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P49005

- DPOD2_HUMAN

UniProt

P49005 - DPOD2_HUMAN

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Protein
DNA polymerase delta subunit 2
Gene
POLD2
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

The function of the small subunit is not yet clear.

Catalytic activityi

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

GO - Molecular functioni

  1. DNA binding Source: InterPro
  2. DNA-directed DNA polymerase activity Source: UniProtKB-KW
  3. protein binding Source: UniProtKB

GO - Biological processi

  1. DNA repair Source: Reactome
  2. DNA replication Source: ProtInc
  3. DNA strand elongation involved in DNA replication Source: Reactome
  4. base-excision repair Source: Reactome
  5. mitotic cell cycle Source: Reactome
  6. nucleotide-excision repair Source: Reactome
  7. nucleotide-excision repair, DNA gap filling Source: Reactome
  8. telomere maintenance Source: Reactome
  9. telomere maintenance via recombination Source: Reactome
  10. telomere maintenance via semi-conservative replication Source: Reactome
  11. transcription-coupled nucleotide-excision repair Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

DNA-directed DNA polymerase, Nucleotidyltransferase, Transferase

Keywords - Biological processi

DNA replication

Enzyme and pathway databases

ReactomeiREACT_1128. Resolution of AP sites via the multiple-nucleotide patch replacement pathway.
REACT_1385. Processive synthesis on the lagging strand.
REACT_1792. Polymerase switching.
REACT_1838. Leading Strand Synthesis.
REACT_1993. Repair synthesis for gap-filling by DNA polymerase in TC-NER.
REACT_2192. Removal of DNA patch containing abasic residue.
REACT_378. Repair synthesis of patch ~27-30 bases long by DNA polymerase.
REACT_70. Removal of the Flap Intermediate.
REACT_7961. Telomere C-strand (Lagging Strand) Synthesis.
REACT_7987. Polymerase switching on the C-strand of the telomere.
REACT_7999. Removal of the Flap Intermediate from the C-strand.
REACT_8027. Processive synthesis on the C-strand of the telomere.

Names & Taxonomyi

Protein namesi
Recommended name:
DNA polymerase delta subunit 2 (EC:2.7.7.7)
Alternative name(s):
DNA polymerase delta subunit p50
Gene namesi
Name:POLD2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 7

Organism-specific databases

HGNCiHGNC:9176. POLD2.

Subcellular locationi

GO - Cellular componenti

  1. delta DNA polymerase complex Source: Ensembl
  2. nucleoplasm Source: Reactome
  3. nucleus Source: HPA
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA33497.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 469469DNA polymerase delta subunit 2
PRO_0000096166Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionine2 Publications
Modified residuei15 – 151Phosphoserine1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiP49005.
PaxDbiP49005.
PeptideAtlasiP49005.
PRIDEiP49005.

PTM databases

PhosphoSiteiP49005.

Expressioni

Gene expression databases

ArrayExpressiP49005.
BgeeiP49005.
CleanExiHS_POLD2.
GenevestigatoriP49005.

Organism-specific databases

HPAiHPA026745.

Interactioni

Subunit structurei

Heterotetramer composed of subunits of 125 kDa, 50 kDa, 66 kDa and 12 kDa. Interacts with KCTD10 By similarity. Interacts with KCTD13/POLDIP1, POLDIP2 and POLDIP3. Interacts with WRNIP1. Interacts with POLD4.4 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
POLD1P283409EBI-372354,EBI-716569
POLD3Q150545EBI-372354,EBI-864956
POLD4Q9HCU83EBI-372354,EBI-864968
WRNIP1Q96S552EBI-372354,EBI-2513471

