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Protein

Keratin, type I cytoskeletal 10

Gene

KRT10

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

Functioni

GO - Molecular functioni

  • structural constituent of epidermis Source: UniProtKB

GO - Biological processi

  • keratinocyte differentiation Source: UniProtKB
Complete GO annotation...

Enzyme and pathway databases

BioCyciZFISH:ENSG00000171440-MONOMER.
ReactomeiR-HSA-6805567. Keratinization.
R-HSA-6809371. Formation of the cornified envelope.

Names & Taxonomyi

Protein namesi
Recommended name:
Keratin, type I cytoskeletal 10
Alternative name(s):
Cytokeratin-10
Short name:
CK-10
Keratin-10
Short name:
K10
Gene namesi
Name:KRT10
Synonyms:KPP
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 17

Organism-specific databases

HGNCiHGNC:6413. KRT10.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: UniProtKB
  • extracellular exosome Source: UniProtKB
  • extracellular space Source: UniProtKB
  • intermediate filament Source: UniProtKB
  • membrane Source: UniProtKB
  • nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Intermediate filament, Keratin

Pathology & Biotechi

Involvement in diseasei

Epidermolytic hyperkeratosis (EHK)9 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionAn autosomal dominant skin disorder characterized by widespread blistering and an ichthyotic erythroderma at birth that persist into adulthood. Histologically there is a diffuse epidermolytic degeneration in the lower spinous layer of the epidermis. Within a few weeks from birth, erythroderma and blister formation diminish and hyperkeratoses develop.
See also OMIM:113800
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_010506150M → R in EHK. 2 PublicationsCorresponds to variant rs58901407dbSNPEnsembl.1
Natural variantiVAR_010507150M → T in EHK; also found in a patient with hyperkeratotic epidermal nevi due to genetic mosaicism. 2 PublicationsCorresponds to variant rs58901407dbSNPEnsembl.1
Natural variantiVAR_003826154N → H in EHK. 1 PublicationCorresponds to variant rs57784225dbSNPEnsembl.1
Natural variantiVAR_003828156R → C in EHK. 4 PublicationsCorresponds to variant rs58852768dbSNPEnsembl.1
Natural variantiVAR_003827156R → H in EHK. 5 PublicationsCorresponds to variant rs58075662dbSNPEnsembl.1
Natural variantiVAR_003829156R → P in EHK. 1 PublicationCorresponds to variant rs58075662dbSNPEnsembl.1
Natural variantiVAR_003830156R → S in EHK. 1 PublicationCorresponds to variant rs58852768dbSNPEnsembl.1
Natural variantiVAR_003831160Y → D in EHK; severe phenotype. 1 PublicationCorresponds to variant rs58414354dbSNPEnsembl.1
Natural variantiVAR_010508160Y → N in EHK; severe phenotype. 1 Publication1
Natural variantiVAR_010509160Y → S in EHK; severe phenotype. 1 PublicationCorresponds to variant rs58735429dbSNPEnsembl.1
Natural variantiVAR_003832161L → S in EHK. 1 PublicationCorresponds to variant rs60118264dbSNPEnsembl.1
Natural variantiVAR_010510439K → E in EHK; mild phenotype. 1 PublicationCorresponds to variant rs61434181dbSNPEnsembl.1
Natural variantiVAR_003833442L → Q in EHK. 1 PublicationCorresponds to variant rs58026994dbSNPEnsembl.1
Natural variantiVAR_071985449Y → C in EHK. 1 PublicationCorresponds to variant rs267607383dbSNPEnsembl.1
Ichthyosis annular epidermolytic (AEI)2 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA skin disorder resembling bullous congenital ichthyosiform erythroderma. Affected individuals present with bullous ichthyosis in early childhood and hyperkeratotic lichenified plaques in the flexural areas and extensor surfaces at later ages. The feature that distinguishes AEI from BCIE is dramatic episodes of flares of annular polycyclic plaques with scale, which coalesce to involve most of the body surface and can persist for several weeks or even months.
See also OMIM:607602
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_033145422R → E in AEI; requires 2 nucleotide substitutions. 1 PublicationCorresponds to variant rs59075499dbSNPEnsembl.1
Natural variantiVAR_010511446I → T in AEI. 1 PublicationCorresponds to variant rs62651994dbSNPEnsembl.1
Erythroderma, ichthyosiform, congenital reticular (CRIE)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA rare skin condition characterized by slowly enlarging islands of normal skin surrounded by erythematous ichthyotic patches in a reticulated pattern. The condition starts in infancy as a lamellar ichthyosis, with small islands of normal skin resembling confetti appearing in late childhood and at puberty. Histopathologic findings include band-like parakeratosis, psoriasiform acanthosis, and vacuolization of keratinocytes with binucleated cells in the upper epidermis, sometimes associated with amyloid deposition in the dermis. Ultrastructural abnormalities include perinuclear shells formed from a network of fine filaments in the upper epidermis.
See also OMIM:609165

