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P16401

- H15_HUMAN

UniProt

P16401 - H15_HUMAN

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Protein
Histone H1.5
Gene
HIST1H1B, H1F5
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. histone deacetylase binding Source: UniProt
  3. poly(A) RNA binding Source: UniProtKB

GO - Biological processi

  1. chromatin organization Source: UniProt
  2. establishment of protein localization to chromatin Source: UniProt
  3. negative regulation of transcription from RNA polymerase II promoter Source: UniProt
  4. nucleosome assembly Source: InterPro
  5. positive regulation of cell growth Source: UniProt
  6. positive regulation of histone H3-K9 methylation Source: UniProt
  7. protein stabilization Source: UniProt
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 H1.5
Alternative name(s):
Histone H1a
Histone H1b
Histone H1s-3
Gene namesi
Synonyms:H1F5
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 6

Organism-specific databases

HGNCiHGNC:4719. HIST1H1B.

Subcellular locationi

Nucleus. Chromosome
Note: According to 1 Publication more commonly found in heterochromatin. According to 1 Publication associates with actively transcribed chromatin and not heterochromatin.3 Publications

GO - Cellular componenti

  1. extracellular vesicular exosome Source: UniProt
  2. nuclear chromatin Source: UniProtKB
  3. nuclear heterochromatin Source: UniProt
  4. nucleosome Source: InterPro
Complete GO annotation...

Keywords - Cellular componenti

Chromosome, Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA29097.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed2 Publications
Chaini2 – 226225Histone H1.5
PRO_0000195909Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserine; partial6 Publications
Modified residuei2 – 21Phosphoserine1 Publication
Modified residuei11 – 111Phosphothreonine; by GSK33 Publications
Modified residuei17 – 171N6-acetyllysine By similarity
Modified residuei18 – 181Phosphoserine5 Publications
Modified residuei27 – 271N6-methyllysine1 Publication
Modified residuei37 – 371N6-succinyllysine By similarity
Modified residuei39 – 391Phosphothreonine1 Publication
Modified residuei49 – 491N6-acetyllysine By similarity
Modified residuei57 – 571Citrulline By similarity
Modified residuei78 – 781N6-acetyllysine By similarity
Modified residuei138 – 1381Phosphothreonine3 Publications
Modified residuei155 – 1551Phosphothreonine1 Publication
Modified residuei168 – 1681N6-acetyllysine1 Publication
Modified residuei173 – 1731Phosphoserine1 Publication
Modified residuei189 – 1891Phosphoserine1 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. Phosphorylated at Thr-11 by GSK3B during mitosis in prometaphase and dephosphorylated in telophase.2 Publications
Citrullination at Arg-57 (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, Methylation, Phosphoprotein

Proteomic databases

MaxQBiP16401.
PaxDbiP16401.
PeptideAtlasiP16401.
PRIDEiP16401.

PTM databases

PhosphoSiteiP16401.

Expressioni

Tissue specificityi

Ubiquitous. Expressed in the majority of the cell lines tested and in testis.1 Publication

Gene expression databases

BgeeiP16401.
CleanExiHS_HIST1H1B.
GenevestigatoriP16401.

Organism-specific databases

HPAiCAB012241.

Interactioni

Protein-protein interaction databases

BioGridi109264. 42 interactions.
IntActiP16401. 4 interactions.
MINTiMINT-3008567.
STRINGi9606.ENSP00000330074.

Structurei

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2FE2model-A2-226[»]
2RHIX-ray1.66B23-27[»]
ProteinModelPortaliP16401.
SMRiP16401. Positions 40-112.

Miscellaneous databases

EvolutionaryTraceiP16401.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini39 – 11274H15
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.
InParanoidiP16401.
KOiK11275.
OMAiTRVAKAK.
OrthoDBiEOG74TX2T.
PhylomeDBiP16401.
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.

P16401-1 [UniParc]FASTAAdd to Basket

« Hide

MSETAPAETA TPAPVEKSPA KKKATKKAAG AGAAKRKATG PPVSELITKA    50
VAASKERNGL SLAALKKALA AGGYDVEKNN SRIKLGLKSL VSKGTLVQTK 100
GTGASGSFKL NKKAASGEAK PKAKKAGAAK AKKPAGATPK KAKKAAGAKK 150
AVKKTPKKAK KPAAAGVKKV AKSPKKAKAA AKPKKATKSP AKPKAVKPKA 200
AKPKAAKPKA AKPKAAKAKK AAAKKK 226
Length:226
Mass (Da):22,580
Last modified:January 23, 2007 - v3
Checksum:i0BA1402101766FDF
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti86 – 861G → D in a colorectal cancer sample; somatic mutation. 1 Publication
VAR_036204
Natural varianti144 – 1441K → R.
Corresponds to variant rs11970638 [ dbSNP | Ensembl ].
VAR_049308
Natural varianti211 – 2111A → T.
Corresponds to variant rs34144478 [ dbSNP | Ensembl ].
VAR_049309

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti216 – 2183Missing AA sequence 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X83509 Genomic DNA. Translation: CAA58498.1.
AF531304 Genomic DNA. Translation: AAN06704.1.
Z98744 Genomic DNA. Translation: CAB11421.1.
BC069101 mRNA. Translation: AAH69101.1.
BC101581 mRNA. Translation: AAI01582.1.
BC101583 mRNA. Translation: AAI01584.1.
CCDSiCCDS4635.1.
PIRiS51660.
RefSeqiNP_005313.1. NM_005322.2.
UniGeneiHs.131956.

