P31943 (HNRH1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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

Cleaved into the following chain:

1. Heterogeneous nuclear ribonucleoprotein H, N-terminally processed

Gene names

Name:	HNRNPH1
Synonyms:	HNRPH, HNRPH1

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › 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. Mediates pre-mRNA alternative splicing regulation. Inhibits, together with CUGBP1, insulin receptor (IR) pre-mRNA exon 11 inclusion in myoblast. Binds to the IR RNA. Binds poly(RG). Ref.10 Ref.14
Subunit structure	Part of a ternary complex containing FUBP2, PTBP1, PTBP2 and HNRNPH1. Identified in the spliceosome C complex. Interacts with IGF2BP1. Interacts with CUGBP1; the interaction is RNA-dependent. Interacts with MBNL1; the interaction in RNA-independent. Ref.10 Ref.11 Ref.14 Ref.15
Subcellular location	Nucleus › nucleoplasm.
Tissue specificity	Expressed ubiquitously.
Induction	Up-regulated in myotonic dystrophy pathophysiology (DM). Ref.14
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	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	mRNA splicing, via spliceosome Inferred by curator Ref.11. Source: UniProtKB regulation of RNA splicing Inferred from direct assay Ref.14. Source: UniProtKB
Cellular_component	actin cytoskeleton Inferred from direct assay. Source: HPA catalytic step 2 spliceosome Inferred from direct assay Ref.11. Source: UniProtKB cytoplasm Inferred from direct assay. Source: HPA nucleoplasm Traceable author statement. Source: Reactome
Molecular_function	nucleotide binding Inferred from electronic annotation. Source: InterPro poly(U) RNA binding Traceable author statement Ref.1. Source: ProtInc
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 H

PRO_0000367119

Initiator methionine

1

1

Removed; alternate Ref.6 Ref.7

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.6

Modified residue

2

1

N-acetylmethionine; in Heterogeneous nuclear ribonucleoprotein H, N-terminally processed Ref.6

Modified residue

23

1

Phosphoserine Ref.18

Modified residue

63

1

Phosphoserine Ref.13 Ref.16 Ref.17 Ref.18 Ref.19 Ref.21

Modified residue

104

1

Phosphoserine By similarity

Modified residue

233

1

Dimethylated arginine; alternate Ref.6

Modified residue

233

1

Omega-N-methylarginine; alternate Ref.6

Modified residue

246

1

Phosphotyrosine Ref.12

Experimental info

Sequence conflict

188

1

R → G in CAG33059. Ref.2

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

449

Helix Strand Turn

Details...

Beta strand

9 – 17

9

Helix

24 – 30

7

Turn

31 – 33

3

Helix

39 – 41

3

Beta strand

42 – 47

6

Beta strand

51 – 62

12

Helix

64 – 71

8

Turn

72 – 75

4

Beta strand

84 – 88

5

Helix

90 – 98

9

Sequences

	Sequence		Length	Mass (Da)
	P31943 [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] [Europe PMC] [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]	"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. , 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]. Tissue: Cerebellum.
[4]	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. , 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 (SEP-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]	"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: Muscle.
[6]	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.
[7]	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.
[8]	"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] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 127-135 AND 153-163.
[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 200-230. Tissue: Keratinocyte.
[10]	"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] [Europe PMC] [Abstract] Cited for: FUNCTION, INTERACTION WITH PTBP1; PTBP2 AND FUBP2.
[11]	"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.
[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] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-246, 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] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-63, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[14]	"Interaction of muscleblind, CUG-BP1 and hnRNP H proteins in DM1-associated aberrant IR splicing." Paul S., Dansithong W., Kim D., Rossi J., Webster N.J., Comai L., Reddy S. EMBO J. 25:4271-4283(2006) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, INTERACTION WITH CUGBP1 AND MBNL1, RNA-BINDING, INDUCTION.
[15]	"Molecular composition of IMP1 ribonucleoprotein granules." Joeson L., Vikesaa J., Krogh A., Nielsen L.K., Hansen T., Borup R., Johnsen A.H., Christiansen J., Nielsen F.C. Mol. Cell. Proteomics 6:798-811(2007) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH IGF2BP1.
[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] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-63, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[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] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-63, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[18]	"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-23 AND SER-63, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[19]	"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-63, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[20]	"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].
[21]	"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-63, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

L22009 mRNA. Translation: AAA91346.1.
CR456778 mRNA. Translation: CAG33059.1.
AK124530 mRNA. Translation: BAG54048.1.
CH471165 Genomic DNA. Translation: EAW53807.1.
CH471165 Genomic DNA. Translation: EAW53808.1.
BC001348 mRNA. Translation: AAH01348.1.

IPI

IPI00013881.

PIR

I39358.

RefSeq

NP_001244222.1. NM_001257293.1.
NP_005511.1. NM_005520.2.

UniGene

Hs.604001.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2LXU	NMR	-	A	7-111	[»]

ProteinModelPortal

P31943.

ModBase

Search...

Protein-protein interaction databases

IntAct

P31943. 43 interactions.

MINT

MINT-1160934.

STRING

9606.ENSP00000349168.

PTM databases

PhosphoSite

P31943.

Polymorphism databases

DMDM

1710632.

2D gel databases

REPRODUCTION-2DPAGE

IPI00013881.
P31943.

Proteomic databases

PaxDb

P31943.

PRIDE

P31943.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000356731; ENSP00000349168; ENSG00000169045.
ENST00000393432; ENSP00000377082; ENSG00000169045.
ENST00000442819; ENSP00000397797; ENSG00000169045.

GeneID

3187.

KEGG

hsa:3187.

UCSC

uc003mke.4. human.

Organism-specific databases

CTD

3187.

GeneCards

GC05M179043.

HGNC

HGNC:5041. HNRNPH1.

HPA

HPA001359.
HPA016884.

MIM

601035. gene.

neXtProt

NX_P31943.

PharmGKB

PA162391284.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG262593.

HOGENOM

HOG000220896.

HOVERGEN

HBG055557.

KO

K12898.

OrthoDB

EOG4CRM03.

Enzyme and pathway databases

Reactome

REACT_1675. mRNA Processing.
REACT_71. Gene Expression.

Gene expression databases

ArrayExpress

P31943.

Bgee

P31943.

CleanEx

HS_HNRNPH1.

Genevestigator

P31943.

GermOnline

ENSG00000169045. Homo sapiens.

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

ChiTaRS

HNRNPH1. human.

GenomeRNAi

3187.

NextBio

12670.

SOURCE

Search...

Entry information

Entry name

HNRH1_HUMAN

Accession

Primary (citable) accession number: P31943
Secondary accession number(s): B3KW86, D3DWQ2, Q6IBM4

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 1, 1993
Last sequence update:	January 23, 2007
Last modified:	May 1, 2013
This is version 150 of the entry and version 4 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

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.