SubmitCancel

Skip Header

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

Q9NRN7

- ADPPT_HUMAN

UniProt

Q9NRN7 - ADPPT_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

L-aminoadipate-semialdehyde dehydrogenase-phosphopantetheinyl transferase

Gene
AASDHPPT, CGI-80, HAH-P, HSPC223, x0005
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Catalyzes the post-translational modification of target proteins by phosphopantetheine. Can transfer the 4'-phosphopantetheine moiety from coenzyme A to a serine residue of a broad range of acceptors, such as the acyl carrier domain of FASN.3 Publications

Catalytic activityi

CoA-[4'-phosphopantetheine] + apo-[acyl-carrier-protein] = adenosine 3',5'-bisphosphate + holo-[acyl-carrier-protein].

Cofactori

Binds 1 magnesium ion.2 Publications

Kineticsi

  1. KM=0.44 mM for magnesium1 Publication
  2. KM=0.025 mM for coenzyme A

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei47 – 471Coenzyme A
Metal bindingi129 – 1291Magnesium
Metal bindingi181 – 1811Magnesium

GO - Molecular functioni

  1. holo-[acyl-carrier-protein] synthase activity Source: UniProtKB
  2. magnesium ion binding Source: UniProtKB
  3. protein binding Source: UniProtKB

GO - Biological processi

  1. macromolecule biosynthetic process Source: InterPro
  2. pantothenate metabolic process Source: Reactome
  3. small molecule metabolic process Source: Reactome
  4. vitamin metabolic process Source: Reactome
  5. water-soluble vitamin metabolic process Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Transferase

Keywords - Ligandi

Magnesium, Metal-binding

Enzyme and pathway databases

BioCyciMetaCyc:HS14278-MONOMER.
ReactomeiREACT_11172. Vitamin B5 (pantothenate) metabolism.
SABIO-RKQ9NRN7.

Names & Taxonomyi

Protein namesi
Recommended name:
L-aminoadipate-semialdehyde dehydrogenase-phosphopantetheinyl transferase (EC:2.7.8.-)
Alternative name(s):
4'-phosphopantetheinyl transferase
Alpha-aminoadipic semialdehyde dehydrogenase-phosphopantetheinyl transferase
Short name:
AASD-PPT
LYS5 ortholog
Gene namesi
ORF Names:CGI-80, HAH-P, HSPC223, x0005
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 11

Organism-specific databases

HGNCiHGNC:14235. AASDHPPT.

Subcellular locationi

Cytoplasm 1 Publication

GO - Cellular componenti

  1. cytosol Source: Reactome
  2. extracellular vesicular exosome Source: UniProt
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi47 – 471R → A: Reduces affinity for magnesium 7-fold, and enzyme activity 2-fold. 1 Publication
Mutagenesisi86 – 861R → A: Reduces affinity for magnesium and coenzyme A, and reduces enzyme activity 7-fold. 1 Publication
Mutagenesisi111 – 1111H → A: Reduces affinity for magnesium 75-fold, and enzyme activity 150-fold. 1 Publication
Mutagenesisi112 – 1121Q → E: Reduces affinity for magnesium 200-fold and abolishes enzyme activity; when associated with Q-181. 1 Publication
Mutagenesisi129 – 1291D → A: Reduces affinity for magnesium 10-fold, and enzyme activity 30000-fold. 1 Publication
Mutagenesisi181 – 1811E → A: Reduces affinity for magnesium 40-fold, and enzyme activity 32000-fold. 1 Publication
Mutagenesisi181 – 1811E → Q: Reduces affinity for magnesium 20-fold, and enzyme activity 6500-fold. 1 Publication
Mutagenesisi185 – 1851K → A: Reduces enzyme activity 2000-fold, with only minor change in the affinity for magnesium and coenzyme A. 1 Publication

Organism-specific databases

PharmGKBiPA24368.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 309309L-aminoadipate-semialdehyde dehydrogenase-phosphopantetheinyl transferasePRO_0000175736Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei258 – 2581Phosphoserine3 Publications

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ9NRN7.
PaxDbiQ9NRN7.
PeptideAtlasiQ9NRN7.
PRIDEiQ9NRN7.

