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Protein

Keratin, type I cytoskeletal 18

Gene

KRT18

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

Functioni

Involved in the uptake of thrombin-antithrombin complexes by hepatic cells (By similarity). When phosphorylated, plays a role in filament reorganization. Involved in the delivery of mutated CFTR to the plasma membrane. Together with KRT8, is involved in interleukin-6 (IL-6)-mediated barrier protection.By similarity7 Publications

Miscellaneous

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

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei271Stutter1
Sitei331Stutter1

GO - Molecular functioni

GO - Biological processi

Keywordsi

Biological processCell cycle, Host-virus interaction

Enzyme and pathway databases

ReactomeiR-HSA-6805567 Keratinization
R-HSA-6809371 Formation of the cornified envelope
SignaLinkiP05783
SIGNORiP05783

Names & Taxonomyi

Protein namesi
Recommended name:
Keratin, type I cytoskeletal 18
Alternative name(s):
Cell proliferation-inducing gene 46 protein
Cytokeratin-18
Short name:
CK-18
Keratin-18
Short name:
K18
Gene namesi
Name:KRT18
Synonyms:CYK18
ORF Names:PIG46
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 12

Organism-specific databases

EuPathDBiHostDB:ENSG00000111057.10
HGNCiHGNC:6430 KRT18
MIMi148070 gene
neXtProtiNX_P05783

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Cytoplasm, Intermediate filament, Keratin, Nucleus

Pathology & Biotechi

Involvement in diseasei

Cirrhosis (CIRRH)2 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA liver disease characterized by severe panlobular liver-cell swelling with Mallory body formation, prominent pericellular fibrosis, and marked deposits of copper. Clinical features include abdomen swelling, jaundice and pulmonary hypertension.
See also OMIM:215600
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_023054103T → A in CIRRH. 1 PublicationCorresponds to variant dbSNP:rs61136606EnsemblClinVar.1
Natural variantiVAR_003852128H → L in CIRRH; interfers with the ability to form normal filaments. 2 PublicationsCorresponds to variant dbSNP:rs57758506EnsemblClinVar.1
Natural variantiVAR_023056261R → Q in CIRRH. 1 PublicationCorresponds to variant dbSNP:rs57354642EnsemblClinVar.1
Natural variantiVAR_023057340G → R in CIRRH. 1 PublicationCorresponds to variant dbSNP:rs57370769EnsemblClinVar.1

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi2S → A: No effect on phosphorylation; when associated with A-7 and A-10. 1 Publication1
Mutagenesisi7S → A: No effect on phosphorylation; when associated with A-2 and A-10. 1 Publication1
Mutagenesisi10S → A: No effect on phosphorylation; when associated with A-2 and A-7. 1 Publication1
Mutagenesisi15S → A: No effect on phosphorylation; when associated with A-18 and A-23. Abolishes phosphorylation; when associated with A-18; A-34; A-47; A-49; A-51 and A-53. 1 Publication1
Mutagenesisi18S → A: No effect on phosphorylation; when associated with A-15 and A-23. Abolishes phosphorylation; when associated with A-15; A-34; A-47; A-49; A-51 and A-53. 1 Publication1
Mutagenesisi23S → A: No effect on phosphorylation; when associated with A-15 and A-18. 1 Publication1
Mutagenesisi30S → A: No effect on phosphorylation; when associated with A-31 and A-34, or with A-31; A-44 and A-51. Abolishes glycosylation but does not affect binding to YWHAE and YWHAZ; when associated with A-31 and A-49. 2 Publications1
Mutagenesisi31S → A: No effect on phosphorylation; when associated with A-30 and A-34, or with A-30; A-44 and A-51. Abolishes glycosylation but does not affect binding to YWHAE and YWHAZ; when associated with A-30 and A-49. 2 Publications1
Mutagenesisi34S → A: No effect on phosphorylation; when associated with A-30 and A-31. Abolishes phosphorylation; when associated with A-15; A-18; A-47; A-49; A-51 and A-53. Abolishes binding to YWHAE and YWHAZ; and when associated with A-53. 2 Publications1
Mutagenesisi34S → D or E: Abolishes binding to YWHAE and YWHAZ. 2 Publications1
Mutagenesisi42S → A: No effect on phosphorylation; when associated with A-44. 1 Publication1
Mutagenesisi44S → A: No effect on phosphorylation; when associated with A-42, or with A-30; A-31 and A-51. 1 Publication1
Mutagenesisi47S → A: No effect on phosphorylation; when associated with A-49. Abolishes phosphorylation; when associated with A-49; A-51 and A-53, or with A-15; A-18; A-34; A-49; A-51 and A-53. 1 Publication1
Mutagenesisi49S → A: No effect on phosphorylation; when associated with A-47. Abolishes phosphorylation; when associated with A-47; A-51 and A-53, or with A-15; A-18; A-34; A-47; A-51 and A-53. Abolishes glycosylation but does not affect binding to YWHAE and YWHAZ; when associated with A-30 and A-31. 2 Publications1
Mutagenesisi51S → A: No effect on phosphorylation; when associated with A-30; A-31 and A-47. Abolishes phosphorylation; when associated with A-47; A-49 and A-53, or with A-15; A-18; A-34; A-47; A-49 and A-53. 1 Publication1
Mutagenesisi53S → A: Abolishes phosphorylation; when associated with A-47; A-49 and A-51, or with A-15; A-18; A-34; A-47; A-49 and A-51. Abolishes binding to YWHAE and YWHAZ; when associated with A-34. No effect on caspase cleavage during apoptosis. 3 Publications1
Mutagenesisi90R → C or H in transgenic mice, induces marked disruption of liver and pancreas keratin filament network. Increases phosphorylation and glycosylation. 1 Publication1
Mutagenesisi238D → E: Prevents cleavage by caspase-6 during apoptosis. Induces aggregates of keratin filaments in an altered organization. 1 Publication1

Keywords - Diseasei

Disease mutation

Organism-specific databases

DisGeNETi3875
MIMi215600 phenotype
OpenTargetsiENSG00000111057
PharmGKBiPA30217

Polymorphism and mutation databases

BioMutaiKRT18
DMDMi125083

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved1 Publication
ChainiPRO_00000636662 – 430Keratin, type I cytoskeletal 18Add BLAST429

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylserine1 Publication1
Modified residuei7PhosphoserineCombined sources1
Modified residuei10PhosphoserineCombined sources1
Modified residuei15PhosphoserineCombined sources1
Modified residuei18PhosphoserineCombined sources1
Modified residuei30Phosphoserine; alternateBy similarity1
GlycosylationiCAR_00017530O-linked (GlcNAc) serine; alternate2 Publications1
Modified residuei31Phosphoserine; alternateBy similarity1
GlycosylationiCAR_00019331O-linked (GlcNAc) serine; alternate2 Publications1
Modified residuei34Phosphoserine; by CDK1Combined sources2 Publications1
Modified residuei36PhosphotyrosineBy similarity1
Modified residuei42PhosphoserineCombined sources1
Modified residuei45Omega-N-methylarginineCombined sources1
Modified residuei49Phosphoserine; alternateCombined sources1
GlycosylationiCAR_00019449O-linked (GlcNAc) serine; alternate2 Publications1
Modified residuei51Phosphoserine; by MAPKAPK2 and MAPKAPK3By similarityCurated1
Modified residuei52PhosphothreonineCombined sources1
Modified residuei53Phosphoserine; by CAMK, PKC/PRKCE and AURKA3 Publications1
Modified residuei55Omega-N-methylarginineCombined sources1
Modified residuei60PhosphoserineCombined sources1
Modified residuei65PhosphothreonineCombined sources1
Cross-linki81Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei93PhosphoserineCombined sources1
Modified residuei100PhosphoserineCombined sources1
Modified residuei131N6-acetyllysineCombined sources1
Modified residuei177PhosphoserineCombined sources1
Cross-linki247Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei302PhosphothreonineCombined sources1
Modified residuei305PhosphoserineCombined sources1
Modified residuei319PhosphoserineCombined sources1
Modified residuei323PhosphoserineCombined sources1
Cross-linki370Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Cross-linki372Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei398PhosphoserineCombined sources1
Modified residuei399PhosphoserineCombined sources1
Modified residuei401PhosphoserineCombined sources1
Modified residuei404PhosphothreonineCombined sources1
Cross-linki417Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei426N6-acetyllysine; alternateCombined sources1
Cross-linki426Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternateCombined sources
Cross-linki426Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateCombined sources