Protein-protein interaction databases

BioGridi111421. 16 interactions.
IntActiP49005. 14 interactions.
STRINGi9606.ENSP00000379148.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi2 – 76
Beta strandi13 – 164
Beta strandi32 – 343
Helixi37 – 393
Helixi55 – 7218
Beta strandi82 – 843
Beta strandi91 – 10010
Beta strandi132 – 1365
Beta strandi141 – 1477
Turni150 – 1523
Beta strandi158 – 1658
Beta strandi169 – 1779
Beta strandi195 – 1995
Helixi209 – 22315
Helixi229 – 2357
Beta strandi238 – 2458
Helixi265 – 28723
Beta strandi292 – 2954
Beta strandi300 – 3023
Beta strandi304 – 3074
Helixi317 – 3204
Beta strandi325 – 3273
Beta strandi330 – 3367
Beta strandi339 – 3435
Helixi347 – 3559
Helixi361 – 37010
Beta strandi400 – 40910
Beta strandi411 – 4166
Beta strandi422 – 4298
Helixi431 – 4344
Beta strandi436 – 4416
Turni442 – 4454
Beta strandi449 – 4546
Turni460 – 4623

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3E0JX-ray3.00A/C/E/G1-469[»]
ProteinModelPortaliP49005.
SMRiP49005. Positions 1-465.

Miscellaneous databases

EvolutionaryTraceiP49005.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG1311.
HOGENOMiHOG000189057.
HOVERGENiHBG051396.
InParanoidiP49005.
KOiK02328.
OMAiATRLIQM.
OrthoDBiEOG7RZ5PQ.
PhylomeDBiP49005.
TreeFamiTF101073.

Family and domain databases

InterProiIPR007185. DNA_pol_alpha/epsilon_bsu.
IPR024826. DNA_pol_delta/II_ssu.
[Graphical view]
PANTHERiPTHR10416. PTHR10416. 1 hit.
PfamiPF04042. DNA_pol_E_B. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P49005-1 [UniParc]FASTAAdd to Basket

« Hide

MFSEQAAQRA HTLLSPPSAN NATFARVPVA TYTNSSQPFR LGERSFSRQY    50
AHIYATRLIQ MRPFLENRAQ QHWGSGVGVK KLCELQPEEK CCVVGTLFKA 100
MPLQPSILRE VSEEHNLLPQ PPRSKYIHPD DELVLEDELQ RIKLKGTIDV 150
SKLVTGTVLA VFGSVRDDGK FLVEDYCFAD LAPQKPAPPL DTDRFVLLVS 200
GLGLGGGGGE SLLGTQLLVD VVTGQLGDEG EQCSAAHVSR VILAGNLLSH 250
STQSRDSINK AKYLTKKTQA ASVEAVKMLD EILLQLSASV PVDVMPGEFD 300
PTNYTLPQQP LHPCMFPLAT AYSTLQLVTN PYQATIDGVR FLGTSGQNVS 350
DIFRYSSMED HLEILEWTLR VRHISPTAPD TLGCYPFYKT DPFIFPECPH 400
VYFCGNTPSF GSKIIRGPED QTVLLVTVPD FSATQTACLV NLRSLACQPI 450
SFSGFGAEDD DLGGLGLGP 469
Length:469
Mass (Da):51,289
Last modified:February 1, 1996 - v1
Checksum:i389EF730999755AC
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti303 – 3031N → S.1 Publication
Corresponds to variant rs3087366 [ dbSNP | Ensembl ].
VAR_014885

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti271 – 2711A → T in BAG35221. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U21090 mRNA. Translation: AAC50216.1.
AF239710 Genomic DNA. Translation: AAG09763.1.
AY116646 Genomic DNA. Translation: AAM51148.1.
AK292347 mRNA. Translation: BAF85036.1.
AK312294 mRNA. Translation: BAG35221.1.
CH236960 Genomic DNA. Translation: EAL23767.1.
CH471128 Genomic DNA. Translation: EAW61118.1.
BC000459 mRNA. Translation: AAH00459.1.
CCDSiCCDS5477.1.
PIRiI38950.
RefSeqiNP_001120690.1. NM_001127218.2.
NP_001243808.1. NM_001256879.1.
NP_006221.2. NM_006230.3.
UniGeneiHs.306791.
Hs.740138.

Genome annotation databases

EnsembliENST00000406581; ENSP00000386105; ENSG00000106628.
ENST00000452185; ENSP00000395231; ENSG00000106628.
GeneIDi5425.
KEGGihsa:5425.
UCSCiuc003tkf.5. human.

Polymorphism databases

DMDMi1352307.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Web resourcesi

NIEHS-SNPs

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U21090 mRNA. Translation: AAC50216.1 .
AF239710 Genomic DNA. Translation: AAG09763.1 .
AY116646 Genomic DNA. Translation: AAM51148.1 .
AK292347 mRNA. Translation: BAF85036.1 .
AK312294 mRNA. Translation: BAG35221.1 .
CH236960 Genomic DNA. Translation: EAL23767.1 .
CH471128 Genomic DNA. Translation: EAW61118.1 .
BC000459 mRNA. Translation: AAH00459.1 .
CCDSi CCDS5477.1.
PIRi I38950.
RefSeqi NP_001120690.1. NM_001127218.2.
NP_001243808.1. NM_001256879.1.
NP_006221.2. NM_006230.3.
UniGenei Hs.306791.
Hs.740138.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
3E0J X-ray 3.00 A/C/E/G 1-469 [» ]
ProteinModelPortali P49005.
SMRi P49005. Positions 1-465.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 111421. 16 interactions.
IntActi P49005. 14 interactions.
STRINGi 9606.ENSP00000379148.

PTM databases

PhosphoSitei P49005.

Polymorphism databases

DMDMi 1352307.

Proteomic databases

MaxQBi P49005.
PaxDbi P49005.
PeptideAtlasi P49005.
PRIDEi P49005.

Protocols and materials databases

DNASUi 5425.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000406581 ; ENSP00000386105 ; ENSG00000106628 .
ENST00000452185 ; ENSP00000395231 ; ENSG00000106628 .
GeneIDi 5425.
KEGGi hsa:5425.
UCSCi uc003tkf.5. human.

Organism-specific databases

CTDi 5425.
GeneCardsi GC07M044120.
HGNCi HGNC:9176. POLD2.
HPAi HPA026745.
MIMi 600815. gene.
neXtProti NX_P49005.
PharmGKBi PA33497.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG1311.
HOGENOMi HOG000189057.
HOVERGENi HBG051396.
InParanoidi P49005.
KOi K02328.
OMAi ATRLIQM.
OrthoDBi EOG7RZ5PQ.
PhylomeDBi P49005.
TreeFami TF101073.

Enzyme and pathway databases

Reactomei REACT_1128. Resolution of AP sites via the multiple-nucleotide patch replacement pathway.
REACT_1385. Processive synthesis on the lagging strand.
REACT_1792. Polymerase switching.
REACT_1838. Leading Strand Synthesis.
REACT_1993. Repair synthesis for gap-filling by DNA polymerase in TC-NER.
REACT_2192. Removal of DNA patch containing abasic residue.
REACT_378. Repair synthesis of patch ~27-30 bases long by DNA polymerase.
REACT_70. Removal of the Flap Intermediate.
REACT_7961. Telomere C-strand (Lagging Strand) Synthesis.
REACT_7987. Polymerase switching on the C-strand of the telomere.
REACT_7999. Removal of the Flap Intermediate from the C-strand.
REACT_8027. Processive synthesis on the C-strand of the telomere.

Miscellaneous databases

ChiTaRSi POLD2. human.
EvolutionaryTracei P49005.
GeneWikii POLD2.
GenomeRNAii 5425.
NextBioi 20989.
PROi P49005.
SOURCEi Search...

Gene expression databases

ArrayExpressi P49005.
Bgeei P49005.
CleanExi HS_POLD2.
Genevestigatori P49005.

