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P31943

- HNRH1_HUMAN

UniProt

P31943 - HNRH1_HUMAN

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Protein
Heterogeneous nuclear ribonucleoprotein H
Gene
HNRNPH1, HNRPH, HNRPH1
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. 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).2 Publications

GO - Molecular functioni

  1. RNA binding Source: UniProtKB
  2. nucleotide binding Source: InterPro
  3. poly(A) RNA binding Source: UniProtKB
  4. poly(U) RNA binding Source: ProtInc
  5. protein binding Source: UniProtKB
Complete GO annotation...

GO - Biological processi

  1. RNA processing Source: ProtInc
  2. RNA splicing Source: Reactome
  3. gene expression Source: Reactome
  4. mRNA splicing, via spliceosome Source: UniProtKB
  5. regulation of RNA splicing Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Ribonucleoprotein

Keywords - Biological processi

mRNA processing, mRNA splicing

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 H
Short name:
hnRNP H
Cleaved into the following chain:
Gene namesi
Name:HNRNPH1
Synonyms:HNRPH, HNRPH1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 5

Organism-specific databases

HGNCiHGNC:5041. HNRNPH1.

Subcellular locationi

GO - Cellular componenti

  1. catalytic step 2 spliceosome Source: UniProtKB
  2. nucleoplasm Source: Reactome
  3. nucleus Source: ProtInc
Complete GO annotation...

Keywords - Cellular componenti

Nucleus, Spliceosome

Pathology & Biotechi

Organism-specific databases

Orphaneti99861. Precursor T-cell acute lymphoblastic leukemia.
PharmGKBiPA162391284.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 449449Heterogeneous nuclear ribonucleoprotein H
PRO_0000367119Add
BLAST
Initiator methioninei1 – 11Removed; alternate2 Publications
Chaini2 – 449448Heterogeneous nuclear ribonucleoprotein H, N-terminally processed
PRO_0000081857Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionine; in Heterogeneous nuclear ribonucleoprotein H; alternate3 Publications
Modified residuei2 – 21N-acetylmethionine; in Heterogeneous nuclear ribonucleoprotein H, N-terminally processed4 Publications
Modified residuei23 – 231Phosphoserine1 Publication
Modified residuei63 – 631Phosphoserine6 Publications
Modified residuei233 – 2331Dimethylated arginine; alternate1 Publication
Modified residuei233 – 2331Omega-N-methylarginine; alternate1 Publication
Modified residuei246 – 2461Phosphotyrosine1 Publication
Modified residuei310 – 3101Phosphoserine By similarity

Keywords - PTMi

Acetylation, Methylation, Phosphoprotein

Proteomic databases

MaxQBiP31943.
PaxDbiP31943.
PRIDEiP31943.

2D gel databases

REPRODUCTION-2DPAGEIPI00013881.
P31943.

PTM databases

PhosphoSiteiP31943.

Expressioni

Tissue specificityi

Expressed ubiquitously.

Inductioni

Up-regulated in myotonic dystrophy pathophysiology (DM).1 Publication

Gene expression databases

ArrayExpressiP31943.
BgeeiP31943.
CleanExiHS_HNRNPH1.
GenevestigatoriP31943.

Organism-specific databases

HPAiHPA001359.
HPA016884.

Interactioni

Subunit structurei

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.4 Publications

Protein-protein interaction databases

BioGridi109428. 137 interactions.
IntActiP31943. 55 interactions.
MINTiMINT-1160934.
STRINGi9606.ENSP00000349168.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi9 – 179
Helixi24 – 307
Turni31 – 333
Helixi39 – 413
Beta strandi42 – 476
Beta strandi51 – 6212
Helixi64 – 718
Turni72 – 754
Beta strandi84 – 885
Helixi90 – 989

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2LXUNMR-A7-111[»]
ProteinModelPortaliP31943.
SMRiP31943. Positions 7-193, 283-393.

Family & Domainsi

Domains and Repeats

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

Region

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

Domaini

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 similaritiesi

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiNOG262593.
HOGENOMiHOG000220896.
HOVERGENiHBG055557.
KOiK12898.
OrthoDBiEOG7BS4BZ.
PhylomeDBiP31943.
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.

