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P55795

- HNRH2_HUMAN

UniProt

P55795 - HNRH2_HUMAN

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Protein

Heterogeneous nuclear ribonucleoprotein H2

Gene

HNRNPH2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

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).

GO - Molecular functioni

  1. nucleotide binding Source: InterPro
  2. poly(A) RNA binding Source: UniProtKB
  3. RNA binding Source: ProtInc

GO - Biological processi

  1. gene expression Source: Reactome
  2. mRNA splicing, via spliceosome Source: Reactome
  3. RNA splicing Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Ribonucleoprotein

Keywords - Ligandi

RNA-binding

Enzyme and pathway databases

ReactomeiREACT_125. Processing of Capped Intron-Containing Pre-mRNA.
REACT_467. mRNA Splicing - Major Pathway.

Names & Taxonomyi

Protein namesi
Recommended name:
Heterogeneous nuclear ribonucleoprotein H2
Short name:
hnRNP H2
Alternative name(s):
FTP-3
Heterogeneous nuclear ribonucleoprotein H'
Short name:
hnRNP H'
Cleaved into the following chain:
Gene namesi
Name:HNRNPH2
Synonyms:FTP3, HNRPH2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome X

Organism-specific databases

HGNCiHGNC:5042. HNRNPH2.

Subcellular locationi

GO - Cellular componenti

  1. membrane Source: UniProtKB
  2. nucleoplasm Source: Reactome
  3. nucleus Source: ProtInc
  4. ribonucleoprotein complex Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA162391316.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 449449Heterogeneous nuclear ribonucleoprotein H2PRO_0000081859Add
BLAST
Initiator methioninei1 – 11Removed; alternateBy similarity
Chaini2 – 449448Heterogeneous nuclear ribonucleoprotein H2, N-terminally processedPRO_0000423273Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionine4 Publications
Modified residuei2 – 21N-acetylmethionine; in Heterogeneous nuclear ribonucleoprotein H2, N-terminally processedBy similarity
Modified residuei23 – 231PhosphoserineBy similarity
Modified residuei63 – 631PhosphoserineBy similarity
Modified residuei233 – 2331Dimethylated arginine; alternateBy similarity
Modified residuei233 – 2331Omega-N-methylarginine; alternateBy similarity
Modified residuei246 – 2461PhosphotyrosineBy similarity
Modified residuei310 – 3101Phosphoserine4 Publications

Keywords - PTMi

Acetylation, Methylation, Phosphoprotein

Proteomic databases

MaxQBiP55795.
PaxDbiP55795.
PeptideAtlasiP55795.
PRIDEiP55795.

2D gel databases

REPRODUCTION-2DPAGEIPI00026230.

PTM databases

PhosphoSiteiP55795.

Expressioni

Tissue specificityi

Expressed ubiquitously.

Gene expression databases

BgeeiP55795.
CleanExiHS_HNRNPH2.
GenevestigatoriP55795.

Organism-specific databases

HPAiCAB004436.
HPA001359.
HPA016884.

Interactioni

Subunit structurei

Interacts with TXNL4/DIM1.1 Publication

Protein-protein interaction databases

BioGridi109429. 60 interactions.
IntActiP55795. 53 interactions.
MINTiMINT-2804293.
STRINGi9606.ENSP00000361927.

