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P49189

- AL9A1_HUMAN

UniProt

P49189 - AL9A1_HUMAN

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Protein

4-trimethylaminobutyraldehyde dehydrogenase

Gene

ALDH9A1

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

Functioni

Converts gamma-trimethylaminobutyraldehyde into gamma-butyrobetaine. Catalyzes the irreversible oxidation of a broad range of aldehydes to the corresponding acids in an NAD-dependent reaction.1 Publication

Catalytic activityi

4-trimethylammoniobutanal + NAD+ + H2O = 4-trimethylammoniobutanoate + NADH.
An aldehyde + NAD+ + H2O = a carboxylate + NADH.
4-aminobutanal + NAD+ + H2O = 4-aminobutanoate + NADH.

Kineticsi

  1. KM=11 µM for 4-aminobutyraldehyde

pH dependencei

Optimum pH is about 9.4 with propionaldehyde as substrate, and 7.5 with 4-aminobutyraldehyde as substrate.

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei157 – 1571Transition state stabilizerBy similarity
Active sitei254 – 2541Proton acceptorPROSITE-ProRule annotation
Active sitei288 – 2881NucleophilePROSITE-ProRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi232 – 2376NADBy similarity

GO - Molecular functioni

  1. 1-pyrroline dehydrogenase activity Source: UniProtKB-EC
  2. 3-chloroallyl aldehyde dehydrogenase activity Source: Reactome
  3. 4-trimethylammoniobutyraldehyde dehydrogenase activity Source: UniProtKB-EC
  4. aldehyde dehydrogenase (NAD) activity Source: UniProtKB
  5. amine binding Source: Ensembl
  6. aminobutyraldehyde dehydrogenase activity Source: UniProtKB
  7. NAD binding Source: Ensembl

GO - Biological processi

  1. carnitine biosynthetic process Source: Reactome
  2. cellular aldehyde metabolic process Source: UniProtKB
  3. cellular nitrogen compound metabolic process Source: Reactome
  4. hormone metabolic process Source: UniProtKB
  5. kidney development Source: Ensembl
  6. liver development Source: Ensembl
  7. neurotransmitter biosynthetic process Source: UniProtKB
  8. oxidation-reduction process Source: UniProtKB
  9. small molecule metabolic process Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

NAD

Enzyme and pathway databases

BioCyciMetaCyc:HS06992-MONOMER.
ReactomeiREACT_2125. Carnitine synthesis.
SABIO-RKP49189.
UniPathwayiUPA00118.

Names & Taxonomyi

Protein namesi
Recommended name:
4-trimethylaminobutyraldehyde dehydrogenase (EC:1.2.1.47)
Short name:
TMABADH
Alternative name(s):
Aldehyde dehydrogenase E3 isozyme
Aldehyde dehydrogenase family 9 member A1 (EC:1.2.1.3)
Gamma-aminobutyraldehyde dehydrogenase (EC:1.2.1.19)
R-aminobutyraldehyde dehydrogenase
Gene namesi
Name:ALDH9A1
Synonyms:ALDH4, ALDH7, ALDH9
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 1, UP000005640: Unplaced

Organism-specific databases

HGNCiHGNC:412. ALDH9A1.

Subcellular locationi

Cytoplasm By similarity

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB
  2. cytosol Source: Reactome
  3. extracellular vesicular exosome Source: UniProtKB
  4. mitochondrion Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA24706.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed4 Publications
Chaini2 – 4944934-trimethylaminobutyraldehyde dehydrogenasePRO_0000056485Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserine4 Publications
Modified residuei30 – 301N6-acetyllysine; alternateBy similarity
Modified residuei30 – 301N6-succinyllysine; alternateBy similarity
Modified residuei59 – 591N6-succinyllysineBy similarity
Modified residuei298 – 2981N6-acetyllysine1 Publication
Modified residuei303 – 3031N6-acetyllysine; alternateBy similarity
Modified residuei303 – 3031N6-succinyllysine; alternateBy similarity
Modified residuei344 – 3441N6-acetyllysineBy similarity

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiP49189.
PaxDbiP49189.
PRIDEiP49189.