PTM databases

PhosphoSiteiQ9NRN7.

Expressioni

Tissue specificityi

Detected in heart, skeletal muscle, placenta, testis, brain, pancreas, liver and kidney.2 Publications

Gene expression databases

ArrayExpressiQ9NRN7.
BgeeiQ9NRN7.
CleanExiHS_AASDHPPT.
GenevestigatoriQ9NRN7.

Organism-specific databases

HPAiHPA026687.

Interactioni

Subunit structurei

Monomer. Interacts with FASN.1 Publication

Protein-protein interaction databases

BioGridi121927. 16 interactions.
IntActiQ9NRN7. 6 interactions.
MINTiMINT-5005661.
STRINGi9606.ENSP00000278618.

Structurei

Secondary structure

1
309
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi17 – 215
Helixi23 – 253
Helixi30 – 389
Helixi42 – 498
Helixi54 – 7421
Helixi79 – 813
Beta strandi84 – 863
Beta strandi92 – 943
Beta strandi102 – 1043
Beta strandi106 – 1127
Beta strandi115 – 13218
Beta strandi137 – 1393
Helixi141 – 1477
Helixi149 – 1513
Helixi154 – 1607
Beta strandi163 – 1653
Helixi166 – 18722
Helixi190 – 1923
Helixi195 – 1973
Beta strandi198 – 2014
Beta strandi203 – 2064
Beta strandi217 – 2204
Beta strandi228 – 2369
Beta strandi239 – 2468
Beta strandi270 – 2723
Helixi274 – 2774
Turni278 – 2803
Helixi289 – 2913
Helixi298 – 3003
Turni305 – 3073

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2BYDX-ray2.00A14-309[»]
2C43X-ray1.93A14-309[»]
2CG5X-ray2.70A14-309[»]
ProteinModelPortaliQ9NRN7.
SMRiQ9NRN7. Positions 14-289.

Miscellaneous databases

EvolutionaryTraceiQ9NRN7.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni86 – 916Coenzyme A binding
Regioni108 – 1114Coenzyme A binding
Regioni181 – 1855Coenzyme A binding

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG2091.
HOGENOMiHOG000265195.
HOVERGENiHBG080822.
InParanoidiQ9NRN7.
KOiK06133.
OMAiSPRGKPY.
PhylomeDBiQ9NRN7.
TreeFamiTF313753.

Family and domain databases

Gene3Di3.90.470.20. 2 hits.
InterProiIPR008278. 4-PPantetheinyl_Trfase_SF.
[Graphical view]
PfamiPF01648. ACPS. 1 hit.
[Graphical view]
SUPFAMiSSF56214. SSF56214. 2 hits.

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q9NRN7-1) [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

MVFPAKRFCL VPSMEGVRWA FSCGTWLPSR AEWLLAVRSI QPEEKERIGQ    50
FVFARDAKAA MAGRLMIRKL VAEKLNIPWN HIRLQRTAKG KPVLAKDSSN 100
PYPNFNFNIS HQGDYAVLAA EPELQVGIDI MKTSFPGRGS IPEFFHIMKR 150
KFTNKEWETI RSFKDEWTQL DMFYRNWALK ESFIKAIGVG LGFELQRLEF 200
DLSPLNLDIG QVYKETRLFL DGEEEKEWAF EESKIDEHHF VAVALRKPDG 250
SRHQDVPSQD DSKPTQRQFT ILNFNDLMSS AVPMTPEDPS FWDCFCFTEE 300
IPIRNGTKS 309
Length:309
Mass (Da):35,776
Last modified:November 8, 2005 - v2
Checksum:i6263E302600FDDED
GO
Isoform 2 (identifier: Q9NRN7-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     138-138: R → T
     139-309: Missing.

Note: No experimental confirmation available.

Show »
Length:138
Mass (Da):15,574
Checksum:iEBB854D6A68B6AAC
GO

Sequence cautioni

The sequence AAD34075.1 differs from that shown. Reason: Frameshift at positions 34 and 63.
The sequence AAF86879.1 differs from that shown. Reason: Erroneous initiation.

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei138 – 1381R → T in isoform 2. VSP_055783
Alternative sequencei139 – 309171Missing in isoform 2. VSP_055784Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti136 – 1416PGRGSI → FQVVVQF in AAG49439. 1 Publication
Sequence conflicti307 – 3093TKS → YKVMMIP in AAG49439. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF302110 mRNA. Translation: AAG30872.1.
AF151838 mRNA. Translation: AAD34075.1. Frameshift.
AF151057 mRNA. Translation: AAF36143.1.
AF136978 mRNA. Translation: AAG49439.1.
AF201943 mRNA. Translation: AAF86879.1. Different initiation.
AK312529 mRNA. Translation: BAG35428.1.
AK293362 mRNA. Translation: BAG56878.1.
AP001001 Genomic DNA. No translation available.
CH471065 Genomic DNA. Translation: EAW67078.1.
BC015470 mRNA. Translation: AAH15470.1.
BC016728 mRNA. Translation: AAH16728.1.
AL050073 mRNA. Translation: CAB43257.1.
CCDSiCCDS31664.1.
PIRiT08733.
RefSeqiNP_056238.2. NM_015423.2.
UniGeneiHs.524009.

Genome annotation databases

EnsembliENST00000278618; ENSP00000278618; ENSG00000149313.
ENST00000525660; ENSP00000437144; ENSG00000149313.
GeneIDi60496.
KEGGihsa:60496.
UCSCiuc001pjc.1. human.

Polymorphism databases

DMDMi81170356.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF302110 mRNA. Translation: AAG30872.1 .
AF151838 mRNA. Translation: AAD34075.1 . Frameshift.
AF151057 mRNA. Translation: AAF36143.1 .
AF136978 mRNA. Translation: AAG49439.1 .
AF201943 mRNA. Translation: AAF86879.1 . Different initiation.
AK312529 mRNA. Translation: BAG35428.1 .
AK293362 mRNA. Translation: BAG56878.1 .
AP001001 Genomic DNA. No translation available.
CH471065 Genomic DNA. Translation: EAW67078.1 .
BC015470 mRNA. Translation: AAH15470.1 .
BC016728 mRNA. Translation: AAH16728.1 .
AL050073 mRNA. Translation: CAB43257.1 .
CCDSi CCDS31664.1.
PIRi T08733.
RefSeqi NP_056238.2. NM_015423.2.
UniGenei Hs.524009.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2BYD X-ray 2.00 A 14-309 [» ]
2C43 X-ray 1.93 A 14-309 [» ]
2CG5 X-ray 2.70 A 14-309 [» ]
ProteinModelPortali Q9NRN7.
SMRi Q9NRN7. Positions 14-289.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 121927. 16 interactions.
IntActi Q9NRN7. 6 interactions.
MINTi MINT-5005661.
STRINGi 9606.ENSP00000278618.

PTM databases

PhosphoSitei Q9NRN7.

Polymorphism databases

DMDMi 81170356.

Proteomic databases

MaxQBi Q9NRN7.
PaxDbi Q9NRN7.
PeptideAtlasi Q9NRN7.
PRIDEi Q9NRN7.

Protocols and materials databases

DNASUi 60496.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000278618 ; ENSP00000278618 ; ENSG00000149313 .
ENST00000525660 ; ENSP00000437144 ; ENSG00000149313 .
GeneIDi 60496.
KEGGi hsa:60496.
UCSCi uc001pjc.1. human.

Organism-specific databases

CTDi 60496.
GeneCardsi GC11P105982.
HGNCi HGNC:14235. AASDHPPT.
HPAi HPA026687.
MIMi 607756. gene.
neXtProti NX_Q9NRN7.
PharmGKBi PA24368.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG2091.
HOGENOMi HOG000265195.
HOVERGENi HBG080822.
InParanoidi Q9NRN7.
KOi K06133.
OMAi SPRGKPY.
PhylomeDBi Q9NRN7.
TreeFami TF313753.