Family and domain databases

InterProi IPR007185. DNA_pol_alpha/epsilon_bsu.
IPR024826. DNA_pol_delta/II_ssu.
[Graphical view ]
PANTHERi PTHR10416. PTHR10416. 1 hit.
Pfami PF04042. DNA_pol_E_B. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning of the cDNAs for the small subunits of bovine and human DNA polymerase delta and chromosomal location of the human gene (POLD2)."
    Zhang J., Tan C.-K., McMullen B., Downey K.M., So A.G.
    Genomics 29:179-186(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "Characterization of the 5'-flanking region of the gene encoding the 50 kDa subunit of human DNA polymerase delta."
    Perez A., Leon A., Lee M.Y.W.T.
    Biochim. Biophys. Acta 1493:231-236(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  3. NIEHS SNPs program
    Submitted (MAY-2002) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT SER-303.
  4. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Cerebellum.
  5. "Human chromosome 7: DNA sequence and biology."
    Scherer S.W., Cheung J., MacDonald J.R., Osborne L.R., Nakabayashi K., Herbrick J.-A., Carson A.R., Parker-Katiraee L., Skaug J., Khaja R., Zhang J., Hudek A.K., Li M., Haddad M., Duggan G.E., Fernandez B.A., Kanematsu E., Gentles S.
    , Christopoulos C.C., Choufani S., Kwasnicka D., Zheng X.H., Lai Z., Nusskern D.R., Zhang Q., Gu Z., Lu F., Zeesman S., Nowaczyk M.J., Teshima I., Chitayat D., Shuman C., Weksberg R., Zackai E.H., Grebe T.A., Cox S.R., Kirkpatrick S.J., Rahman N., Friedman J.M., Heng H.H.Q., Pelicci P.G., Lo-Coco F., Belloni E., Shaffer L.G., Pober B., Morton C.C., Gusella J.F., Bruns G.A.P., Korf B.R., Quade B.J., Ligon A.H., Ferguson H., Higgins A.W., Leach N.T., Herrick S.R., Lemyre E., Farra C.G., Kim H.-G., Summers A.M., Gripp K.W., Roberts W., Szatmari P., Winsor E.J.T., Grzeschik K.-H., Teebi A., Minassian B.A., Kere J., Armengol L., Pujana M.A., Estivill X., Wilson M.D., Koop B.F., Tosi S., Moore G.E., Boright A.P., Zlotorynski E., Kerem B., Kroisel P.M., Petek E., Oscier D.G., Mould S.J., Doehner H., Doehner K., Rommens J.M., Vincent J.B., Venter J.C., Li P.W., Mural R.J., Adams M.D., Tsui L.-C.
    Science 300:767-772(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  7. "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].
    Tissue: Lung.
  8. "A tumor necrosis factor alpha- and interleukin 6-inducible protein that interacts with the small subunit of DNA polymerase delta and proliferating cell nuclear antigen."
    He H., Tan C.-K., Downey K.M., So A.G.
    Proc. Natl. Acad. Sci. U.S.A. 98:11979-11984(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH KCTD13/POLDIP1.
  9. "Identification of a novel protein, PDIP38, that interacts with the p50 subunit of DNA polymerase delta and proliferating cell nuclear antigen."
    Liu L., Rodriguez-Belmonte E.M., Mazloum N., Xie B., Lee M.Y.W.T.
    J. Biol. Chem. 278:10041-10047(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH POLDIP2 AND POLDIP3.
  10. "Human Werner helicase interacting protein 1 (WRNIP1) functions as a novel modulator for DNA polymerase delta."
    Tsurimoto T., Shinozaki A., Yano M., Seki M., Enomoto T.
    Genes Cells 10:13-22(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH WRNIP1.
  11. "Functional roles of p12, the fourth subunit of human DNA polymerase delta."
    Li H., Xie B., Zhou Y., Rahmeh A., Trusa S., Zhang S., Gao Y., Lee E.Y., Lee M.Y.
    J. Biol. Chem. 281:14748-14755(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH POLD4.
  12. "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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-15, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  13. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  14. "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 MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  15. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiDPOD2_HUMAN
AccessioniPrimary (citable) accession number: P49005
Secondary accession number(s): A4D2J4, B2R5S4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: February 1, 1996
Last modified: September 3, 2014
This is version 139 of the entry and version 1 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

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 7
    Human chromosome 7: 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