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Protein

Polymerase delta-interacting protein 3

Gene

POLDIP3

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

Functioni

Is involved in regulation of translation. Is preferentially associated with CBC-bound spliced mRNA-protein complexes during the pioneer round of mRNA translation. Contributes to enhanced translational efficiency of spliced over nonspliced mRNAs. Recruits activated ribosomal protein S6 kinase beta-1 I/RPS6KB1 to newly synthesized mRNA. Involved in nuclear mRNA export; probably mediated by assoociation with the TREX complex.2 Publications

GO - Molecular functioni

  • nucleotide binding Source: InterPro
  • poly(A) RNA binding Source: UniProtKB

GO - Biological processi

  • poly(A)+ mRNA export from nucleus Source: UniProtKB
  • positive regulation of translation Source: UniProtKB
Complete GO annotation...

Keywords - Biological processi

mRNA transport, Translation regulation, Transport

Keywords - Ligandi

RNA-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Polymerase delta-interacting protein 3
Alternative name(s):
46 kDa DNA polymerase delta interaction protein
Short name:
p46
S6K1 Aly/REF-like target
Short name:
SKAR
Gene namesi
Name:POLDIP3
Synonyms:KIAA1649, PDIP46
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 22

Organism-specific databases

HGNCiHGNC:23782. POLDIP3.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: UniProtKB
  • intracellular membrane-bounded organelle Source: HPA
  • nuclear speck Source: UniProtKB
  • nucleoplasm Source: HPA
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi383 – 3831S → A: Reduces in vitro phosphorylation by RPS6KB1. Abolishes in vitro phosphorylation by RPS6KB1; when associated with A-385. 1 Publication
Mutagenesisi385 – 3851S → A: Reduces in vitro phosphorylation by RPS6KB1. Reduces in vitro phosphorylation by RPS6KB1; when associated with A-383. 1 Publication

Organism-specific databases

PharmGKBiPA134899124.

Polymorphism and mutation databases

BioMutaiPOLDIP3.
DMDMi50403796.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedCombined sources1 Publication
Chaini2 – 421420Polymerase delta-interacting protein 3PRO_0000081722Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanineCombined sources1 Publication
Modified residuei5 – 51PhosphoserineCombined sources
Modified residuei127 – 1271PhosphoserineCombined sources1 Publication
Modified residuei140 – 1401PhosphothreonineCombined sources
Modified residuei275 – 2751PhosphoserineCombined sources1 Publication
Cross-linki372 – 372Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei383 – 3831Phosphoserine; by RPS6KB11 Publication
Modified residuei385 – 3851Phosphoserine; by RPS6KB11 Publication

Post-translational modificationi

Phosphorylated at Ser-383 and Ser-385 by RPS6KB1.1 Publication

Keywords - PTMi

Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiQ9BY77.
MaxQBiQ9BY77.
PaxDbiQ9BY77.
PRIDEiQ9BY77.

PTM databases

iPTMnetiQ9BY77.
PhosphoSiteiQ9BY77.

Miscellaneous databases

PMAP-CutDBQ9BY77.

Expressioni

Gene expression databases

BgeeiQ9BY77.
CleanExiHS_POLDIP3.
ExpressionAtlasiQ9BY77. baseline and differential.
GenevisibleiQ9BY77. HS.

Organism-specific databases

HPAiHPA018419.
HPA048790.

Interactioni

Subunit structurei

Interacts with POLD2. Interacts with NCBP1 and EIF4A3. Associates with the multiprotein exon junction complex (EJC). Interacts with RPS6KB1 (activated). Interacts with ERH. Interacts with THOC2, DDX39B and ZC3H11A; the interactions are ATP-dependent and indicative for an association with the TREX complex.5 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
NCBP1Q091613EBI-1776152,EBI-464743

Protein-protein interaction databases

BioGridi123998. 53 interactions.
IntActiQ9BY77. 23 interactions.
MINTiMINT-4538762.
STRINGi9606.ENSP00000252115.

Structurei

3D structure databases

ProteinModelPortaliQ9BY77.
SMRiQ9BY77. Positions 279-348.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini280 – 35172RRMPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 1 RRM (RNA recognition motif) domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiKOG0533. Eukaryota.
ENOG4111JAW. LUCA.
GeneTreeiENSGT00390000018868.
HOVERGENiHBG053550.
InParanoidiQ9BY77.
PhylomeDBiQ9BY77.
TreeFamiTF313312.

Family and domain databases

Gene3Di3.30.70.330. 1 hit.
InterProiIPR012677. Nucleotide-bd_a/b_plait.
IPR000504. RRM_dom.
[Graphical view]
PfamiPF00076. RRM_1. 1 hit.
[Graphical view]
SMARTiSM00360. RRM. 1 hit.
[Graphical view]
SUPFAMiSSF54928. SSF54928. 1 hit.
PROSITEiPS50102. RRM. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

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

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q9BY77-1) [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
MADISLDELI RKRGAAAKGR LNARPGVGGV RSRVGIQQGL LSQSTRTATF
60 70 80 90 100
QQRFDARQKI GLSDARLKLG VKDAREKLLQ KDARFRIKGK VQDAREMLNS
110 120 130 140 150
RKQQTTVPQK PRQVADAREK ISLKRSSPAA FINPPIGTVT PALKLTKTIQ
160 170 180 190 200
VPQQKAMAPL HPHPAGMRIN VVNNHQAKQN LYDLDEDDDG IASVPTKQMK
210 220 230 240 250
FAASGGFLHH MAGLSSSKLS MSKALPLTKV VQNDAYTAPA LPSSIRTKAL
260 270 280 290 300
TNMSRTLVNK EEPPKELPAA EPVLSPLEGT KMTVNNLHPR VTEEDIVELF
310 320 330 340 350
CVCGALKRAR LVHPGVAEVV FVKKDDAITA YKKYNNRCLD GQPMKCNLHM
360 370 380 390 400
NGNVITSDQP ILLRLSDSPS MKKESELPRR VNSASSSNPP AEVDPDTILK
410 420
ALFKSSGASV TTQPTEFKIK L
Length:421
Mass (Da):46,089
Last modified:July 19, 2004 - v2
Checksum:i39A4A2362852E020
GO
Isoform 2 (identifier: Q9BY77-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     151-179: Missing.

Show »
Length:392
Mass (Da):42,895
Checksum:i79AA8DA00FD5D6C6
GO

Sequence cautioni

The sequence BAB33368.2 differs from that shown. Reason: Erroneous initiation. Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei151 – 17929Missing in isoform 2. 3 PublicationsVSP_011056Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY422990 Genomic DNA. Translation: AAQ94604.1.
AB055760 mRNA. Translation: BAB33368.2. Different initiation.
AL160111 mRNA. Translation: CAB77058.1.
AL160112 mRNA. Translation: CAB77059.1.
CR456456 mRNA. Translation: CAG30342.1.
AK291623 mRNA. Translation: BAF84312.1.
AK291774 mRNA. Translation: BAF84463.1.
Z93241 Genomic DNA. Translation: CAI19835.1.
Z93241 Genomic DNA. Translation: CAQ08413.1.
BC049840 mRNA. Translation: AAH49840.1.
BC056912 mRNA. Translation: AAH56912.2.
BC095411 mRNA. Translation: AAH95411.1.
DQ887818 mRNA. Translation: ABI74675.1.
CCDSiCCDS14038.1. [Q9BY77-1]
CCDS14039.1. [Q9BY77-2]
RefSeqiNP_115687.2. NM_032311.4. [Q9BY77-1]
NP_835237.1. NM_178136.2. [Q9BY77-2]
UniGeneiHs.505802.

