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Protein
Submitted name:

Long-chain-fatty-acid--CoA ligase 1

Gene

ACSL1

Organism
Homo sapiens (Human)
Status
Unreviewed-Annotation score: Annotation score: 1 out of 5-Experimental evidence at protein leveli

Functioni

GO - Molecular functioni

  1. catalytic activity Source: InterPro
Complete GO annotation...

Names & Taxonomyi

Protein namesi
Submitted name:
Long-chain-fatty-acid--CoA ligase 1Imported
Gene namesi
Name:ACSL1Imported
OrganismiHomo sapiens (Human)Imported
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 4

Organism-specific databases

HGNCiHGNC:3569. ACSL1.

Expressioni

Gene expression databases

BgeeiE7EPM6.
ExpressionAtlasiE7EPM6. baseline and differential.

Structurei

3D structure databases

ProteinModelPortaliE7EPM6.
SMRiE7EPM6. Positions 147-605.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Phylogenomic databases

GeneTreeiENSGT00690000101725.
KOiK01897.

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]

Sequencei

Sequence statusi: Complete.

E7EPM6-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MQAHELFRYF RMPELVDFRQ YVRTLPTNTL MGFGAFAALT TFWYATRPKP
60 70 80 90 100
LKPPCDLSMQ SVEVAGSGGA RRSALLDSDE PLVYFYDDVT TLYEGFQRGI
110 120 130 140 150
QVSNNGPCLG SRKPDQPYEW LSYKQWVIIE QGCFAYSMVI VPLYDTLGNE
160 170 180 190 200
AITYIVNKAE LSLVFVDKPE KAKLLLEGVE NKLIPGLKII VVMDAYGSEL
210 220 230 240 250
VERGQRCGVE VTSMKAMEDL GRANRRKPKP PAPEDLAVIC FTSGTTGNPK
260 270 280 290 300
GAMVTHRNIV SDCSAFVKAT ENTVNPCPDD TLISFLPLAH MFERVVECVM
310 320 330 340 350
LCHGAKIGFF QGDIRLLMDD LKVLQPTVFP VVPRLLNRMF DRIFGQANTT
360 370 380 390 400
LKRWLLDFAS KRKEAELRSG IIRNNSLWDR LIFHKVQSSL GGRVRLMVTG
410 420 430 440 450
AAPVSATVLT FLRAALGCQF YEGYGQTECT AGCCLTMPGD WTAGHVGAPM
460 470 480 490 500
PCNLIKLVDV EEMNYMAAEG EGEVCVKGPN VFQGYLKDPA KTAEALDKDG
510 520 530 540 550
WLHTGDIGKW LPNGTLKIID RKKHIFKLAQ GEYIAPEKIE NIYMRSEPVA
560 570 580 590 600
QVFVHGESLQ AFLIAIVVPD VETLCSWAQK RGFEGSFEEL CRNKDVKKAI
610 620 630 640 650
LEDMVRLGKD SGLKPFEQVK GITLHPELFS IDNGLLTPTM KAKRPELRNY
660
FRSQIDDLYS TIKV
Length:664
Mass (Da):74,282
Last modified:March 8, 2011 - v1
Checksum:iD10CABE7AC7A4D4A
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AC079257 Genomic DNA. No translation available.
AC084871 Genomic DNA. No translation available.
RefSeqiNP_001273640.1. NM_001286711.1.
UniGeneiHs.406678.

Genome annotation databases

EnsembliENST00000507295; ENSP00000426244; ENSG00000151726.
GeneIDi2180.
KEGGihsa:2180.
UCSCiuc011ckn.1. human.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AC079257 Genomic DNA. No translation available.
AC084871 Genomic DNA. No translation available.
RefSeqiNP_001273640.1. NM_001286711.1.
UniGeneiHs.406678.

3D structure databases

ProteinModelPortaliE7EPM6.
SMRiE7EPM6. Positions 147-605.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000507295; ENSP00000426244; ENSG00000151726.
GeneIDi2180.
KEGGihsa:2180.
UCSCiuc011ckn.1. human.

Organism-specific databases

CTDi2180.
HGNCiHGNC:3569. ACSL1.
GenAtlasiSearch...

Phylogenomic databases

GeneTreeiENSGT00690000101725.
KOiK01897.

Miscellaneous databases

ChiTaRSiACSL1. human.
GenomeRNAii2180.
NextBioi35499768.

Gene expression databases

BgeeiE7EPM6.
ExpressionAtlasiE7EPM6. baseline and differential.

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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "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].
  2. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  3. Ensembl
    Submitted (JUL-2011) to UniProtKB
    Cited for: IDENTIFICATION.
  4. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiE7EPM6_HUMAN
AccessioniPrimary (citable) accession number: E7EPM6
Secondary accession number(s): E7EQJ5
Entry historyi
Integrated into UniProtKB/TrEMBL: March 8, 2011
Last sequence update: March 8, 2011
Last modified: April 29, 2015
This is version 28 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)
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

Caution

The sequence shown here is derived from an Ensembl automatic analysis pipeline and should be considered as preliminary data.Imported

Keywords - Technical termi

Complete proteome, Proteomics identificationCombined sources, Reference proteomeImported

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.