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.

P33121

- ACSL1_HUMAN

UniProt

P33121 - ACSL1_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
Long-chain-fatty-acid--CoA ligase 1
Gene
ACSL1, FACL1, FACL2, LACS, LACS1, LACS2
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Activation of long-chain fatty acids for both synthesis of cellular lipids, and degradation via beta-oxidation. Preferentially uses palmitoleate, oleate and linoleate.

Catalytic activityi

ATP + a long-chain fatty acid + CoA = AMP + diphosphate + an acyl-CoA.

Cofactori

Magnesium.

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. long-chain fatty acid-CoA ligase activity Source: UniProtKB

GO - Biological processi

  1. adiponectin-activated signaling pathway Source: Ensembl
  2. alpha-linolenic acid metabolic process Source: Reactome
  3. cellular lipid metabolic process Source: Reactome
  4. linoleic acid metabolic process Source: Reactome
  5. lipid biosynthetic process Source: UniProtKB
  6. long-chain fatty acid import Source: UniProtKB
  7. long-chain fatty acid metabolic process Source: UniProtKB
  8. long-chain fatty-acyl-CoA biosynthetic process Source: Reactome
  9. positive regulation of protein serine/threonine kinase activity Source: Ensembl
  10. response to drug Source: Ensembl
  11. response to nutrient Source: Ensembl
  12. response to oleic acid Source: Ensembl
  13. response to organic cyclic compound Source: Ensembl
  14. small molecule metabolic process Source: Reactome
  15. triglyceride biosynthetic process Source: Reactome
  16. unsaturated fatty acid metabolic process Source: Reactome
  17. xenobiotic catabolic process Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

Ligase

Keywords - Biological processi

Fatty acid metabolism, Lipid metabolism

Keywords - Ligandi

ATP-binding, Magnesium, Nucleotide-binding

Enzyme and pathway databases

BioCyciMetaCyc:HS07766-MONOMER.
BRENDAi6.2.1.3. 2681.
ReactomeiREACT_116145. PPARA activates gene expression.
REACT_121100. Linoleic acid (LA) metabolism.
REACT_121147. alpha-linolenic acid (ALA) metabolism.
REACT_380. Synthesis of very long-chain fatty acyl-CoAs.

Names & Taxonomyi

Protein namesi
Recommended name:
Long-chain-fatty-acid--CoA ligase 1 (EC:6.2.1.3)
Alternative name(s):
Acyl-CoA synthetase 1
Short name:
ACS1
Long-chain acyl-CoA synthetase 1
Short name:
LACS 1
Long-chain acyl-CoA synthetase 2
Short name:
LACS 2
Long-chain fatty acid-CoA ligase 2
Palmitoyl-CoA ligase 1
Palmitoyl-CoA ligase 2
Gene namesi
Name:ACSL1
Synonyms:FACL1, FACL2, LACS, LACS1, LACS2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 4

Organism-specific databases

HGNCiHGNC:3569. ACSL1.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei25 – 4521Helical; Signal-anchor for type III membrane protein; Reviewed prediction
Add
BLAST
Topological domaini46 – 698653Cytoplasmic Reviewed prediction
Add
BLAST

GO - Cellular componenti

  1. endoplasmic reticulum membrane Source: Reactome
  2. integral component of membrane Source: UniProtKB-KW
  3. mitochondrial outer membrane Source: Reactome
  4. mitochondrion Source: UniProtKB
  5. peroxisomal membrane Source: UniProtKB-SubCell
  6. plasma membrane Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane, Microsome, Mitochondrion, Mitochondrion outer membrane, Peroxisome

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA27966.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 698698Long-chain-fatty-acid--CoA ligase 1
PRO_0000193104Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionine1 Publication
Modified residuei9 – 91Nitrated tyrosine By similarity
Modified residuei84 – 841Phosphotyrosine By similarity
Glycosylationi135 – 1351O-linked (GlcNAc) By similarity
Modified residuei207 – 2071N6-acetyllysine By similarity
Modified residuei356 – 3561N6-acetyllysine By similarity
Modified residuei386 – 3861N6-acetyllysine By similarity
Modified residuei620 – 6201Phosphoserine By similarity
Modified residuei632 – 6321N6-acetyllysine By similarity

Keywords - PTMi

Acetylation, Glycoprotein, Nitration, Phosphoprotein

Proteomic databases

MaxQBiP33121.
PaxDbiP33121.
PRIDEiP33121.

PTM databases

PhosphoSiteiP33121.

Expressioni

Tissue specificityi

Highly expressed in liver, heart, skeletal muscle, kidney and erythroid cells, and to a lesser extent in brain, lung, placenta and pancreas.1 Publication

Developmental stagei

Expressed during the early stages of erythroid development while expression is very low in reticulocytes and young erythrocytes.

Gene expression databases

ArrayExpressiP33121.
BgeeiP33121.
CleanExiHS_ACSL1.
GenevestigatoriP33121.

Organism-specific databases

HPAiHPA011316.
HPA011964.

Interactioni

Protein-protein interaction databases

BioGridi108476. 6 interactions.
IntActiP33121. 3 interactions.
STRINGi9606.ENSP00000281455.

Structurei

3D structure databases

ProteinModelPortaliP33121.
SMRiP33121. Positions 81-639.

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Signal-anchor, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG1022.
HOGENOMiHOG000159459.
HOVERGENiHBG050452.
InParanoidiP33121.
KOiK01897.
OMAiWDRLIFH.
OrthoDBiEOG71CFKN.
PhylomeDBiP33121.
TreeFamiTF313877.

Family and domain databases

InterProiIPR020845. AMP-binding_CS.
IPR000873. AMP-dep_Synth/Lig.
[Graphical view]
PfamiPF00501. AMP-binding. 1 hit.
[Graphical view]
PROSITEiPS00455. AMP_BINDING. 1 hit.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: P33121-1) [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

MQAHELFRYF RMPELVDFRQ YVRTLPTNTL MGFGAFAALT TFWYATRPKP    50
LKPPCDLSMQ SVEVAGSGGA RRSALLDSDE PLVYFYDDVT TLYEGFQRGI 100
QVSNNGPCLG SRKPDQPYEW LSYKQVAELS ECIGSALIQK GFKTAPDQFI 150
GIFAQNRPEW VIIEQGCFAY SMVIVPLYDT LGNEAITYIV NKAELSLVFV 200
DKPEKAKLLL EGVENKLIPG LKIIVVMDAY GSELVERGQR CGVEVTSMKA 250
MEDLGRANRR KPKPPAPEDL AVICFTSGTT GNPKGAMVTH RNIVSDCSAF 300
VKATENTVNP CPDDTLISFL PLAHMFERVV ECVMLCHGAK IGFFQGDIRL 350
LMDDLKVLQP TVFPVVPRLL NRMFDRIFGQ ANTTLKRWLL DFASKRKEAE 400
LRSGIIRNNS LWDRLIFHKV QSSLGGRVRL MVTGAAPVSA TVLTFLRAAL 450
GCQFYEGYGQ TECTAGCCLT MPGDWTAGHV GAPMPCNLIK LVDVEEMNYM 500
AAEGEGEVCV KGPNVFQGYL KDPAKTAEAL DKDGWLHTGD IGKWLPNGTL 550
KIIDRKKHIF KLAQGEYIAP EKIENIYMRS EPVAQVFVHG ESLQAFLIAI 600
VVPDVETLCS WAQKRGFEGS FEELCRNKDV KKAILEDMVR LGKDSGLKPF 650
EQVKGITLHP ELFSIDNGLL TPTMKAKRPE LRNYFRSQID DLYSTIKV 698
Length:698
Mass (Da):77,943
Last modified:October 1, 1993 - v1
Checksum:iFD6669453589D362
GO
Isoform 2 (identifier: P33121-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     508-517: Missing.

Note: May be due to a competing acceptor splice site. No experimental confirmation available.

Show »
Length:688
Mass (Da):76,871
Checksum:i815DF2AA8EE8A6B4
GO
Isoform 3 (identifier: P33121-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     306-331: NTVNPCPDDTLISFLPLAHMFERVVE → KALPLSASDTHISYLPLAHIYEQLLK

Note: No experimental confirmation available.

Show »
Length:698
Mass (Da):77,907
Checksum:i1EDBB04923DD129F
GO

Sequence cautioni

The sequence BAC04704.1 differs from that shown. Reason: Erroneous initiation.