Keywords - Diseasei

Disease mutation, Ichthyosis

Organism-specific databases

DisGeNETi3858.
MalaCardsiKRT10.
MIMi113800. phenotype.
607602. phenotype.
609165. phenotype.
OpenTargetsiENSG00000186395.
Orphaneti281139. Annular epidermolytic ichthyosis.
281190. Congenital reticular ichthyosiform erythroderma.
312. Epidermolytic ichthyosis.
PharmGKBiPA30200.

Polymorphism and mutation databases

BioMutaiKRT10.
DMDMi269849769.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000636421 – 584Keratin, type I cytoskeletal 10Add BLAST584

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei14PhosphoserineCombined sources1
Modified residuei16PhosphoserineCombined sources1
Modified residuei42PhosphoserineCombined sources1
Modified residuei53PhosphoserineCombined sources1
Modified residuei56PhosphoserineCombined sources1
Modified residuei170PhosphoserineCombined sources1

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiP13645.
PaxDbiP13645.
PeptideAtlasiP13645.
PRIDEiP13645.
TopDownProteomicsiP13645.

2D gel databases

REPRODUCTION-2DPAGEP13645.
SWISS-2DPAGEP13645.

PTM databases

iPTMnetiP13645.
PhosphoSitePlusiP13645.
SwissPalmiP13645.

Expressioni

Tissue specificityi

Seen in all suprabasal cell layers including stratum corneum.

Gene expression databases

BgeeiENSG00000186395.
CleanExiHS_KRT10.
GenevisibleiP13645. HS.

Organism-specific databases

HPAiCAB000132.
HPA012014.

Interactioni

Subunit structurei

Heterotetramer of two type I and two type II keratins. keratin-10 is generally associated with keratin-1.

Protein-protein interaction databases

BioGridi110056. 59 interactors.
IntActiP13645. 19 interactors.
MINTiMINT-1132575.
STRINGi9606.ENSP00000269576.

Structurei

Secondary structure

1584
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi348 – 455Combined sources108
Beta strandi479 – 481Combined sources3
Beta strandi483 – 486Combined sources4
Beta strandi500 – 508Combined sources9

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3ASWX-ray2.60B473-487[»]
4F1ZX-ray2.30Q499-512[»]
4ZRYX-ray3.30A337-456[»]
ProteinModelPortaliP13645.
SMRiP13645.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni1 – 145HeadAdd BLAST145
Regioni146 – 456RodAdd BLAST311
Regioni146 – 181Coil 1AAdd BLAST36
Regioni182 – 202Linker 1Add BLAST21
Regioni203 – 294Coil 1BAdd BLAST92
Regioni295 – 317Linker 12Add BLAST23
Regioni318 – 456Coil 2Add BLAST139
Regioni457 – 584TailAdd BLAST128

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi17 – 575Gly-richAdd BLAST559
Compositional biasi477 – 579Ser-richAdd BLAST103

Sequence similaritiesi

Belongs to the intermediate filament family.Curated

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiENOG410IGJX. Eukaryota.
ENOG410YDXS. LUCA.
GeneTreeiENSGT00760000118808.
HOGENOMiHOG000230975.
HOVERGENiHBG013015.
InParanoidiP13645.
KOiK07604.
OMAiHGNSHQG.
OrthoDBiEOG091G087I.
PhylomeDBiP13645.
TreeFamiTF332742.

