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P05141 (ADT2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 163. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
ADP/ATP translocase 2
Alternative name(s):
ADP,ATP carrier protein 2
ADP,ATP carrier protein, fibroblast isoform
Adenine nucleotide translocator 2
Short name=ANT 2
Solute carrier family 25 member 5

Cleaved into the following chain:

  1. ADP/ATP translocase 2, N-terminally processed
Gene names
Name:SLC25A5
Synonyms:ANT2
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length298 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Catalyzes the exchange of cytoplasmic ADP with mitochondrial ATP across the mitochondrial inner membrane. As part of the mitotic spindle-associated MMXD complex it may play a role in chromosome segregation. Ref.13

Subunit structure

Homodimer. Component of the MMXD complex, which includes CIAO1, ERCC2, FAM96B, MMS19 and SLC25A5. Interacts with HIV-1 Vpr. Ref.10 Ref.13

Subcellular location

Mitochondrion inner membrane; Multi-pass membrane protein.

Miscellaneous

The transmembrane helices are not perpendicular to the plane of the membrane, but cross the membrane at an angle. Odd-numbered transmembrane helices exhibit a sharp kink, due to the presence of a conserved proline residue By similarity.

Sequence similarities

Belongs to the mitochondrial carrier (TC 2.A.29) family. [View classification]

Contains 3 Solcar repeats.

Ontologies

Keywords
   Biological processChromosome partition
Host-virus interaction
Transport
   Cellular componentMembrane
Mitochondrion
Mitochondrion inner membrane
   Coding sequence diversityPolymorphism
   DomainRepeat
Transmembrane
Transmembrane helix
   PTMAcetylation
Methylation
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processadenine transport

Traceable author statement Ref.1. Source: GOC

chromosome segregation

Inferred from electronic annotation. Source: UniProtKB-KW

energy reserve metabolic process

Traceable author statement. Source: Reactome

negative regulation of mitochondrial outer membrane permeabilization involved in apoptotic signaling pathway

Inferred from mutant phenotype PubMed 19154410. Source: UniProtKB

positive regulation of cell proliferation

Inferred from mutant phenotype PubMed 19154410. Source: UniProtKB

regulation of insulin secretion

Traceable author statement. Source: Reactome

small molecule metabolic process

Traceable author statement. Source: Reactome

transport

Traceable author statement Ref.1. Source: ProtInc

viral process

Traceable author statement. Source: Reactome

   Cellular_componentMMXD complex

Inferred from direct assay Ref.13. Source: UniProtKB

integral component of plasma membrane

Traceable author statement Ref.1. Source: ProtInc

mitochondrial inner membrane

Traceable author statement. Source: Reactome

mitochondrial nucleoid

Inferred from direct assay PubMed 18063578. Source: BHF-UCL

mitochondrion

Inferred from direct assay PubMed 20833797. Source: UniProt

   Molecular_functionadenine transmembrane transporter activity

Traceable author statement Ref.1. Source: ProtInc

poly(A) RNA binding

Inferred from direct assay PubMed 22658674. Source: UniProtKB

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

SIRT4Q9Y6E72EBI-355133,EBI-2606540
SLC35F6Q8N3572EBI-355133,EBI-713484

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 298298ADP/ATP translocase 2
PRO_0000423220
Initiator methionine11Removed; alternate Ref.7 Ref.8
Chain2 – 298297ADP/ATP translocase 2, N-terminally processed
PRO_0000090579

Regions

Transmembrane5 – 3935Helical; Name=1; By similarity
Transmembrane75 – 10026Helical; Name=2; By similarity
Transmembrane109 – 14335Helical; Name=3; By similarity
Transmembrane176 – 20227Helical; Name=4; By similarity
Transmembrane207 – 24135Helical; Name=5; By similarity
Transmembrane273 – 29826Helical; Name=6; By similarity
Repeat6 – 9893Solcar 1
Repeat111 – 20191Solcar 2
Repeat212 – 29786Solcar 3
Motif235 – 2406Substrate recognition By similarity

