Reviewed, UniProtKB/Swiss-Prot P31943 (HNRH1_HUMAN)

Names and origin

Protein names

Recommended name:
    Heterogeneous nuclear ribonucleoprotein H
      Short name=hnRNP H
Cleaved into the following chain:
    1- Recommended name:
            Heterogeneous nuclear ribonucleoprotein H, N-terminally processed

Gene names

Name:	HNRNPH1
Synonyms:	HNRPH, HNRPH1

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 further processed into a mature form.
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). Ref.8
Subunit structure	Part of a ternary complex containing FUBP2, PTBP1, PTBP2 and HNRNPH1. Identified in the spliceosome C complex, at least composed of AQR, ASCC3L1, C19orf29, CDC40, CDC5L, CRNKL1, DDX23, DDX41, DDX48, DDX5, DGCR14, DHX35, DHX38, DHX8, EFTUD2, FRG1, GPATC1, HNRPA1, HNRPA2B1, HNRPA3, HNRPC, HNRPF, HNRNPH1, HNRPK, HNRPM, HNRPR, HNRPU, KIAA1160, KIAA1604, LSM2, LSM3, MAGOH, MORG1, PABPC1, PLRG1, PNN, PPIE, PPIL1, PPIL3, PPWD1, PRPF19, PRPF4B, PRPF6, PRPF8, RALY, RBM22, RBM8A, RBMX, SART1, SF3A1, SF3A2, SF3A3, SF3B1, SF3B2, SF3B3, SFRS1, SKIV2L2, SNRPA1, SNRPB, SNRPB2, SNRPD1, SNRPD2, SNRPD3, SNRPE, SNRPF, SNRPG, SNW1, SRRM1, SRRM2, SYF2, SYNCRIP, TFIP11, THOC4, U2AF1, WDR57, XAB2 and ZCCHC8.
Subcellular location	Nucleus › nucleoplasm.
Tissue specificity	Expressed ubiquitously.
Domain	Each quasi-RRM repeat bound poly(RG), while only the N-terminal QRRM bound poly(RC) and poly(RU). None of the repeats bound detectable amounts of poly(RA).
Sequence similarities	Contains 3 RRM (RNA recognition motif) domains.

Ontologies

Keywords
Biological process	mRNA processing mRNA splicing
Cellular component	Nucleus Spliceosome
Domain	Repeat
Ligand	RNA-binding
Molecular function	Ribonucleoprotein
PTM	Acetylation Methylation Phosphoprotein
Technical term	Complete proteome Direct protein sequencing
Gene Ontology (GO)
Biological process	nuclear mRNA splicing, via spliceosome Inferred from Experiment. Source: Reactome
Cellular component	cytoskeleton Inferred from direct assay. Source: HPA heterogeneous nuclear ribonucleoprotein complex Ref.1 Traceable author statement. Source: ProtInc nucleoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell spliceosome Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	nucleotide binding Inferred from electronic annotation. Source: InterPro poly(U) binding Ref.1 Traceable author statement. Source: ProtInc protein binding Inferred from physical interaction. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
NDRG1	Q92597	1	EBI-351590,EBI-716486
TOB1	P50616	1	EBI-351590,EBI-723281