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei306 – 33126NTVNP…ERVVE → KALPLSASDTHISYLPLAHI YEQLLK in isoform 3.
VSP_054391Add
BLAST
Alternative sequencei508 – 51710Missing in isoform 2.
VSP_009604

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti21 – 233YVR → CV in AAB00959. 1 Publication
Sequence conflicti37 – 382AA → SRR in AAB00959. 1 Publication
Sequence conflicti44 – 474YATR → RPRH in AAB00959. 1 Publication
Sequence conflicti55 – 562CD → WH in AAB00959. 1 Publication
Sequence conflicti229 – 2291A → S in AAB00959. 1 Publication
Sequence conflicti385 – 3851L → V in AAB00959. 1 Publication
Sequence conflicti400 – 4012EL → DV in AAB00959. 1 Publication
Sequence conflicti477 – 4771A → T in AAB00959. 1 Publication
Sequence conflicti492 – 4943VDV → GWQL in AAB00959. 1 Publication
Sequence conflicti502 – 5021A → S in AAB00959. 1 Publication
Sequence conflicti695 – 6951T → I in AAB00959. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
D10040 mRNA. Translation: BAA00931.1.
L09229 mRNA. Translation: AAB00959.1.
AK096117 mRNA. Translation: BAC04704.1. Different initiation.
AK296826 mRNA. Translation: BAH12438.1.
AC079257 Genomic DNA. No translation available.
AC084871 Genomic DNA. No translation available.
CH471056 Genomic DNA. Translation: EAX04662.1.
CH471056 Genomic DNA. Translation: EAX04663.1.
CH471056 Genomic DNA. Translation: EAX04665.1.
BC026290 mRNA. Translation: AAH26290.1.
BC050073 mRNA. Translation: AAH50073.1.
CCDSiCCDS3839.1. [P33121-1]
CCDS68826.1. [P33121-3]
PIRiJX0202.
RefSeqiNP_001273637.1. NM_001286708.1. [P33121-1]
NP_001273639.1. NM_001286710.1. [P33121-3]
NP_001273640.1. NM_001286711.1.
NP_001273641.1. NM_001286712.1.
NP_001986.2. NM_001995.3. [P33121-1]
XP_005262885.1. XM_005262828.1. [P33121-1]
XP_005262886.1. XM_005262829.1. [P33121-1]
XP_005262888.1. XM_005262831.1. [P33121-1]
UniGeneiHs.406678.

Genome annotation databases

EnsembliENST00000281455; ENSP00000281455; ENSG00000151726. [P33121-1]
ENST00000504342; ENSP00000425006; ENSG00000151726. [P33121-1]
ENST00000513317; ENSP00000426150; ENSG00000151726.
ENST00000515030; ENSP00000422607; ENSG00000151726. [P33121-1]
GeneIDi2180.
KEGGihsa:2180.
UCSCiuc003iwt.1. human. [P33121-1]

Polymorphism databases

DMDMi417241.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
D10040 mRNA. Translation: BAA00931.1 .
L09229 mRNA. Translation: AAB00959.1 .
AK096117 mRNA. Translation: BAC04704.1 . Different initiation.
AK296826 mRNA. Translation: BAH12438.1 .
AC079257 Genomic DNA. No translation available.
AC084871 Genomic DNA. No translation available.
CH471056 Genomic DNA. Translation: EAX04662.1 .
CH471056 Genomic DNA. Translation: EAX04663.1 .
CH471056 Genomic DNA. Translation: EAX04665.1 .
BC026290 mRNA. Translation: AAH26290.1 .
BC050073 mRNA. Translation: AAH50073.1 .
CCDSi CCDS3839.1. [P33121-1 ]
CCDS68826.1. [P33121-3 ]
PIRi JX0202.
RefSeqi NP_001273637.1. NM_001286708.1. [P33121-1 ]
NP_001273639.1. NM_001286710.1. [P33121-3 ]
NP_001273640.1. NM_001286711.1.
NP_001273641.1. NM_001286712.1.
NP_001986.2. NM_001995.3. [P33121-1 ]
XP_005262885.1. XM_005262828.1. [P33121-1 ]
XP_005262886.1. XM_005262829.1. [P33121-1 ]
XP_005262888.1. XM_005262831.1. [P33121-1 ]
UniGenei Hs.406678.