Family and domain databases

InterProiIPR001664. IF.
IPR018039. Intermediate_filament_CS.
IPR002957. Keratin_I.
IPR009053. Prefoldin.
[Graphical view]
PANTHERiPTHR23239. PTHR23239. 1 hit.
PfamiPF00038. Filament. 1 hit.
[Graphical view]
PRINTSiPR01248. TYPE1KERATIN.
SMARTiSM01391. Filament. 1 hit.
[Graphical view]
SUPFAMiSSF46579. SSF46579. 1 hit.
PROSITEiPS00226. IF. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P13645-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSVRYSSSKH YSSSRSGGGG GGGGCGGGGG VSSLRISSSK GSLGGGFSSG
60 70 80 90 100
GFSGGSFSRG SSGGGCFGGS SGGYGGLGGF GGGSFRGSYG SSSFGGSYGG
110 120 130 140 150
IFGGGSFGGG SFGGGSFGGG GFGGGGFGGG FGGGFGGDGG LLSGNEKVTM
160 170 180 190 200
QNLNDRLASY LDKVRALEES NYELEGKIKE WYEKHGNSHQ GEPRDYSKYY
210 220 230 240 250
KTIDDLKNQI LNLTTDNANI LLQIDNARLA ADDFRLKYEN EVALRQSVEA
260 270 280 290 300
DINGLRRVLD ELTLTKADLE MQIESLTEEL AYLKKNHEEE MKDLRNVSTG
310 320 330 340 350
DVNVEMNAAP GVDLTQLLNN MRSQYEQLAE QNRKDAEAWF NEKSKELTTE
360 370 380 390 400
IDNNIEQISS YKSEITELRR NVQALEIELQ SQLALKQSLE ASLAETEGRY
410 420 430 440 450
CVQLSQIQAQ ISALEEQLQQ IRAETECQNT EYQQLLDIKI RLENEIQTYR
460 470 480 490 500
SLLEGEGSSG GGGRGGGSFG GGYGGGSSGG GSSGGGHGGG HGGSSGGGYG
510 520 530 540 550
GGSSGGGSSG GGYGGGSSSG GHGGSSSGGY GGGSSGGGGG GYGGGSSGGG
560 570 580
SSSGGGYGGG SSSGGHKSSS SGSVGESSSK GPRY
Length:584
Mass (Da):58,827
Last modified:November 24, 2009 - v6
Checksum:i4941ECD2AE46D417
GO

Sequence cautioni

The sequence AAA59468 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti9 – 11KHY → SKQF in AAA60544 (PubMed:2459124).Curated3
Sequence conflicti24 – 31Missing in AAA60544 (PubMed:2459124).Curated8
Sequence conflicti86R → H in CAA32649 (PubMed:2464696).Curated1
Sequence conflicti106S → N in CAA32649 (PubMed:2464696).Curated1
Sequence conflicti181 – 184WYEK → RYDQ in AAA60544 (PubMed:2459124).Curated4
Sequence conflicti189H → R in AAA60544 (PubMed:2459124).Curated1
Sequence conflicti197S → G in AAA59199 (PubMed:1378806).Curated1
Sequence conflicti266K → Q in AAA60544 (PubMed:2459124).Curated1
Sequence conflicti279 – 280EL → YV in AAA59468 (PubMed:2448602).Curated2
Sequence conflicti287H → R in AAA60544 (PubMed:2459124).Curated1
Sequence conflicti293D → H in AAA60544 (PubMed:2459124).Curated1
Sequence conflicti312V → I in AAA59468 (PubMed:2448602).Curated1
Sequence conflicti323S → N in AAA60544 (PubMed:2459124).Curated1
Sequence conflicti340F → V in AAA59468 (PubMed:2448602).Curated1
Sequence conflicti374A → R in AAA59468 (PubMed:2448602).Curated1
Sequence conflicti408Q → H in CAA32649 (PubMed:2464696).Curated1
Sequence conflicti420Q → E in AAA60544 (PubMed:2459124).Curated1
Sequence conflicti436L → T in AAA60544 (PubMed:2459124).Curated1
Sequence conflicti451S → G in AAA59199 (PubMed:1378806).Curated1
Sequence conflicti460 – 461GG → RS in AAA59468 (PubMed:2448602).Curated2
Sequence conflicti477S → T in AAA59468 (PubMed:2448602).Curated1
Sequence conflicti482S → T in AAA59468 (PubMed:2448602).Curated1
Sequence conflicti487 – 490Missing in AAA59199 (PubMed:1378806).Curated4
Sequence conflicti491 – 516Missing in AAA60544 (PubMed:2459124).CuratedAdd BLAST26
Sequence conflicti503S → T in AAA59468 (PubMed:2448602).Curated1
Sequence conflicti508S → T in AAA59468 (PubMed:2448602).Curated1
Sequence conflicti513 – 519YGGGSSS → LRGELH in AAA59468 (PubMed:2448602).Curated7
Sequence conflicti523 – 527GGSSS → AHST in AAA59468 (PubMed:2448602).Curated5
Sequence conflicti524G → GGSSSGGHGG in CAA32649 (PubMed:2464696).Curated1
Sequence conflicti534S → N in AAA59468 (PubMed:2448602).Curated1
Sequence conflicti535S → F in AAA60544 (PubMed:2459124).Curated1
Sequence conflicti542 – 546YGGGS → LRGRH in AAA59468 (PubMed:2448602).Curated5
Sequence conflicti565G → GGYGGGSSSGG in AAA60544 (PubMed:2459124).Curated1

