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Q16695

- H31T_HUMAN

UniProt

Q16695 - H31T_HUMAN

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Protein

Histone H3.1t

Gene

HIST3H3

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

Functioni

Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling.

GO - Molecular functioni

  1. DNA binding Source: UniProtKB-KW

GO - Biological processi

  1. telomere maintenance Source: Reactome
Complete GO annotation...

Keywords - Ligandi

DNA-binding

Enzyme and pathway databases

ReactomeiREACT_169185. DNA Damage/Telomere Stress Induced Senescence.
REACT_172744. Condensation of Prophase Chromosomes.
REACT_200753. formation of the beta-catenin:TCF transactivating complex.
REACT_27271. Meiotic recombination.
REACT_75792. Meiotic synapsis.
REACT_7963. Packaging Of Telomere Ends.

Names & Taxonomyi

Protein namesi
Recommended name:
Histone H3.1t
Short name:
H3/t
Short name:
H3t
Alternative name(s):
H3/g
Gene namesi
Name:HIST3H3
Synonyms:H3FT
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 1

Organism-specific databases

HGNCiHGNC:4778. HIST3H3.

Subcellular locationi

GO - Cellular componenti

  1. extracellular vesicular exosome Source: UniProt
  2. nucleoplasm Source: Reactome
  3. nucleosome Source: UniProtKB-KW
  4. nucleus Source: UniProt
Complete GO annotation...

Keywords - Cellular componenti

Chromosome, Nucleosome core, Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA29153.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11RemovedBy similarity
Chaini2 – 136135Histone H3.1tPRO_0000221248Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei3 – 31Asymmetric dimethylarginine; by PRMT6; alternateBy similarity
Modified residuei3 – 31Citrulline; alternateBy similarity
Modified residuei4 – 41Phosphothreonine; by GSG2By similarity
Modified residuei5 – 51Allysine; alternateBy similarity
Modified residuei5 – 51N6,N6,N6-trimethyllysine; alternateBy similarity
Modified residuei5 – 51N6,N6-dimethyllysine; alternateBy similarity
Modified residuei5 – 51N6-acetyllysine; alternateBy similarity
Modified residuei5 – 51N6-methyllysine; alternateBy similarity
Modified residuei7 – 71Phosphothreonine; by PKCBy similarity
Modified residuei9 – 91Citrulline; alternateBy similarity
Modified residuei9 – 91Symmetric dimethylarginine; by PRMT5; alternateBy similarity
Modified residuei10 – 101N6,N6,N6-trimethyllysine; alternateBy similarity
Modified residuei10 – 101N6,N6-dimethyllysine; alternateBy similarity
Modified residuei10 – 101N6-acetyllysine; alternateBy similarity
Modified residuei10 – 101N6-methyllysine; alternateBy similarity
Modified residuei11 – 111Phosphoserine; by AURKB, AURKC, RPS6KA3, RPS6KA4 and RPS6KA5By similarity
Modified residuei12 – 121Phosphothreonine; by PKCBy similarity
Modified residuei15 – 151N6-acetyllysineBy similarity
Modified residuei18 – 181Asymmetric dimethylarginine; by CARM1; alternateBy similarity
Modified residuei18 – 181Citrulline; alternateBy similarity
Modified residuei19 – 191N6-acetyllysine; alternate1 Publication
Modified residuei19 – 191N6-methyllysine; alternateBy similarity
Modified residuei24 – 241N6-acetyllysine; alternate1 Publication
Modified residuei24 – 241N6-methyllysine; alternateBy similarity
Modified residuei27 – 271CitrullineBy similarity
Modified residuei28 – 281N6,N6,N6-trimethyllysine; alternateBy similarity
Modified residuei28 – 281N6,N6-dimethyllysine; alternateBy similarity
Modified residuei28 – 281N6-acetyllysine; alternateBy similarity
Modified residuei28 – 281N6-methyllysine; alternateBy similarity
Modified residuei29 – 291Phosphoserine; by AURKB, AURKC and RPS6KA51 Publication
Modified residuei37 – 371N6,N6,N6-trimethyllysine; alternateBy similarity
Modified residuei37 – 371N6,N6-dimethyllysine; alternateBy similarity
Modified residuei37 – 371N6-acetyllysine; alternateBy similarity
Modified residuei37 – 371N6-methyllysine; alternateBy similarity
Modified residuei38 – 381N6-methyllysineBy similarity
Modified residuei42 – 421PhosphotyrosineBy similarity
Modified residuei57 – 571N6,N6,N6-trimethyllysine; alternateBy similarity
Modified residuei57 – 571N6-acetyllysine; alternateBy similarity
Modified residuei57 – 571N6-methyllysine; by EHMT2; alternateBy similarity
Modified residuei58 – 581Phosphoserine1 Publication
Modified residuei65 – 651N6-methyllysineBy similarity
Modified residuei80 – 801N6,N6,N6-trimethyllysine; alternateBy similarity
Modified residuei80 – 801N6,N6-dimethyllysine; alternateBy similarity
Modified residuei80 – 801N6-acetyllysine; alternateBy similarity
Modified residuei80 – 801N6-methyllysine; alternateBy similarity
Modified residuei81 – 811Phosphothreonine1 Publication
Modified residuei108 – 1081PhosphothreonineBy similarity
Modified residuei116 – 1161N6-acetyllysineBy similarity
Modified residuei123 – 1231N6-acetyllysine; alternateBy similarity
Modified residuei123 – 1231N6-methyllysine; alternateBy similarity

Post-translational modificationi

Acetylation is generally linked to gene activation. Acetylation on Lys-10 (H3K9ac) impairs methylation at Arg-9 (H3R8me2s). Acetylation on Lys-19 (H3K18ac) and Lys-24 (H3K24ac) favors methylation at Arg-18 (H3R17me). Acetylation at Lys-123 (H3K122ac) by EP300/p300 plays a central role in chromatin structure: localizes at the surface of the histone octamer and stimulates transcription, possibly by promoting nucleosome instability (By similarity).By similarity
Citrullination at Arg-9 (H3R8ci) and/or Arg-18 (H3R17ci) by PADI4 impairs methylation and represses transcription.By similarity
Asymmetric dimethylation at Arg-18 (H3R17me2a) by CARM1 is linked to gene activation. Symmetric dimethylation at Arg-9 (H3R8me2s) by PRMT5 is linked to gene repression. Asymmetric dimethylation at Arg-3 (H3R2me2a) by PRMT6 is linked to gene repression and is mutually exclusive with H3 Lys-5 methylation (H3K4me2 and H3K4me3). H3R2me2a is present at the 3' of genes regardless of their transcription state and is enriched on inactive promoters, while it is absent on active promoters (By similarity).By similarity
Methylation at Lys-5 (H3K4me), Lys-37 (H3K36me) and Lys-80 (H3K79me) are linked to gene activation. Methylation at Lys-5 (H3K4me) facilitates subsequent acetylation of H3 and H4. Methylation at Lys-80 (H3K79me) is associated with DNA double-strand break (DSB) responses and is a specific target for TP53BP1. Methylation at Lys-10 (H3K9me) and Lys-28 (H3K27me) are linked to gene repression. Methylation at Lys-10 (H3K9me) is a specific target for HP1 proteins (CBX1, CBX3 and CBX5) and prevents subsequent phosphorylation at Ser-11 (H3S10ph) and acetylation of H3 and H4. Methylation at Lys-5 (H3K4me) and Lys-80 (H3K79me) require preliminary monoubiquitination of H2B at 'Lys-120'. Methylation at Lys-10 (H3K9me) and Lys-28 (H3K27me) are enriched in inactive X chromosome chromatin. Monomethylation at Lys-57 (H3K56me1) by EHMT2/G9A in G1 phase promotes interaction with PCNA and is required for DNA replication (By similarity).By similarity
Phosphorylated at Thr-4 (H3T3ph) by GSG2/haspin during prophase and dephosphorylated during anaphase. Phosphorylation at Ser-11 (H3S10ph) by AURKB is crucial for chromosome condensation and cell-cycle progression during mitosis and meiosis. In addition phosphorylation at Ser-11 (H3S10ph) by RPS6KA4 and RPS6KA5 is important during interphase because it enables the transcription of genes following external stimulation, like mitogens, stress, growth factors or UV irradiation and result in the activation of genes, such as c-fos and c-jun. Phosphorylation at Ser-11 (H3S10ph), which is linked to gene activation, prevents methylation at Lys-10 (H3K9me) but facilitates acetylation of H3 and H4. Phosphorylation at Ser-11 (H3S10ph) by AURKB mediates the dissociation of HP1 proteins (CBX1, CBX3 and CBX5) from heterochromatin. Phosphorylation at Ser-11 (H3S10ph) is also an essential regulatory mechanism for neoplastic cell transformation. Phosphorylated at Ser-29 (H3S28ph) by MLTK isoform 1, RPS6KA5 or AURKB during mitosis or upon ultraviolet B irradiation. Phosphorylation at Thr-7 (H3T6ph) by PRKCB is a specific tag for epigenetic transcriptional activation that prevents demethylation of Lys-5 (H3K4me) by LSD1/KDM1A. At centromeres, specifically phosphorylated at Thr-12 (H3T11ph) from prophase to early anaphase, by DAPK3 and PKN1. Phosphorylation at Thr-12 (H3T11ph) by PKN1 is a specific tag for epigenetic transcriptional activation that promotes demethylation of Lys-10 (H3K9me) by KDM4C/JMJD2C. Phosphorylation at Tyr-42 (H3Y41ph) by JAK2 promotes exclusion of CBX5 (HP1 alpha) from chromatin (By similarity).By similarity
Ubiquitinated.By similarity
Lysine deamination at Lys-5 (H3K4all) to form allysine is mediated by LOXL2. Allysine formation by LOXL2 only takes place on H3K4me3 and results in gene repression (By similarity).By similarity