Structurei

Secondary structure

1
449
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi112 – 1176Combined sources
Helixi124 – 1307Combined sources
Turni131 – 1333Combined sources
Beta strandi136 – 1427Combined sources
Beta strandi147 – 1493Combined sources
Beta strandi153 – 1619Combined sources
Helixi162 – 1698Combined sources
Turni170 – 1734Combined sources
Beta strandi176 – 1794Combined sources
Beta strandi182 – 1865Combined sources
Turni188 – 1903Combined sources
Beta strandi286 – 2883Combined sources
Beta strandi290 – 2956Combined sources
Helixi302 – 3076Combined sources
Beta strandi315 – 32511Combined sources
Beta strandi327 – 3348Combined sources
Beta strandi336 – 3383Combined sources
Helixi339 – 3457Combined sources
Beta strandi352 – 3554Combined sources
Beta strandi358 – 3625Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1WEZNMR-A281-369[»]
1WG5NMR-A103-193[»]
ProteinModelPortaliP55795.
SMRiP55795. Positions 4-193, 277-401.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP55795.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini11 – 9080RRM 1PROSITE-ProRule annotationAdd
BLAST
Domaini111 – 18878RRM 2PROSITE-ProRule annotationAdd
BLAST
Repeati234 – 249161-1Add
BLAST
Domaini289 – 36476RRM 3PROSITE-ProRule annotationAdd
BLAST
Repeati354 – 372192-1Add
BLAST
Repeati374 – 392192-2Add
BLAST
Repeati418 – 433161-2Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni234 – 4332002 X 16 AA Gly-rich approximate repeatsAdd
BLAST
Regioni354 – 392392 X 19 AA perfect repeatsAdd
BLAST

Sequence similaritiesi

Contains 3 RRM (RNA recognition motif) domains.PROSITE-ProRule annotation

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiNOG262593.
GeneTreeiENSGT00760000119102.
HOGENOMiHOG000220896.
HOVERGENiHBG055557.
InParanoidiP55795.
KOiK12898.
OMAiPPRKLMT.
OrthoDBiEOG7BS4BZ.
PhylomeDBiP55795.
TreeFamiTF316157.

Family and domain databases

Gene3Di3.30.70.330. 3 hits.
InterProiIPR012677. Nucleotide-bd_a/b_plait.
IPR000504. RRM_dom.
IPR012996. Znf_CHHC.
[Graphical view]
PfamiPF08080. zf-RNPHF. 1 hit.
[Graphical view]
SMARTiSM00360. RRM. 3 hits.
[Graphical view]
PROSITEiPS50102. RRM. 3 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P55795-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MMLSTEGREG FVVKVRGLPW SCSADEVMRF FSDCKIQNGT SGIRFIYTRE
60 70 80 90 100
GRPSGEAFVE LESEEEVKLA LKKDRETMGH RYVEVFKSNS VEMDWVLKHT
110 120 130 140 150
GPNSPDTAND GFVRLRGLPF GCSKEEIVQF FSGLEIVPNG MTLPVDFQGR
160 170 180 190 200
STGEAFVQFA SQEIAEKALK KHKERIGHRY IEIFKSSRAE VRTHYDPPRK
210 220 230 240 250
LMAMQRPGPY DRPGAGRGYN SIGRGAGFER MRRGAYGGGY GGYDDYGGYN
260 270 280 290 300
DGYGFGSDRF GRDLNYCFSG MSDHRYGDGG SSFQSTTGHC VHMRGLPYRA
310 320 330 340 350
TENDIYNFFS PLNPMRVHIE IGPDGRVTGE ADVEFATHED AVAAMAKDKA
360 370 380 390 400
NMQHRYVELF LNSTAGTSGG AYDHSYVELF LNSTAGASGG AYGSQMMGGM
410 420 430 440
GLSNQSSYGG PASQQLSGGY GGGYGGQSSM SGYDQVLQEN SSDYQSNLA
Length:449
Mass (Da):49,264
Last modified:November 1, 1997 - v1
Checksum:iC892523A638F07C7
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U01923 mRNA. No translation available.
U78027 Genomic DNA. Translation: AAB64202.1.
AL035422 Genomic DNA. Translation: CAB55879.2.
CH471115 Genomic DNA. Translation: EAX02864.1.
BC130343 mRNA. Translation: AAI30344.1.
BC130345 mRNA. Translation: AAI30346.1.
CCDSiCCDS14485.1.
RefSeqiNP_001027565.1. NM_001032393.2.
NP_062543.1. NM_019597.4.
UniGeneiHs.432485.

Genome annotation databases

EnsembliENST00000316594; ENSP00000361927; ENSG00000126945.
GeneIDi3188.
KEGGihsa:3188.
UCSCiuc004ehm.3. human.

Polymorphism databases

DMDMi2500576.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U01923 mRNA. No translation available.
U78027 Genomic DNA. Translation: AAB64202.1 .
AL035422 Genomic DNA. Translation: CAB55879.2 .
CH471115 Genomic DNA. Translation: EAX02864.1 .
BC130343 mRNA. Translation: AAI30344.1 .
BC130345 mRNA. Translation: AAI30346.1 .
CCDSi CCDS14485.1.
RefSeqi NP_001027565.1. NM_001032393.2.
NP_062543.1. NM_019597.4.
UniGenei Hs.432485.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1WEZ NMR - A 281-369 [» ]
1WG5 NMR - A 103-193 [» ]
ProteinModelPortali P55795.
SMRi P55795. Positions 4-193, 277-401.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 109429. 60 interactions.
IntActi P55795. 53 interactions.
MINTi MINT-2804293.
STRINGi 9606.ENSP00000361927.

PTM databases

PhosphoSitei P55795.

Polymorphism databases

DMDMi 2500576.

2D gel databases

REPRODUCTION-2DPAGE IPI00026230.

Proteomic databases

MaxQBi P55795.
PaxDbi P55795.
PeptideAtlasi P55795.
PRIDEi P55795.

Protocols and materials databases

DNASUi 3188.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000316594 ; ENSP00000361927 ; ENSG00000126945 .
GeneIDi 3188.
KEGGi hsa:3188.
UCSCi uc004ehm.3. human.

Organism-specific databases

CTDi 3188.
GeneCardsi GC0XP100663.
HGNCi HGNC:5042. HNRNPH2.
HPAi CAB004436.
HPA001359.
HPA016884.
MIMi 300610. gene.
neXtProti NX_P55795.
PharmGKBi PA162391316.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG262593.
GeneTreei ENSGT00760000119102.
HOGENOMi HOG000220896.
HOVERGENi HBG055557.
InParanoidi P55795.
KOi K12898.
OMAi PPRKLMT.
OrthoDBi EOG7BS4BZ.
PhylomeDBi P55795.
TreeFami TF316157.

Enzyme and pathway databases

Reactomei REACT_125. Processing of Capped Intron-Containing Pre-mRNA.
REACT_467. mRNA Splicing - Major Pathway.

Miscellaneous databases

EvolutionaryTracei P55795.
GeneWikii HNRPH2.
GenomeRNAii 3188.
NextBioi 12674.
PROi P55795.
SOURCEi Search...

Gene expression databases

Bgeei P55795.
CleanExi HS_HNRNPH2.
Genevestigatori P55795.

Family and domain databases

Gene3Di 3.30.70.330. 3 hits.
InterProi IPR012677. Nucleotide-bd_a/b_plait.
IPR000504. RRM_dom.
IPR012996. Znf_CHHC.
[Graphical view ]
Pfami PF08080. zf-RNPHF. 1 hit.
[Graphical view ]
SMARTi SM00360. RRM. 3 hits.
[Graphical view ]
PROSITEi PS50102. RRM. 3 hits.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "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: PARTIAL NUCLEOTIDE SEQUENCE [MRNA].
  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].
    Tissue: Brain.
  7. 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, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Ovarian carcinoma.
  8. 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, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Fetal brain cortex.
  9. "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] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH TXNL4.
  10. "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-310, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  11. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-310, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  12. "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] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  13. "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-310, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  14. "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-310, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  15. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  16. "Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
    Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
    Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  17. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  18. "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.

Entry informationi

Entry nameiHNRH2_HUMAN
AccessioniPrimary (citable) accession number: P55795
Secondary accession number(s): A1L400, Q9HHA7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1997
Last modified: November 26, 2014
This is version 160 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome X
    Human chromosome X: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3