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Protein

Histone H1.4

Gene

HIST1H1E

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: 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).By similarity

GO - Molecular functioni

  • chromatin DNA binding Source: UniProtKB
  • poly(A) RNA binding Source: UniProtKB

GO - Biological processi

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 H1.4
Alternative name(s):
Histone H1b
Histone H1s-4
Gene namesi
Name:HIST1H1E
Synonyms:H1F4
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 6

Organism-specific databases

HGNCiHGNC:4718. HIST1H1E.

Subcellular locationi

  • Nucleus
  • Chromosome

  • Note: Mainly localizes in heterochromatin. Dysplays a punctuate staining pattern in the nucleus.

GO - Cellular componenti

  • extracellular exosome Source: UniProtKB
  • nuclear heterochromatin Source: UniProtKB
  • nucleosome Source: InterPro
  • nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Chromosome, Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA29096.

Polymorphism and mutation databases

BioMutaiHIST1H1E.
DMDMi121919.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed6 Publications
Chaini2 – 219218Histone H1.4PRO_0000195908Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserine5 Publications
Modified residuei2 – 21PhosphoserineBy similarity
Modified residuei17 – 171N6-acetyllysineBy similarity
Modified residuei18 – 181Phosphothreonine6 Publications
Modified residuei26 – 261N6-acetyllysine; alternate1 Publication
Modified residuei26 – 261N6-methyllysine; alternate1 Publication
Modified residuei34 – 341N6-methyllysine; alternateBy similarity
Modified residuei34 – 341N6-succinyllysine; alternateBy similarity
Modified residuei36 – 361PhosphoserineBy similarity
Modified residuei46 – 461N6-acetyllysineBy similarity
Modified residuei54 – 541CitrullineBy similarity
Modified residuei75 – 751N6-acetyllysineBy similarity
Modified residuei90 – 901N6-acetyllysineBy similarity
Modified residuei97 – 971N6-succinyllysineBy similarity
Modified residuei104 – 1041PhosphoserineBy similarity
Modified residuei146 – 1461Phosphothreonine1 Publication
Modified residuei154 – 1541PhosphothreonineBy similarity
Modified residuei168 – 1681N6-acetyllysineBy similarity
Modified residuei172 – 1721PhosphoserineBy similarity
Modified residuei186 – 1861N6-methyllysineBy similarity
Modified residuei187 – 1871Phosphoserine3 Publications

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
Acetylated at Lys-26. Deacetylated at Lys-26 by SIRT1.1 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, Methylation, Phosphoprotein

Proteomic databases

MaxQBiP10412.
PeptideAtlasiP10412.
PRIDEiP10412.

PTM databases

PhosphoSiteiP10412.

Expressioni

Gene expression databases

BgeeiP10412.
CleanExiHS_HIST1H1E.
ExpressionAtlasiP10412. baseline and differential.
GenevestigatoriP10412.

Organism-specific databases

HPAiCAB011506.
HPA055907.

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
L3MBTL1Q9Y4687EBI-358163,EBI-1265089
NCK1P163332EBI-358163,EBI-389883

Protein-protein interaction databases

BioGridi109263. 112 interactions.
IntActiP10412. 15 interactions.
MINTiMINT-1136873.
STRINGi9606.ENSP00000307705.

Structurei

Secondary structure

1
219
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi20 – 256Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3TZDX-ray1.81T19-36[»]
ProteinModelPortaliP10412.
SMRiP10412. Positions 36-109.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini36 – 10974H15PROSITE-ProRule annotationAdd
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.PROSITE-ProRule annotation
Contains 1 H15 (linker histone H1/H5 globular) domain.PROSITE-ProRule annotation

Phylogenomic databases

GeneTreeiENSGT00670000097781.
HOGENOMiHOG000251627.
HOVERGENiHBG009035.
InParanoidiP10412.
KOiK11275.
OrthoDBiEOG74TX2T.
PhylomeDBiP10412.
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.

P10412-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSETAPAAPA APAPAEKTPV KKKARKSAGA AKRKASGPPV SELITKAVAA
60 70 80 90 100
SKERSGVSLA ALKKALAAAG YDVEKNNSRI KLGLKSLVSK GTLVQTKGTG
110 120 130 140 150
ASGSFKLNKK AASGEAKPKA KKAGAAKAKK PAGAAKKPKK ATGAATPKKS
160 170 180 190 200
AKKTPKKAKK PAAAAGAKKA KSPKKAKAAK PKKAPKSPAK AKAVKPKAAK
210
PKTAKPKAAK PKKAAAKKK
Length:219
Mass (Da):21,865
Last modified:January 23, 2007 - v2
Checksum:i1720FECCCBEBCC7F
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti128 – 1281A → V in a colorectal cancer sample; somatic mutation. 1 Publication
VAR_036203
Natural varianti152 – 1521K → R.
Corresponds to variant rs2298090 [ dbSNP | Ensembl ].
VAR_049307