Keywords - PTMi

Acetylation, Citrullination, Methylation, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiQ16695.
PaxDbiQ16695.
PRIDEiQ16695.

PTM databases

PhosphoSiteiQ16695.

Expressioni

Tissue specificityi

Expressed in testicular cells.

Developmental stagei

Expressed during S phase, then expression strongly decreases as cell division slows down during the process of differentiation.

Gene expression databases

BgeeiQ16695.
CleanExiHS_HIST3H3.
GenevestigatoriQ16695.

Organism-specific databases

HPAiCAB001386.
CAB003812.

Interactioni

Subunit structurei

The nucleosome is a histone octamer containing two molecules each of H2A, H2B, H3 and H4 assembled in one H3-H4 heterotetramer and two H2A-H2B heterodimers. The octamer wraps approximately 147 bp of DNA.

Binary interactionsi

WithEntry#Exp.IntActNotes
H2AFXP1610411EBI-358900,EBI-494830
KDM1AO603412EBI-358900,EBI-710124
KDM4AO751646EBI-358900,EBI-936709
SFMBT1Q9UHJ34EBI-358900,EBI-747398

Protein-protein interaction databases

BioGridi113895. 149 interactions.
DIPiDIP-922N.
IntActiQ16695. 19 interactions.
MINTiMINT-1155005.
STRINGi9606.ENSP00000355657.

Structurei

Secondary structure

1
136
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi3 – 53Combined sources
Helixi46 – 5712Combined sources
Helixi65 – 7612Combined sources
Turni77 – 793Combined sources
Beta strandi80 – 823Combined sources
Helixi87 – 11428Combined sources
Beta strandi118 – 1203Combined sources
Helixi122 – 13110Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2V1DX-ray3.10C2-22[»]
2YBPX-ray2.02C/D31-42[»]
2YBSX-ray2.32C/D31-42[»]
3A6NX-ray2.70A/E1-136[»]
3T6RX-ray1.95D2-8[»]
ProteinModelPortaliQ16695.
SMRiQ16695. Positions 17-136.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ16695.

