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P16403

- H12_HUMAN

UniProt

P16403 - H12_HUMAN

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Protein
Histone H1.2
Gene
HIST1H1C, H1F2
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Histone H1 protein binds to linker DNA between nucleosomes forming the macromolecular structure known as the chromatin fiber. Histones H1 are necessary for the condensation of nucleosome chains into higher-order structured fibers. Acts also as a regulator of individual gene transcription through chromatin remodeling, nucleosome spacing and DNA methylation By similarity.

GO - Molecular functioni

  1. chromatin DNA binding Source: UniProt
  2. poly(A) RNA binding Source: UniProtKB
  3. protein binding Source: UniProt
Complete GO annotation...

GO - Biological processi

  1. nucleosome assembly Source: InterPro
  2. nucleosome positioning Source: Ensembl
Complete GO annotation...

Keywords - Ligandi

DNA-binding

Enzyme and pathway databases

ReactomeiREACT_13462. Activation of DNA fragmentation factor.
REACT_169121. Formation of Senescence-Associated Heterochromatin Foci (SAHF).

Names & Taxonomyi

Protein namesi
Recommended name:
Histone H1.2
Alternative name(s):
Histone H1c
Histone H1d
Histone H1s-1
Gene namesi
Synonyms:H1F2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 6

Organism-specific databases

HGNCiHGNC:4716. HIST1H1C.

Subcellular locationi

Nucleus. Chromosome
Note: Mainly localizes in euchromatin. Distribution goes in parallel with DNA concentration.2 Publications

GO - Cellular componenti

  1. nuclear euchromatin Source: UniProt
  2. nucleosome Source: InterPro
  3. nucleus Source: UniProt
Complete GO annotation...

Keywords - Cellular componenti

Chromosome, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi187 – 1871K → R: Abolishes methylation. 1 Publication

Organism-specific databases

PharmGKBiPA29094.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed3 Publications
Chaini2 – 213212Histone H1.2
PRO_0000195906Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserine; partial7 Publications
Modified residuei2 – 21Phosphoserine2 Publications
Modified residuei17 – 171N6-acetyllysine; alternate By similarity
Cross-linki17 – 17Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate
Modified residuei34 – 341N6-crotonyllysine; alternate1 Publication
Modified residuei34 – 341N6-methyllysine; alternate1 Publication
Modified residuei54 – 541Citrulline By similarity
Modified residuei64 – 641N6-crotonyllysine1 Publication
Modified residuei85 – 851N6-crotonyllysine1 Publication
Modified residuei90 – 901N6-crotonyllysine1 Publication
Modified residuei97 – 971N6-crotonyllysine; alternate1 Publication
Modified residuei97 – 971N6-succinyllysine; alternate By similarity
Modified residuei104 – 1041Phosphoserine; by PKC By similarity
Modified residuei146 – 1461Phosphothreonine1 Publication
Modified residuei159 – 1591N6-crotonyllysine1 Publication
Modified residuei168 – 1681N6-crotonyllysine1 Publication
Modified residuei187 – 1871N6-methyllysine; by EHMT1 and EHMT21 Publication
Cross-linki206 – 206Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication

Post-translational modificationi

H1 histones are progressively phosphorylated during the cell cycle, becoming maximally phosphorylated during late G2 phase and M phase, and being dephosphorylated sharply thereafter By similarity.
Crotonylation (Kcr) is specifically present in male germ cells and marks testis-specific genes in post-meiotic cells, including X-linked genes that escape sex chromosome inactivation in haploid cells. Crotonylation marks active promoters and enhancers and confers resistance to transcriptional repressors. It is also associated with post-meiotically activated genes on autosomes.1 Publication
Citrullination at Arg-54 (H1R54ci) by PADI4 takes place within the DNA-binding site of H1 and results in its displacement from chromatin and global chromatin decondensation, thereby promoting pluripotency and stem cell maintenance By similarity.

Keywords - PTMi

Acetylation, Citrullination, Isopeptide bond, Methylation, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiP16403.
PaxDbiP16403.
PeptideAtlasiP16403.
PRIDEiP16403.

PTM databases

PhosphoSiteiP16403.

Expressioni

Gene expression databases

BgeeiP16403.
CleanExiHS_HIST1H1C.
GenevestigatoriP16403.

Organism-specific databases

HPAiCAB011507.

Interactioni

Protein-protein interaction databases

BioGridi109261. 66 interactions.
IntActiP16403. 21 interactions.
MINTiMINT-1149485.
STRINGi9606.ENSP00000339566.

Structurei

3D structure databases

ProteinModelPortaliP16403.
SMRiP16403. Positions 36-109.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini36 – 10974H15
Add
BLAST

Domaini

The C-terminal domain is required for high-affinity binding to chromatin By similarity.

Sequence similaritiesi

Belongs to the histone H1/H5 family.

Phylogenomic databases

eggNOGiNOG258621.
HOGENOMiHOG000251627.
HOVERGENiHBG009035.
InParanoidiP16403.
KOiK11275.
OMAiMSETAPX.
OrthoDBiEOG74TX2T.
PhylomeDBiP16403.
TreeFamiTF313664.