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 449	449	Heterogeneous nuclear ribonucleoprotein H		PRO_0000367119
	Initiator methionine	1	1	Removed; alternate Ref.4 Ref.5
	Chain	2 – 449	448	Heterogeneous nuclear ribonucleoprotein H, N-terminally processed		PRO_0000081857
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; in Heterogeneous nuclear ribonucleoprotein H; alternate Ref.4
	Modified residue	2	1	N-acetylmethionine; in Heterogeneous nuclear ribonucleoprotein H, N-terminally processed Ref.4
	Modified residue	23	1	Phosphoserine Ref.11
	Modified residue	63	1	Phosphoserine Ref.13 Ref.16 Ref.17
	Modified residue	100	1	Phosphothreonine Ref.10
	Modified residue	104	1	Phosphoserine Ref.17 Ref.14 Ref.15
	Modified residue	107	1	Phosphothreonine Ref.17
	Modified residue	217	1	Asymmetric dimethylarginine By similarity
	Modified residue	233	1	Dimethylated arginine; alternate Ref.4
	Modified residue	233	1	Omega-N-methylarginine; alternate Ref.4
	Modified residue	246	1	Phosphotyrosine Ref.12
	Modified residue	306	1	Phosphotyrosine Ref.12
	Modified residue	310	1	Phosphoserine Ref.14
Experimental info
	Sequence conflict	188	1	R → G in CAG33059. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	P31943-1 [UniParc]. Last modified January 23, 2007. Version 4. Checksum: 4ECF7A075C2526FF	FASTA	449	49,229
	10 20 30 40 50 60 MMLGTEGGEG FVVKVRGLPW SCSADEVQRF FSDCKIQNGA QGIRFIYTRE GRPSGEAFVE 70 80 90 100 110 120 LESEDEVKLA LKKDRETMGH RYVEVFKSNN VEMDWVLKHT GPNSPDTAND GFVRLRGLPF 130 140 150 160 170 180 GCSKEEIVQF FSGLEIVPNG ITLPVDFQGR STGEAFVQFA SQEIAEKALK KHKERIGHRY 190 200 210 220 230 240 IEIFKSSRAE VRTHYDPPRK LMAMQRPGPY DRPGAGRGYN SIGRGAGFER MRRGAYGGGY 250 260 270 280 290 300 GGYDDYNGYN DGYGFGSDRF GRDLNYCFSG MSDHRYGDGG STFQSTTGHC VHMRGLPYRA 310 320 330 340 350 360 TENDIYNFFS PLNPVRVHIE IGPDGRVTGE ADVEFATHED AVAAMSKDKA NMQHRYVELF 370 380 390 400 410 420 LNSTAGASGG AYEHRYVELF LNSTAGASGG AYGSQMMGGM GLSNQSSYGG PASQQLSGGY 430 440 GGGYGGQSSM SGYDQVLQEN SSDFQSNIA

