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O43399 (TPD54_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 132. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Tumor protein D54

Short name=hD54
Alternative name(s):
Tumor protein D52-like 2
Gene names
Name:TPD52L2
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length206 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Subunit structure

Forms a homodimer or heterodimer with other members of the family By similarity. Interacts with MAL2. Ref.7

Sequence similarities

Belongs to the TPD52 family.

Sequence caution

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

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Tpd52Q623932EBI-782616,EBI-782591From a different organism.

Alternative products

This entry describes 7 isoforms produced by alternative splicing. [Align] [Select]

Note: Additional isoforms seem to exist.
Isoform 1 (identifier: O43399-1)

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.
Isoform 2 (identifier: O43399-2)

Also known as: HD54-ins2;

The sequence of this isoform differs from the canonical sequence as follows:
     106-125: Missing.
Isoform 3 (identifier: O43399-3)

The sequence of this isoform differs from the canonical sequence as follows:
     106-125: Missing.
     159-159: R → RAHPFSHSFSSYSIRHSISMPAMR
Isoform 4 (identifier: O43399-4)

The sequence of this isoform differs from the canonical sequence as follows:
     106-125: Missing.
     157-157: D → DMSSYSIRHSISMPA
Isoform 5 (identifier: O43399-5)

The sequence of this isoform differs from the canonical sequence as follows:
     157-157: D → DMSSYSIRHSISMPA
Note: No experimental confirmation available.
Isoform 6 (identifier: O43399-6)

The sequence of this isoform differs from the canonical sequence as follows:
     7-29: Missing.
     106-125: Missing.
Isoform 7 (identifier: O43399-7)

The sequence of this isoform differs from the canonical sequence as follows:
     157-157: D → DMRAHPFSHSFSSYSIRHSISMPA
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 206206Tumor protein D54
PRO_0000185744

Regions

Coiled coil38 – 8245 Potential

Amino acid modifications

Modified residue11N-acetylmethionine Ref.12 Ref.14 Ref.16 Ref.17
Modified residue31Phosphoserine Ref.11 Ref.16
Modified residue121Phosphoserine Ref.8 Ref.10 Ref.11 Ref.14 Ref.16
Modified residue191Phosphoserine Ref.14
Modified residue211Phosphoserine Ref.14
Modified residue961Phosphoserine Ref.11 Ref.13 Ref.14
Modified residue1491Phosphoserine Ref.13
Modified residue1661Phosphoserine Ref.8 Ref.9 Ref.10 Ref.11 Ref.13 Ref.14 Ref.16
Modified residue1921Phosphoserine By similarity

Natural variations

Alternative sequence7 – 2923Missing in isoform 6.
VSP_045154
Alternative sequence106 – 12520Missing in isoform 2, isoform 3, isoform 4 and isoform 6.
VSP_006547
Alternative sequence1571D → DMSSYSIRHSISMPA in isoform 4 and isoform 5.
VSP_038361
Alternative sequence1571D → DMRAHPFSHSFSSYSIRHSI SMPA in isoform 7.
VSP_047409
Alternative sequence1591R → RAHPFSHSFSSYSIRHSISM PAMR in isoform 3.
VSP_036756

Experimental info

Sequence conflict721R → K in AAC98478. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (HD54+ins2) [UniParc].

Last modified January 23, 2002. Version 2.
Checksum: 58F01BC67B1E3DE9

FASTA20622,238
        10         20         30         40         50         60 
MDSAGQDINL NSPNKGLLSD SMTDVPVDTG VAARTPAVEG LTEAEEEELR AELTKVEEEI 

        70         80         90        100        110        120 
VTLRQVLAAK ERHCGELKRR LGLSTLGELK QNLSRSWHDV QVSSAYVKTS EKLGEWNEKV 

       130        140        150        160        170        180 
TQSDLYKKTQ ETLSQAGQKT SAALSTVGSA ISRKLGDMRN SATFKSFEDR VGTIKSKVVG 

       190        200 
DRENGSDNLP SSAGSGDKPL SDPAPF 

« Hide

Isoform 2 (HD54-ins2) [UniParc].

Checksum: 002CD68479D8250C
Show »

FASTA18619,901
Isoform 3 [UniParc].

Checksum: 5087B635B9155443
Show »

FASTA20922,517
Isoform 4 [UniParc].

Checksum: 9BAD0A523C8F14DB
Show »

FASTA20021,450
Isoform 5 [UniParc].

Checksum: 0A47C22C7C285FFF
Show »

FASTA22023,787
Isoform 6 [UniParc].

Checksum: 1CF34D45DF97AABC
Show »

FASTA16317,473
Isoform 7 [UniParc].

Checksum: 0AF18A6C7059BE30
Show »

FASTA22924,854

References

« Hide 'large scale' references
[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. expand/collapse author list , 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. expand/collapse author list , 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]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
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]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
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]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
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]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS13540.1. [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]
RefSeqNP_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]
UniGeneHs.473296.

3D structure databases

ProteinModelPortalO43399.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid113018. 46 interactions.
IntActO43399. 8 interactions.
STRING9606.ENSP00000217121.

PTM databases

PhosphoSiteO43399.

2D gel databases

OGPO43399.

Proteomic databases

MaxQBO43399.
PaxDbO43399.
PRIDEO43399.

Protocols and materials databases

DNASU7165.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000217121; 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]
GeneID7165.
KEGGhsa:7165.
UCSCuc002ygz.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

CTD7165.
GeneCardsGC20P062490.
HGNCHGNC:12007. TPD52L2.
HPAHPA047489.
MIM603747. gene.
neXtProtNX_O43399.
PharmGKBPA36688.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG329468.
HOGENOMHOG000231968.
HOVERGENHBG058643.
OMARARPFSH.
OrthoDBEOG744TBQ.
PhylomeDBO43399.
TreeFamTF317562.

Enzyme and pathway databases

SignaLinkO43399.

Gene expression databases

ArrayExpressO43399.
BgeeO43399.
CleanExHS_TPD52L2.
GenevestigatorO43399.

Family and domain databases

InterProIPR007327. TPD52.
[Graphical view]
PANTHERPTHR19307. PTHR19307. 1 hit.
PfamPF04201. TPD52. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSTPD52L2. human.
GeneWikiTPD52L2.
GenomeRNAi7165.
NextBio28048.
PROO43399.
SOURCESearch...

Entry information

Entry nameTPD54_HUMAN
AccessionPrimary (citable) accession number: O43399
Secondary accession number(s): B4DPJ6 expand/collapse secondary AC list , E1P5G7, O43398, Q5JWU5, Q5JWU6, Q5JWU8, Q5U0E0, Q9H3Z6
Entry history
Integrated into UniProtKB/Swiss-Prot: January 24, 2001
Last sequence update: January 23, 2002
Last modified: July 9, 2014
This is version 132 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 20

Human chromosome 20: entries, gene names and cross-references to MIM