: Liver.
[7]	"Solid tumor proteome and phosphoproteome analysis by high resolution mass spectrometry." Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J., Faessler R., Mann M. J. Proteome Res. 7:5314-5326(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-104 AND THR-107, MASS SPECTROMETRY. Tissue: Melanoma.
[8]	"Large scale localization of protein phosphorylation by use of electron capture dissociation mass spectrometry." Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J. Mol. Cell. Proteomics 8:904-912(2009) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-104, MASS SPECTROMETRY. Tissue: Embryonic fibroblast.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	U58105 Genomic DNA. Translation: AAB47243.1. AK077716 mRNA. Translation: BAC36976.1. AK164115 mRNA. Translation: BAE37634.1. AK168116 mRNA. Translation: BAE40087.1. AK169104 mRNA. Translation: BAE40886.1. BC005461 mRNA. Translation: AAH05461.1.
IPI	IPI00108143.
RefSeq	NP_063921.1. NM_019868.3.
UniGene	Mm.315909.
3D structure databases
ProteinModelPortal	P70333.
SMR	P70333. Positions 4-193, 277-401.
ModBase	Search...
PTM databases
PhosphoSite	P70333.
Proteomic databases
PaxDb	P70333.
PRIDE	P70333.
Protocols and materials databases
DNASU	56258.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000050331; ENSMUSP00000108827; ENSMUSG00000045427. ENSMUST00000059297; ENSMUSP00000050838; ENSMUSG00000045427. ENSMUST00000074950; ENSMUSP00000074483; ENSMUSG00000045427. ENSMUST00000113202; ENSMUSP00000108828; ENSMUSG00000045427. ENSMUST00000113203; ENSMUSP00000108829; ENSMUSG00000045427.
GeneID	56258.
KEGG	mmu:56258.
Organism-specific databases
CTD	3188.
MGI	MGI:1201779. Hnrnph2.
Phylogenomic databases
eggNOG	NOG262593.
GeneTree	ENSGT00620000087736.
HOGENOM	HOG000220896.
HOVERGEN	HBG055557.
InParanoid	P70333.
KO	K12898.
OrthoDB	EOG4CRM03.
Gene expression databases
ArrayExpress	P70333.
Bgee	P70333.
Genevestigator	P70333.
GermOnline	ENSMUSG00000045427. Mus musculus.
Family and domain databases
Gene3D	3.30.70.330. 3 hits.
InterPro	IPR012677. Nucleotide-bd_a/b_plait. IPR000504. RRM_dom. IPR012996. Znf_CHHC. [Graphical view]
Pfam	PF08080. zf-RNPHF. 1 hit. [Graphical view]
SMART	SM00360. RRM. 3 hits. [Graphical view]
PROSITE	PS50102. RRM. 3 hits. [Graphical view]
ProtoNet	Search...
Other
NextBio	312148.
SOURCE	Search...

Entry information

Entry name

HNRH2_MOUSE

Accession

Primary (citable) accession number: P70333
Secondary accession number(s): Q3THV9

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 26, 2004
Last sequence update:	February 1, 1997
Last modified:	May 1, 2013
This is version 102 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program