Family and domain databases

Gene3Di1.10.10.10. 1 hit.
InterProiIPR005818. Histone_H1/H5_H15.
IPR005819. Histone_H5.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view]
PfamiPF00538. Linker_histone. 1 hit.
[Graphical view]
PRINTSiPR00624. HISTONEH5.
SMARTiSM00526. H15. 1 hit.
[Graphical view]
PROSITEiPS51504. H15. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P16403-1 [UniParc]FASTAAdd to Basket

« Hide

MSETAPAAPA AAPPAEKAPV KKKAAKKAGG TPRKASGPPV SELITKAVAA    50
SKERSGVSLA ALKKALAAAG YDVEKNNSRI KLGLKSLVSK GTLVQTKGTG 100
ASGSFKLNKK AASGEAKPKV KKAGGTKPKK PVGAAKKPKK AAGGATPKKS 150
AKKTPKKAKK PAAATVTKKV AKSPKKAKVA KPKKAAKSAA KAVKPKAAKP 200
KVVKPKKAAP KKK 213
Length:213
Mass (Da):21,365
Last modified:January 23, 2007 - v2
Checksum:iAA66EA1901D8D56B
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti18 – 181A → V.
Corresponds to variant rs2230653 [ dbSNP | Ensembl ].
VAR_003618
Natural varianti113 – 1131S → A.
Corresponds to variant rs34810376 [ dbSNP | Ensembl ].
VAR_049304
Natural varianti124 – 1241G → A.
Corresponds to variant rs12111009 [ dbSNP | Ensembl ].
VAR_049305

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X57129 Genomic DNA. Translation: CAA40408.1.
AF531300 Genomic DNA. Translation: AAN06700.1.
AK290947 mRNA. Translation: BAF83636.1.
AB451259 mRNA. Translation: BAG70073.1.
AB451385 mRNA. Translation: BAG70199.1.
U91328 Genomic DNA. No translation available.
CH471087 Genomic DNA. Translation: EAW55515.1.
BC002649 mRNA. No translation available.
CCDSiCCDS4577.1.
PIRiS26364. HSHU11.
RefSeqiNP_005310.1. NM_005319.3.
UniGeneiHs.7644.

Genome annotation databases

EnsembliENST00000343677; ENSP00000339566; ENSG00000187837.
GeneIDi3006.
KEGGihsa:3006.
UCSCiuc003nfw.3. human.

Polymorphism databases

DMDMi417101.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X57129 Genomic DNA. Translation: CAA40408.1 .
AF531300 Genomic DNA. Translation: AAN06700.1 .
AK290947 mRNA. Translation: BAF83636.1 .
AB451259 mRNA. Translation: BAG70073.1 .
AB451385 mRNA. Translation: BAG70199.1 .
U91328 Genomic DNA. No translation available.
CH471087 Genomic DNA. Translation: EAW55515.1 .
BC002649 mRNA. No translation available.
CCDSi CCDS4577.1.
PIRi S26364. HSHU11.
RefSeqi NP_005310.1. NM_005319.3.
UniGenei Hs.7644.

3D structure databases

ProteinModelPortali P16403.
SMRi P16403. Positions 36-109.
ModBasei Search...

Protein-protein interaction databases

BioGridi 109261. 66 interactions.
IntActi P16403. 21 interactions.
MINTi MINT-1149485.
STRINGi 9606.ENSP00000339566.

PTM databases

PhosphoSitei P16403.

Polymorphism databases

DMDMi 417101.

Proteomic databases

MaxQBi P16403.
PaxDbi P16403.
PeptideAtlasi P16403.
PRIDEi P16403.

Protocols and materials databases

DNASUi 3006.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000343677 ; ENSP00000339566 ; ENSG00000187837 .
GeneIDi 3006.
KEGGi hsa:3006.
UCSCi uc003nfw.3. human.

Organism-specific databases

CTDi 3006.
GeneCardsi GC06M026055.
HGNCi HGNC:4716. HIST1H1C.
HPAi CAB011507.
MIMi 142710. gene.
neXtProti NX_P16403.
PharmGKBi PA29094.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG258621.
HOGENOMi HOG000251627.
HOVERGENi HBG009035.
InParanoidi P16403.
KOi K11275.
OMAi MSETAPX.
OrthoDBi EOG74TX2T.
PhylomeDBi P16403.
TreeFami TF313664.

Enzyme and pathway databases

Reactomei REACT_13462. Activation of DNA fragmentation factor.
REACT_169121. Formation of Senescence-Associated Heterochromatin Foci (SAHF).

Miscellaneous databases

GeneWikii HIST1H1C.
GenomeRNAii 3006.
NextBioi 11920.
PROi P16403.
SOURCEi Search...

Gene expression databases

Bgeei P16403.
CleanExi HS_HIST1H1C.
Genevestigatori P16403.