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"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: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 180-184; 193-197 AND 200-230.
[2]	"Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)." Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B. Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Muscle.
[4]	Bienvenut W.V., Boldt K., von Kriegsheim A., Matallanas D., Cooper W.N., Calvo F., Kolch W., Vousden K.H., Lukashchuk N., Lilla S., Lempens A. Submitted (DEC-2008) to UniProtKB Cited for: PROTEIN SEQUENCE OF 1-14; 17-44; 50-68; 82-114; 151-167; 180-185; 233-259; 276-294; 300-347 AND 356-375, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT MET-1 AND MET-2, METHYLATION AT ARG-233, MASS SPECTROMETRY. Tissue: B-cell lymphoma, Cervix carcinoma, Hepatoma, Lung carcinoma, Mammary carcinoma and Ovarian carcinoma.
[5]	Lubec G., Vishwanath V., Chen W.-Q., Sun Y. Submitted (DEC-2008) to UniProtKB Cited for: PROTEIN SEQUENCE OF 2-14; 17-29; 88-114; 151-167; 263-275; 300-347; 344-375; 377-386; 418-432; 473-483 AND 542-553, MASS SPECTROMETRY. Tissue: Brain, Cajal-Retzius cell and Fetal brain cortex.
[6]	"The hnRNP F protein: unique primary structure, nucleic acid-binding properties, and subcellular localization." Matunis M.J., Xing J., Dreyfuss G. Nucleic Acids Res. 22:1059-1067(1994) [PubMed: 7512260] [Abstract] Cited for: PROTEIN SEQUENCE OF 127-135 AND 153-163.
[7]	"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: 1286667] [Abstract] Cited for: PROTEIN SEQUENCE OF 200-230. Tissue: Keratinocyte.
[8]	"Cooperative assembly of an hnRNP complex induced by a tissue-specific homolog of polypyrimidine tract binding protein." Markovtsov V., Nikolic J.M., Goldman J.A., Turck C.W., Chou M.-Y., Black D.L. Mol. Cell. Biol. 20:7463-7479(2000) [PubMed: 11003644] [Abstract] Cited for: FUNCTION, INTERACTION WITH PTBP1; PTBP2 AND FUBP2.
[9]	"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: 11991638] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN THE SPICEOSOMAL C COMPLEX.
[10]	"Robust phosphoproteomic profiling of tyrosine phosphorylation sites from human T cells using immobilized metal affinity chromatography and tandem mass spectrometry." Brill L.M., Salomon A.R., Ficarro S.B., Mukherji M., Stettler-Gill M., Peters E.C. Anal. Chem. 76:2763-2772(2004) [PubMed: 15144186] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-100, MASS SPECTROMETRY. Tissue: T-cell.
[11]	"Large-scale characterization of HeLa cell nuclear phosphoproteins." Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J., Li J., Cohn M.A., Cantley L.C., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004) [PubMed: 15302935] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-23, MASS SPECTROMETRY. Tissue: Epithelium.
[12]	"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: 15592455] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-246 AND TYR-306, MASS SPECTROMETRY.
[13]	"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-63, MASS SPECTROMETRY. Tissue: Epithelium.
[14]	"Improved titanium dioxide enrichment of phosphopeptides from HeLa cells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra." Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D. J. Proteome Res. 6:4150-4162(2007) [PubMed: 17924679] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-104 AND SER-310, MASS SPECTROMETRY. Tissue: Epithelium.
[15]	"Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column." Imami K., Sugiyama N., Kyono Y., Tomita M., Ishihama Y. Anal. Sci. 24:161-166(2008) [PubMed: 18187866] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-104, MASS SPECTROMETRY.
[16]	"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-63, MASS SPECTROMETRY.
[17]	"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-63; SER-104 AND THR-107, MASS SPECTROMETRY.
[18]	Colinge J., Superti-Furga G., Bennett K.L. Submitted (OCT-2008) to UniProtKB Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.

Cross-references

Sequence databases
EMBLGenBankDDBJ	L22009 mRNA. Translation: AAA91346.1. CR456778 mRNA. Translation: CAG33059.1. BC001348 mRNA. Translation: AAH01348.1.
IPI	IPI00013881.
PIR	I39358.
RefSeq	NP_005511.1.
UniGene	Hs.604001
3D structure databases
SMR	P31943. Positions 1-102, 104-192, 105-193, 282-364, 283-365.
ModBase	Search...
Protein-protein interaction databases
IntAct	P31943. 17 interactions.
PTM databases
PhosphoSite	P31943.
2-D gel databases
Aarhus/Ghent-2DPAGE	4410. IEF. 4429. IEF. 5416. IEF.
REPRODUCTION-2DPAGE	IPI00013881. P31943.
Proteomic databases
PRIDE	P31943.
Genome annotation databases
Ensembl	ENSG00000169045. Homo sapiens. [Contig view]
GeneID	3187.
KEGG	hsa:3187.
UCSC	uc003mke.2. human.
Organism-specific databases
GeneCards	GC05M178974.
H-InvDB	HIX0005482.
HGNC	HGNC:5041. HNRNPH1.
HPA	HPA001359. HPA016884.
MIM	601035. gene.
PharmGKB	PA29365.
GenAtlas	Search...
Phylogenomic databases
HOVERGEN	P31943.
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	P31943.
Bgee	P31943.
CleanEx	HS_HNRNPH1.
GermOnline	ENSG00000169045. 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	12670.
SOURCE	Search...

Entry information

Entry name

HNRH1_HUMAN

Accession

Primary (citable) accession number: P31943
Secondary accession number(s): Q6IBM4

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 1, 1993
Last sequence update:	January 23, 2007
Last modified:	July 7, 2009
This is version 108 of the entry and version 4 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)