Sites

Binding site801Nucleotide By similarity

Amino acid modifications

Modified residue11N-acetylmethionine Ref.11
Modified residue21N-acetylthreonine; in ADP/ATP translocase 2, N-terminally processed Ref.7 Ref.8 Ref.11 Ref.16
Modified residue231N6-malonyllysine Ref.15
Modified residue431N6-succinyllysine By similarity
Modified residue521N6,N6-dimethyllysine; alternate Ref.8
Modified residue521N6-methyllysine; alternate Ref.8
Modified residue921N6-malonyllysine Ref.15
Modified residue961N6-malonyllysine Ref.15
Modified residue1051N6-acetyllysine; alternate Ref.12
Modified residue1051N6-succinyllysine; alternate By similarity
Modified residue1471N6-acetyllysine; alternate By similarity
Modified residue1471N6-malonyllysine; alternate Ref.15
Modified residue1471N6-succinyllysine; alternate By similarity
Modified residue1631N6-acetyllysine Ref.12
Modified residue1661N6-acetyllysine By similarity
Modified residue2681N6-acetyllysine; alternate By similarity
Modified residue2681N6-succinyllysine; alternate By similarity

Natural variations

Natural variant1111L → R. Ref.1 Ref.2 Ref.3 Ref.6
Corresponds to variant rs371749 [ dbSNP | Ensembl ].
VAR_030039

Experimental info

Sequence conflict61V → L in AAA35579. Ref.2
Sequence conflict431K → M in BAG37698. Ref.4
Sequence conflict661G → E in AAA35579. Ref.2
Sequence conflict1621V → G in AAA36749. Ref.9

Sequences

Sequence LengthMass (Da)Tools
P05141 [UniParc].

Last modified January 11, 2011. Version 7.
Checksum: DC53D083E7217AFE

FASTA29832,852
        10         20         30         40         50         60 
MTDAAVSFAK DFLAGGVAAA ISKTAVAPIE RVKLLLQVQH ASKQITADKQ YKGIIDCVVR 

        70         80         90        100        110        120 
IPKEQGVLSF WRGNLANVIR YFPTQALNFA FKDKYKQIFL GGVDKRTQFW LYFAGNLASG 

       130        140        150        160        170        180 
GAAGATSLCF VYPLDFARTR LAADVGKAGA EREFRGLGDC LVKIYKSDGI KGLYQGFNVS 

       190        200        210        220        230        240 
VQGIIIYRAA YFGIYDTAKG MLPDPKNTHI VISWMIAQTV TAVAGLTSYP FDTVRRRMMM 

       250        260        270        280        290 
QSGRKGTDIM YTGTLDCWRK IARDEGGKAF FKGAWSNVLR GMGGAFVLVL YDEIKKYT 

« Hide

References

« Hide 'large scale' references
[1]"The human fibroblast adenine nucleotide translocator gene. Molecular cloning and sequence."
Ku D.-H., Kagan J., Chen S.-T., Chang C.-D., Baserga R., Wurzel J.
J. Biol. Chem. 265:16060-16063(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT ARG-111.
Tissue: Placenta.
[2]"Molecular cloning of a cDNA for a human ADP/ATP carrier which is growth-regulated."
Battini R., Ferrari S., Kaczmarek L., Calabretta B., Chen S.T., Baserga R.
J. Biol. Chem. 262:4355-4358(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT ARG-111.
[3]"Ordered shotgun sequencing of a 135 kb Xq25 YAC containing ANT2 and four possible genes, including three confirmed by EST matches."
Chen C.N., Su Y., Baybayan P., Siruno A., Nagaraja R., Mazzarella R., Schlessinger D., Chen E.
Nucleic Acids Res. 24:4034-4041(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT ARG-111.
[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. 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].
Tissue: Brain.
[5]"The DNA sequence of the human X chromosome."
Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D., Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C. expand/collapse author list , Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S., Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S., Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D., Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H., McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K., Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D., Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R., Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A., Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F., Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S., Rogers J., Bentley D.R.
Nature 434:325-337(2005) [PubMed] [Europe PMC] [Abstract]
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], VARIANT ARG-111.
Tissue: Eye.
[7]Bienvenut W.V.
Submitted (OCT-2004) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 2-31; 34-43; 64-92; 141-147; 189-199 AND 273-296, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT THR-2, IDENTIFICATION BY MASS SPECTROMETRY.
Tissue: B-cell lymphoma.
[8]Bienvenut W.V., Waridel P., Quadroni M.
Submitted (MAR-2009) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 2-23; 32-43; 50-60; 64-92; 81-92; 97-106; 112-138; 172-199; 207-235; 245-259 AND 281-295, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT THR-2, METHYLATION AT LYS-52, IDENTIFICATION BY MASS SPECTROMETRY.
Tissue: Embryonic kidney.
[9]"Two distinct genes for ADP/ATP translocase are expressed at the mRNA level in adult human liver."
Houldsworth J., Attardi G.
Proc. Natl. Acad. Sci. U.S.A. 85:377-381(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 46-297.
Tissue: Liver.
[10]"Mitochondrial membrane permeabilization by HIV-1 Vpr."
Deniaud A., Brenner C., Kroemer G.
Mitochondrion 4:223-233(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH HIV-1 VPR.
[11]"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 AND THR-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[12]"Lysine acetylation targets protein complexes and co-regulates major cellular functions."
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-105 AND LYS-163, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[13]"MMXD, a TFIIH-independent XPD-MMS19 protein complex involved in chromosome segregation."
Ito S., Tan L.J., Andoh D., Narita T., Seki M., Hirano Y., Narita K., Kuraoka I., Hiraoka Y., Tanaka K.
Mol. Cell 39:632-640(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, IDENTIFICATION IN MMXD COMPLEX.
[14]"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].
[15]"The first identification of lysine malonylation substrates and its regulatory enzyme."
Peng C., Lu Z., Xie Z., Cheng Z., Chen Y., Tan M., Luo H., Zhang Y., He W., Yang K., Zwaans B.M., Tishkoff D., Ho L., Lombard D., He T.C., Dai J., Verdin E., Ye Y., Zhao Y.
Mol. Cell. Proteomics 10:M111.012658.01-M111.012658.12(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: MALONYLATION AT LYS-23; LYS-92; LYS-96 AND LYS-147.
[16]"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 THR-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M57424 Genomic DNA. Translation: AAA51737.1.
J02683 mRNA. Translation: AAA35579.1.
L78810 Genomic DNA. Translation: AAB39266.1.
AK315292 mRNA. Translation: BAG37698.1.
AC004000 Genomic DNA. Translation: AAB96347.1.
BC056160 mRNA. Translation: AAH56160.1.
J03591 mRNA. Translation: AAA36749.1.
PIRA29132.
RefSeqNP_001143.2. NM_001152.4.
UniGeneHs.632282.

