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P31942

- HNRH3_HUMAN

UniProt

P31942 - HNRH3_HUMAN

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Protein
Heterogeneous nuclear ribonucleoprotein H3
Gene
HNRNPH3, HNRPH3
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Involved in the splicing process and participates in early heat shock-induced splicing arrest. Due to their great structural variations the different isoforms may possess different functions in the splicing reaction.

GO - Molecular functioni

  1. RNA binding Source: UniProtKB
  2. nucleotide binding Source: InterPro
  3. poly(A) RNA binding Source: UniProtKB
  4. protein binding Source: UniProt

GO - Biological processi

  1. RNA processing Source: ProtInc
  2. RNA splicing Source: ProtInc
  3. epithelial cell differentiation Source: UniProt
  4. mRNA splicing, via spliceosome Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Ribonucleoprotein

Keywords - Biological processi

mRNA processing

Keywords - Ligandi

RNA-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Heterogeneous nuclear ribonucleoprotein H3
Short name:
hnRNP H3
Alternative name(s):
Heterogeneous nuclear ribonucleoprotein 2H9
Short name:
hnRNP 2H9
Gene namesi
Name:HNRNPH3
Synonyms:HNRPH3
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 10

Organism-specific databases

HGNCiHGNC:5043. HNRNPH3.

Subcellular locationi

Nucleus 1 Publication

GO - Cellular componenti

  1. nucleus Source: UniProt
  2. spliceosomal complex Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA162391325.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 346346Heterogeneous nuclear ribonucleoprotein H3
PRO_0000081861Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionine1 Publication
Modified residuei121 – 1211Asymmetric dimethylarginine1 Publication
Modified residuei216 – 2161Phosphoserine7 Publications
Modified residuei287 – 2871Omega-N-methylarginine1 Publication
Modified residuei298 – 2981Phosphoserine3 Publications
Modified residuei314 – 3141Phosphothreonine1 Publication

Keywords - PTMi

Acetylation, Methylation, Phosphoprotein

Proteomic databases

MaxQBiP31942.
PaxDbiP31942.
PRIDEiP31942.

PTM databases

PhosphoSiteiP31942.

Expressioni

Gene expression databases

ArrayExpressiP31942.
BgeeiP31942.
CleanExiHS_HNRNPH3.
GenevestigatoriP31942.

Organism-specific databases

HPAiHPA038264.

Interactioni

Protein-protein interaction databases

BioGridi109430. 65 interactions.
IntActiP31942. 46 interactions.
MINTiMINT-5004191.

Structurei

3D structure databases

ProteinModelPortaliP31942.
SMRiP31942. Positions 10-97, 194-270.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini16 – 9378RRM 1
Add
BLAST
Domaini195 – 27076RRM 2
Add
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi108 – 344237Gly-rich
Add
BLAST

Sequence similaritiesi

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiNOG262593.
HOVERGENiHBG055557.
InParanoidiP31942.
KOiK12898.
OMAiPYDRPLG.
OrthoDBiEOG7BS4BZ.
PhylomeDBiP31942.
TreeFamiTF316157.

Family and domain databases

Gene3Di3.30.70.330. 2 hits.
InterProiIPR012677. Nucleotide-bd_a/b_plait.
IPR000504. RRM_dom.
[Graphical view]
SMARTiSM00360. RRM. 2 hits.
[Graphical view]
PROSITEiPS50102. RRM. 2 hits.
[Graphical view]

Sequences (6)i

Sequence statusi: Complete.