Family & Domainsi

Sequence similaritiesi

Belongs to the histone H3 family.Curated

Phylogenomic databases

eggNOGiCOG2036.
GeneTreeiENSGT00760000118967.
HOGENOMiHOG000155290.
HOVERGENiHBG001172.
InParanoidiQ16695.
KOiK11253.
OMAiNEIWRKK.
OrthoDBiEOG7HB5C2.
PhylomeDBiQ16695.
TreeFamiTF314241.

Family and domain databases

Gene3Di1.10.20.10. 1 hit.
InterProiIPR009072. Histone-fold.
IPR007125. Histone_core_D.
IPR000164. Histone_H3/CENP-A.
[Graphical view]
PANTHERiPTHR11426. PTHR11426. 1 hit.
PfamiPF00125. Histone. 1 hit.
[Graphical view]
PRINTSiPR00622. HISTONEH3.
SMARTiSM00428. H3. 1 hit.
[Graphical view]
SUPFAMiSSF47113. SSF47113. 1 hit.
PROSITEiPS00322. HISTONE_H3_1. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

Q16695-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MARTKQTARK STGGKAPRKQ LATKVARKSA PATGGVKKPH RYRPGTVALR
60 70 80 90 100
EIRRYQKSTE LLIRKLPFQR LMREIAQDFK TDLRFQSSAV MALQEACESY
110 120 130
LVGLFEDTNL CVIHAKRVTI MPKDIQLARR IRGERA
Length:136
Mass (Da):15,508
Last modified:January 23, 2007 - v3
Checksum:i37375A2C3A377B2B
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z49861 Genomic DNA. Translation: CAA90020.1.
AF531308 Genomic DNA. Translation: AAN39284.1.
CR542013 mRNA. Translation: CAG46810.1.
AK312217 mRNA. Translation: BAG35150.1.
AL139288 Genomic DNA. Translation: CAI23333.1.
CH471098 Genomic DNA. Translation: EAW69877.1.
BC069079 mRNA. Translation: AAH69079.1.
BC101837 mRNA. Translation: AAI01838.1.
BC101839 mRNA. Translation: AAI01840.1.
CCDSiCCDS1572.1.
PIRiS57473.
RefSeqiNP_003484.1. NM_003493.2.
UniGeneiHs.248171.

Genome annotation databases

EnsembliENST00000366696; ENSP00000355657; ENSG00000168148.
GeneIDi8290.
KEGGihsa:8290.
UCSCiuc001hsx.1. human.

Polymorphism databases

DMDMi18202512.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z49861 Genomic DNA. Translation: CAA90020.1 .
AF531308 Genomic DNA. Translation: AAN39284.1 .
CR542013 mRNA. Translation: CAG46810.1 .
AK312217 mRNA. Translation: BAG35150.1 .
AL139288 Genomic DNA. Translation: CAI23333.1 .
CH471098 Genomic DNA. Translation: EAW69877.1 .
BC069079 mRNA. Translation: AAH69079.1 .
BC101837 mRNA. Translation: AAI01838.1 .
BC101839 mRNA. Translation: AAI01840.1 .
CCDSi CCDS1572.1.
PIRi S57473.
RefSeqi NP_003484.1. NM_003493.2.
UniGenei Hs.248171.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2V1D X-ray 3.10 C 2-22 [» ]
2YBP X-ray 2.02 C/D 31-42 [» ]
2YBS X-ray 2.32 C/D 31-42 [» ]
3A6N X-ray 2.70 A/E 1-136 [» ]
3T6R X-ray 1.95 D 2-8 [» ]
ProteinModelPortali Q16695.
SMRi Q16695. Positions 17-136.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 113895. 149 interactions.
DIPi DIP-922N.
IntActi Q16695. 19 interactions.
MINTi MINT-1155005.
STRINGi 9606.ENSP00000355657.