3D structure databases

ProteinModelPortali P33121.
SMRi P33121. Positions 81-639.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 108476. 6 interactions.
IntActi P33121. 3 interactions.
STRINGi 9606.ENSP00000281455.

Chemistry

DrugBanki DB00131. Adenosine monophosphate.
DB00171. Adenosine triphosphate.

PTM databases

PhosphoSitei P33121.

Polymorphism databases

DMDMi 417241.

Proteomic databases

MaxQBi P33121.
PaxDbi P33121.
PRIDEi P33121.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000281455 ; ENSP00000281455 ; ENSG00000151726 . [P33121-1 ]
ENST00000504342 ; ENSP00000425006 ; ENSG00000151726 . [P33121-1 ]
ENST00000513317 ; ENSP00000426150 ; ENSG00000151726 .
ENST00000515030 ; ENSP00000422607 ; ENSG00000151726 . [P33121-1 ]
GeneIDi 2180.
KEGGi hsa:2180.
UCSCi uc003iwt.1. human. [P33121-1 ]

Organism-specific databases

CTDi 2180.
GeneCardsi GC04M185676.
HGNCi HGNC:3569. ACSL1.
HPAi HPA011316.
HPA011964.
MIMi 152425. gene.
neXtProti NX_P33121.
PharmGKBi PA27966.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG1022.
HOGENOMi HOG000159459.
HOVERGENi HBG050452.
InParanoidi P33121.
KOi K01897.
OMAi WDRLIFH.
OrthoDBi EOG71CFKN.
PhylomeDBi P33121.
TreeFami TF313877.

Enzyme and pathway databases

BioCyci MetaCyc:HS07766-MONOMER.
BRENDAi 6.2.1.3. 2681.
Reactomei REACT_116145. PPARA activates gene expression.
REACT_121100. Linoleic acid (LA) metabolism.
REACT_121147. alpha-linolenic acid (ALA) metabolism.
REACT_380. Synthesis of very long-chain fatty acyl-CoAs.

Miscellaneous databases

ChiTaRSi ACSL1. human.
GeneWikii ACSL1.
GenomeRNAii 2180.
NextBioi 35479388.
PROi P33121.
SOURCEi Search...

Gene expression databases

ArrayExpressi P33121.
Bgeei P33121.
CleanExi HS_ACSL1.
Genevestigatori P33121.

Family and domain databases

InterProi IPR020845. AMP-binding_CS.
IPR000873. AMP-dep_Synth/Lig.
[Graphical view ]
Pfami PF00501. AMP-binding. 1 hit.
[Graphical view ]
PROSITEi PS00455. AMP_BINDING. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Human long-chain acyl-CoA synthetase: structure and chromosomal location."
    Abe T., Fujino T., Fukuyama R., Minoshima S., Shimizu N., Toh H., Suzuki H., Yamamoto T.
    J. Biochem. 111:123-128(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Tissue: Liver.
  2. "Molecular cloning and sequencing of human palmitoyl-CoA ligase and its tissue specific expression."
    Ghosh B., Barbosa E., Singh I.
    Mol. Cell. Biochem. 151:77-81(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  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] (ISOFORM 3), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 395-698 (ISOFORM 2).
  4. "Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
    Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H.
    , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
    Nature 434:724-731(2005) [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] (ISOFORM 1).
    Tissue: Testis.
  7. Bienvenut W.V.
    Submitted (JUN-2005) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 1-8; 12-19; 341-349; 377-386; 562-572; 633-640 AND 655-675, ACETYLATION AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: B-cell lymphoma.
  8. "Identification and molecular characterization of acyl-CoA synthetase in human red cells and erythroid precursor."
    Malhotra K.T., Malhotra K., Lubin B.H., Kuypers F.A.
    Biochem. J. 344:135-143(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY.
  9. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiACSL1_HUMAN
AccessioniPrimary (citable) accession number: P33121
Secondary accession number(s): B7Z452
, D3DP57, P41215, Q8N8V7, Q8TA99
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1993
Last sequence update: October 1, 1993
Last modified: September 3, 2014
This is version 139 of the entry and version 1 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 4
    Human chromosome 4: 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

Similar proteinsi