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O43399

- TPD54_HUMAN

UniProt

O43399 - TPD54_HUMAN

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Protein

Tumor protein D54

Gene

TPD52L2

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

Functioni

GO - Molecular functioni

  1. poly(A) RNA binding Source: UniProtKB
  2. protein heterodimerization activity Source: UniProtKB
  3. protein homodimerization activity Source: UniProtKB

GO - Biological processi

  1. regulation of cell proliferation Source: UniProtKB
Complete GO annotation...

Enzyme and pathway databases

SignaLinkiO43399.

Names & Taxonomyi

Protein namesi
Recommended name:
Tumor protein D54
Short name:
hD54
Alternative name(s):
Tumor protein D52-like 2
Gene namesi
Name:TPD52L2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 20

Organism-specific databases

HGNCiHGNC:12007. TPD52L2.

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB
  2. perinuclear region of cytoplasm Source: UniProtKB
Complete GO annotation...

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA36688.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 206206Tumor protein D54PRO_0000185744Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionine4 Publications
Modified residuei3 – 31Phosphoserine2 Publications
Modified residuei12 – 121Phosphoserine5 Publications
Modified residuei19 – 191Phosphoserine1 Publication
Modified residuei21 – 211Phosphoserine1 Publication
Modified residuei96 – 961Phosphoserine3 Publications
Modified residuei149 – 1491Phosphoserine1 Publication
Modified residuei166 – 1661Phosphoserine7 Publications
Modified residuei192 – 1921PhosphoserineBy similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiO43399.
PaxDbiO43399.
PRIDEiO43399.

2D gel databases

OGPiO43399.

PTM databases

PhosphoSiteiO43399.

Expressioni

Gene expression databases

BgeeiO43399.
CleanExiHS_TPD52L2.
ExpressionAtlasiO43399. baseline and differential.
GenevestigatoriO43399.

Organism-specific databases

HPAiHPA047489.

Interactioni

Subunit structurei

Forms a homodimer or heterodimer with other members of the family (By similarity). Interacts with MAL2.By similarity1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
Tpd52Q623932EBI-782616,EBI-782591From a different organism.

Protein-protein interaction databases

BioGridi113018. 51 interactions.
IntActiO43399. 8 interactions.
STRINGi9606.ENSP00000217121.

Structurei

3D structure databases

ProteinModelPortaliO43399.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili38 – 8245Sequence AnalysisAdd
BLAST

Sequence similaritiesi

Belongs to the TPD52 family.Curated

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiNOG329468.
GeneTreeiENSGT00390000015988.
HOGENOMiHOG000231968.
HOVERGENiHBG058643.
InParanoidiO43399.
OMAiRARPFSH.
OrthoDBiEOG744TBQ.
PhylomeDBiO43399.
TreeFamiTF317562.

Family and domain databases

InterProiIPR007327. TPD52.
[Graphical view]
PANTHERiPTHR19307. PTHR19307. 1 hit.
PfamiPF04201. TPD52. 1 hit.
[Graphical view]

Sequences (7)i

Sequence statusi: Complete.

This entry describes 7 isoformsi produced by alternative splicing. Align

Note: Additional isoforms seem to exist.

Isoform 1 (identifier: O43399-1) [UniParc]FASTAAdd to Basket

Also known as: HD54+ins2

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
MDSAGQDINL NSPNKGLLSD SMTDVPVDTG VAARTPAVEG LTEAEEEELR
60 70 80 90 100
AELTKVEEEI VTLRQVLAAK ERHCGELKRR LGLSTLGELK QNLSRSWHDV
110 120 130 140 150
QVSSAYVKTS EKLGEWNEKV TQSDLYKKTQ ETLSQAGQKT SAALSTVGSA
160 170 180 190 200
ISRKLGDMRN SATFKSFEDR VGTIKSKVVG DRENGSDNLP SSAGSGDKPL

SDPAPF
Length:206
Mass (Da):22,238
Last modified:January 23, 2002 - v2
Checksum:i58F01BC67B1E3DE9
GO
Isoform 2 (identifier: O43399-2) [UniParc]FASTAAdd to Basket

Also known as: HD54-ins2

The sequence of this isoform differs from the canonical sequence as follows:
     106-125: Missing.

Show »
Length:186
Mass (Da):19,901
Checksum:i002CD68479D8250C
GO
Isoform 3 (identifier: O43399-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     106-125: Missing.
     159-159: R → RAHPFSHSFSSYSIRHSISMPAMR

Show »
Length:209
Mass (Da):22,517
Checksum:i5087B635B9155443
GO
Isoform 4 (identifier: O43399-4) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     106-125: Missing.
     157-157: D → DMSSYSIRHSISMPA

Show »
Length:200
Mass (Da):21,450
Checksum:i9BAD0A523C8F14DB
GO
Isoform 5 (identifier: O43399-5) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     157-157: D → DMSSYSIRHSISMPA

Note: No experimental confirmation available.

Show »
Length:220
Mass (Da):23,787
Checksum:i0A47C22C7C285FFF
GO
Isoform 6 (identifier: O43399-6) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     7-29: Missing.
     106-125: Missing.

Show »
Length:163
Mass (Da):17,473
Checksum:i1CF34D45DF97AABC
GO
Isoform 7 (identifier: O43399-7) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     157-157: D → DMRAHPFSHSFSSYSIRHSISMPA

Note: No experimental confirmation available.

Show »
Length:229
Mass (Da):24,854
Checksum:i0AF18A6C7059BE30
GO

Sequence cautioni

The sequence BU165202 differs from that shown. Reason: Frameshift at positions 155, 157, 173 and 188.

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti72 – 721R → K in AAC98478. (PubMed:9838088)Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei7 – 2923Missing in isoform 6. 1 PublicationVSP_045154Add
BLAST
Alternative sequencei106 – 12520Missing in isoform 2, isoform 3, isoform 4 and isoform 6. 1 PublicationVSP_006547Add
BLAST
Alternative sequencei157 – 1571D → DMSSYSIRHSISMPA in isoform 4 and isoform 5. 2 PublicationsVSP_038361
Alternative sequencei157 – 1571D → DMRAHPFSHSFSSYSIRHSI SMPA in isoform 7. 1 PublicationVSP_047409
Alternative sequencei159 – 1591R → RAHPFSHSFSSYSIRHSISM PAMR in isoform 3. CuratedVSP_036756

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF004429 mRNA. Translation: AAC98477.1.
AF004430 mRNA. Translation: AAC98478.1.
AK055068 mRNA. Translation: BAG51460.1.
AK298366 mRNA. Translation: BAG60608.1.
BT019631 mRNA. Translation: AAV38437.1.
AL118506 Genomic DNA. Translation: CAC15492.1.
AL118506 Genomic DNA. Translation: CAI21899.1.
AL118506 Genomic DNA. Translation: CAI21900.1.
AL118506 Genomic DNA. Translation: CAI21902.1.
CH471077 Genomic DNA. Translation: EAW75195.1.
CH471077 Genomic DNA. Translation: EAW75197.1.
CH471077 Genomic DNA. Translation: EAW75198.1.
CH471077 Genomic DNA. Translation: EAW75199.1.
CH471077 Genomic DNA. Translation: EAW75201.1.
BC006804 mRNA. Translation: AAH06804.1.
BU165202 mRNA. No translation available.
CCDSiCCDS13540.1. [O43399-1]
CCDS13541.1. [O43399-2]
CCDS13542.1. [O43399-7]
CCDS13543.1. [O43399-3]
CCDS13544.1. [O43399-5]
CCDS13545.1. [O43399-4]
CCDS58785.1. [O43399-6]
RefSeqiNP_001230821.1. NM_001243892.1. [O43399-6]
NP_003279.2. NM_003288.3. [O43399-1]
NP_955392.1. NM_199360.2. [O43399-7]
NP_955393.1. NM_199361.2. [O43399-3]
NP_955394.1. NM_199362.2. [O43399-5]
NP_955395.1. NM_199363.2. [O43399-4]
UniGeneiHs.473296.

Genome annotation databases

EnsembliENST00000217121; ENSP00000217121; ENSG00000101150. [O43399-7]
ENST00000346249; ENSP00000343547; ENSG00000101150. [O43399-1]
ENST00000348257; ENSP00000343554; ENSG00000101150. [O43399-2]
ENST00000351424; ENSP00000340006; ENSG00000101150. [O43399-3]
ENST00000352482; ENSP00000344647; ENSG00000101150. [O43399-5]
ENST00000358548; ENSP00000351350; ENSG00000101150. [O43399-4]
ENST00000369927; ENSP00000358943; ENSG00000101150. [O43399-6]
GeneIDi7165.
KEGGihsa:7165.
UCSCiuc002ygy.3. human.
uc002ygz.3. human. [O43399-5]
uc002yha.3. human. [O43399-3]
uc002yhb.3. human. [O43399-4]
uc002yhc.3. human. [O43399-1]
uc011abl.2. human.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF004429 mRNA. Translation: AAC98477.1 .
AF004430 mRNA. Translation: AAC98478.1 .
AK055068 mRNA. Translation: BAG51460.1 .
AK298366 mRNA. Translation: BAG60608.1 .
BT019631 mRNA. Translation: AAV38437.1 .
AL118506 Genomic DNA. Translation: CAC15492.1 .
AL118506 Genomic DNA. Translation: CAI21899.1 .
AL118506 Genomic DNA. Translation: CAI21900.1 .
AL118506 Genomic DNA. Translation: CAI21902.1 .
CH471077 Genomic DNA. Translation: EAW75195.1 .
CH471077 Genomic DNA. Translation: EAW75197.1 .
CH471077 Genomic DNA. Translation: EAW75198.1 .
CH471077 Genomic DNA. Translation: EAW75199.1 .
CH471077 Genomic DNA. Translation: EAW75201.1 .
BC006804 mRNA. Translation: AAH06804.1 .
BU165202 mRNA. No translation available.
CCDSi CCDS13540.1. [O43399-1 ]
CCDS13541.1. [O43399-2 ]
CCDS13542.1. [O43399-7 ]
CCDS13543.1. [O43399-3 ]
CCDS13544.1. [O43399-5 ]
CCDS13545.1. [O43399-4 ]
CCDS58785.1. [O43399-6 ]
RefSeqi NP_001230821.1. NM_001243892.1. [O43399-6 ]
NP_003279.2. NM_003288.3. [O43399-1 ]
NP_955392.1. NM_199360.2. [O43399-7 ]
NP_955393.1. NM_199361.2. [O43399-3 ]
NP_955394.1. NM_199362.2. [O43399-5 ]
NP_955395.1. NM_199363.2. [O43399-4 ]
UniGenei Hs.473296.

3D structure databases

ProteinModelPortali O43399.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 113018. 51 interactions.
IntActi O43399. 8 interactions.
STRINGi 9606.ENSP00000217121.

PTM databases

PhosphoSitei O43399.

2D gel databases

OGPi O43399.

Proteomic databases

MaxQBi O43399.
PaxDbi O43399.
PRIDEi O43399.

Protocols and materials databases

DNASUi 7165.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000217121 ; ENSP00000217121 ; ENSG00000101150 . [O43399-7 ]
ENST00000346249 ; ENSP00000343547 ; ENSG00000101150 . [O43399-1 ]
ENST00000348257 ; ENSP00000343554 ; ENSG00000101150 . [O43399-2 ]
ENST00000351424 ; ENSP00000340006 ; ENSG00000101150 . [O43399-3 ]
ENST00000352482 ; ENSP00000344647 ; ENSG00000101150 . [O43399-5 ]
ENST00000358548 ; ENSP00000351350 ; ENSG00000101150 . [O43399-4 ]
ENST00000369927 ; ENSP00000358943 ; ENSG00000101150 . [O43399-6 ]
GeneIDi 7165.
KEGGi hsa:7165.
UCSCi uc002ygy.3. human.
uc002ygz.3. human. [O43399-5 ]
uc002yha.3. human. [O43399-3 ]
uc002yhb.3. human. [O43399-4 ]
uc002yhc.3. human. [O43399-1 ]
uc011abl.2. human.

Organism-specific databases

CTDi 7165.
GeneCardsi GC20P062490.
HGNCi HGNC:12007. TPD52L2.
HPAi HPA047489.
MIMi 603747. gene.
neXtProti NX_O43399.
PharmGKBi PA36688.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG329468.
GeneTreei ENSGT00390000015988.
HOGENOMi HOG000231968.
HOVERGENi HBG058643.
InParanoidi O43399.
OMAi RARPFSH.
OrthoDBi EOG744TBQ.
PhylomeDBi O43399.
TreeFami TF317562.

Enzyme and pathway databases

SignaLinki O43399.

Miscellaneous databases

ChiTaRSi TPD52L2. human.
GeneWikii TPD52L2.
GenomeRNAii 7165.
NextBioi 28048.
PROi O43399.
SOURCEi Search...

Gene expression databases

Bgeei O43399.
CleanExi HS_TPD52L2.
ExpressionAtlasi O43399. baseline and differential.
Genevestigatori O43399.

Family and domain databases

InterProi IPR007327. TPD52.
[Graphical view ]
PANTHERi PTHR19307. PTHR19307. 1 hit.
Pfami PF04201. TPD52. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning of a third member of the D52 gene family indicates alternative coding sequence usage in D52-like transcripts."
    Nourse C.R., Mattei M.-G., Gunning P., Byrne J.A.
    Biochim. Biophys. Acta 1443:155-168(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), ALTERNATIVE SPLICING.
    Tissue: Mammary gland.
  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] (ISOFORMS 4 AND 6).
    Tissue: Brain and Kidney.
  3. "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
    Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
    Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 5).
  4. "The DNA sequence and comparative analysis of human chromosome 20."
    Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R., Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L., Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P., Bird C.P., Blakey S.E.
    , Bridgeman A.M., Brown A.J., Buck D., Burrill W.D., Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G., Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E., Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D., Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P., Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E., Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J., Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D., Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S., Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D., Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A., Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T., Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I., Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M., Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D., Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M., Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A., Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L., Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L., Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.
    Nature 414:865-871(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. "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 7).
    Tissue: Placenta and Retinoblastoma.
  7. "Identification of MAL2, a novel member of the mal proteolipid family, though interactions with TPD52-like proteins in the yeast two-hybrid system."
    Wilson S.H.D., Bailey A.M., Nourse C.R., Mattei M.-G., Byrne J.A.
    Genomics 76:81-88(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH MAL2.
  8. "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-12 AND SER-166, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  9. "Phosphorylation analysis of primary human T lymphocytes using sequential IMAC and titanium oxide enrichment."
    Carrascal M., Ovelleiro D., Casas V., Gay M., Abian J.
    J. Proteome Res. 7:5167-5176(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-166, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: T-cell.
  10. "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-12 AND SER-166, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  11. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-3; SER-12; SER-96 AND SER-166, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  12. "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: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  13. "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 SER-96; SER-149 AND SER-166, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  14. "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 MET-1, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-12; SER-19; SER-21; SER-96 AND SER-166, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  15. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  16. "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: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-3; SER-12 AND SER-166, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  17. "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].
  18. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiTPD54_HUMAN
AccessioniPrimary (citable) accession number: O43399
Secondary accession number(s): B4DPJ6
, E1P5G7, O43398, Q5JWU5, Q5JWU6, Q5JWU8, Q5U0E0, Q9H3Z6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 24, 2001
Last sequence update: January 23, 2002
Last modified: October 29, 2014
This is version 135 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, Reference proteome

Documents

  1. Human chromosome 20
    Human chromosome 20: 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

External Data

Dasty 3