Reviewed, UniProtKB/Swiss-Prot P55795 (HNRH2_HUMAN)

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'
    FTP-3

Gene names

Name:	HNRNPH2
Synonyms:	FTP3, HNRPH2

Organism

Homo sapiens (Human) [Complete proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	449 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
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).
Subunit structure	Interacts with TXNL4/DIM1. Ref.7
Subcellular location	Nucleus › nucleoplasm.
Tissue specificity	Expressed ubiquitously.
Sequence similarities	Contains 3 RRM (RNA recognition motif) domains.

Ontologies

Keywords
Cellular component	Nucleus
Domain	Repeat
Ligand	RNA-binding
Molecular function	Ribonucleoprotein
PTM	Acetylation Methylation Phosphoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing
Gene Ontology (GO)
Biological process	nuclear mRNA splicing, via spliceosome Inferred from Experiment. Source: Reactome
Cellular component	cytoplasm Inferred from direct assay. Source: HPA cytoskeleton Inferred from direct assay. Source: HPA heterogeneous nuclear ribonucleoprotein complex Ref.4 Traceable author statement. Source: ProtInc nucleoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	RNA binding Ref.4 Traceable author statement. Source: ProtInc nucleotide binding Inferred from electronic annotation. Source: InterPro protein binding Inferred from physical interaction. Source: IntAct
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
TOB1	P50616	1	EBI-352823,EBI-723281

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 449

449

Heterogeneous nuclear ribonucleoprotein H2

PRO_0000081859

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 Ref.5

Modified residue

104

1

Phosphoserine Ref.8 Ref.9 Ref.10 Ref.11

Modified residue

107

1

Phosphothreonine Ref.9

Modified residue

217

1

Asymmetric dimethylarginine By similarity

Modified residue

310

1

Phosphoserine Ref.11 Ref.12

Secondary structure

1

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449

Helix Strand Turn

Details...

Beta strand

112 – 117

6

Helix

124 – 130

7

Turn

131 – 133

3

Beta strand

136 – 142

7

Beta strand

147 – 149

3

Beta strand

153 – 161

9

Helix

162 – 169

8

Turn

170 – 173

4

Beta strand

176 – 179

4

Beta strand

182 – 186

5

Turn

188 – 190

3

Beta strand

286 – 288

3

Beta strand

290 – 295

6

Helix

302 – 307

6

Beta strand

315 – 325

11

Beta strand

327 – 334

8

Beta strand

336 – 338

3

Helix

339 – 345

7

Beta strand

352 – 355

4

Beta strand

358 – 362

5

Sequences

	Sequence		Length	Mass (Da)
	P55795-1 [UniParc]. Last modified November 1, 1997. Version 1. Checksum: C892523A638F07C7	FASTA	449	49,264
	10 20 30 40 50 60 MMLSTEGREG FVVKVRGLPW SCSADEVMRF FSDCKIQNGT SGIRFIYTRE GRPSGEAFVE 70 80 90 100 110 120 LESEEEVKLA 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 LMAMQRPGPY 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]	"Isolation of cosmid and cDNA clones in the region surrounding the BTK gene at Xq21.3-q22." Vorechovsky I., Vetrie D., Holland J., Bentley D.R., Thomas K., Zhou J.N., Notarangelo L.D., Plebani A., Fontan G., Ochs H.D. Genomics 21:517-524(1994) [PubMed: 7959728] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"Large-scale comparative sequence analysis of the human and murine Bruton's tyrosine kinase loci reveals conserved regulatory domains." Oeltjen J.C., Malley T.M., Muzny D.M., Miller W., Gibbs R.A., Belmont J.W. Genome Res. 7:315-329(1997) [PubMed: 9110171] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]	"The DNA sequence of the human X chromosome." Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D., Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C. , Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S., Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S., Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D., Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H., McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K., Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D., Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R., Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A., Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F., Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S., Rogers J., Bentley D.R. Nature 434:325-337(2005) [PubMed: 15772651] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]	"Heterogeneous nuclear ribonucleoproteins H, H', and F are members of a ubiquitously expressed subfamily of related but distinct proteins encoded by genes mapping to different chromosomes." Honore B., Rasmussen H.H., Vorum H., Dejgaard K., Liu X., Gromov P., Madsen P., Gesser B., Tommerup N., Celis J.E. J. Biol. Chem. 270:28780-28789(1995) [PubMed: 7499401] [Abstract] Cited for: PARTIAL NUCLEOTIDE SEQUENCE [MRNA].
[5]	Bienvenut W.V., Lilla S., von Kriegsheim A., Lempens A., Kolch W. Submitted (DEC-2008) to UniProtKB Cited for: PROTEIN SEQUENCE OF 1-8; 88-114; 151-167; 276-294 AND 300-326, ACETYLATION AT MET-1, MASS SPECTROMETRY. Tissue: Ovarian carcinoma.
[6]	Lubec G., Chen W.-Q., Sun Y. Submitted (DEC-2008) to UniProtKB Cited for: PROTEIN SEQUENCE OF 17-29; 36-44; 88-98; 151-167; 263-275; 300-316 AND 327-347, MASS SPECTROMETRY. Tissue: Fetal brain cortex.
[7]	"Evidence that Dim1 associates with proteins involved in pre-mRNA splicing, and delineation of residues essential for Dim1 interactions with hnRNP F and Npw38/PQBP-1." Zhang Y.-Z., Lindblom T., Chang A., Sudol M., Sluder A.E., Golemis E.A. Gene 257:33-43(2000) [PubMed: 11054566] [Abstract] Cited for: INTERACTION WITH TXNL4.
[8]	"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: 17081983] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-104, MASS SPECTROMETRY. Tissue: Epithelium.
[9]	"Global proteomic profiling of phosphopeptides using electron transfer dissociation tandem mass spectrometry." Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A. Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007) [PubMed: 17287340] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-104 AND THR-107, MASS SPECTROMETRY.
[10]	"Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis." Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III J. Proteome Res. 7:1346-1351(2008) [PubMed: 18220336] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-104, MASS SPECTROMETRY.
[11]	"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: 18691976] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-104 AND SER-310, MASS SPECTROMETRY.
[12]	"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: 18669648] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-310, MASS SPECTROMETRY.
[13]	Colinge J., Superti-Furga G., Bennett K.L. Submitted (OCT-2008) to UniProtKB Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[14]	"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: 19413330] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, MASS SPECTROMETRY.
[15]	"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: 19690332] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-310, MASS SPECTROMETRY. Tissue: T-cell.
[16]	"Solution structure of RRM domains in heterogeneous nuclear ribonucleoprotein H." RIKEN structural genomics initiative (RSGI) Submitted (NOV-2004) to the PDB data bank Cited for: STRUCTURE BY NMR OF 103-193 AND 280-369.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBLGenBankDDBJ

U01923 mRNA. No translation available.
U78027 Genomic DNA. Translation: AAB64202.1.
AL035422 Genomic DNA. Translation: CAB55879.2.

IPI

IPI00026230.

RefSeq

NP_001027565.1.
NP_062543.1.

UniGene

Hs.632828
Hs.69089

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1WEZ	NMR	-	A	281-369	[»]
1WG5	NMR	-	A	103-193	[»]

SMR

P55795. Positions 1-111.

ModBase

Search...

Protein-protein interaction databases

IntAct

P55795. 3 interactions.

STRING

P55795.

PTM databases

PhosphoSite

P55795.

2-D gel databases

Aarhus/Ghent-2DPAGE

4432. IEF.

REPRODUCTION-2DPAGE

IPI00026230.

Proteomic databases

PeptideAtlas

P55795.

PRIDE

P55795.

Genome annotation databases

Ensembl

ENST00000316594; ENSP00000361927; ENSG00000126945; Homo sapiens. [Genome view]
ENST00000395130; ENSP00000378562; ENSG00000126945; Homo sapiens. [Genome view]
ENST00000455741; ENSP00000393203; ENSG00000126945; Homo sapiens. [Genome view]

GeneID

3188.

KEGG

hsa:3188.

UCSC

uc004ehm.1. human.

Organism-specific databases

CTD

3188.

GeneCards

GC0XP100533.
GC15P033023.
GC18M013909.

H-InvDB

HIX0056232.

HGNC

HGNC:5042. HNRNPH2.

HPA

CAB004436.
HPA001359.
HPA016884.

MIM

300610. gene.

PharmGKB

PA29366.

GenAtlas

Search...

Phylogenomic databases

HOGENOM

P55795.

HOVERGEN

P55795.

OMA

CSAEEVM

OrthoDB

EOG9X3KKJ

Enzyme and pathway databases

Reactome

REACT_125. Processing of Capped Intron-Containing Pre-mRNA.
REACT_6167. Influenza Infection.
REACT_71. Gene Expression.

Gene expression databases

ArrayExpress

P55795.

Bgee

P55795.

CleanEx

HS_HNRNPH2.

Genevestigator

P55795.

GermOnline

ENSG00000126945. Homo sapiens.

Family and domain databases

InterPro

IPR012677. a_b_plait_nuc_bd.
IPR000504. RRM_RNP1.
IPR012996. Znf_CHHC.
[Graphical view]

Gene3D

G3DSA:3.30.70.330. a_b_plait_nuc_bd. 3 hits.

Pfam

PF00076. RRM_1. 3 hits.
PF08080. zf-RNPHF. 1 hit.
[Graphical view]

SMART

SM00360. RRM. 3 hits.
[Graphical view]

PROSITE

PS50102. RRM. 3 hits.
[Graphical view]

ProtoNet

Search...

Other Resources

NextBio

12674.

SOURCE

Search...

Entry information

Entry name

HNRH2_HUMAN

Accession

Primary (citable) accession number: P55795
Secondary accession number(s): Q9HHA7

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	November 1, 1997
Last modified:	November 24, 2009
This is version 108 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

Disclaimer

Any 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.