This entry describes 6 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: P31942-1) [UniParc]FASTAAdd to Basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

MDWVMKHNGP NDASDGTVRL RGLPFGCSKE EIVQFFQGLE IVPNGITLTM    50
DYQGRSTGEA FVQFASKEIA ENALGKHKER IGHRYIEIFR SSRSEIKGFY 100
DPPRRLLGQR PGPYDRPIGG RGGYYGAGRG SMYDRMRRGG DGYDGGYGGF 150
DDYGGYNNYG YGNDGFDDRM RDGRGMGGHG YGGAGDASSG FHGGHFVHMR 200
GLPFRATEND IANFFSPLNP IRVHIDIGAD GRATGEADVE FVTHEDAVAA 250
MSKDKNNMQH RYIELFLNST PGGGSGMGGS GMGGYGRDGM DNQGGYGSVG 300
RMGMGNNYSG GYGTPDGLGG YGRGGGGSGG YYGQGGMSGG GWRGMY 346
Length:346
Mass (Da):36,926
Last modified:September 19, 2002 - v2
Checksum:iF7D14C2947930E9E
GO
Isoform 2 (identifier: P31942-2) [UniParc]FASTAAdd to Basket

Also known as: 2H9A

The sequence of this isoform differs from the canonical sequence as follows:
     132-146: Missing.

Show »
Length:331
Mass (Da):35,239
Checksum:iA3BA8D0F5FC07369
GO
Isoform 3 (identifier: P31942-3) [UniParc]FASTAAdd to Basket

Also known as: 2H9B

The sequence of this isoform differs from the canonical sequence as follows:
     1-49: Missing.

Show »
Length:297
Mass (Da):31,525
Checksum:iAAE63A29063E5153
GO
Isoform 4 (identifier: P31942-4) [UniParc]FASTAAdd to Basket

Also known as: 2H9C

The sequence of this isoform differs from the canonical sequence as follows:
     1-131: Missing.

Show »
Length:215
Mass (Da):22,322
Checksum:i969F8FE2710D2646
GO
Isoform 5 (identifier: P31942-5) [UniParc]FASTAAdd to Basket

Also known as: 2H9D

The sequence of this isoform differs from the canonical sequence as follows:
     1-131: Missing.
     259-276: QHRYIELFLNSTPGGGSG → RKWCLWHTILFPKREFIK
     277-346: Missing.

Show »
Length:145
Mass (Da):16,084
Checksum:i286234CBE7C9C996
GO
Isoform 6 (identifier: P31942-6) [UniParc]FASTAAdd to Basket

Also known as: 2H9E

The sequence of this isoform differs from the canonical sequence as follows:
     1-137: Missing.
     138-145: RGGDGYDG → MCFSLNYT
     259-276: QHRYIELFLNSTPGGGSG → RKWCLWHTILFPKREFIK
     277-346: Missing.

Show »
Length:139
Mass (Da):15,413
Checksum:iF1E137E637675D93
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti163 – 1631N → S.
Corresponds to variant rs2273903 [ dbSNP | Ensembl ].
VAR_020333
Natural varianti284 – 2841G → A.
Corresponds to variant rs16925347 [ dbSNP | Ensembl ].
VAR_052226

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 137137Missing in isoform 6.
VSP_005841Add
BLAST
Alternative sequencei1 – 131131Missing in isoform 4 and isoform 5.
VSP_005839Add
BLAST
Alternative sequencei1 – 4949Missing in isoform 3.
VSP_005838Add
BLAST
Alternative sequencei132 – 14615Missing in isoform 2.
VSP_005840Add
BLAST
Alternative sequencei138 – 1458RGGDGYDG → MCFSLNYT in isoform 6.
VSP_005842
Alternative sequencei259 – 27618QHRYI…GGGSG → RKWCLWHTILFPKREFIK in isoform 5 and isoform 6.
VSP_005843Add
BLAST
Alternative sequencei277 – 34670Missing in isoform 5 and isoform 6.
VSP_005844Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
L32610 mRNA. Translation: AAD45179.1.
AF132360 Genomic DNA. Translation: AAF68843.1.
AF132360 Genomic DNA. Translation: AAF68844.1.
AF132360 Genomic DNA. Translation: AAF68845.1.
AF132360 Genomic DNA. Translation: AAF68846.1.
AF132360 Genomic DNA. Translation: AAF68847.1.
AF132360 Genomic DNA. Translation: AAF68848.1.
AF132361 mRNA. Translation: AAF68849.1.
AF132362 mRNA. Translation: AAF68850.1.
AF132363 mRNA. Translation: AAF68851.1.
AF132364 mRNA. Translation: AAF68852.1.
AK091411 mRNA. Translation: BAG52353.1.
AK291547 mRNA. Translation: BAF84236.1.
AL117395 mRNA. Translation: CAB55897.1.
CH471083 Genomic DNA. Translation: EAW54281.1.
CH471083 Genomic DNA. Translation: EAW54282.1.
BC004511 mRNA. Translation: AAH04511.2.
BC039824 mRNA. Translation: AAH39824.1.
CCDSiCCDS7278.1. [P31942-1]
CCDS7279.1. [P31942-2]
PIRiT17207.
RefSeqiNP_036339.1. NM_012207.2. [P31942-1]
NP_067676.2. NM_021644.3. [P31942-2]
XP_005269805.1. XM_005269748.2. [P31942-1]
XP_005269806.1. XM_005269749.2. [P31942-2]
XP_005269808.1. XM_005269751.2. [P31942-4]
XP_005269809.1. XM_005269752.2. [P31942-4]
XP_006717879.1. XM_006717816.1. [P31942-1]
XP_006717880.1. XM_006717817.1. [P31942-2]
UniGeneiHs.643472.

