Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

Q15054

- DPOD3_HUMAN

UniProt

Q15054 - DPOD3_HUMAN

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

DNA polymerase delta subunit 3

Gene

POLD3

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

Required for optimal DNA polymerase delta activity.3 Publications

GO - Molecular functioni

  1. DNA-directed DNA polymerase activity Source: UniProtKB

GO - Biological processi

  1. base-excision repair Source: Reactome
  2. DNA repair Source: Reactome
  3. DNA strand elongation involved in DNA replication Source: Reactome
  4. DNA synthesis involved in DNA repair Source: UniProtKB
  5. mismatch repair Source: UniProtKB
  6. mitotic cell cycle Source: Reactome
  7. nucleotide-excision repair Source: Reactome
  8. nucleotide-excision repair, DNA gap filling Source: UniProtKB
  9. telomere maintenance Source: Reactome
  10. telomere maintenance via recombination Source: Reactome
  11. telomere maintenance via semi-conservative replication Source: Reactome
  12. 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 3
Alternative name(s):
DNA polymerase delta subunit p66
Gene namesi
Name:POLD3
Synonyms:KIAA0039
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 11

Organism-specific databases

HGNCiHGNC:20932. POLD3.

Subcellular locationi

GO - Cellular componenti

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

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA134868595.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed2 Publications
Chaini2 – 466465DNA polymerase delta subunit 3PRO_0000186047Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine2 Publications
Modified residuei307 – 3071Phosphoserine6 Publications
Modified residuei407 – 4071Phosphoserine1 Publication
Modified residuei409 – 4091Phosphoserine1 Publication
Modified residuei411 – 4111Phosphothreonine1 Publication
Modified residuei413 – 4131Phosphoserine1 Publication
Modified residuei458 – 4581Phosphoserine1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ15054.
PaxDbiQ15054.
PeptideAtlasiQ15054.
PRIDEiQ15054.

PTM databases

PhosphoSiteiQ15054.

Expressioni

Gene expression databases

BgeeiQ15054.
ExpressionAtlasiQ15054. baseline and differential.
GenevestigatoriQ15054.

Organism-specific databases

HPAiHPA039627.

Interactioni

Subunit structurei

Heterotetramer composed of subunits of 125 kDa, 50 kDa, 66 kDa and 12 kDa. Interacts with POLD2. Interacts with PCNA.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
PCNAP120044EBI-864956,EBI-358311
POLD2P490055EBI-864956,EBI-372354

Protein-protein interaction databases

BioGridi115940. 25 interactions.
DIPiDIP-35772N.
IntActiQ15054. 6 interactions.
MINTiMINT-2789689.
STRINGi9606.ENSP00000263681.

Structurei

Secondary structure

1
466
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi3 – 1412
Turni15 – 173
Helixi23 – 308
Helixi34 – 5219
Beta strandi58 – 8124
Turni82 – 843
Helixi85 – 917
Beta strandi93 – 10614
Beta strandi109 – 1113
Helixi113 – 12513
Helixi129 – 1313
Beta strandi134 – 1363
Helixi459 – 4613

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1U76X-ray2.60B/D/F452-466[»]
3E0JX-ray3.00B/D/F/H1-144[»]
ProteinModelPortaliQ15054.
SMRiQ15054. Positions 2-144.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ15054.

Family & Domainsi

Phylogenomic databases

eggNOGiNOG83700.
GeneTreeiENSGT00390000015282.
HOGENOMiHOG000008055.
HOVERGENiHBG051397.
InParanoidiQ15054.
KOiK03504.
OMAiVMSNFFG.
PhylomeDBiQ15054.
TreeFamiTF103006.

Family and domain databases

InterProiIPR019038. DNA_polymerase_subunit_Cdc27.
[Graphical view]
PfamiPF09507. CDC27. 1 hit.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

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

This entry describes 3 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q15054-1) [UniParc]FASTAAdd to Basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MADQLYLENI DEFVTDQNKI VTYKWLSYTL GVHVNQAKQM LYDYVERKRK
60 70 80 90 100
ENSGAQLHVT YLVSGSLIQN GHSCHKVAVV REDKLEAVKS KLAVTASIHV
110 120 130 140 150
YSIQKAMLKD SGPLFNTDYD ILKSNLQNCS KFSAIQCAAA VPRAPAESSS
160 170 180 190 200
SSKKFEQSHL HMSSETQANN ELTTNGHGPP ASKQVSQQPK GIMGMFASKA
210 220 230 240 250
AAKTQETNKE TKTEAKEVTN ASAAGNKAPG KGNMMSNFFG KAAMNKFKVN
260 270 280 290 300
LDSEQAVKEE KIVEQPTVSV TEPKLATPAG LKKSSKKAEP VKVLQKEKKR
310 320 330 340 350
GKRVALSDDE TKETENMRKK RRRIKLPESD SSEDEVFPDS PGAYEAESPS
360 370 380 390 400
PPPPPSPPLE PVPKTEPEPP SVKSSSGENK RKRKRVLKSK TYLDGEGCIV
410 420 430 440 450
TEKVYESESC TDSEEELNMK TSSVHRPPAM TVKKEPREER KGPKKGTAAL
460
GKANRQVSIT GFFQRK
Length:466
Mass (Da):51,400
Last modified:September 26, 2001 - v2
Checksum:iE9625E0188725F45
GO
Isoform 2 (identifier: Q15054-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-39: Missing.

Note: No experimental confirmation available.

Show »
Length:427
Mass (Da):46,801
Checksum:i29070FF3F00F0BCB
GO
Isoform 3 (identifier: Q15054-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-106: Missing.

Note: No experimental confirmation available.

Show »
Length:360
Mass (Da):39,320
Checksum:i70ACBAD78175C9BC
GO

Sequence cautioni

The sequence BAA05039.1 differs from that shown. Reason: Erroneous initiation.

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti194 – 1941G → V Found in a renal cell carcinoma sample; somatic mutation. 1 Publication
VAR_064745
Natural varianti195 – 1951M → L Found in a renal cell carcinoma sample; somatic mutation. 1 Publication
VAR_064746

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 106106Missing in isoform 3. 1 PublicationVSP_054149Add
BLAST
Alternative sequencei1 – 3939Missing in isoform 2. 1 PublicationVSP_054150Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
D26018 mRNA. Translation: BAA05039.1. Different initiation.
AK316301 mRNA. Translation: BAH14672.1.
AP001104 Genomic DNA. No translation available.
AP001324 Genomic DNA. No translation available.
AP001372 Genomic DNA. No translation available.
CH471076 Genomic DNA. Translation: EAW74942.1.
BC108908 mRNA. Translation: AAI08909.1.
BC108909 mRNA. Translation: AAI08910.1.
CCDSiCCDS8233.1. [Q15054-1]
RefSeqiNP_006582.1. NM_006591.2. [Q15054-1]
UniGeneiHs.82502.

Genome annotation databases

EnsembliENST00000263681; ENSP00000263681; ENSG00000077514. [Q15054-1]
ENST00000527458; ENSP00000432951; ENSG00000077514. [Q15054-2]
ENST00000532497; ENSP00000436018; ENSG00000077514. [Q15054-3]
GeneIDi10714.
KEGGihsa:10714.
UCSCiuc001ovf.2. human. [Q15054-1]

Polymorphism databases

DMDMi17375506.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
D26018 mRNA. Translation: BAA05039.1 . Different initiation.
AK316301 mRNA. Translation: BAH14672.1 .
AP001104 Genomic DNA. No translation available.
AP001324 Genomic DNA. No translation available.
AP001372 Genomic DNA. No translation available.
CH471076 Genomic DNA. Translation: EAW74942.1 .
BC108908 mRNA. Translation: AAI08909.1 .
BC108909 mRNA. Translation: AAI08910.1 .
CCDSi CCDS8233.1. [Q15054-1 ]
RefSeqi NP_006582.1. NM_006591.2. [Q15054-1 ]
UniGenei Hs.82502.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1U76 X-ray 2.60 B/D/F 452-466 [» ]
3E0J X-ray 3.00 B/D/F/H 1-144 [» ]
ProteinModelPortali Q15054.
SMRi Q15054. Positions 2-144.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 115940. 25 interactions.
DIPi DIP-35772N.
IntActi Q15054. 6 interactions.
MINTi MINT-2789689.
STRINGi 9606.ENSP00000263681.

PTM databases

PhosphoSitei Q15054.

Polymorphism databases

DMDMi 17375506.

Proteomic databases

MaxQBi Q15054.
PaxDbi Q15054.
PeptideAtlasi Q15054.
PRIDEi Q15054.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000263681 ; ENSP00000263681 ; ENSG00000077514 . [Q15054-1 ]
ENST00000527458 ; ENSP00000432951 ; ENSG00000077514 . [Q15054-2 ]
ENST00000532497 ; ENSP00000436018 ; ENSG00000077514 . [Q15054-3 ]
GeneIDi 10714.
KEGGi hsa:10714.
UCSCi uc001ovf.2. human. [Q15054-1 ]

Organism-specific databases

CTDi 10714.
GeneCardsi GC11P074207.
HGNCi HGNC:20932. POLD3.
HPAi HPA039627.
MIMi 611415. gene.
neXtProti NX_Q15054.
PharmGKBi PA134868595.
HUGEi Search...
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG83700.
GeneTreei ENSGT00390000015282.
HOGENOMi HOG000008055.
HOVERGENi HBG051397.
InParanoidi Q15054.
KOi K03504.
OMAi VMSNFFG.
PhylomeDBi Q15054.
TreeFami TF103006.

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

EvolutionaryTracei Q15054.
GeneWikii POLD3.
GenomeRNAii 10714.
NextBioi 40675.
PROi Q15054.
SOURCEi Search...

Gene expression databases

Bgeei Q15054.
ExpressionAtlasi Q15054. baseline and differential.
Genevestigatori Q15054.

Family and domain databases

InterProi IPR019038. DNA_polymerase_subunit_Cdc27.
[Graphical view ]
Pfami PF09507. CDC27. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Prediction of the coding sequences of unidentified human genes. I. The coding sequences of 40 new genes (KIAA0001-KIAA0040) deduced by analysis of randomly sampled cDNA clones from human immature myeloid cell line KG-1."
    Nomura N., Miyajima N., Sazuka T., Tanaka A., Kawarabayasi Y., Sato S., Nagase T., Seki N., Ishikawa K., Tabata S.
    DNA Res. 1:27-35(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Bone marrow.
  2. "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] (ISOFORM 1).
    Tissue: Placenta.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "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] (ISOFORMS 2 AND 3).
  6. Bienvenut W.V., Waridel P., Quadroni M.
    Submitted (MAR-2009) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 2-19 AND 110-123, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Embryonic kidney.
  7. "Isolation and identification of the third subunit of mammalian DNA polymerase delta by PCNA-affinity chromatography of mouse FM3A cell extracts."
    Hughes P., Tratner I., Ducoux M., Piard K., Baldacci G.
    Nucleic Acids Res. 27:2108-2114(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  8. "Evidence that DNA polymerase delta isolated by immunoaffinity chromatography exhibits high-molecular weight characteristics and is associated with the KIAA0039 protein and RPA."
    Mo J.-Y., Liu L., Leon A., Mazloum N., Lee M.Y.W.T.
    Biochemistry 39:7245-7254(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  9. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
    Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
    Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-307, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  10. "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: FUNCTION, INTERACTION WITH PCNA.
  11. "Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
    Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
    Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-307, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  12. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-307; SER-407; SER-409; THR-411; SER-413 AND SER-458, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  13. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
    Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
    Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  14. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-307, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  15. "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-307, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  16. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  17. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
    Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
    Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-307, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  18. "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 ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  19. Cited for: VARIANTS VAL-194 AND LEU-195.

Entry informationi

Entry nameiDPOD3_HUMAN
AccessioniPrimary (citable) accession number: Q15054
Secondary accession number(s): B7ZAI6, Q32MZ9, Q32N00
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: September 26, 2001
Last modified: October 29, 2014
This is version 126 of the entry and version 2 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, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 11
    Human chromosome 11: 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

External Data

Dasty 3