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M60748 Genomic DNA. Translation: AAA63187.1.
AF531302 Genomic DNA. Translation: AAN06702.1.
AL353759 Genomic DNA. Translation: CAC04132.1.
BC096168 mRNA. Translation: AAH96168.1.
BC096169 mRNA. Translation: AAH96169.1.
BC099632 mRNA. Translation: AAH99632.1.
CCDSiCCDS4586.1.
PIRiC40335. HSHU1B.
RefSeqiNP_005312.1. NM_005321.2.
UniGeneiHs.248133.

Genome annotation databases

EnsembliENST00000304218; ENSP00000307705; ENSG00000168298.
GeneIDi3008.
KEGGihsa:3008.
UCSCiuc003ngq.3. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M60748 Genomic DNA. Translation: AAA63187.1.
AF531302 Genomic DNA. Translation: AAN06702.1.
AL353759 Genomic DNA. Translation: CAC04132.1.
BC096168 mRNA. Translation: AAH96168.1.
BC096169 mRNA. Translation: AAH96169.1.
BC099632 mRNA. Translation: AAH99632.1.
CCDSiCCDS4586.1.
PIRiC40335. HSHU1B.
RefSeqiNP_005312.1. NM_005321.2.
UniGeneiHs.248133.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3TZDX-ray1.81T19-36[»]
ProteinModelPortaliP10412.
SMRiP10412. Positions 36-109.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi109263. 112 interactions.
IntActiP10412. 15 interactions.
MINTiMINT-1136873.
STRINGi9606.ENSP00000307705.

PTM databases

PhosphoSiteiP10412.

Polymorphism and mutation databases

BioMutaiHIST1H1E.
DMDMi121919.

Proteomic databases

MaxQBiP10412.
PeptideAtlasiP10412.
PRIDEiP10412.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000304218; ENSP00000307705; ENSG00000168298.
GeneIDi3008.
KEGGihsa:3008.
UCSCiuc003ngq.3. human.

Organism-specific databases

CTDi3008.
GeneCardsiGC06P026156.
HGNCiHGNC:4718. HIST1H1E.
HPAiCAB011506.
HPA055907.
MIMi142220. gene.
neXtProtiNX_P10412.
PharmGKBiPA29096.
GenAtlasiSearch...

Phylogenomic databases

GeneTreeiENSGT00670000097781.
HOGENOMiHOG000251627.
HOVERGENiHBG009035.
InParanoidiP10412.
KOiK11275.
OrthoDBiEOG74TX2T.
PhylomeDBiP10412.
TreeFamiTF313664.

Enzyme and pathway databases

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

Miscellaneous databases

ChiTaRSiHIST1H1E. human.
GeneWikiiHIST1H1E.
GenomeRNAii3008.
NextBioi11928.
PROiP10412.
SOURCEiSearch...

Gene expression databases

BgeeiP10412.
CleanExiHS_HIST1H1E.
ExpressionAtlasiP10412. baseline and differential.
GenevestigatoriP10412.

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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Isolation and characterization of two human H1 histone genes within clusters of core histone genes."
    Albig W., Kardalinou E., Drabent B., Zimmer A., Doenecke D.
    Genomics 10:940-948(1991) [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. "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].
  5. "Human spleen histone H1. Isolation and amino acid sequence of a main variant, H1b."
    Ohe Y., Hayashi H., Iwai K.
    J. Biochem. 100:359-368(1986) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-219, METHYLATION AT LYS-26.
    Tissue: Spleen.
  6. "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.
  7. "Human SirT1 interacts with histone H1 and promotes formation of facultative heterochromatin."
    Vaquero A., Scher M., Lee D., Erdjument-Bromage H., Tempst P., Reinberg D.
    Mol. Cell 16:93-105(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION AT LYS-26.
  8. "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.
  9. "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 THR-18 AND SER-187, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  10. "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 THR-18, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  11. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-18, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  12. "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], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
  13. "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 THR-18; THR-146 AND SER-187, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  14. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  15. "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 THR-18 AND SER-187, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
  16. "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], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
  17. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
  18. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-18, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  19. Cited for: VARIANT [LARGE SCALE ANALYSIS] VAL-128.

Entry informationi

Entry nameiH14_HUMAN
AccessioniPrimary (citable) accession number: P10412
Secondary accession number(s): Q4VB25
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: January 23, 2007
Last modified: May 27, 2015
This is version 150 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

Miscellaneous

This variant accounts for 60% of histone H1.

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

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.