P31943-1 [UniParc]FASTAAdd to Basket

« Hide

MMLGTEGGEG FVVKVRGLPW SCSADEVQRF FSDCKIQNGA QGIRFIYTRE    50
GRPSGEAFVE LESEDEVKLA LKKDRETMGH RYVEVFKSNN VEMDWVLKHT 100
GPNSPDTAND GFVRLRGLPF GCSKEEIVQF FSGLEIVPNG ITLPVDFQGR 150
STGEAFVQFA SQEIAEKALK KHKERIGHRY IEIFKSSRAE VRTHYDPPRK 200
LMAMQRPGPY DRPGAGRGYN SIGRGAGFER MRRGAYGGGY GGYDDYNGYN 250
DGYGFGSDRF GRDLNYCFSG MSDHRYGDGG STFQSTTGHC VHMRGLPYRA 300
TENDIYNFFS PLNPVRVHIE IGPDGRVTGE ADVEFATHED AVAAMSKDKA 350
NMQHRYVELF LNSTAGASGG AYEHRYVELF LNSTAGASGG AYGSQMMGGM 400
GLSNQSSYGG PASQQLSGGY GGGYGGQSSM SGYDQVLQEN SSDFQSNIA 449
Length:449
Mass (Da):49,229
Last modified:January 23, 2007 - v4
Checksum:i4ECF7A075C2526FF
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti188 – 1881R → G in CAG33059. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSiCCDS4446.1.
PIRiI39358.
RefSeqiNP_001244222.1. NM_001257293.1.
NP_005511.1. NM_005520.2.
UniGeneiHs.604001.

Genome annotation databases

EnsembliENST00000356731; ENSP00000349168; ENSG00000169045.
ENST00000393432; ENSP00000377082; ENSG00000169045.
ENST00000442819; ENSP00000397797; ENSG00000169045.
GeneIDi3187.
KEGGihsa:3187.
UCSCiuc003mke.4. human.

Polymorphism databases

DMDMi1710632.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
CCDSi CCDS4446.1.
PIRi I39358.
RefSeqi NP_001244222.1. NM_001257293.1.
NP_005511.1. NM_005520.2.
UniGenei Hs.604001.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2LXU NMR - A 7-111 [» ]
ProteinModelPortali P31943.
SMRi P31943. Positions 7-193, 283-393.
ModBasei Search...

Protein-protein interaction databases

BioGridi 109428. 137 interactions.
IntActi P31943. 55 interactions.
MINTi MINT-1160934.
STRINGi 9606.ENSP00000349168.

PTM databases

PhosphoSitei P31943.

Polymorphism databases

DMDMi 1710632.

2D gel databases

REPRODUCTION-2DPAGE IPI00013881.
P31943.

Proteomic databases

MaxQBi P31943.
PaxDbi P31943.
PRIDEi P31943.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000356731 ; ENSP00000349168 ; ENSG00000169045 .
ENST00000393432 ; ENSP00000377082 ; ENSG00000169045 .
ENST00000442819 ; ENSP00000397797 ; ENSG00000169045 .
GeneIDi 3187.
KEGGi hsa:3187.
UCSCi uc003mke.4. human.

Organism-specific databases

CTDi 3187.
GeneCardsi GC05M179043.
HGNCi HGNC:5041. HNRNPH1.
HPAi HPA001359.
HPA016884.
MIMi 601035. gene.
neXtProti NX_P31943.
Orphaneti 99861. Precursor T-cell acute lymphoblastic leukemia.
PharmGKBi PA162391284.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG262593.
HOGENOMi HOG000220896.
HOVERGENi HBG055557.
KOi K12898.
OrthoDBi EOG7BS4BZ.
PhylomeDBi P31943.
TreeFami TF316157.

Enzyme and pathway databases

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

Miscellaneous databases

ChiTaRSi HNRNPH1. human.
GeneWikii HNRPH1.
GenomeRNAii 3187.
NextBioi 12670.
PROi P31943.
SOURCEi Search...

Gene expression databases

ArrayExpressi P31943.
Bgeei P31943.
CleanExi HS_HNRNPH1.
Genevestigatori P31943.

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. "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. 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. 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, IDENTIFICATION BY 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, IDENTIFICATION BY 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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    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. 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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  17. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-63, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  18. "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 AND MET-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  19. "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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  20. "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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  21. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  22. "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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  23. "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-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  24. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1 AND MET-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiHNRH1_HUMAN
AccessioniPrimary (citable) accession number: P31943
Secondary accession number(s): B3KW86, D3DWQ2, Q6IBM4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1993
Last sequence update: January 23, 2007
Last modified: September 3, 2014
This is version 163 of the entry and version 4 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 5
    Human chromosome 5: 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

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