Enzyme and pathway databases

BioCyci MetaCyc:HS14278-MONOMER.
Reactomei REACT_11172. Vitamin B5 (pantothenate) metabolism.
SABIO-RK Q9NRN7.

Miscellaneous databases

EvolutionaryTracei Q9NRN7.
GeneWikii AASDHPPT.
GenomeRNAii 60496.
NextBioi 65403.
PROi Q9NRN7.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q9NRN7.
Bgeei Q9NRN7.
CleanExi HS_AASDHPPT.
Genevestigatori Q9NRN7.

Family and domain databases

Gene3Di 3.90.470.20. 2 hits.
InterProi IPR008278. 4-PPantetheinyl_Trfase_SF.
[Graphical view ]
Pfami PF01648. ACPS. 1 hit.
[Graphical view ]
SUPFAMi SSF56214. SSF56214. 2 hits.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Identification of the alpha-aminoadipic semialdehyde dehydrogenase-phosphopantetheinyl transferase gene, the human ortholog of the yeast LYS5 gene."
    Praphanphoj V., Sacksteder K.A., Gould S.J., Thomas G.H., Geraghty M.T.
    Mol. Genet. Metab. 72:336-342(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, TISSUE SPECIFICITY.
  2. "Identification of novel human genes evolutionarily conserved in Caenorhabditis elegans by comparative proteomics."
    Lai C.-H., Chou C.-Y., Ch'ang L.-Y., Liu C.-S., Lin W.-C.
    Genome Res. 10:703-713(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
  3. "Cloning and functional analysis of cDNAs with open reading frames for 300 previously undefined genes expressed in CD34+ hematopoietic stem/progenitor cells."
    Zhang Q.-H., Ye M., Wu X.-Y., Ren S.-X., Zhao M., Zhao C.-J., Fu G., Shen Y., Fan H.-Y., Lu G., Zhong M., Xu X.-R., Han Z.-G., Zhang J.-W., Tao J., Huang Q.-H., Zhou J., Hu G.-X.
    , Gu J., Chen S.-J., Chen Z.
    Genome Res. 10:1546-1560(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Umbilical cord blood.
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Adrenal gland.
  5. "Novel genes expressed in human dendritic cell."
    Li N., Peng Y., Li Y., Gu W., Han Z., Fu G., Chen Z.
    Submitted (NOV-1999) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Dendritic cell.
  6. "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: Tongue and Urinary bladder.
  7. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  8. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  9. "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] (ISOFORM 1).
    Tissue: Urinary bladder and Uterus.
  10. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 99-309 (ISOFORM 1).
    Tissue: Kidney.
  11. Lubec G., Afjehi-Sadat L.
    Submitted (MAR-2007) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 235-246, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Brain and Cajal-Retzius cell.
  12. "Cloning, expression, and characterization of a human 4'-phosphopantetheinyl transferase with broad substrate specificity."
    Joshi A.K., Zhang L., Rangan V.S., Smith S.
    J. Biol. Chem. 278:33142-33149(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, COFACTOR, IDENTIFICATION BY MASS SPECTROMETRY, TISSUE SPECIFICITY.
  13. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-258, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic kidney.
  14. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-258, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  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-258, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  16. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  17. "Mechanism and substrate recognition of human holo ACP synthase."
    Bunkoczi G., Pasta S., Joshi A., Wu X., Kavanagh K.L., Smith S., Oppermann U.
    Chem. Biol. 14:1243-1253(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.93 ANGSTROMS) OF 14-309 IN COMPLEXES WITH COENZYME A; MAGNESIUM IONS AND FASN, FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, COFACTOR, MUTAGENESIS OF ARG-47; ARG-86; HIS-111; GLN-112; ASP-129; GLU-181 AND LYS-185.

Entry informationi

Entry nameiADPPT_HUMAN
AccessioniPrimary (citable) accession number: Q9NRN7
Secondary accession number(s): B2R6D1
, B4DDW7, Q9C068, Q9P0Q3, Q9UG80, Q9Y389
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 8, 2005
Last sequence update: November 8, 2005
Last modified: September 3, 2014
This is version 102 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. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi