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Protein

DNA replication licensing factor MCM2

Gene

MCM2

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

Functioni

Acts as component of the MCM2-7 complex (MCM complex) which is the putative replicative helicase essential for 'once per cell cycle' DNA replication initiation and elongation in eukaryotic cells. The active ATPase sites in the MCM2-7 ring are formed through the interaction surfaces of two neighboring subunits such that a critical structure of a conserved arginine finger motif is provided in trans relative to the ATP-binding site of the Walker A box of the adjacent subunit. The six ATPase active sites, however, are likely to contribute differentially to the complex helicase activity. Required for the entry in S phase and for cell division. Plays a role in terminally differentiated hair cells development of the cochlea and induces cells apoptosis.2 Publications

Miscellaneous

Early fractionation of eukaryotic MCM proteins yielded a variety of dimeric, trimeric and tetrameric complexes with unclear biological significance. Specifically a MCM467 subcomplex is shown to have in vitro helicase activity which is inhibited by the MCM2 subunit. The MCM2-7 hexamer is the proposed physiological active complex.

Catalytic activityi

ATP + H2O = ADP + phosphate.

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri329 – 355C4-typeSequence analysisAdd BLAST27
Nucleotide bindingi523 – 530ATPSequence analysis8

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionDNA-binding, Helicase, Hydrolase
Biological processCell cycle, DNA replication
LigandATP-binding, Metal-binding, Nucleotide-binding, Zinc

Enzyme and pathway databases

ReactomeiR-HSA-176187 Activation of ATR in response to replication stress
R-HSA-176974 Unwinding of DNA
R-HSA-68867 Assembly of the pre-replicative complex
R-HSA-68949 Orc1 removal from chromatin
R-HSA-68962 Activation of the pre-replicative complex
R-HSA-69052 Switching of origins to a post-replicative state
SIGNORiP49736

Names & Taxonomyi

Protein namesi
Recommended name:
DNA replication licensing factor MCM2 (EC:3.6.4.12)
Alternative name(s):
Minichromosome maintenance protein 2 homolog
Nuclear protein BM28
Gene namesi
Name:MCM2
Synonyms:BM28, CCNL1, CDCL1, KIAA0030
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 3

Organism-specific databases

EuPathDBiHostDB:ENSG00000073111.13
HGNCiHGNC:6944 MCM2
MIMi116945 gene
neXtProtiNX_P49736

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

Nucleus

Pathology & Biotechi

Involvement in diseasei

Deafness, autosomal dominant, 70 (DFNA70)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA form of non-syndromic sensorineural hearing loss. Sensorineural deafness results from damage to the neural receptors of the inner ear, the nerve pathways to the brain, or the area of the brain that receives sound information. DFNA70 is characterized by slowly progressive, postlingual hearing impairment.
See also OMIM:616968
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_07704944R → C in DFNA70; increases the apoptotic process; no effect on cell proliferation and cell cycle phase. 1 PublicationCorresponds to variant dbSNP:rs375851208EnsemblClinVar.1

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi27S → A: Impairs ATPase activity of the MCM-2-7 complex and reduces phosphorylation by the CDC7-DBF4 complex; when associated with A-41 and A-139. 1 Publication1
Mutagenesisi41S → A: Impairs ATPase activity of the MCM-2-7 complex and reduces phosphorylation by the CDC7-DBF4 complex; when associated with A-27 and A-139. 1 Publication1
Mutagenesisi108S → A: Reduces phosphorylation by ATR. 1 Publication1
Mutagenesisi139S → A: Impairs ATPase activity of the MCM-2-7 complex and reduces phosphorylation by the CDC7-DBF4 complex; when associated with A-27 and A-41. 1 Publication1

Keywords - Diseasei

Deafness, Disease mutation, Non-syndromic deafness

Organism-specific databases

DisGeNETi4171
MalaCardsiMCM2
MIMi616968 phenotype
OpenTargetsiENSG00000073111
Orphaneti90635 Autosomal dominant non-syndromic sensorineural deafness type DFNA
PharmGKBiPA164742061

Chemistry databases

ChEMBLiCHEMBL3308910

Polymorphism and mutation databases

DMDMi41019490

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedCombined sources
ChainiPRO_00001940872 – 904DNA replication licensing factor MCM2Add BLAST903

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylalanineCombined sources1
Modified residuei12PhosphoserineBy similarity1
Modified residuei13PhosphoserineCombined sources1
Modified residuei25PhosphothreonineCombined sources1
Modified residuei26PhosphoserineCombined sources1
Modified residuei27PhosphoserineCombined sources1 Publication1
Modified residuei32PhosphoserineCombined sources1
Modified residuei39PhosphothreonineCombined sources1
Modified residuei40Phosphoserine; by CDC7Combined sources1 Publication1
Modified residuei41PhosphoserineCombined sources1 Publication1
Modified residuei53Phosphoserine; by CDC7Combined sources2 Publications1
Modified residuei59PhosphothreonineCombined sources1
Modified residuei108Phosphoserine; by ATRCombined sources2 Publications1
Modified residuei137PhosphotyrosineCombined sources1
Modified residuei139PhosphoserineCombined sources1 Publication1
Cross-linki178Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei216N6-acetyllysineCombined sources1
Modified residuei381PhosphoserineCombined sources1
Modified residuei484PhosphoserineCombined sources1

Post-translational modificationi

Phosphorylated on Ser-108 by ATR in proliferating cells. Ser-108 proliferation is increased by genotoxic agents. Ser-40 is mediated by the CDC7-DBF4 and CDC7-DBF4B complexes, while Ser-53 phosphorylation is only mediated by the CDC7-DBF4 complex. Phosphorylation by the CDC7-DBF4 complex during G1/S phase is required for the initiation of DNA replication.3 Publications

Keywords - PTMi

Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiP49736
MaxQBiP49736
PaxDbiP49736
PeptideAtlasiP49736
PRIDEiP49736
ProteomicsDBi56058

PTM databases

iPTMnetiP49736
PhosphoSitePlusiP49736
SwissPalmiP49736

Miscellaneous databases

PMAP-CutDBiP49736

Expressioni

Gene expression databases

BgeeiENSG00000073111 Expressed in 187 organ(s), highest expression level in oocyte
CleanExiHS_CCNL1
HS_MCM2
ExpressionAtlasiP49736 baseline and differential
GenevisibleiP49736 HS

Organism-specific databases

HPAiCAB000303
HPA031495
HPA031496

Interactioni

Subunit structurei

Component of the MCM2-7 complex. The complex forms a toroidal hexameric ring with the proposed subunit order MCM2-MCM6-MCM4-MCM7-MCM3-MCM5 (Probable). Interacts with DBF4 (By similarity). Interacts with KAT7. May interact with MCM10. Component of the replisome complex composed of at least DONSON, MCM2, MCM7, PCNA and TICRR (PubMed:28191891).By similarityCurated6 Publications

Binary interactionsi

GO - Molecular functioni

Protein-protein interaction databases

BioGridi110339, 946 interactors
ComplexPortaliCPX-2940 MCM complex
CORUMiP49736
DIPiDIP-31732N
ELMiP49736
IntActiP49736, 69 interactors
MINTiP49736
STRINGi9606.ENSP00000265056

Structurei

Secondary structure

1904
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

ProteinModelPortaliP49736
SMRiP49736
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini473 – 679MCMAdd BLAST207

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni2 – 257Interaction with KAT7By similarityAdd BLAST256

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi655 – 658Arginine finger4

Sequence similaritiesi

Belongs to the MCM family.Curated

Zinc finger

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri329 – 355C4-typeSequence analysisAdd BLAST27

Keywords - Domaini

Zinc-finger

Phylogenomic databases

eggNOGiKOG0477 Eukaryota
COG1241 LUCA
GeneTreeiENSGT00930000150968
HOVERGENiHBG106398
InParanoidiP49736
KOiK02540
OMAiDCVKCGY
OrthoDBiEOG091G026H
PhylomeDBiP49736
TreeFamiTF300772

Family and domain databases

InterProiView protein in InterPro
IPR031327 MCM
IPR008045 MCM2
IPR018525 MCM_CS
IPR001208 MCM_dom
IPR027925 MCM_N
IPR033762 MCM_OB
IPR012340 NA-bd_OB-fold
IPR027417 P-loop_NTPase
PANTHERiPTHR11630 PTHR11630, 1 hit
PTHR11630:SF44 PTHR11630:SF44, 1 hit
PfamiView protein in Pfam
PF00493 MCM, 1 hit
PF12619 MCM2_N, 1 hit
PF14551 MCM_N, 1 hit
PF17207 MCM_OB, 1 hit
PRINTSiPR01657 MCMFAMILY
PR01658 MCMPROTEIN2
SMARTiView protein in SMART
SM00350 MCM, 1 hit
SUPFAMiSSF50249 SSF50249, 1 hit
SSF52540 SSF52540, 1 hit
PROSITEiView protein in PROSITE
PS00847 MCM_1, 1 hit
PS50051 MCM_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 5 potential isoforms that are computationally mapped.Show allAlign All

P49736-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MAESSESFTM ASSPAQRRRG NDPLTSSPGR SSRRTDALTS SPGRDLPPFE
60 70 80 90 100
DESEGLLGTE GPLEEEEDGE ELIGDGMERD YRAIPELDAY EAEGLALDDE
110 120 130 140 150
DVEELTASQR EAAERAMRQR DREAGRGLGR MRRGLLYDSD EEDEERPARK
160 170 180 190 200
RRQVERATED GEEDEEMIES IENLEDLKGH SVREWVSMAG PRLEIHHRFK
210 220 230 240 250
NFLRTHVDSH GHNVFKERIS DMCKENRESL VVNYEDLAAR EHVLAYFLPE
260 270 280 290 300
APAELLQIFD EAALEVVLAM YPKYDRITNH IHVRISHLPL VEELRSLRQL
310 320 330 340 350
HLNQLIRTSG VVTSCTGVLP QLSMVKYNCN KCNFVLGPFC QSQNQEVKPG
360 370 380 390 400
SCPECQSAGP FEVNMEETIY QNYQRIRIQE SPGKVAAGRL PRSKDAILLA
410 420 430 440 450
DLVDSCKPGD EIELTGIYHN NYDGSLNTAN GFPVFATVIL ANHVAKKDNK
460 470 480 490 500
VAVGELTDED VKMITSLSKD QQIGEKIFAS IAPSIYGHED IKRGLALALF
510 520 530 540 550
GGEPKNPGGK HKVRGDINVL LCGDPGTAKS QFLKYIEKVS SRAIFTTGQG
560 570 580 590 600
ASAVGLTAYV QRHPVSREWT LEAGALVLAD RGVCLIDEFD KMNDQDRTSI
610 620 630 640 650
HEAMEQQSIS ISKAGIVTSL QARCTVIAAA NPIGGRYDPS LTFSENVDLT
660 670 680 690 700
EPIISRFDIL CVVRDTVDPV QDEMLARFVV GSHVRHHPSN KEEEGLANGS
710 720 730 740 750
AAEPAMPNTY GVEPLPQEVL KKYIIYAKER VHPKLNQMDQ DKVAKMYSDL
760 770 780 790 800
RKESMATGSI PITVRHIESM IRMAEAHARI HLRDYVIEDD VNMAIRVMLE
810 820 830 840 850
SFIDTQKFSV MRSMRKTFAR YLSFRRDNNE LLLFILKQLV AEQVTYQRNR
860 870 880 890 900
FGAQQDTIEV PEKDLVDKAR QINIHNLSAF YDSELFRMNK FSHDLKRKMI

LQQF
Length:904
Mass (Da):101,896
Last modified:January 16, 2004 - v4
Checksum:i52C6DC61F128B404
GO

Computationally mapped potential isoform sequencesi

There are 5 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
H0Y8E6H0Y8E6_HUMAN
DNA helicase
MCM2
836Annotation score:
C9JZ21C9JZ21_HUMAN
DNA replication licensing factor MC...
MCM2
128Annotation score:
C9J013C9J013_HUMAN
DNA replication licensing factor MC...
MCM2
103Annotation score:
H7C4N9H7C4N9_HUMAN
DNA replication licensing factor MC...
MCM2
91Annotation score:
F8WDM3F8WDM3_HUMAN
DNA replication licensing factor MC...
MCM2
146Annotation score:

Sequence cautioni

The sequence BAA04642 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated
The sequence BAA12177 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence CAA47749 differs from that shown. Reason: Frameshift at positions 115, 124, 127, 129, 154, 158, 773 and 811.Curated
The sequence CAA47749 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti1M → S in CAA47749 (PubMed:8175912).Curated1
Sequence conflicti109Q → R in CAA47749 (PubMed:8175912).Curated1
Sequence conflicti388G → R in CAA47749 (PubMed:8175912).Curated1
Sequence conflicti407 – 408KP → NA in CAA47749 (PubMed:8175912).Curated2
Sequence conflicti407 – 408KP → NA in BAA12177 (Ref. 5) Curated2
Sequence conflicti495L → P in CAA47749 (PubMed:8175912).Curated1
Sequence conflicti555 – 556GL → AV in CAA47749 (PubMed:8175912).Curated2

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_07704944R → C in DFNA70; increases the apoptotic process; no effect on cell proliferation and cell cycle phase. 1 PublicationCorresponds to variant dbSNP:rs375851208EnsemblClinVar.1
Natural variantiVAR_02111168D → E1 PublicationCorresponds to variant dbSNP:rs3087452Ensembl.1
Natural variantiVAR_021112135L → F1 PublicationCorresponds to variant dbSNP:rs2307314Ensembl.1
Natural variantiVAR_033298166E → Q1 PublicationCorresponds to variant dbSNP:rs1048225Ensembl.1
Natural variantiVAR_016137396A → T1 PublicationCorresponds to variant dbSNP:rs3087450EnsemblClinVar.1
Natural variantiVAR_033299501G → R1 PublicationCorresponds to variant dbSNP:rs13087457EnsemblClinVar.1
Natural variantiVAR_016138667V → M1 PublicationCorresponds to variant dbSNP:rs2307311Ensembl.1
Natural variantiVAR_016139727A → T2 PublicationsCorresponds to variant dbSNP:rs2307313Ensembl.1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X67334 mRNA Translation: CAA47749.1 Sequence problems.
D21063 mRNA Translation: BAA04642.1 Different initiation.
AY675259 Genomic DNA Translation: AAT70723.1
BC006165 mRNA Translation: AAH06165.3
BC007670 mRNA Translation: AAH07670.2
BC007938 mRNA Translation: AAH07938.2
BC014272 mRNA Translation: AAH14272.2
BC017258 mRNA Translation: AAH17258.2
BC017490 mRNA Translation: AAH17490.2
BC030131 mRNA Translation: AAH30131.2
D83987 mRNA Translation: BAA12177.1 Different initiation.
BT009734 mRNA Translation: AAP88736.1
CCDSiCCDS3043.1
PIRiS42228
RefSeqiNP_004517.2, NM_004526.3
UniGeneiHs.477481

Genome annotation databases

EnsembliENST00000265056; ENSP00000265056; ENSG00000073111
GeneIDi4171
KEGGihsa:4171
UCSCiuc003ejp.5 human

Keywords - Coding sequence diversityi

Polymorphism

Similar proteinsi

Cross-referencesi

Web resourcesi

NIEHS-SNPs

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X67334 mRNA Translation: CAA47749.1 Sequence problems.
D21063 mRNA Translation: BAA04642.1 Different initiation.
AY675259 Genomic DNA Translation: AAT70723.1
BC006165 mRNA Translation: AAH06165.3
BC007670 mRNA Translation: AAH07670.2
BC007938 mRNA Translation: AAH07938.2
BC014272 mRNA Translation: AAH14272.2
BC017258 mRNA Translation: AAH17258.2
BC017490 mRNA Translation: AAH17490.2
BC030131 mRNA Translation: AAH30131.2
D83987 mRNA Translation: BAA12177.1 Different initiation.
BT009734 mRNA Translation: AAP88736.1
CCDSiCCDS3043.1
PIRiS42228
RefSeqiNP_004517.2, NM_004526.3
UniGeneiHs.477481

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4UUZX-ray2.90C69-138[»]
5BNVX-ray2.79C/F61-130[»]
5BNXX-ray2.31C61-130[»]
5BO0X-ray2.91C61-130[»]
5C3IX-ray3.50D/H/L/P/T/X63-124[»]
5JA4X-ray2.42C61-130[»]
ProteinModelPortaliP49736
SMRiP49736
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi110339, 946 interactors
ComplexPortaliCPX-2940 MCM complex
CORUMiP49736
DIPiDIP-31732N
ELMiP49736
IntActiP49736, 69 interactors
MINTiP49736
STRINGi9606.ENSP00000265056

Chemistry databases

ChEMBLiCHEMBL3308910

PTM databases

iPTMnetiP49736
PhosphoSitePlusiP49736
SwissPalmiP49736

Polymorphism and mutation databases

DMDMi41019490

Proteomic databases

EPDiP49736
MaxQBiP49736
PaxDbiP49736
PeptideAtlasiP49736
PRIDEiP49736
ProteomicsDBi56058

Protocols and materials databases

DNASUi4171
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000265056; ENSP00000265056; ENSG00000073111
GeneIDi4171
KEGGihsa:4171
UCSCiuc003ejp.5 human

Organism-specific databases

CTDi4171
DisGeNETi4171
EuPathDBiHostDB:ENSG00000073111.13
GeneCardsiMCM2
HGNCiHGNC:6944 MCM2
HPAiCAB000303
HPA031495
HPA031496
MalaCardsiMCM2
MIMi116945 gene
616968 phenotype
neXtProtiNX_P49736
OpenTargetsiENSG00000073111
Orphaneti90635 Autosomal dominant non-syndromic sensorineural deafness type DFNA
PharmGKBiPA164742061
HUGEiSearch...
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG0477 Eukaryota
COG1241 LUCA
GeneTreeiENSGT00930000150968
HOVERGENiHBG106398
InParanoidiP49736
KOiK02540
OMAiDCVKCGY
OrthoDBiEOG091G026H
PhylomeDBiP49736
TreeFamiTF300772

Enzyme and pathway databases

ReactomeiR-HSA-176187 Activation of ATR in response to replication stress
R-HSA-176974 Unwinding of DNA
R-HSA-68867 Assembly of the pre-replicative complex
R-HSA-68949 Orc1 removal from chromatin
R-HSA-68962 Activation of the pre-replicative complex
R-HSA-69052 Switching of origins to a post-replicative state
SIGNORiP49736

Miscellaneous databases

ChiTaRSiMCM2 human
GeneWikiiMCM2
GenomeRNAii4171
PMAP-CutDBiP49736
PROiPR:P49736
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000073111 Expressed in 187 organ(s), highest expression level in oocyte
CleanExiHS_CCNL1
HS_MCM2
ExpressionAtlasiP49736 baseline and differential
GenevisibleiP49736 HS

Family and domain databases

InterProiView protein in InterPro
IPR031327 MCM
IPR008045 MCM2
IPR018525 MCM_CS
IPR001208 MCM_dom
IPR027925 MCM_N
IPR033762 MCM_OB
IPR012340 NA-bd_OB-fold
IPR027417 P-loop_NTPase
PANTHERiPTHR11630 PTHR11630, 1 hit
PTHR11630:SF44 PTHR11630:SF44, 1 hit
PfamiView protein in Pfam
PF00493 MCM, 1 hit
PF12619 MCM2_N, 1 hit
PF14551 MCM_N, 1 hit
PF17207 MCM_OB, 1 hit
PRINTSiPR01657 MCMFAMILY
PR01658 MCMPROTEIN2
SMARTiView protein in SMART
SM00350 MCM, 1 hit
SUPFAMiSSF50249 SSF50249, 1 hit
SSF52540 SSF52540, 1 hit
PROSITEiView protein in PROSITE
PS00847 MCM_1, 1 hit
PS50051 MCM_2, 1 hit
ProtoNetiSearch...

Entry informationi

Entry nameiMCM2_HUMAN
AccessioniPrimary (citable) accession number: P49736
Secondary accession number(s): Q14577
, Q15023, Q8N2V1, Q969W7, Q96AE1, Q9BRM7
Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: January 16, 2004
Last modified: November 7, 2018
This is version 205 of the entry and version 4 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

3D-structure, Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. Human chromosome 3
    Human chromosome 3: 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
  6. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
UniProt is an ELIXIR core data resource
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