3D structure databases

ProteinModelPortalP05141.
SMRP05141. Positions 2-294.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid106789. 103 interactions.
DIPDIP-33873N.
IntActP05141. 51 interactions.
MINTMINT-1162449.
STRING9606.ENSP00000360671.

Chemistry

DrugBankDB00720. Clodronate.

Protein family/group databases

TCDB2.A.29.1.1. the mitochondrial carrier (mc) family.

PTM databases

PhosphoSiteP05141.

Polymorphism databases

DMDM317373597.

Proteomic databases

PaxDbP05141.
PRIDEP05141.

Protocols and materials databases

DNASU292.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000317881; ENSP00000360671; ENSG00000005022.
GeneID292.
KEGGhsa:292.
UCSCuc004erh.4. human.

Organism-specific databases

CTD292.
GeneCardsGC0XP118602.
H-InvDBHIX0028379.
HGNCHGNC:10991. SLC25A5.
MIM300150. gene.
neXtProtNX_P05141.
PharmGKBPA35867.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG238123.
HOVERGENHBG108348.
InParanoidP05141.
KOK05863.
OMACFARTYK.
OrthoDBEOG7T1RBR.
PhylomeDBP05141.
TreeFamTF300743.

Enzyme and pathway databases

ReactomeREACT_111217. Metabolism.
REACT_116125. Disease.

Gene expression databases

ArrayExpressP05141.
BgeeP05141.
CleanExHS_SLC25A5.
GenevestigatorP05141.

Family and domain databases

Gene3D1.50.40.10. 1 hit.
InterProIPR002113. Aden_trnslctor.
IPR002067. Mit_carrier.
IPR018108. Mitochondrial_sb/sol_carrier.
IPR023395. Mt_carrier_dom.
[Graphical view]
PfamPF00153. Mito_carr. 3 hits.
[Graphical view]
PRINTSPR00927. ADPTRNSLCASE.
PR00926. MITOCARRIER.
SUPFAMSSF103506. SSF103506. 1 hit.
PROSITEPS50920. SOLCAR. 3 hits.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSSLC25A5. human.
GenomeRNAi292.
NextBio1191.
PROP05141.
SOURCESearch...

Entry information

Entry nameADT2_HUMAN
AccessionPrimary (citable) accession number: P05141
Secondary accession number(s): B2RCV1, O43350
Entry history
Integrated into UniProtKB/Swiss-Prot: August 13, 1987
Last sequence update: January 11, 2011
Last modified: April 16, 2014
This is version 163 of the entry and version 7 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 polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome X

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