Genome annotation databases

EnsembliENST00000331442; ENSP00000330074; ENSG00000184357.
GeneIDi3009.
KEGGihsa:3009.
UCSCiuc003njx.3. human.

Polymorphism databases

DMDMi19856407.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X83509 Genomic DNA. Translation: CAA58498.1 .
AF531304 Genomic DNA. Translation: AAN06704.1 .
Z98744 Genomic DNA. Translation: CAB11421.1 .
BC069101 mRNA. Translation: AAH69101.1 .
BC101581 mRNA. Translation: AAI01582.1 .
BC101583 mRNA. Translation: AAI01584.1 .
CCDSi CCDS4635.1.
PIRi S51660.
RefSeqi NP_005313.1. NM_005322.2.
UniGenei Hs.131956.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2FE2 model - A 2-226 [» ]
2RHI X-ray 1.66 B 23-27 [» ]
ProteinModelPortali P16401.
SMRi P16401. Positions 40-112.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 109264. 42 interactions.
IntActi P16401. 4 interactions.
MINTi MINT-3008567.
STRINGi 9606.ENSP00000330074.

PTM databases

PhosphoSitei P16401.

Polymorphism databases

DMDMi 19856407.

Proteomic databases

MaxQBi P16401.
PaxDbi P16401.
PeptideAtlasi P16401.
PRIDEi P16401.

Protocols and materials databases

DNASUi 3009.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000331442 ; ENSP00000330074 ; ENSG00000184357 .
GeneIDi 3009.
KEGGi hsa:3009.
UCSCi uc003njx.3. human.

Organism-specific databases

CTDi 3009.
GeneCardsi GC06M027835.
HGNCi HGNC:4719. HIST1H1B.
HPAi CAB012241.
MIMi 142711. gene.
neXtProti NX_P16401.
PharmGKBi PA29097.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG258621.
HOGENOMi HOG000251627.
HOVERGENi HBG009035.
InParanoidi P16401.
KOi K11275.
OMAi TRVAKAK.
OrthoDBi EOG74TX2T.
PhylomeDBi P16401.
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

EvolutionaryTracei P16401.
GeneWikii HIST1H1B.
GenomeRNAii 3009.
NextBioi 11932.
PROi P16401.
SOURCEi Search...

Gene expression databases

Bgeei P16401.
CleanExi HS_HIST1H1B.
Genevestigatori P16401.

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. "Characterization of the H1.5 gene completes the set of human H1 subtype genes."
    Albig W., Meergans T., Doenecke D.
    Gene 184:141-148(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], TISSUE SPECIFICITY.
  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. "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].
  4. "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: Liver.
  5. "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 2-226.
    Tissue: Spleen.
  6. Bienvenut W.V., Lilla S., von Kriegsheim A., Lempens A., Kolch W.
    Submitted (DEC-2008) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 2-17; 37-49; 58-78 AND 89-100, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Ovarian carcinoma.
  7. "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.
  8. "Distribution of somatic H1 subtypes is non-random on active vs. inactive chromatin II: distribution in human adult fibroblasts."
    Parseghian M.H., Newcomb R.L., Hamkalo B.A.
    J. Cell. Biochem. 83:643-659(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
  9. "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.
  10. "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.
  11. "Histone H1 phosphorylation occurs site-specifically during interphase and mitosis: identification of a novel phosphorylation site on histone H1."
    Sarg B., Helliger W., Talasz H., Forg B., Lindner H.H.
    J. Biol. Chem. 281:6573-6580(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT THR-11; SER-18; THR-138; THR-155; SER-173 AND SER-189.
  12. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-11; SER-18 AND THR-39, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  13. "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].
  14. "M phase-specific phosphorylation of histone H1.5 at threonine 10 by GSK-3."
    Happel N., Stoldt S., Schmidt B., Doenecke D.
    J. Mol. Biol. 386:339-350(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT THR-11 BY GSK3B.
  15. "Mapping of lysine monomethylation of linker histones in human breast and its cancer."
    Lu A., Zougman A., Pudelko M., Bebenek M., Ziolkowski P., Mann M., Wisniewski J.R.
    J. Proteome Res. 8:4207-4215(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: METHYLATION AT LYS-27.
  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-18, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  17. "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-168, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  18. "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-18 AND THR-138, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  19. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  20. "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; SER-18 AND THR-138, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  21. "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].
  22. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  23. Cited for: VARIANT [LARGE SCALE ANALYSIS] ASP-86.

Entry informationi

Entry nameiH15_HUMAN
AccessioniPrimary (citable) accession number: P16401
Secondary accession number(s): Q14529, Q3MJ42
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1990
Last sequence update: January 23, 2007
Last modified: September 3, 2014
This is version 137 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, 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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi