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Protein

DNA polymerase epsilon catalytic subunit A

Gene

POLE

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

Functioni

Participates in DNA repair and in chromosomal DNA replication.

Catalytic activityi

Deoxynucleoside triphosphate + DNA(n) = diphosphate + DNA(n+1).

Cofactori

[4Fe-4S] clusterBy similarityNote: Binds 1 [4Fe-4S] cluster.By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi2158ZincBy similarity1
Metal bindingi2161ZincBy similarity1
Metal bindingi2187ZincBy similarity1
Metal bindingi2190ZincBy similarity1
Metal bindingi2221Iron-sulfur (4Fe-4S)By similarity1
Metal bindingi2224Iron-sulfur (4Fe-4S)By similarity1
Metal bindingi2236Iron-sulfur (4Fe-4S)By similarity1
Metal bindingi2238Iron-sulfur (4Fe-4S)By similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri2158 – 2190CysA-typeAdd BLAST33

GO - Molecular functioni

  • 4 iron, 4 sulfur cluster binding Source: UniProtKB-KW
  • chromatin binding Source: UniProtKB
  • DNA binding Source: UniProtKB
  • DNA-directed DNA polymerase activity Source: UniProtKB
  • nucleotide binding Source: InterPro
  • single-stranded DNA 3'-5' exodeoxyribonuclease activity Source: GO_Central
  • zinc ion binding Source: InterPro

GO - Biological processi

  • base-excision repair, gap-filling Source: UniProtKB
  • DNA replication Source: UniProtKB
  • DNA replication proofreading Source: GO_Central
  • DNA synthesis involved in DNA repair Source: UniProtKB
  • embryonic organ development Source: Ensembl
  • G1/S transition of mitotic cell cycle Source: UniProtKB
  • leading strand elongation Source: GO_Central
  • nucleotide-excision repair, DNA gap filling Source: UniProtKB

Keywordsi

Molecular functionDNA-binding, DNA-directed DNA polymerase, Nucleotidyltransferase, Transferase
Biological processDNA damage, DNA repair, DNA replication
Ligand4Fe-4S, Iron, Iron-sulfur, Metal-binding, Zinc

Enzyme and pathway databases

ReactomeiR-HSA-110314 Recognition of DNA damage by PCNA-containing replication complex
R-HSA-174430 Telomere C-strand synthesis initiation
R-HSA-5651801 PCNA-Dependent Long Patch Base Excision Repair
R-HSA-5656169 Termination of translesion DNA synthesis
R-HSA-5685942 HDR through Homologous Recombination (HRR)
R-HSA-5696397 Gap-filling DNA repair synthesis and ligation in GG-NER
R-HSA-5696400 Dual Incision in GG-NER
R-HSA-6782135 Dual incision in TC-NER
R-HSA-6782210 Gap-filling DNA repair synthesis and ligation in TC-NER
R-HSA-68952 DNA replication initiation
R-HSA-68962 Activation of the pre-replicative complex

Names & Taxonomyi

Protein namesi
Recommended name:
DNA polymerase epsilon catalytic subunit A (EC:2.7.7.7)
Alternative name(s):
DNA polymerase II subunit A
Gene namesi
Name:POLE
Synonyms:POLE1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 12

Organism-specific databases

EuPathDBiHostDB:ENSG00000177084.16
HGNCiHGNC:9177 POLE
MIMi174762 gene
neXtProtiNX_Q07864

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

Colorectal cancer 12 (CRCS12)4 Publications
Disease susceptibility is associated with variations affecting the gene represented in this entry.
Disease descriptionA complex disease characterized by malignant lesions arising from the inner wall of the large intestine (the colon) and the rectum. Genetic alterations are often associated with progression from premalignant lesion (adenoma) to invasive adenocarcinoma. Risk factors for cancer of the colon and rectum include colon polyps, long-standing ulcerative colitis, and genetic family history. CRCS12 is characterized by a high-penetrance predisposition to the development of colorectal adenomas and carcinomas, with a variable tendency to develop multiple and large tumors. Onset is usually before age 40 years. The histologic features of the tumors are unremarkable.
See also OMIM:615083
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_069343411V → L in CRCS12; associated with disease susceptibility. 2 PublicationsCorresponds to variant dbSNP:rs1057519945Ensembl.1
Natural variantiVAR_069344424L → V in CRCS12; associated with disease susceptibility. 2 PublicationsCorresponds to variant dbSNP:rs483352909EnsemblClinVar.1
Natural variantiVAR_077350458Y → F in CRCS12. 1 Publication1
Facial dysmorphism, immunodeficiency, livedo, and short stature (FILS)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA syndrome characterized by mild facial dysmorphism, mainly malar hypoplasia, livedo on the skin since birth, and immunodeficiency resulting in recurrent infections. Growth impairment is observed during early childhood and results in variable short stature in adulthood.
See also OMIM:615139

Keywords - Diseasei

Disease mutation

Organism-specific databases

DisGeNETi5426
MalaCardsiPOLE
MIMi615083 phenotype
615139 phenotype
OpenTargetsiENSG00000177084
Orphaneti352712 Facial dysmorphism - immunodeficiency - livedo - short stature
PharmGKBiPA277

Chemistry databases

ChEMBLiCHEMBL2363042
DrugBankiDB00242 Cladribine

Polymorphism and mutation databases

BioMutaiPOLE
DMDMi116241339

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000464551 – 2286DNA polymerase epsilon catalytic subunit AAdd BLAST2286

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei1184PhosphoserineCombined sources1
Modified residuei1297PhosphoserineCombined sources1
Modified residuei1317PhosphoserineCombined sources1
Modified residuei1940PhosphoserineCombined sources1

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiQ07864
MaxQBiQ07864
PaxDbiQ07864
PeptideAtlasiQ07864
PRIDEiQ07864
ProteomicsDBi58543

PTM databases

iPTMnetiQ07864
PhosphoSitePlusiQ07864

Expressioni

Gene expression databases

BgeeiENSG00000177084
CleanExiHS_POLE
ExpressionAtlasiQ07864 baseline and differential
GenevisibleiQ07864 HS

Organism-specific databases

HPAiHPA058210
HPA067385

Interactioni

Subunit structurei

Catalytic and central component of the epsilon DNA polymerase complex consisting of four subunits: POLE, POLE2, POLE3 and POLE4. Interacts with RAD17 and TOPBP1.3 Publications

Binary interactionsi

Show more details

Protein-protein interaction databases

BioGridi111422, 49 interactors
ComplexPortaliCPX-2108 epsilon DNA polymerase complex
CORUMiQ07864
DIPiDIP-24243N
IntActiQ07864, 18 interactors
MINTiQ07864
STRINGi9606.ENSP00000322570

Structurei

Secondary structure

12286
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi2152 – 2157Combined sources6
Turni2159 – 2161Combined sources3
Beta strandi2164 – 2168Combined sources5
Turni2169 – 2171Combined sources3
Beta strandi2188 – 2190Combined sources3
Helixi2196 – 2216Combined sources21
Beta strandi2219 – 2224Combined sources6
Beta strandi2230 – 2232Combined sources3
Beta strandi2237 – 2239Combined sources3
Beta strandi2241 – 2246Combined sources6
Helixi2248 – 2265Combined sources18
Helixi2268 – 2279Combined sources12

3D structure databases

ProteinModelPortaliQ07864
SMRiQ07864
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi2221 – 2238CysB motifAdd BLAST18

Domaini

The DNA polymerase activity domain resides in the N-terminal half of the protein, while the C-terminus is necessary for complexing subunits B and C. The C-terminus may also regulate the catalytic activities of the enzyme.
The CysB motif binds 1 4Fe-4S cluster and is required for the formation of polymerase complexes.By similarity

Sequence similaritiesi

Belongs to the DNA polymerase type-B family.Curated

Zinc finger

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri2158 – 2190CysA-typeAdd BLAST33

Keywords - Domaini

Zinc-finger

Phylogenomic databases

eggNOGiKOG1798 Eukaryota
COG0417 LUCA
GeneTreeiENSGT00390000010194
HOVERGENiHBG051398
InParanoidiQ07864
KOiK02324
OMAiIHSKEIF
OrthoDBiEOG091G006J
PhylomeDBiQ07864
TreeFamiTF105017

Family and domain databases

Gene3Di3.30.420.10, 1 hit
InterProiView protein in InterPro
IPR006172 DNA-dir_DNA_pol_B
IPR006133 DNA-dir_DNA_pol_B_exonuc
IPR006134 DNA-dir_DNA_pol_B_multi_dom
IPR013697 DNA_pol_e_suA_C
IPR029703 POL2
IPR012337 RNaseH-like_sf
IPR036397 RNaseH_sf
PANTHERiPTHR10670 PTHR10670, 1 hit
PfamiView protein in Pfam
PF00136 DNA_pol_B, 1 hit
PF03104 DNA_pol_B_exo1, 1 hit
PF08490 DUF1744, 1 hit
SMARTiView protein in SMART
SM01159 DUF1744, 1 hit
SM00486 POLBc, 1 hit
SUPFAMiSSF53098 SSF53098, 2 hits

Sequencei

Sequence statusi: Complete.

Q07864-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSLRSGGRRR ADPGADGEAS RDDGATSSVS ALKRLERSQW TDKMDLRFGF
60 70 80 90 100
ERLKEPGEKT GWLINMHPTE ILDEDKRLGS AVDYYFIQDD GSRFKVALPY
110 120 130 140 150
KPYFYIATRK GCEREVSSFL SKKFQGKIAK VETVPKEDLD LPNHLVGLKR
160 170 180 190 200
NYIRLSFHTV EDLVKVRKEI SPAVKKNREQ DHASDAYTAL LSSVLQRGGV
210 220 230 240 250
ITDEEETSKK IADQLDNIVD MREYDVPYHI RLSIDLKIHV AHWYNVRYRG
260 270 280 290 300
NAFPVEITRR DDLVERPDPV VLAFDIETTK LPLKFPDAET DQIMMISYMI
310 320 330 340 350
DGQGYLITNR EIVSEDIEDF EFTPKPEYEG PFCVFNEPDE AHLIQRWFEH
360 370 380 390 400
VQETKPTIMV TYNGDFFDWP FVEARAAVHG LSMQQEIGFQ KDSQGEYKAP
410 420 430 440 450
QCIHMDCLRW VKRDSYLPVG SHNLKAAAKA KLGYDPVELD PEDMCRMATE
460 470 480 490 500
QPQTLATYSV SDAVATYYLY MKYVHPFIFA LCTIIPMEPD EVLRKGSGTL
510 520 530 540 550
CEALLMVQAF HANIIFPNKQ EQEFNKLTDD GHVLDSETYV GGHVEALESG
560 570 580 590 600
VFRSDIPCRF RMNPAAFDFL LQRVEKTLRH ALEEEEKVPV EQVTNFEEVC
610 620 630 640 650
DEIKSKLASL KDVPSRIECP LIYHLDVGAM YPNIILTNRL QPSAMVDEAT
660 670 680 690 700
CAACDFNKPG ANCQRKMAWQ WRGEFMPASR SEYHRIQHQL ESEKFPPLFP
710 720 730 740 750
EGPARAFHEL SREEQAKYEK RRLADYCRKA YKKIHITKVE ERLTTICQRE
760 770 780 790 800
NSFYVDTVRA FRDRRYEFKG LHKVWKKKLS AAVEVGDAAE VKRCKNMEVL
810 820 830 840 850
YDSLQLAHKC ILNSFYGYVM RKGARWYSME MAGIVCFTGA NIITQARELI
860 870 880 890 900
EQIGRPLELD TDGIWCVLPN SFPENFVFKT TNVKKPKVTI SYPGAMLNIM
910 920 930 940 950
VKEGFTNDQY QELAEPSSLT YVTRSENSIF FEVDGPYLAM ILPASKEEGK
960 970 980 990 1000
KLKKRYAVFN EDGSLAELKG FEVKRRGELQ LIKIFQSSVF EAFLKGSTLE
1010 1020 1030 1040 1050
EVYGSVAKVA DYWLDVLYSK AANMPDSELF ELISENRSMS RKLEDYGEQK
1060 1070 1080 1090 1100
STSISTAKRL AEFLGDQMVK DAGLSCRYII SRKPEGSPVT ERAIPLAIFQ
1110 1120 1130 1140 1150
AEPTVRKHFL RKWLKSSSLQ DFDIRAILDW DYYIERLGSA IQKIITIPAA
1160 1170 1180 1190 1200
LQQVKNPVPR VKHPDWLHKK LLEKNDVYKQ KKISELFTLE GRRQVTMAEA