Genome annotation databases

EnsembliENST00000265866; ENSP00000265866; ENSG00000096746. [P31942-1]
ENST00000354695; ENSP00000346726; ENSG00000096746. [P31942-2]
GeneIDi3189.
KEGGihsa:3189.
UCSCiuc001jnw.4. human. [P31942-1]
uc001jnx.4. human. [P31942-2]

Polymorphism databases

DMDMi23503095.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
L32610 mRNA. Translation: AAD45179.1 .
AF132360 Genomic DNA. Translation: AAF68843.1 .
AF132360 Genomic DNA. Translation: AAF68844.1 .
AF132360 Genomic DNA. Translation: AAF68845.1 .
AF132360 Genomic DNA. Translation: AAF68846.1 .
AF132360 Genomic DNA. Translation: AAF68847.1 .
AF132360 Genomic DNA. Translation: AAF68848.1 .
AF132361 mRNA. Translation: AAF68849.1 .
AF132362 mRNA. Translation: AAF68850.1 .
AF132363 mRNA. Translation: AAF68851.1 .
AF132364 mRNA. Translation: AAF68852.1 .
AK091411 mRNA. Translation: BAG52353.1 .
AK291547 mRNA. Translation: BAF84236.1 .
AL117395 mRNA. Translation: CAB55897.1 .
CH471083 Genomic DNA. Translation: EAW54281.1 .
CH471083 Genomic DNA. Translation: EAW54282.1 .
BC004511 mRNA. Translation: AAH04511.2 .
BC039824 mRNA. Translation: AAH39824.1 .
CCDSi CCDS7278.1. [P31942-1 ]
CCDS7279.1. [P31942-2 ]
PIRi T17207.
RefSeqi NP_036339.1. NM_012207.2. [P31942-1 ]
NP_067676.2. NM_021644.3. [P31942-2 ]
XP_005269805.1. XM_005269748.2. [P31942-1 ]
XP_005269806.1. XM_005269749.2. [P31942-2 ]
XP_005269808.1. XM_005269751.2. [P31942-4 ]
XP_005269809.1. XM_005269752.2. [P31942-4 ]
XP_006717879.1. XM_006717816.1. [P31942-1 ]
XP_006717880.1. XM_006717817.1. [P31942-2 ]
UniGenei Hs.643472.

3D structure databases

ProteinModelPortali P31942.
SMRi P31942. Positions 10-97, 194-270.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 109430. 65 interactions.
IntActi P31942. 46 interactions.
MINTi MINT-5004191.

PTM databases

PhosphoSitei P31942.

Polymorphism databases

DMDMi 23503095.