2D gel databases

REPRODUCTION-2DPAGEIPI00479877.

PTM databases

PhosphoSiteiP49189.

Expressioni

Tissue specificityi

High expression in adult liver, skeletal muscle, and kidney. Low levels in heart, pancreas, lung and brain. Expressed in all regions of the brain. Expression levels are variable in the different brain areas, with the highest levels in the spinal cord and the lowest in the occipital pole.1 Publication

Developmental stagei

Strongly expressed in human embryonic brain (gestational age 12 weeks).

Gene expression databases

BgeeiP49189.
CleanExiHS_ALDH9A1.
ExpressionAtlasiP49189. baseline.
GenevestigatoriP49189.

Organism-specific databases

HPAiHPA006077.
HPA010873.

Interactioni

Subunit structurei

Homotetramer.

Protein-protein interaction databases

BioGridi106725. 15 interactions.
IntActiP49189. 5 interactions.
MINTiMINT-5006004.
STRINGi9606.ENSP00000346827.

Structurei

3D structure databases

ProteinModelPortaliP49189.
SMRiP49189. Positions 2-494.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the aldehyde dehydrogenase family.Curated

Phylogenomic databases

eggNOGiCOG1012.
HOVERGENiHBG000097.
InParanoidiP49189.
KOiK00149.
OrthoDBiEOG7327P4.
PhylomeDBiP49189.
TreeFamiTF314257.

Family and domain databases

Gene3Di3.40.309.10. 1 hit.
3.40.605.10. 1 hit.
InterProiIPR016161. Ald_DH/histidinol_DH.
IPR016163. Ald_DH_C.
IPR016160. Ald_DH_CS_CYS.
IPR029510. Ald_DH_CS_GLU.
IPR016162. Ald_DH_N.
IPR015590. Aldehyde_DH_dom.
[Graphical view]
PfamiPF00171. Aldedh. 1 hit.
[Graphical view]
SUPFAMiSSF53720. SSF53720. 1 hit.
PROSITEiPS00070. ALDEHYDE_DEHYDR_CYS. 1 hit.
PS00687. ALDEHYDE_DEHYDR_GLU. 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. Align

Isoform 1 (identifier: P49189-1) [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
MSTGTFVVSQ PLNYRGGARV EPADASGTEK AFEPATGRVI ATFTCSGEKE
60 70 80 90 100
VNLAVQNAKA AFKIWSQKSG MERCRILLEA ARIIREREDE IATMECINNG
110 120 130 140 150
KSIFEARLDI DISWQCLEYY AGLAASMAGE HIQLPGGSFG YTRREPLGVC
160 170 180 190 200
VGIGAWNYPF QIASWKSAPA LACGNAMVFK PSPFTPVSAL LLAEIYSEAG
210 220 230 240 250
VPPGLFNVVQ GGAATGQFLC QHPDVAKVSF TGSVPTGMKI MEMSAKGIKP
260 270 280 290 300
VTLELGGKSP LIIFSDCDMN NAVKGALMAN FLTQGQVCCN GTRVFVQKEI
310 320 330 340 350
LDKFTEEVVK QTQRIKIGDP LLEDTRMGPL INRPHLERVL GFVKVAKEQG
360 370 380 390 400
AKVLCGGDIY VPEDPKLKDG YYMRPCVLTN CRDDMTCVKE EIFGPVMSIL
410 420 430 440 450
SFDTEAEVLE RANDTTFGLA AGVFTRDIQR AHRVVAELQA GTCFINNYNV
460 470 480 490
SPVELPFGGY KKSGFGRENG RVTIEYYSQL KTVCVEMGDV ESAF
Length:494
Mass (Da):53,802
Last modified:February 1, 2005 - v3
Checksum:i1E1CDF910D763BA1
GO
Isoform 2 (identifier: P49189-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-70: Missing.

Note: No experimental confirmation available.

Show »
Length:424
Mass (Da):46,455
Checksum:i211F5F4B06E9B453
GO

Sequence cautioni

The sequence CAH74061.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti19 – 257RVEPADA → AGAGGR in AAB18827. (PubMed:8786138)Curated
Sequence conflicti150 – 1501C → Q AA sequence (PubMed:8269919)Curated
Sequence conflicti159 – 1591P → W AA sequence (PubMed:8269919)Curated
Sequence conflicti172 – 1721A → R AA sequence (PubMed:8269919)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti116 – 1161C → S in allele ALDH9A1*2. 2 Publications
VAR_011304

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 7070Missing in isoform 2. 1 PublicationVSP_056305Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U34252 mRNA. Translation: AAB18827.1.
AF172093 mRNA. Translation: AAF43600.1.
AK302183 mRNA. Translation: BAG63549.1.
AK302191 mRNA. Translation: BAG63554.1.
AK312751 mRNA. Translation: BAG35618.1.
AL451074 Genomic DNA. Translation: CAH74061.1. Different initiation.
U50203 mRNA. Translation: AAB06721.1.
X75425 mRNA. Translation: CAA53176.1.
PIRiG02054. S39532.
RefSeqiNP_000687.3. NM_000696.3.
UniGeneiHs.2533.

Genome annotation databases

EnsembliENST00000354775; ENSP00000346827; ENSG00000143149.
ENST00000538148; ENSP00000440026; ENSG00000143149.
GeneIDi223.
KEGGihsa:223.
UCSCiuc010pky.1. human. [P49189-1]

Polymorphism databases

DMDMi62511242.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U34252 mRNA. Translation: AAB18827.1 .
AF172093 mRNA. Translation: AAF43600.1 .
AK302183 mRNA. Translation: BAG63549.1 .
AK302191 mRNA. Translation: BAG63554.1 .
AK312751 mRNA. Translation: BAG35618.1 .
AL451074 Genomic DNA. Translation: CAH74061.1 . Different initiation.
U50203 mRNA. Translation: AAB06721.1 .
X75425 mRNA. Translation: CAA53176.1 .
PIRi G02054. S39532.
RefSeqi NP_000687.3. NM_000696.3.
UniGenei Hs.2533.

3D structure databases

ProteinModelPortali P49189.
SMRi P49189. Positions 2-494.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 106725. 15 interactions.
IntActi P49189. 5 interactions.
MINTi MINT-5006004.
STRINGi 9606.ENSP00000346827.

PTM databases

PhosphoSitei P49189.

Polymorphism databases

DMDMi 62511242.

2D gel databases

REPRODUCTION-2DPAGE IPI00479877.

Proteomic databases

MaxQBi P49189.
PaxDbi P49189.
PRIDEi P49189.

Protocols and materials databases

DNASUi 223.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000354775 ; ENSP00000346827 ; ENSG00000143149 .
ENST00000538148 ; ENSP00000440026 ; ENSG00000143149 .
GeneIDi 223.
KEGGi hsa:223.
UCSCi uc010pky.1. human. [P49189-1 ]

Organism-specific databases

CTDi 223.
GeneCardsi GC01M165632.
H-InvDB HIX0199965.
HGNCi HGNC:412. ALDH9A1.
HPAi HPA006077.
HPA010873.
MIMi 602733. gene.
neXtProti NX_P49189.
PharmGKBi PA24706.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG1012.
HOVERGENi HBG000097.
InParanoidi P49189.
KOi K00149.
OrthoDBi EOG7327P4.
PhylomeDBi P49189.
TreeFami TF314257.

Enzyme and pathway databases

UniPathwayi UPA00118 .
BioCyci MetaCyc:HS06992-MONOMER.
Reactomei REACT_2125. Carnitine synthesis.
SABIO-RK P49189.

Miscellaneous databases

ChiTaRSi ALDH9A1. human.
GeneWikii Aldehyde_dehydrogenase_9_family,_member_A1.
GenomeRNAii 223.
NextBioi 35476095.
PROi P49189.
SOURCEi Search...

Gene expression databases

Bgeei P49189.
CleanExi HS_ALDH9A1.
ExpressionAtlasi P49189. baseline.
Genevestigatori P49189.

Family and domain databases

Gene3Di 3.40.309.10. 1 hit.
3.40.605.10. 1 hit.
InterProi IPR016161. Ald_DH/histidinol_DH.
IPR016163. Ald_DH_C.
IPR016160. Ald_DH_CS_CYS.
IPR029510. Ald_DH_CS_GLU.
IPR016162. Ald_DH_N.
IPR015590. Aldehyde_DH_dom.
[Graphical view ]
Pfami PF00171. Aldedh. 1 hit.
[Graphical view ]
SUPFAMi SSF53720. SSF53720. 1 hit.
PROSITEi PS00070. ALDEHYDE_DEHYDR_CYS. 1 hit.
PS00687. ALDEHYDE_DEHYDR_GLU. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Human gamma-aminobutyraldehyde dehydrogenase (ALDH9): cDNA sequence, genomic organization, polymorphism, chromosomal localization, and tissue expression."
    Lin S.W., Chen J.C., Hsu L.C., Hsieh C.-L., Yoshida A.
    Genomics 34:376-380(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT SER-116.
    Tissue: Liver.
  2. "Molecular and biochemical characterization of rat gamma-trimethylaminobutyraldehyde dehydrogenase and evidence for the involvement of human aldehyde dehydrogenase 9 in carnitine biosynthesis."
    Vaz F.M., Fouchier S.W., Ofman R., Sommer M., Wanders R.J.A.
    J. Biol. Chem. 275:7390-7394(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION.
    Tissue: Liver.
  3. "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: Spleen and Testis.
  4. "The DNA sequence and biological annotation of human chromosome 1."
    Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
    , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
    Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. Bienvenut W.V., Heiserich L., Gottlieb E.
    Submitted (MAR-2008) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 2-15; 247-258; 299-310; 315-326 AND 472-481, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Colon carcinoma.
  6. "Aldehyde dehydrogenase from adult human brain that dehydrogenates gamma-aminobutyraldehyde: purification, characterization, cloning and distribution."
    Kikonyogo A., Pietruszko R.
    Biochem. J. 316:317-324(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 259-274; 353-366; 412-426 AND 434-453, NUCLEOTIDE SEQUENCE [MRNA] OF 29-494, CHARACTERIZATION, TISSUE SPECIFICITY, VARIANT SER-116.
    Tissue: Brain.
  7. "Human aldehyde dehydrogenase. cDNA cloning and primary structure of the enzyme that catalyzes dehydrogenation of 4-aminobutyraldehyde."
    Kurys G., Shah P.C., Kikonyogo A., Reed D., Ambroziak W., Pietruszko R.
    Eur. J. Biochem. 218:311-320(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 33-494 (ISOFORM 1), PARTIAL PROTEIN SEQUENCE.
  8. "Human aldehyde dehydrogenase. Purification and characterization of a third isozyme with low Km for gamma-aminobutyraldehyde."
    Kurys G., Ambroziak W., Pietruszko R.
    J. Biol. Chem. 264:4715-4721(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION.
    Tissue: Liver.
  9. "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 SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  10. "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-298, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  11. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  12. "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 SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  13. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiAL9A1_HUMAN
AccessioniPrimary (citable) accession number: P49189
Secondary accession number(s): B2R6X1
, B4DXY7, Q5VV90, Q6LCL1, Q9NZT7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: February 1, 2005
Last modified: October 29, 2014
This is version 136 of the entry and version 3 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 1
    Human chromosome 1: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3