Polymorphismi

A number of alleles are known that mainly differ in the Gly-rich region (positions 490-560).

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_058202101I → S.2 PublicationsCorresponds to variant rs4261597dbSNPEnsembl.1
Natural variantiVAR_010505126G → S.2 PublicationsCorresponds to variant rs77919366dbSNPEnsembl.1
Natural variantiVAR_010506150M → R in EHK. 2 PublicationsCorresponds to variant rs58901407dbSNPEnsembl.1
Natural variantiVAR_010507150M → T in EHK; also found in a patient with hyperkeratotic epidermal nevi due to genetic mosaicism. 2 PublicationsCorresponds to variant rs58901407dbSNPEnsembl.1
Natural variantiVAR_003826154N → H in EHK. 1 PublicationCorresponds to variant rs57784225dbSNPEnsembl.1
Natural variantiVAR_003828156R → C in EHK. 4 PublicationsCorresponds to variant rs58852768dbSNPEnsembl.1
Natural variantiVAR_003827156R → H in EHK. 5 PublicationsCorresponds to variant rs58075662dbSNPEnsembl.1
Natural variantiVAR_003829156R → P in EHK. 1 PublicationCorresponds to variant rs58075662dbSNPEnsembl.1
Natural variantiVAR_003830156R → S in EHK. 1 PublicationCorresponds to variant rs58852768dbSNPEnsembl.1
Natural variantiVAR_003831160Y → D in EHK; severe phenotype. 1 PublicationCorresponds to variant rs58414354dbSNPEnsembl.1
Natural variantiVAR_010508160Y → N in EHK; severe phenotype. 1 Publication1
Natural variantiVAR_010509160Y → S in EHK; severe phenotype. 1 PublicationCorresponds to variant rs58735429dbSNPEnsembl.1
Natural variantiVAR_003832161L → S in EHK. 1 PublicationCorresponds to variant rs60118264dbSNPEnsembl.1
Natural variantiVAR_033145422R → E in AEI; requires 2 nucleotide substitutions. 1 PublicationCorresponds to variant rs59075499dbSNPEnsembl.1
Natural variantiVAR_010510439K → E in EHK; mild phenotype. 1 PublicationCorresponds to variant rs61434181dbSNPEnsembl.1
Natural variantiVAR_003833442L → Q in EHK. 1 PublicationCorresponds to variant rs58026994dbSNPEnsembl.1
Natural variantiVAR_010511446I → T in AEI. 1 PublicationCorresponds to variant rs62651994dbSNPEnsembl.1
Natural variantiVAR_071985449Y → C in EHK. 1 PublicationCorresponds to variant rs267607383dbSNPEnsembl.1
Natural variantiVAR_060723487H → Y.4 PublicationsCorresponds to variant rs17855579dbSNPEnsembl.1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J04029 mRNA. Translation: AAA60544.1.
X14487 Genomic DNA. Translation: CAA32649.1.
AC090283 mRNA. No translation available.
BC034697 mRNA. Translation: AAH34697.1.
M19156 mRNA. Translation: AAA59468.1. Different initiation.
L20218 Genomic DNA. Translation: AAB59438.1.
L20219 Genomic DNA. Translation: AAB59439.1.
M77663 mRNA. Translation: AAA59199.1.
CCDSiCCDS11377.1.
PIRiA31994.
S02158. KRHU0.
RefSeqiNP_000412.3. NM_000421.3.
UniGeneiHs.99936.