Proteomic databases

MaxQBi P31942.
PaxDbi P31942.
PRIDEi P31942.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000265866 ; ENSP00000265866 ; ENSG00000096746 . [P31942-1 ]
ENST00000354695 ; ENSP00000346726 ; ENSG00000096746 . [P31942-2 ]
GeneIDi 3189.
KEGGi hsa:3189.
UCSCi uc001jnw.4. human. [P31942-1 ]
uc001jnx.4. human. [P31942-2 ]

Organism-specific databases

CTDi 3189.
GeneCardsi GC10P070090.
HGNCi HGNC:5043. HNRNPH3.
HPAi HPA038264.
MIMi 602324. gene.
neXtProti NX_P31942.
PharmGKBi PA162391325.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG262593.
HOVERGENi HBG055557.
InParanoidi P31942.
KOi K12898.
OMAi PYDRPLG.
OrthoDBi EOG7BS4BZ.
PhylomeDBi P31942.
TreeFami TF316157.

Miscellaneous databases

ChiTaRSi HNRNPH3. human.
GeneWikii HNRPH3.
GenomeRNAii 3189.
NextBioi 12680.
PROi P31942.
SOURCEi Search...

Gene expression databases

ArrayExpressi P31942.
Bgeei P31942.
CleanExi HS_HNRNPH3.
Genevestigatori P31942.

Family and domain databases

Gene3Di 3.30.70.330. 2 hits.
InterProi IPR012677. Nucleotide-bd_a/b_plait.
IPR000504. RRM_dom.
[Graphical view ]
SMARTi SM00360. RRM. 2 hits.
[Graphical view ]
PROSITEi PS50102. RRM. 2 hits.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning of human 2H9 heterogeneous nuclear ribonucleoproteins. Relation with splicing and early heat shock-induced splicing arrest."
    Mahe D., Mahl P., Gattoni R., Fischer N., Mattei M.-G., Stevenin J., Fuchs J.-P.
    J. Biol. Chem. 272:1827-1836(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SUBCELLULAR LOCATION.
  2. "The hnRNP 2H9 gene, which is involved in the splicing reaction, is a multiply spliced gene."
    Honore B.
    Biochim. Biophys. Acta 1492:108-119(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORMS 1; 2; 3; 4; 5 AND 6).
  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] (ISOFORMS 2 AND 4).
    Tissue: Brain and Placenta.
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
    Tissue: Uterus.
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  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] (ISOFORM 2).
    Tissue: Ovary and Skin.
  7. Bienvenut W.V., Lilla S., von Kriegsheim A., Lempens A., Kolch W.
    Submitted (DEC-2008) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 1-6; 56-76; 85-90; 98-104; 175-200; 223-253 AND 262-323, ACETYLATION AT MET-1, METHYLATION AT ARG-287, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Ovarian carcinoma.
  8. Lubec G., Vishwanath V., Chen W.-Q., Sun Y.
    Submitted (DEC-2008) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 56-67; 206-222; 233-253 AND 262-287, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Brain, Cajal-Retzius cell and Fetal brain cortex.
  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 94-104 AND 288-298.
    Tissue: Keratinocyte.
  10. "A post-translational modification of nuclear proteins, N(G),N(G)-dimethyl-Arg, found in a natural HLA class I peptide ligand."
    Yague J., Vazquez J., Lopez de Castro J.A.
    Protein Sci. 9:2210-2217(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 116-127, METHYLATION AT ARG-121.
  11. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  12. "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-216, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  13. "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-216, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  14. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-216, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  15. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-216, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  16. "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-216; SER-298 AND THR-314, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  17. "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-216 AND SER-298, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  18. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  19. "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-216 AND SER-298, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiHNRH3_HUMAN
AccessioniPrimary (citable) accession number: P31942
Secondary accession number(s): A8K682
, B3KRE1, Q9BSX1, Q9NP53, Q9NP96, Q9NPA7, Q9NPI4, Q9UFU4, Q9Y4J5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1993
Last sequence update: September 19, 2002
Last modified: September 3, 2014
This is version 147 of the entry and version 2 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

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 10
    Human chromosome 10: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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