Family and domain databases

Gene3Di 1.10.10.10. 1 hit.
InterProi IPR005818. Histone_H1/H5_H15.
IPR005819. Histone_H5.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view ]
Pfami PF00538. Linker_histone. 1 hit.
[Graphical view ]
PRINTSi PR00624. HISTONEH5.
SMARTi SM00526. H15. 1 hit.
[Graphical view ]
PROSITEi PS51504. H15. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Human H1 histones: conserved and varied sequence elements in two H1 subtype genes."
    Eick S., Nicolai M., Mumberg D., Doenecke D.
    Eur. J. Cell Biol. 49:110-115(1989) [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. "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].
  4. "Human protein factory for converting the transcriptome into an in vitro-expressed proteome."
    Goshima N., Kawamura Y., Fukumoto A., Miura A., Honma R., Satoh R., Wakamatsu A., Yamamoto J., Kimura K., Nishikawa T., Andoh T., Iida Y., Ishikawa K., Ito E., Kagawa N., Kaminaga C., Kanehori K., Kawakami B.
    , Kenmochi K., Kimura R., Kobayashi M., Kuroita T., Kuwayama H., Maruyama Y., Matsuo K., Minami K., Mitsubori M., Mori M., Morishita R., Murase A., Nishikawa A., Nishikawa S., Okamoto T., Sakagami N., Sakamoto Y., Sasaki Y., Seki T., Sono S., Sugiyama A., Sumiya T., Takayama T., Takayama Y., Takeda H., Togashi T., Yahata K., Yamada H., Yanagisawa Y., Endo Y., Imamoto F., Kisu Y., Tanaka S., Isogai T., Imai J., Watanabe S., Nomura N.
    Nat. Methods 5:1011-1017(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  5. "The DNA sequence and analysis of human chromosome 6."
    Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D.
    , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.
    Nature 425:805-811(2003) [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: Uterus.
  8. "Human spleen histone H1. Isolation and amino acid sequences of three minor variants, H1a, H1c, and H1d."
    Ohe Y., Hayashi H., Iwai K.
    J. Biochem. 106:844-857(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-213.
    Tissue: Spleen.
  9. Bienvenut W.V., Lilla S., von Kriegsheim A., Lempens A., Kolch W.
    Submitted (DEC-2008) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 2-17; 34-46; 55-75 AND 86-97, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT SER-2, METHYLATION AT LYS-34, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Ovarian carcinoma.
  10. Bienvenut W.V., Waridel P., Quadroni M.
    Submitted (MAR-2009) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 2-17; 34-46; 55-63 AND 65-75, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Cervix carcinoma.
  11. "A proposal for a coherent mammalian histone H1 nomenclature correlated with amino acid sequences."
    Parseghian M.H., Henschen A.H., Krieglstein K.G., Hamkalo B.A.
    Protein Sci. 3:575-587(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NOMENCLATURE.
  12. "The distribution of somatic H1 subtypes is non-random on active vs. inactive chromatin: distribution in human fetal fibroblasts."
    Parseghian M.H., Newcomb R.L., Winokur S.T., Hamkalo B.A.
    Chromosome Res. 8:405-424(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
  13. "H1 family histones in the nucleus. Control of binding and localization by the C-terminal domain."
    Th'ng J.P., Sung R., Ye M., Hendzel M.J.
    J. Biol. Chem. 280:27809-27814(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
  14. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  15. "Tryptic digestion of ubiquitin standards reveals an improved strategy for identifying ubiquitinated proteins by mass spectrometry."
    Denis N.J., Vasilescu J., Lambert J.-P., Smith J.C., Figeys D.
    Proteomics 7:868-874(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-206.
    Tissue: Mammary cancer.
  16. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  17. "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 SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  18. "Histone H1 variant-specific lysine methylation by G9a/KMT1C and Glp1/KMT1D."
    Weiss T., Hergeth S., Zeissler U., Izzo A., Tropberger P., Zee B.M., Dundr M., Garcia B.A., Daujat S., Schneider R.
    Epigenetics Chromatin 3:7-7(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: METHYLATION AT LYS-187 BY EHMT1 AND EHMT2, MUTAGENESIS OF LYS-187, IDENTIFICATION BY MASS SPECTROMETRY.
  19. "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: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2 AND THR-146, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  20. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  21. "Identification of 67 histone marks and histone lysine crotonylation as a new type of histone modification."
    Tan M., Luo H., Lee S., Jin F., Yang J.S., Montellier E., Buchou T., Cheng Z., Rousseaux S., Rajagopal N., Lu Z., Ye Z., Zhu Q., Wysocka J., Ye Y., Khochbin S., Ren B., Zhao Y.
    Cell 146:1016-1028(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: CROTONYLATION AT LYS-34; LYS-64; LYS-85; LYS-90; LYS-97; LYS-159 AND LYS-168.
  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: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2, 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 SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  24. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiH12_HUMAN
AccessioniPrimary (citable) accession number: P16403
Secondary accession number(s): A8K4I2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1990
Last sequence update: January 23, 2007
Last modified: September 3, 2014
This is version 149 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 6
    Human chromosome 6: 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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