Genome annotation databases

EnsembliENST00000252115; ENSP00000252115; ENSG00000100227. [Q9BY77-1]
ENST00000348657; ENSP00000252116; ENSG00000100227. [Q9BY77-2]
GeneIDi84271.
UCSCiuc003bcu.4. human. [Q9BY77-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY422990 Genomic DNA. Translation: AAQ94604.1.
AB055760 mRNA. Translation: BAB33368.2. Different initiation.
AL160111 mRNA. Translation: CAB77058.1.
AL160112 mRNA. Translation: CAB77059.1.
CR456456 mRNA. Translation: CAG30342.1.
AK291623 mRNA. Translation: BAF84312.1.
AK291774 mRNA. Translation: BAF84463.1.
Z93241 Genomic DNA. Translation: CAI19835.1.
Z93241 Genomic DNA. Translation: CAQ08413.1.
BC049840 mRNA. Translation: AAH49840.1.
BC056912 mRNA. Translation: AAH56912.2.
BC095411 mRNA. Translation: AAH95411.1.
DQ887818 mRNA. Translation: ABI74675.1.
CCDSiCCDS14038.1. [Q9BY77-1]
CCDS14039.1. [Q9BY77-2]
RefSeqiNP_115687.2. NM_032311.4. [Q9BY77-1]
NP_835237.1. NM_178136.2. [Q9BY77-2]
UniGeneiHs.505802.

3D structure databases

ProteinModelPortaliQ9BY77.
SMRiQ9BY77. Positions 279-348.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi123998. 53 interactions.
IntActiQ9BY77. 23 interactions.
MINTiMINT-4538762.
STRINGi9606.ENSP00000252115.

PTM databases

iPTMnetiQ9BY77.
PhosphoSiteiQ9BY77.

Polymorphism and mutation databases

BioMutaiPOLDIP3.
DMDMi50403796.

Proteomic databases

EPDiQ9BY77.
MaxQBiQ9BY77.
PaxDbiQ9BY77.
PRIDEiQ9BY77.

Protocols and materials databases

DNASUi84271.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000252115; ENSP00000252115; ENSG00000100227. [Q9BY77-1]
ENST00000348657; ENSP00000252116; ENSG00000100227. [Q9BY77-2]
GeneIDi84271.
UCSCiuc003bcu.4. human. [Q9BY77-1]

Organism-specific databases

CTDi84271.
GeneCardsiPOLDIP3.
HGNCiHGNC:23782. POLDIP3.
HPAiHPA018419.
HPA048790.
MIMi611520. gene.
neXtProtiNX_Q9BY77.
PharmGKBiPA134899124.
HUGEiSearch...
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG0533. Eukaryota.
ENOG4111JAW. LUCA.
GeneTreeiENSGT00390000018868.
HOVERGENiHBG053550.
InParanoidiQ9BY77.
PhylomeDBiQ9BY77.
TreeFamiTF313312.

Miscellaneous databases

ChiTaRSiPOLDIP3. human.
GeneWikiiPOLDIP3.
GenomeRNAii84271.
NextBioi73832.
PMAP-CutDBQ9BY77.
PROiQ9BY77.
SOURCEiSearch...

Gene expression databases

BgeeiQ9BY77.
CleanExiHS_POLDIP3.
ExpressionAtlasiQ9BY77. baseline and differential.
GenevisibleiQ9BY77. HS.

Family and domain databases

Gene3Di3.30.70.330. 1 hit.
InterProiIPR012677. Nucleotide-bd_a/b_plait.
IPR000504. RRM_dom.
[Graphical view]
PfamiPF00076. RRM_1. 1 hit.
[Graphical view]
SMARTiSM00360. RRM. 1 hit.
[Graphical view]
SUPFAMiSSF54928. SSF54928. 1 hit.
PROSITEiPS50102. RRM. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "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: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1), INTERACTION WITH POLD2.
  2. "Identification of novel transcribed sequences on human chromosome 22 by expressed sequence tag mapping."
    Hirosawa M., Nagase T., Murahashi Y., Kikuno R., Ohara O.
    DNA Res. 8:1-9(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Brain and Placenta.
  3. "Reevaluating human gene annotation: a second-generation analysis of chromosome 22."
    Collins J.E., Goward M.E., Cole C.G., Smink L.J., Huckle E.J., Knowles S., Bye J.M., Beare D.M., Dunham I.
    Genome Res. 13:27-36(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
  5. "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] (ISOFORMS 1 AND 2).
    Tissue: Placenta.
  6. "The DNA sequence of human chromosome 22."
    Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M., Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C., Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E., Bridgeman A.M.
    , Buck D., Burgess J., Burrill W.D., Burton J., Carder C., Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G., Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V., Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M., Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A., Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C., Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E., Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F., Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M., Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A., Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D., Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y., Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S., Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E., Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L., Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L., Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N., Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A., Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L., Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P., Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P., Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q., Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J., Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J., Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D., Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T., Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P., Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K., Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R., Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L., McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J., Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E., Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P., Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y., Wright H.
    Nature 402:489-495(1999) [PubMed] [Europe PMC] [Abstract]
    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] (ISOFORMS 1 AND 2).
    Tissue: Brain.
  8. Bienvenut W.V., Lilla S., von Kriegsheim A., Lempens A., Kolch W.
    Submitted (DEC-2008) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 2-11; 34-46; 148-155; 311-323 AND 405-418, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Ovarian carcinoma.
  9. "SKAR links pre-mRNA splicing to mTOR/S6K1-mediated enhanced translation efficiency of spliced mRNAs."
    Ma X.M., Yoon S.O., Richardson C.J., Julich K., Blenis J.
    Cell 133:303-313(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 259-421, FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH NCBP1 AND EIF4A3.
  10. "SKAR is a specific target of S6 kinase 1 in cell growth control."
    Richardson C.J., Broenstrup M., Fingar D.C., Julich K., Ballif B.A., Gygi S., Blenis J.
    Curr. Biol. 14:1540-1549(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH RPS6KB1, SUBCELLULAR LOCATION, PHOSPHORYLATION AT SER-127; SER-275; SER-383 AND SER-385, MUTAGENESIS OF SER-383 AND SER-385, IDENTIFICATION BY MASS SPECTROMETRY.
  11. "Human enhancer of rudimentary is a molecular partner of PDIP46/SKAR, a protein interacting with DNA polymerase delta and S6K1 and regulating cell growth."
    Smyk A., Szuminska M., Uniewicz K.A., Graves L.M., Kozlowski P.
    FEBS J. 273:4728-4741(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH ERH, SUBCELLULAR LOCATION, IDENTIFICATION BY MASS SPECTROMETRY.
  12. "Improved titanium dioxide enrichment of phosphopeptides from HeLa cells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra."
    Yu L.R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.
    J. Proteome Res. 6:4150-4162(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  13. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic kidney.
  14. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  15. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
    Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
    Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-140, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  16. "ATP is required for interactions between UAP56 and two conserved mRNA export proteins, Aly and CIP29, to assemble the TREX complex."
    Dufu K., Livingstone M.J., Seebacher J., Gygi S.P., Wilson S.A., Reed R.
    Genes Dev. 24:2043-2053(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: ASSOCIATION WITH THE TREX COMPLEX.
  17. "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: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-5; SER-127 AND SER-275, CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS], IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  18. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  19. "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, CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS], IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  20. "The proteins PDIP3 and ZC11A associate with the human TREX complex in an ATP-dependent manner and function in mRNA export."
    Folco E.G., Lee C.S., Dufu K., Yamazaki T., Reed R.
    PLoS ONE 7:E43804-E43804(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH THOC2; DDX39B AND ZC3H11A, ASSOCIATION WITH THE TREX COMPLEX.
  21. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS], IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  22. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  23. "System-wide analysis of SUMOylation dynamics in response to replication stress reveals novel small ubiquitin-like modified target proteins and acceptor lysines relevant for genome stability."
    Xiao Z., Chang J.G., Hendriks I.A., Sigurdsson J.O., Olsen J.V., Vertegaal A.C.
    Mol. Cell. Proteomics 14:1419-1434(2015) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-372, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiPDIP3_HUMAN
AccessioniPrimary (citable) accession number: Q9BY77
Secondary accession number(s): A8K6F8
, A8K6V9, Q009A7, Q5H972, Q6PGN6, Q7Z6Z0, Q9NSP5, Q9NSP6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 19, 2002
Last sequence update: July 19, 2004
Last modified: April 13, 2016
This is version 127 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

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 22
    Human chromosome 22: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. SIMILARITY comments
    Index of protein domains and families

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 one 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.