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Protein

DNA polymerase delta subunit 2

Gene

POLD2

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: 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

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

DNA-directed DNA polymerase, Nucleotidyltransferase, Transferase

Keywords - Biological processi

DNA replication

Enzyme and pathway databases

ReactomeiREACT_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_264347. Mismatch repair (MMR) directed by MSH2:MSH3 (MutSbeta).
REACT_264501. Mismatch repair (MMR) directed by MSH2:MSH6 (MutSalpha).
REACT_355250. Termination of translesion DNA synthesis.
REACT_355480. Recognition of DNA damage by PCNA-containing replication complex.
REACT_355510. PCNA-Dependent Long Patch Base Excision Repair.
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 Componenti: Chromosome 7

Organism-specific databases

HGNCiHGNC:9176. POLD2.

Subcellular locationi

GO - Cellular componenti

  • nucleoplasm Source: HPA
  • nucleus Source: ProtInc
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA33497.

Polymorphism and mutation databases

BioMutaiPOLD2.
DMDMi1352307.

PTM / Processingi

Molecule processing

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

BgeeiP49005.
CleanExiHS_POLD2.
ExpressionAtlasiP49005. baseline and differential.
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.By similarity4 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. 21 interactions.
IntActiP49005. 15 interactions.
STRINGi9606.ENSP00000379148.

Structurei

Secondary structure

1
469
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi2 – 76Combined sources
Beta strandi13 – 164Combined sources
Beta strandi32 – 343Combined sources
Helixi37 – 393Combined sources
Helixi55 – 7218Combined sources
Beta strandi82 – 843Combined sources
Beta strandi91 – 10010Combined sources
Beta strandi132 – 1365Combined sources
Beta strandi141 – 1477Combined sources
Turni150 – 1523Combined sources
Beta strandi158 – 1658Combined sources
Beta strandi169 – 1779Combined sources
Beta strandi195 – 1995Combined sources
Helixi209 – 22315Combined sources
Helixi229 – 2357Combined sources
Beta strandi238 – 2458Combined sources
Helixi265 – 28723Combined sources
Beta strandi292 – 2954Combined sources
Beta strandi300 – 3023Combined sources
Beta strandi304 – 3074Combined sources
Helixi317 – 3204Combined sources
Beta strandi325 – 3273Combined sources
Beta strandi330 – 3367Combined sources
Beta strandi339 – 3435Combined sources
Helixi347 – 3559Combined sources
Helixi361 – 37010Combined sources
Beta strandi400 – 40910Combined sources
Beta strandi411 – 4166Combined sources
Beta strandi422 – 4298Combined sources
Helixi431 – 4344Combined sources
Beta strandi436 – 4416Combined sources
Turni442 – 4454Combined sources
Beta strandi449 – 4546Combined sources
Turni460 – 4623Combined sources

3D structure databases

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

Miscellaneous databases

EvolutionaryTraceiP49005.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG1311.
GeneTreeiENSGT00390000006780.
HOGENOMiHOG000189057.
HOVERGENiHBG051396.
InParanoidiP49005.
KOiK02328.
OMAiTRLIQMR.
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

        10         20         30         40         50
MFSEQAAQRA HTLLSPPSAN NATFARVPVA TYTNSSQPFR LGERSFSRQY
60 70 80 90 100
AHIYATRLIQ MRPFLENRAQ QHWGSGVGVK KLCELQPEEK CCVVGTLFKA
110 120 130 140 150
MPLQPSILRE VSEEHNLLPQ PPRSKYIHPD DELVLEDELQ RIKLKGTIDV
160 170 180 190 200
SKLVTGTVLA VFGSVRDDGK FLVEDYCFAD LAPQKPAPPL DTDRFVLLVS
210 220 230 240 250
GLGLGGGGGE SLLGTQLLVD VVTGQLGDEG EQCSAAHVSR VILAGNLLSH
260 270 280 290 300
STQSRDSINK AKYLTKKTQA ASVEAVKMLD EILLQLSASV PVDVMPGEFD
310 320 330 340 350
PTNYTLPQQP LHPCMFPLAT AYSTLQLVTN PYQATIDGVR FLGTSGQNVS
360 370 380 390 400
DIFRYSSMED HLEILEWTLR VRHISPTAPD TLGCYPFYKT DPFIFPECPH
410 420 430 440 450
VYFCGNTPSF GSKIIRGPED QTVLLVTVPD FSATQTACLV NLRSLACQPI
460
SFSGFGAEDD DLGGLGLGP
Length:469
Mass (Da):51,289
Last modified:February 1, 1996 - v1
Checksum:i389EF730999755AC
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti271 – 2711A → T in BAG35221 (PubMed:14702039).Curated

Natural variant

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

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Web resourcesi

NIEHS-SNPs

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

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

Protein-protein interaction databases

BioGridi111421. 21 interactions.
IntActiP49005. 15 interactions.
STRINGi9606.ENSP00000379148.

PTM databases

PhosphoSiteiP49005.

Polymorphism and mutation databases

BioMutaiPOLD2.
DMDMi1352307.

Proteomic databases

MaxQBiP49005.
PaxDbiP49005.
PeptideAtlasiP49005.
PRIDEiP49005.

Protocols and materials databases

DNASUi5425.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi5425.
GeneCardsiGC07M044120.
HGNCiHGNC:9176. POLD2.
HPAiHPA026745.
MIMi600815. gene.
neXtProtiNX_P49005.
PharmGKBiPA33497.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG1311.
GeneTreeiENSGT00390000006780.
HOGENOMiHOG000189057.
HOVERGENiHBG051396.
InParanoidiP49005.
KOiK02328.
OMAiTRLIQMR.
OrthoDBiEOG7RZ5PQ.
PhylomeDBiP49005.
TreeFamiTF101073.

Enzyme and pathway databases

ReactomeiREACT_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_264347. Mismatch repair (MMR) directed by MSH2:MSH3 (MutSbeta).
REACT_264501. Mismatch repair (MMR) directed by MSH2:MSH6 (MutSalpha).
REACT_355250. Termination of translesion DNA synthesis.
REACT_355480. Recognition of DNA damage by PCNA-containing replication complex.
REACT_355510. PCNA-Dependent Long Patch Base Excision Repair.
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

ChiTaRSiPOLD2. human.
EvolutionaryTraceiP49005.
GeneWikiiPOLD2.
GenomeRNAii5425.
NextBioi20989.
PROiP49005.
SOURCEiSearch...

Gene expression databases

BgeeiP49005.
CleanExiHS_POLD2.
ExpressionAtlasiP49005. baseline and differential.
GenevestigatoriP49005.

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]
ProtoNetiSearch...

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: May 27, 2015
This is version 148 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

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 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.