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P31943

- HNRH1_HUMAN

UniProt

P31943 - HNRH1_HUMAN

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Protein

Heterogeneous nuclear ribonucleoprotein H

Gene

HNRNPH1

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

GO - Biological processi

  1. gene expression Source: Reactome
  2. mRNA splicing, via spliceosome Source: UniProtKB
  3. regulation of RNA splicing Source: UniProtKB
  4. RNA processing Source: ProtInc
  5. RNA splicing Source: Reactome
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. membrane Source: UniProtKB
  3. nucleoplasm Source: Reactome
  4. 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 HPRO_0000367119Add
BLAST
Initiator methioninei1 – 11Removed; alternate3 Publications
Chaini2 – 449448Heterogeneous nuclear ribonucleoprotein H, N-terminally processedPRO_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 – 3101PhosphoserineBy 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

BgeeiP31943.
CleanExiHS_HNRNPH1.
ExpressionAtlasiP31943. baseline and differential.
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. 144 interactions.
IntActiP31943. 55 interactions.
MINTiMINT-1160934.
STRINGi9606.ENSP00000349168.

Structurei

Secondary structure

1
449
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi9 – 179Combined sources
Helixi24 – 307Combined sources
Turni31 – 333Combined sources
Helixi39 – 413Combined sources
Beta strandi42 – 476Combined sources
Beta strandi51 – 6212Combined sources
Helixi64 – 718Combined sources
Turni72 – 754Combined sources
Beta strandi84 – 885Combined sources
Helixi90 – 989Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2LXUNMR-A7-111[»]
ProteinModelPortaliP31943.
SMRiP31943. Positions 7-193, 283-393.
ModBaseiSearch...
MobiDBiSearch...

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

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

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

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiNOG262593.
GeneTreeiENSGT00760000119102.
HOGENOMiHOG000220896.
HOVERGENiHBG055557.
InParanoidiP31943.
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

        10         20         30         40         50
MMLGTEGGEG FVVKVRGLPW SCSADEVQRF FSDCKIQNGA QGIRFIYTRE
60 70 80 90 100
GRPSGEAFVE LESEDEVKLA LKKDRETMGH RYVEVFKSNN VEMDWVLKHT
110 120 130 140 150
GPNSPDTAND GFVRLRGLPF GCSKEEIVQF FSGLEIVPNG ITLPVDFQGR
160 170 180 190 200
STGEAFVQFA SQEIAEKALK KHKERIGHRY IEIFKSSRAE VRTHYDPPRK
210 220 230 240 250
LMAMQRPGPY DRPGAGRGYN SIGRGAGFER MRRGAYGGGY GGYDDYNGYN
260 270 280 290 300
DGYGFGSDRF GRDLNYCFSG MSDHRYGDGG STFQSTTGHC VHMRGLPYRA
310 320 330 340 350
TENDIYNFFS PLNPVRVHIE IGPDGRVTGE ADVEFATHED AVAAMSKDKA
360 370 380 390 400
NMQHRYVELF LNSTAGASGG AYEHRYVELF LNSTAGASGG AYGSQMMGGM
410 420 430 440
GLSNQSSYGG PASQQLSGGY GGGYGGQSSM SGYDQVLQEN SSDFQSNIA
Length:449
Mass (Da):49,229
Last modified:January 23, 2007 - v4
Checksum:i4ECF7A075C2526FF
GO

Experimental Info

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

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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:
PDBei
RCSB PDBi
PDBji
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...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 109428. 144 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.
GeneTreei ENSGT00760000119102.
HOGENOMi HOG000220896.
HOVERGENi HBG055557.
InParanoidi P31943.
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

Bgeei P31943.
CleanExi HS_HNRNPH1.
ExpressionAtlasi P31943. baseline and differential.
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: November 26, 2014
This is version 166 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