Genome annotation databases

EnsembliENST00000269576; ENSP00000269576; ENSG00000186395.
GeneIDi3858.
KEGGihsa:3858.
UCSCiuc002hvi.4. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Web resourcesi

Human Intermediate Filament Mutation Database
Wikipedia

Keratin-10 entry

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J04029 mRNA. Translation: AAA60544.1.
X14487 Genomic DNA. Translation: CAA32649.1.
AC090283 mRNA. No translation available.
BC034697 mRNA. Translation: AAH34697.1.
M19156 mRNA. Translation: AAA59468.1. Different initiation.
L20218 Genomic DNA. Translation: AAB59438.1.
L20219 Genomic DNA. Translation: AAB59439.1.
M77663 mRNA. Translation: AAA59199.1.
CCDSiCCDS11377.1.
PIRiA31994.
S02158. KRHU0.
RefSeqiNP_000412.3. NM_000421.3.
UniGeneiHs.99936.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3ASWX-ray2.60B473-487[»]
4F1ZX-ray2.30Q499-512[»]
4ZRYX-ray3.30A337-456[»]
ProteinModelPortaliP13645.
SMRiP13645.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi110056. 59 interactors.
IntActiP13645. 19 interactors.
MINTiMINT-1132575.
STRINGi9606.ENSP00000269576.

PTM databases

iPTMnetiP13645.
PhosphoSitePlusiP13645.
SwissPalmiP13645.

Polymorphism and mutation databases

BioMutaiKRT10.
DMDMi269849769.

2D gel databases

REPRODUCTION-2DPAGEP13645.
SWISS-2DPAGEP13645.

Proteomic databases

EPDiP13645.
PaxDbiP13645.
PeptideAtlasiP13645.
PRIDEiP13645.
TopDownProteomicsiP13645.

Protocols and materials databases

DNASUi3858.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000269576; ENSP00000269576; ENSG00000186395.
GeneIDi3858.
KEGGihsa:3858.
UCSCiuc002hvi.4. human.

Organism-specific databases

CTDi3858.
DisGeNETi3858.
GeneCardsiKRT10.
HGNCiHGNC:6413. KRT10.
HPAiCAB000132.
HPA012014.
MalaCardsiKRT10.
MIMi113800. phenotype.
148080. gene.
607602. phenotype.
609165. phenotype.
neXtProtiNX_P13645.
OpenTargetsiENSG00000186395.
Orphaneti281139. Annular epidermolytic ichthyosis.
281190. Congenital reticular ichthyosiform erythroderma.
312. Epidermolytic ichthyosis.
PharmGKBiPA30200.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiENOG410IGJX. Eukaryota.
ENOG410YDXS. LUCA.
GeneTreeiENSGT00760000118808.
HOGENOMiHOG000230975.
HOVERGENiHBG013015.
InParanoidiP13645.
KOiK07604.
OMAiHGNSHQG.
OrthoDBiEOG091G087I.
PhylomeDBiP13645.
TreeFamiTF332742.

Enzyme and pathway databases

BioCyciZFISH:ENSG00000171440-MONOMER.
ReactomeiR-HSA-6805567. Keratinization.
R-HSA-6809371. Formation of the cornified envelope.

Miscellaneous databases

ChiTaRSiKRT10. human.
GeneWikiiKeratin_10.
GenomeRNAii3858.
PROiP13645.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000186395.
CleanExiHS_KRT10.
GenevisibleiP13645. HS.

Family and domain databases

InterProiIPR001664. IF.
IPR018039. Intermediate_filament_CS.
IPR002957. Keratin_I.
IPR009053. Prefoldin.
[Graphical view]
PANTHERiPTHR23239. PTHR23239. 1 hit.
PfamiPF00038. Filament. 1 hit.
[Graphical view]
PRINTSiPR01248. TYPE1KERATIN.
SMARTiSM01391. Filament. 1 hit.
[Graphical view]
SUPFAMiSSF46579. SSF46579. 1 hit.
PROSITEiPS00226. IF. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiK1C10_HUMAN
AccessioniPrimary (citable) accession number: P13645
Secondary accession number(s): Q14664, Q8N175
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 1, 1990
Last sequence update: November 24, 2009
Last modified: November 30, 2016
This is version 181 of the entry and version 6 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

There are two types of cytoskeletal and microfibrillar keratin: I (acidic; 40-55 kDa) and II (neutral to basic; 56-70 kDa).

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 17
    Human chromosome 17: 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

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 one 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.