Post-translational modificationi

Phosphorylation at Ser-34 increases during mitosis. Hyperphosphorylated at Ser-53 in diseased cirrhosis liver. Phosphorylation increases by IL-6.6 Publications
Proteolytically cleaved by caspases during epithelial cell apoptosis. Cleavage occurs at Asp-238 by either caspase-3, caspase-6 or caspase-7.1 Publication
O-GlcNAcylation increases solubility, and decreases stability by inducing proteasomal degradation.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei238 – 239Cleavage; by caspase-3, caspase-6 or caspase-72

Keywords - PTMi

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

Proteomic databases

EPDiP05783
MaxQBiP05783
PaxDbiP05783
PeptideAtlasiP05783
PRIDEiP05783
ProteomicsDBi51857
TopDownProteomicsiP05783

2D gel databases

SWISS-2DPAGEiP05783

PTM databases

GlyConnecti312
iPTMnetiP05783
PhosphoSitePlusiP05783
SwissPalmiP05783
UniCarbKBiP05783

Miscellaneous databases

PMAP-CutDBiP05783

Expressioni

Tissue specificityi

Expressed in colon, placenta, liver and very weakly in exocervix. Increased expression observed in lymph nodes of breast carcinoma.4 Publications

Inductioni

By IL6/interleukin-6.1 Publication

Gene expression databases

BgeeiENSG00000111057 Expressed in 90 organ(s), highest expression level in adenohypophysis
CleanExiHS_KRT18
ExpressionAtlasiP05783 baseline and differential
GenevisibleiP05783 HS

Organism-specific databases

HPAiCAB000008
CAB000030
HPA001605

Interactioni

Subunit structurei

Heterotetramer of two type I and two type II keratins. KRT18 associates with KRT8. Interacts with the thrombin-antithrombin complex (By similarity). Interacts with PNN and mutated CFTR. Interacts with YWHAE, YWHAH and YWHAZ only when phosphorylated. Interacts with DNAJB6, TCHP and TRADD. Interacts with FAM83H (PubMed:23902688). Interacts with EPPK1 (By similarity).By similarity8 Publications
(Microbial infection) Interacts with hepatitis C virus/HCV core protein.1 Publication

Binary interactionsi

GO - Molecular functioni

Protein-protein interaction databases

BioGridi110073, 99 interactors
DIPiDIP-633N
IntActiP05783, 78 interactors
MINTiP05783
STRINGi9606.ENSP00000373487

Structurei

3D structure databases

ProteinModelPortaliP05783
SMRiP05783
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini80 – 391IF rodPROSITE-ProRule annotationAdd BLAST312

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni2 – 79HeadAdd BLAST78
Regioni70 – 373Necessary for interaction with PNN1 PublicationAdd BLAST304
Regioni77 – 128Interaction with TRADD1 PublicationAdd BLAST52
Regioni80 – 115Coil 1AAdd BLAST36
Regioni116 – 132Linker 1Add BLAST17
Regioni133 – 224Coil 1BAdd BLAST92
Regioni225 – 248Linker 12Add BLAST24
Regioni243 – 391Interaction with DNAJB61 PublicationAdd BLAST149
Regioni249 – 387Coil 2Add BLAST139
Regioni388 – 430TailAdd BLAST43

Sequence similaritiesi

Belongs to the intermediate filament family.PROSITE-ProRule annotation

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiENOG410IEYR Eukaryota
ENOG4111DJ8 LUCA
GeneTreeiENSGT00900000140814
HOGENOMiHOG000230975
HOVERGENiHBG013015
InParanoidiP05783
KOiK07604
OMAiRAKYEKM
OrthoDBiEOG091G0A3U
PhylomeDBiP05783
TreeFamiTF332742

Family and domain databases

InterProiView protein in InterPro
IPR001664 IF
IPR018039 IF_conserved
IPR039008 IF_rod_dom
IPR027695 Keratin-18
IPR002957 Keratin_I
PANTHERiPTHR23239 PTHR23239, 1 hit
PTHR23239:SF35 PTHR23239:SF35, 1 hit
PfamiView protein in Pfam
PF00038 Filament, 1 hit
PRINTSiPR01248 TYPE1KERATIN
SMARTiView protein in SMART
SM01391 Filament, 1 hit
PROSITEiView protein in PROSITE
PS00226 IF_ROD_1, 1 hit
PS51842 IF_ROD_2, 1 hit

Sequence (1+)i

Sequence statusi: Complete.

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

This entry has 1 described isoform and 1 potential isoform that is computationally mapped.Show allAlign All

P05783-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MSFTTRSTFS TNYRSLGSVQ APSYGARPVS SAASVYAGAG GSGSRISVSR
60 70 80 90 100
STSFRGGMGS GGLATGIAGG LAGMGGIQNE KETMQSLNDR LASYLDRVRS
110 120 130 140 150
LETENRRLES KIREHLEKKG PQVRDWSHYF KIIEDLRAQI FANTVDNARI
160 170 180 190 200
VLQIDNARLA ADDFRVKYET ELAMRQSVEN DIHGLRKVID DTNITRLQLE
210 220 230 240 250
TEIEALKEEL LFMKKNHEEE VKGLQAQIAS SGLTVEVDAP KSQDLAKIMA
260 270 280 290 300
DIRAQYDELA RKNREELDKY WSQQIEESTT VVTTQSAEVG AAETTLTELR
310 320 330 340 350
RTVQSLEIDL DSMRNLKASL ENSLREVEAR YALQMEQLNG ILLHLESELA
360 370 380 390 400
QTRAEGQRQA QEYEALLNIK VKLEAEIATY RRLLEDGEDF NLGDALDSSN
410 420 430
SMQTIQKTTT RRIVDGKVVS ETNDTKVLRH
Length:430
Mass (Da):48,058
Last modified:January 23, 2007 - v2
Checksum:i1E5604C6BCC7A17A
GO

Computationally mapped potential isoform sequencesi

There is 1 potential isoform mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
F8VZY9F8VZY9_HUMAN
Keratin, type I cytoskeletal 18
KRT18
391Annotation score:

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti168Y → H in AAH00698 (PubMed:15489334).Curated1
Sequence conflicti202E → Q in CAA31369 (PubMed:2422083).Curated1
Sequence conflicti208E → G in BAD96813 (Ref. 3) Curated1
Sequence conflicti246A → S in CAA31369 (PubMed:2422083).Curated1
Sequence conflicti309D → R in CAA31369 (PubMed:2422083).Curated1
Sequence conflicti312S → R in CAA31369 (PubMed:2422083).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_023054103T → A in CIRRH. 1 PublicationCorresponds to variant dbSNP:rs61136606EnsemblClinVar.1
Natural variantiVAR_003852128H → L in CIRRH; interfers with the ability to form normal filaments. 2 PublicationsCorresponds to variant dbSNP:rs57758506EnsemblClinVar.1
Natural variantiVAR_023055230S → T1 PublicationCorresponds to variant dbSNP:rs58472472EnsemblClinVar.1
Natural variantiVAR_023056261R → Q in CIRRH. 1 PublicationCorresponds to variant dbSNP:rs57354642EnsemblClinVar.1
Natural variantiVAR_023057340G → R in CIRRH. 1 PublicationCorresponds to variant dbSNP:rs57370769EnsemblClinVar.1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X12881 mRNA Translation: CAA31375.1
AY762101 mRNA Translation: AAX07828.1
BT019412 mRNA Translation: AAV38219.1
AK223093 mRNA Translation: BAD96813.1
BC000180 mRNA Translation: AAH00180.1
BC000698 mRNA Translation: AAH00698.1
BC004253 mRNA Translation: AAH04253.1
BC008636 mRNA Translation: AAH08636.1
BC020982 mRNA Translation: AAH20982.1
BC072017 mRNA Translation: AAH72017.1
AF179904 Genomic DNA Translation: AAA59461.1
X12883 mRNA Translation: CAA31377.1
X12876 mRNA Translation: CAA31369.1
CCDSiCCDS31809.1
PIRiS05481
RefSeqiNP_000215.1, NM_000224.2
NP_954657.1, NM_199187.1
UniGeneiHs.406013

Genome annotation databases

EnsembliENST00000388835; ENSP00000373487; ENSG00000111057
ENST00000388837; ENSP00000373489; ENSG00000111057
GeneIDi3875
KEGGihsa:3875
UCSCiuc001sbe.4 human

Keywords - Coding sequence diversityi

Polymorphism

Similar proteinsi

Cross-referencesi

Web resourcesi

Human Intermediate Filament Mutation Database

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X12881 mRNA Translation: CAA31375.1
AY762101 mRNA Translation: AAX07828.1
BT019412 mRNA Translation: AAV38219.1
AK223093 mRNA Translation: BAD96813.1
BC000180 mRNA Translation: AAH00180.1
BC000698 mRNA Translation: AAH00698.1
BC004253 mRNA Translation: AAH04253.1
BC008636 mRNA Translation: AAH08636.1
BC020982 mRNA Translation: AAH20982.1
BC072017 mRNA Translation: AAH72017.1
AF179904 Genomic DNA Translation: AAA59461.1
X12883 mRNA Translation: CAA31377.1
X12876 mRNA Translation: CAA31369.1
CCDSiCCDS31809.1
PIRiS05481
RefSeqiNP_000215.1, NM_000224.2
NP_954657.1, NM_199187.1
UniGeneiHs.406013

3D structure databases

ProteinModelPortaliP05783
SMRiP05783
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi110073, 99 interactors
DIPiDIP-633N
IntActiP05783, 78 interactors
MINTiP05783
STRINGi9606.ENSP00000373487

PTM databases

GlyConnecti312
iPTMnetiP05783
PhosphoSitePlusiP05783
SwissPalmiP05783
UniCarbKBiP05783

Polymorphism and mutation databases

BioMutaiKRT18
DMDMi125083

2D gel databases

SWISS-2DPAGEiP05783

Proteomic databases

EPDiP05783
MaxQBiP05783
PaxDbiP05783
PeptideAtlasiP05783
PRIDEiP05783
ProteomicsDBi51857
TopDownProteomicsiP05783

Protocols and materials databases

DNASUi3875
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000388835; ENSP00000373487; ENSG00000111057
ENST00000388837; ENSP00000373489; ENSG00000111057
GeneIDi3875
KEGGihsa:3875
UCSCiuc001sbe.4 human

Organism-specific databases

CTDi3875
DisGeNETi3875
EuPathDBiHostDB:ENSG00000111057.10
GeneCardsiKRT18
H-InvDBiHIX0040371
HGNCiHGNC:6430 KRT18
HPAiCAB000008
CAB000030
HPA001605
MIMi148070 gene
215600 phenotype
neXtProtiNX_P05783
OpenTargetsiENSG00000111057
PharmGKBiPA30217
GenAtlasiSearch...

Phylogenomic databases

eggNOGiENOG410IEYR Eukaryota
ENOG4111DJ8 LUCA
GeneTreeiENSGT00900000140814
HOGENOMiHOG000230975
HOVERGENiHBG013015
InParanoidiP05783
KOiK07604
OMAiRAKYEKM
OrthoDBiEOG091G0A3U
PhylomeDBiP05783
TreeFamiTF332742

Enzyme and pathway databases

ReactomeiR-HSA-6805567 Keratinization
R-HSA-6809371 Formation of the cornified envelope
SignaLinkiP05783
SIGNORiP05783

Miscellaneous databases

ChiTaRSiKRT18 human
GeneWikiiKeratin_18
GenomeRNAii3875
PMAP-CutDBiP05783
PROiPR:P05783
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000111057 Expressed in 90 organ(s), highest expression level in adenohypophysis
CleanExiHS_KRT18
ExpressionAtlasiP05783 baseline and differential
GenevisibleiP05783 HS

Family and domain databases

InterProiView protein in InterPro
IPR001664 IF
IPR018039 IF_conserved
IPR039008 IF_rod_dom
IPR027695 Keratin-18
IPR002957 Keratin_I
PANTHERiPTHR23239 PTHR23239, 1 hit
PTHR23239:SF35 PTHR23239:SF35, 1 hit
PfamiView protein in Pfam
PF00038 Filament, 1 hit
PRINTSiPR01248 TYPE1KERATIN
SMARTiView protein in SMART
SM01391 Filament, 1 hit
PROSITEiView protein in PROSITE
PS00226 IF_ROD_1, 1 hit
PS51842 IF_ROD_2, 1 hit
ProtoNetiSearch...

Entry informationi

Entry nameiK1C18_HUMAN
AccessioniPrimary (citable) accession number: P05783
Secondary accession number(s): Q53G38, Q5U0N8, Q9BW26
Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 1, 1988
Last sequence update: January 23, 2007
Last modified: October 10, 2018
This is version 210 of the entry and version 2 of the sequence. See 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. SIMILARITY comments
    Index of protein domains and families
  2. Human chromosome 12
    Human chromosome 12: entries, gene names and cross-references to MIM
  3. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  4. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  5. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
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