PTM databases

PhosphoSitei Q16695.

Polymorphism databases

DMDMi 18202512.

Proteomic databases

MaxQBi Q16695.
PaxDbi Q16695.
PRIDEi Q16695.

Protocols and materials databases

DNASUi 8290.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000366696 ; ENSP00000355657 ; ENSG00000168148 .
GeneIDi 8290.
KEGGi hsa:8290.
UCSCi uc001hsx.1. human.

Organism-specific databases

CTDi 8290.
GeneCardsi GC01M228612.
HGNCi HGNC:4778. HIST3H3.
HPAi CAB001386.
CAB003812.
MIMi 602820. gene.
neXtProti NX_Q16695.
PharmGKBi PA29153.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG2036.
GeneTreei ENSGT00760000118967.
HOGENOMi HOG000155290.
HOVERGENi HBG001172.
InParanoidi Q16695.
KOi K11253.
OMAi NEIWRKK.
OrthoDBi EOG7HB5C2.
PhylomeDBi Q16695.
TreeFami TF314241.

Enzyme and pathway databases

Reactomei REACT_169185. DNA Damage/Telomere Stress Induced Senescence.
REACT_172744. Condensation of Prophase Chromosomes.
REACT_200753. formation of the beta-catenin:TCF transactivating complex.
REACT_27271. Meiotic recombination.
REACT_75792. Meiotic synapsis.
REACT_7963. Packaging Of Telomere Ends.

Miscellaneous databases

EvolutionaryTracei Q16695.
GeneWikii HIST3H3.
GenomeRNAii 8290.
NextBioi 31067.
PROi Q16695.
SOURCEi Search...

Gene expression databases

Bgeei Q16695.
CleanExi HS_HIST3H3.
Genevestigatori Q16695.

Family and domain databases

Gene3Di 1.10.20.10. 1 hit.
InterProi IPR009072. Histone-fold.
IPR007125. Histone_core_D.
IPR000164. Histone_H3/CENP-A.
[Graphical view ]
PANTHERi PTHR11426. PTHR11426. 1 hit.
Pfami PF00125. Histone. 1 hit.
[Graphical view ]
PRINTSi PR00622. HISTONEH3.
SMARTi SM00428. H3. 1 hit.
[Graphical view ]
SUPFAMi SSF47113. SSF47113. 1 hit.
PROSITEi PS00322. HISTONE_H3_1. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "A solitary human H3 histone gene on chromosome 1."
    Albig W., Ebentheuer J., Klobeck H., Kunz J., Doenecke D.
    Hum. Genet. 97:486-491(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "The human and mouse replication-dependent histone genes."
    Marzluff W.F., Gongidi P., Woods K.R., Jin J., Maltais L.J.
    Genomics 80:487-498(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  3. "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].
  4. "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: Testis.
  5. "The DNA sequence and biological annotation of human chromosome 1."
    Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
    , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
    Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  7. "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: Lung and Placenta.
  8. "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-29, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  9. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
    Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
    Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-19 AND LYS-24, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  10. "Quantitative interaction proteomics and genome-wide profiling of epigenetic histone marks and their readers."
    Vermeulen M., Eberl H.C., Matarese F., Marks H., Denissov S., Butter F., Lee K.K., Olsen J.V., Hyman A.A., Stunnenberg H.G., Mann M.
    Cell 142:967-980(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT SER-58 AND THR-81.

Entry informationi

Entry nameiH31T_HUMAN
AccessioniPrimary (citable) accession number: Q16695
Secondary accession number(s): B2R5K3, Q6FGU4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 26, 2001
Last sequence update: January 23, 2007
Last modified: November 26, 2014
This is version 144 of the entry and version 3 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, Reference proteome

Documents

  1. Human chromosome 1
    Human chromosome 1: 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