1210 1220 1230 1240 1250
SEDSPRPSAP DMEDFGLVKL PHPAAPVTVK RKRVLWESQE ESQDLTPTVP
1260 1270 1280 1290 1300
WQEILGQPPA LGTSQEEWLV WLRFHKKKWQ LQARQRLARR KRQRLESAEG
1310 1320 1330 1340 1350
VLRPGAIRDG PATGLGSFLR RTARSILDLP WQIVQISETS QAGLFRLWAL
1360 1370 1380 1390 1400
VGSDLHCIRL SIPRVFYVNQ RVAKAEEGAS YRKVNRVLPR SNMVYNLYEY
1410 1420 1430 1440 1450
SVPEDMYQEH INEINAELSA PDIEGVYETQ VPLLFRALVH LGCVCVVNKQ
1460 1470 1480 1490 1500
LVRHLSGWEA ETFALEHLEM RSLAQFSYLE PGSIRHIYLY HHAQAHKALF
1510 1520 1530 1540 1550
GIFIPSQRRA SVFVLDTVRS NQMPSLGALY SAEHGLLLEK VGPELLPPPK
1560 1570 1580 1590 1600
HTFEVRAETD LKTICRAIQR FLLAYKEERR GPTLIAVQSS WELKRLASEI
1610 1620 1630 1640 1650
PVLEEFPLVP ICVADKINYG VLDWQRHGAR RMIRHYLNLD TCLSQAFEMS
1660 1670 1680 1690 1700
RYFHIPIGNL PEDISTFGSD LFFARHLQRH NHLLWLSPTA RPDLGGKEAD
1710 1720 1730 1740 1750
DNCLVMEFDD QATVEINSSG CYSTVCVELD LQNLAVNTIL QSHHVNDMEG
1760 1770 1780 1790 1800
ADSMGISFDV IQQASLEDMI TGGQAASAPA SYDETALCSN TFRILKSMVV
1810 1820 1830 1840 1850
GWVKEITQYH NIYADNQVMH FYRWLRSPSS LLHDPALHRT LHNMMKKLFL
1860 1870 1880 1890 1900
QLIAEFKRLG SSVIYANFNR IILCTKKRRV EDAIAYVEYI TSSIHSKETF
1910 1920 1930 1940 1950
HSLTISFSRC WEFLLWMDPS NYGGIKGKVS SRIHCGLQDS QKAGGAEDEQ
1960 1970 1980 1990 2000
ENEDDEEERD GEEEEEAEES NVEDLLENNW NILQFLPQAA SCQNYFLMIV
2010 2020 2030 2040 2050
SAYIVAVYHC MKDGLRRSAP GSTPVRRRGA SQLSQEAEGA VGALPGMITF
2060 2070 2080 2090 2100
SQDYVANELT QSFFTITQKI QKKVTGSRNS TELSEMFPVL PGSHLLLNNP
2110 2120 2130 2140 2150
ALEFIKYVCK VLSLDTNITN QVNKLNRDLL RLVDVGEFSE EAQFRDPCRS
2160 2170 2180 2190 2200
YVLPEVICRS CNFCRDLDLC KDSSFSEDGA VLPQWLCSNC QAPYDSSAIE
2210 2220 2230 2240 2250
MTLVEVLQKK LMAFTLQDLV CLKCRGVKET SMPVYCSCAG DFALTIHTQV
2260 2270 2280
FMEQIGIFRN IAQHYGMSYL LETLEWLLQK NPQLGH
Length:2,286
Mass (Da):261,518
Last modified:October 17, 2006 - v5
Checksum:iA213AE1EA8437DEC
GO

Sequence cautioni

The sequence AAA15448 differs from that shown.Curated
The sequence AAA15448 differs from that shown. Reason: Frameshift at positions 443 and 448.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti2237S → T in AAA15448 (PubMed:8486689).Curated1
Sequence conflicti2237S → T in AAC19148 (PubMed:8486689).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_06113831A → S. Corresponds to variant dbSNP:rs34047482EnsemblClinVar.1
Natural variantiVAR_02842999P → L. Corresponds to variant dbSNP:rs5744739EnsemblClinVar.1
Natural variantiVAR_069339189A → T Found in a colorectal sample; somatic mutation. 1 Publication1
Natural variantiVAR_069340231R → H Found in a colorectal sample; somatic mutation. 1 PublicationCorresponds to variant dbSNP:rs1060500835Ensembl.1
Natural variantiVAR_020276252A → V. Corresponds to variant dbSNP:rs5744751EnsemblClinVar.1
Natural variantiVAR_028430260R → Q. Corresponds to variant dbSNP:rs5744752EnsemblClinVar.1
Natural variantiVAR_069341286P → H Found in a colorectal sample; somatic mutation. 1 PublicationCorresponds to variant dbSNP:rs1057519943Ensembl.1
Natural variantiVAR_077349286P → R Found in a colorectal sample; somatic mutation. 1 Publication1
Natural variantiVAR_020277336N → S. Corresponds to variant dbSNP:rs5744760EnsemblClinVar.1
Natural variantiVAR_069342367F → S Found in a colorectal sample; somatic mutation. 1 Publication1
Natural variantiVAR_069343411V → L in CRCS12; associated with disease susceptibility. 2 PublicationsCorresponds to variant dbSNP:rs1057519945Ensembl.1
Natural variantiVAR_069344424L → V in CRCS12; associated with disease susceptibility. 2 PublicationsCorresponds to variant dbSNP:rs483352909EnsemblClinVar.1
Natural variantiVAR_069345436P → R Found in a colorectal sample; somatic mutation. 1 PublicationCorresponds to variant dbSNP:rs864622766EnsemblClinVar.1
Natural variantiVAR_077350458Y → F in CRCS12. 1 Publication1
Natural variantiVAR_069346459S → F Found in a colorectal sample; somatic mutation. 1 Publication1
Natural variantiVAR_020278695F → I. Corresponds to variant dbSNP:rs5744799EnsemblClinVar.1
Natural variantiVAR_069347762R → W Found in a colorectal sample; somatic mutation. 1 PublicationCorresponds to variant dbSNP:rs1064794759Ensembl.1
Natural variantiVAR_069348777K → N Found in a colorectal sample; somatic mutation. 1 Publication1
Natural variantiVAR_0693491008K → N Found in a colorectal sample; somatic mutation. 1 Publication1
Natural variantiVAR_0693501255L → V Found in a colorectal sample; somatic mutation. 1 Publication1
Natural variantiVAR_0693511368V → M Found in a colorectal sample; somatic mutation. 1 PublicationCorresponds to variant dbSNP:rs770558983EnsemblClinVar.1
Natural variantiVAR_0284311382R → C Found in a colorectal sample; somatic mutation. 1 PublicationCorresponds to variant dbSNP:rs5744904EnsemblClinVar.1
Natural variantiVAR_0202791395Y → C. Corresponds to variant dbSNP:rs5744933EnsemblClinVar.1
Natural variantiVAR_0202801396N → S. Corresponds to variant dbSNP:rs5744934EnsemblClinVar.1
Natural variantiVAR_0202811399E → Q. Corresponds to variant dbSNP:rs5744935EnsemblClinVar.1
Natural variantiVAR_0693521421P → S1 Publication1
Natural variantiVAR_0284321577E → A. Corresponds to variant dbSNP:rs5744948EnsemblClinVar.1
Natural variantiVAR_0284331712A → V. Corresponds to variant dbSNP:rs5744950EnsemblClinVar.1
Natural variantiVAR_0693531752D → N Found in a colorectal sample; somatic mutation. 1 Publication1
Natural variantiVAR_0284341857K → R. Corresponds to variant dbSNP:rs5744971EnsemblClinVar.1
Natural variantiVAR_0773511925I → T Found in a colorectal sample; somatic mutation. 1 Publication1
Natural variantiVAR_0284351935C → Y. Corresponds to variant dbSNP:rs5744991EnsemblClinVar.1
Natural variantiVAR_0693542013D → N1 Publication1
Natural variantiVAR_0202822040A → V. Corresponds to variant dbSNP:rs5745021EnsemblClinVar.1
Natural variantiVAR_0693552056A → T Found in a colorectal sample; somatic mutation. 1 PublicationCorresponds to variant dbSNP:rs58916399Ensembl.1
Natural variantiVAR_0488812140E → K. Corresponds to variant dbSNP:rs5745066EnsemblClinVar.1
Natural variantiVAR_0488822159R → C. Corresponds to variant dbSNP:rs5745067EnsemblClinVar.1
Natural variantiVAR_0202832165R → H. Corresponds to variant dbSNP:rs5745068EnsemblClinVar.1
Natural variantiVAR_0693562213A → V Found in a colorectal sample; somatic mutation. 1 Publication1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
S60080 mRNA Translation: AAA15448.1 Sequence problems.
L09561 mRNA Translation: AAC19148.1
U49356 mRNA Translation: AAA90924.1
AY273166 Genomic DNA Translation: AAP12650.1
CCDSiCCDS9278.1
PIRiG02434
RefSeqiNP_006222.2, NM_006231.3
UniGeneiHs.524871

Genome annotation databases

EnsembliENST00000320574; ENSP00000322570; ENSG00000177084
GeneIDi5426
KEGGihsa:5426
UCSCiuc001uks.3 human

Keywords - Coding sequence diversityi

Polymorphism

Similar proteinsi

Entry informationi

Entry nameiDPOE1_HUMAN
AccessioniPrimary (citable) accession number: Q07864
Secondary accession number(s): Q13533, Q86VH9
Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 1, 1994
Last sequence update: October 17, 2006
Last modified: July 18, 2018
This is version 186 of the entry and version 5 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, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 12
    Human chromosome 12: 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

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