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Protein

Lysocardiolipin acyltransferase 1

Gene

LCLAT1

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

Functioni

Acyl-CoA:lysocardiolipin acyltransferase. Possesses both lysophosphatidylinositol acyltransferase (LPIAT) and lysophosphatidylglycerol acyltransferase (LPGAT) activities. Recognizes both monolysocardiolipin and dilysocardiolipin as substrates with a preference for linoleoyl-CoA and oleoyl-CoA as acyl donors. Acts as a remodeling enzyme for cardiolipin, a major membrane polyglycerophospholipid. Converts lysophosphatidic acid (LPA) into phosphatidic acid (PA) with a relatively low activity. Required for establishment of the hematopoietic and endothelial lineages.2 Publications

Catalytic activityi

Acyl-CoA + 1-acyl-sn-glycerol 3-phosphate = CoA + 1,2-diacyl-sn-glycerol 3-phosphate.

Kineticsi

  1. KM=39 µM for arachidonoyl-CoA (20:4) for LPIAT activity1 Publication
  2. KM=289 µM for oleoyl-CoA (18:1) for LPIAT activity1 Publication
  3. KM=134 µM for linoleoyl-CoA (18:2) for LPIAT activity1 Publication
  4. KM=34 µM for stearoyl-CoA (18:0) for LPIAT activity1 Publication
  5. KM=53 µM for palmitoyl-CoA (16:0) for LPIAT activity1 Publication
  6. KM=54 µM for oleoyl-CoA (18:1) for LPGAT activity1 Publication
  7. KM=36 µM for linoleoyl-CoA (18:2) for LPGAT activity1 Publication
  8. KM=70 µM for stearoyl-CoA (18:0) for LPGAT activity1 Publication
  9. KM=34 µM for palmitoyl-CoA (16:0) for LPGAT activity1 Publication

Vmax=3230 nmol/min/mg enzyme toward arachidonoyl-CoA (20:4) for LPIAT activity1 Publication

Vmax=7489 nmol/min/mg enzyme toward oleoyl-CoA (18:1) for LPIAT activity1 Publication

Vmax=4696 nmol/min/mg enzyme toward linoleoyl-CoA (18:2) for LPIAT activity1 Publication

Vmax=1078 nmol/min/mg enzyme toward stearoyl-CoA (18:0) for LPIAT activity1 Publication

Vmax=11203 nmol/min/mg enzyme toward palmitoyl-CoA (16:0) for LPIAT activity1 Publication

Vmax=5514 nmol/min/mg enzyme toward oleoyl-CoA (18:1) for LPGAT activity1 Publication

Vmax=1358 nmol/min/mg enzyme toward linoleoyl-CoA (18:2) for LPGAT activity1 Publication

Vmax=3530 nmol/min/mg enzyme toward stearoyl-CoA (18:0) for LPGAT activity1 Publication

Vmax=1673 nmol/min/mg enzyme toward palmitoyl-CoA (16:0) for LPGAT activity1 Publication

Pathwayi

GO - Molecular functioni

  1. 1-acylglycerol-3-phosphate O-acyltransferase activity Source: UniProtKB-EC

GO - Biological processi

  1. cardiolipin acyl-chain remodeling Source: Reactome
  2. CDP-diacylglycerol biosynthetic process Source: UniProtKB-UniPathway
  3. cellular lipid metabolic process Source: Reactome
  4. glycerophospholipid biosynthetic process Source: Reactome
  5. multicellular organismal development Source: UniProtKB-KW
  6. phosphatidic acid biosynthetic process Source: Reactome
  7. phospholipid metabolic process Source: Reactome
  8. small molecule metabolic process Source: Reactome
  9. triglyceride biosynthetic process Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Acyltransferase, Developmental protein, Transferase

Keywords - Biological processi

Lipid biosynthesis, Lipid metabolism, Phospholipid biosynthesis, Phospholipid metabolism

Enzyme and pathway databases

ReactomeiREACT_1190. Triglyceride Biosynthesis.
REACT_120906. Synthesis of PA.
REACT_121006. Acyl chain remodeling of CL.
UniPathwayiUPA00557; UER00613.

Names & Taxonomyi

Protein namesi
Recommended name:
Lysocardiolipin acyltransferase 1 (EC:2.3.1.-, EC:2.3.1.51)
Alternative name(s):
1-acylglycerol-3-phosphate O-acyltransferase 8
Short name:
1-AGP acyltransferase 8
Short name:
1-AGPAT 8
Acyl-CoA:lysocardiolipin acyltransferase 1
Gene namesi
Name:LCLAT1
Synonyms:AGPAT8, ALCAT1, LYCAT
ORF Names:UNQ1849/PRO3579
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 2

Organism-specific databases

HGNCiHGNC:26756. LCLAT1.

Subcellular locationi

  1. Endoplasmic reticulum membrane 1 Publication; Multi-pass membrane protein 1 Publication

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei47 – 6721HelicalSequence AnalysisAdd
BLAST
Transmembranei86 – 10621HelicalSequence AnalysisAdd
BLAST
Transmembranei340 – 36021HelicalSequence AnalysisAdd
BLAST
Transmembranei362 – 38221HelicalSequence AnalysisAdd
BLAST

GO - Cellular componenti

  1. endoplasmic reticulum membrane Source: Reactome
  2. integral component of membrane Source: UniProtKB-KW
  3. membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi206 – 2061D → C: Abolishes LPIAT and LPGAT activities. 2 Publications
Mutagenesisi206 – 2061D → R: Does not increase enzyme activity. 2 Publications
Mutagenesisi207 – 2071L → T: Abolishes LPIAT activity. No effect on LPGAT activity. 1 Publication

Organism-specific databases

PharmGKBiPA164722072.

Polymorphism and mutation databases

BioMutaiLCLAT1.
DMDMi74749398.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 414414Lysocardiolipin acyltransferase 1PRO_0000291577Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei221 – 2211N6-acetyllysine1 Publication

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiQ6UWP7.
PaxDbiQ6UWP7.
PRIDEiQ6UWP7.

PTM databases

PhosphoSiteiQ6UWP7.

Expressioni

Tissue specificityi

Expressed at higher level in heart, kidney and pancreas than in brain, spleen, liver, lung, small intestine and placenta.2 Publications

Gene expression databases

BgeeiQ6UWP7.
CleanExiHS_LCLAT1.
ExpressionAtlasiQ6UWP7. baseline and differential.
GenevestigatoriQ6UWP7.

Organism-specific databases

HPAiHPA031880.
HPA049217.

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
GOPCQ9HD263EBI-10254507,EBI-349832
LNX1Q8TBB13EBI-10254507,EBI-739832

Protein-protein interaction databases

BioGridi128972. 14 interactions.
IntActiQ6UWP7. 2 interactions.
STRINGi9606.ENSP00000310551.

Structurei

3D structure databases

ProteinModelPortaliQ6UWP7.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi123 – 1286HXXXXD motif

Domaini

The HXXXXD motif is essential for acyltransferase activity and may constitute the binding site for the phosphate moiety of the glycerol-3-phosphate.By similarity

Sequence similaritiesi

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG0204.
GeneTreeiENSGT00530000062943.
HOGENOMiHOG000290725.
HOVERGENiHBG055624.
InParanoidiQ6UWP7.
KOiK13513.
OMAiDFPKEIH.
PhylomeDBiQ6UWP7.
TreeFamiTF314346.

Family and domain databases

InterProiIPR002123. Plipid/glycerol_acylTrfase.
[Graphical view]
PfamiPF01553. Acyltransferase. 1 hit.
[Graphical view]
SMARTiSM00563. PlsC. 1 hit.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q6UWP7-1) [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
MHSRGREIVV LLNPWSINEA VSSYCTYFIK QDSKSFGIMV SWKGIYFILT
60 70 80 90 100
LFWGSFFGSI FMLSPFLPLM FVNPSWYRWI NNRLVATWLT LPVALLETMF
110 120 130 140 150
GVKVIITGDA FVPGERSVII MNHRTRMDWM FLWNCLMRYS YLRLEKICLK
160 170 180 190 200
ASLKGVPGFG WAMQAAAYIF IHRKWKDDKS HFEDMIDYFC DIHEPLQLLI
210 220 230 240 250
FPEGTDLTEN SKSRSNAFAE KNGLQKYEYV LHPRTTGFTF VVDRLREGKN
260 270 280 290 300
LDAVHDITVA YPHNIPQSEK HLLQGDFPRE IHFHVHRYPI DTLPTSKEDL
310 320 330 340 350
QLWCHKRWEE KEERLRSFYQ GEKNFYFTGQ SVIPPCKSEL RVLVVKLLSI
360 370 380 390 400
LYWTLFSPAM CLLIYLYSLV KWYFIITIVI FVLQERIFGG LEIIELACYR
410
LLHKQPHLNS KKNE
Length:414
Mass (Da):48,920
Last modified:July 5, 2004 - v1
Checksum:iF83A1911CC19F959
GO
Isoform 2 (identifier: Q6UWP7-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     249-308: KNLDAVHDIT...DLQLWCHKRW → RRQSEGSKGP...SNLQIQCYSH
     309-414: Missing.

Note: No experimental confirmation available.

Show »
Length:308
Mass (Da):36,045
Checksum:i6325F89469A35016
GO
Isoform 3 (identifier: Q6UWP7-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-38: Missing.

Show »
Length:376
Mass (Da):44,561
Checksum:iFB658F500239F789
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti290 – 2901I → V.
Corresponds to variant rs12471868 [ dbSNP | Ensembl ].
VAR_032830

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 3838Missing in isoform 3. 1 PublicationVSP_044307Add
BLAST
Alternative sequencei249 – 30860KNLDA…CHKRW → RRQSEGSKGPLQGELQITAQ GNQRGHKQMEKHSMLMDWKN QYREIGHTAQSNLQIQCYSH in isoform 2. 1 PublicationVSP_026181Add
BLAST
Alternative sequencei309 – 414106Missing in isoform 2. 1 PublicationVSP_026182Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY358702 mRNA. Translation: AAQ89065.1.
AK095284 mRNA. Translation: BAC04522.1.
AC073255 Genomic DNA. No translation available.
AC132154 Genomic DNA. No translation available.
BC146817 mRNA. Translation: AAI46818.1.
CCDSiCCDS1772.1. [Q6UWP7-1]
CCDS42670.1. [Q6UWP7-3]
RefSeqiNP_001002257.1. NM_001002257.2. [Q6UWP7-3]
NP_872357.2. NM_182551.4. [Q6UWP7-1]
XP_005264301.1. XM_005264244.1. [Q6UWP7-1]
XP_005264302.1. XM_005264245.2. [Q6UWP7-3]
UniGeneiHs.468048.
Hs.662770.

Genome annotation databases

EnsembliENST00000309052; ENSP00000310551; ENSG00000172954. [Q6UWP7-1]
ENST00000319406; ENSP00000368826; ENSG00000172954. [Q6UWP7-2]
ENST00000379509; ENSP00000368823; ENSG00000172954. [Q6UWP7-3]
GeneIDi253558.
KEGGihsa:253558.
UCSCiuc002rnj.3. human. [Q6UWP7-1]
uc002rnk.1. human. [Q6UWP7-2]

Polymorphism and mutation databases

BioMutaiLCLAT1.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY358702 mRNA. Translation: AAQ89065.1.
AK095284 mRNA. Translation: BAC04522.1.
AC073255 Genomic DNA. No translation available.
AC132154 Genomic DNA. No translation available.
BC146817 mRNA. Translation: AAI46818.1.
CCDSiCCDS1772.1. [Q6UWP7-1]
CCDS42670.1. [Q6UWP7-3]
RefSeqiNP_001002257.1. NM_001002257.2. [Q6UWP7-3]
NP_872357.2. NM_182551.4. [Q6UWP7-1]
XP_005264301.1. XM_005264244.1. [Q6UWP7-1]
XP_005264302.1. XM_005264245.2. [Q6UWP7-3]
UniGeneiHs.468048.
Hs.662770.

3D structure databases

ProteinModelPortaliQ6UWP7.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi128972. 14 interactions.
IntActiQ6UWP7. 2 interactions.
STRINGi9606.ENSP00000310551.

PTM databases

PhosphoSiteiQ6UWP7.

Polymorphism and mutation databases

BioMutaiLCLAT1.
DMDMi74749398.

Proteomic databases

MaxQBiQ6UWP7.
PaxDbiQ6UWP7.
PRIDEiQ6UWP7.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000309052; ENSP00000310551; ENSG00000172954. [Q6UWP7-1]
ENST00000319406; ENSP00000368826; ENSG00000172954. [Q6UWP7-2]
ENST00000379509; ENSP00000368823; ENSG00000172954. [Q6UWP7-3]
GeneIDi253558.
KEGGihsa:253558.
UCSCiuc002rnj.3. human. [Q6UWP7-1]
uc002rnk.1. human. [Q6UWP7-2]

Organism-specific databases

CTDi253558.
GeneCardsiGC02P030670.
HGNCiHGNC:26756. LCLAT1.
HPAiHPA031880.
HPA049217.
neXtProtiNX_Q6UWP7.
PharmGKBiPA164722072.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG0204.
GeneTreeiENSGT00530000062943.
HOGENOMiHOG000290725.
HOVERGENiHBG055624.
InParanoidiQ6UWP7.
KOiK13513.
OMAiDFPKEIH.
PhylomeDBiQ6UWP7.
TreeFamiTF314346.

Enzyme and pathway databases

UniPathwayiUPA00557; UER00613.
ReactomeiREACT_1190. Triglyceride Biosynthesis.
REACT_120906. Synthesis of PA.
REACT_121006. Acyl chain remodeling of CL.

Miscellaneous databases

ChiTaRSiLCLAT1. human.
GenomeRNAii253558.
NextBioi92116.
PROiQ6UWP7.

Gene expression databases

BgeeiQ6UWP7.
CleanExiHS_LCLAT1.
ExpressionAtlasiQ6UWP7. baseline and differential.
GenevestigatoriQ6UWP7.

Family and domain databases

InterProiIPR002123. Plipid/glycerol_acylTrfase.
[Graphical view]
PfamiPF01553. Acyltransferase. 1 hit.
[Graphical view]
SMARTiSM00563. PlsC. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
  2. "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 2).
    Tissue: Tongue.
  3. "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].
  4. "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 3).
  5. "Functional characterization of human 1-acylglycerol-3-phosphate acyltransferase isoform 8: cloning, tissue distribution, gene structure, and enzymatic activity."
    Agarwal A.K., Barnes R.I., Garg A.
    Arch. Biochem. Biophys. 449:64-76(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, TISSUE SPECIFICITY, MUTAGENESIS OF ASP-206.
  6. "The microsomal cardiolipin remodeling enzyme acyl-CoA lysocardiolipin acyltransferase is an acyltransferase of multiple anionic lysophospholipids."
    Zhao Y., Chen Y.-Q., Li S., Konrad R.J., Cao G.
    J. Lipid Res. 50:945-956(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, MUTAGENESIS OF ASP-206 AND LEU-207.
  7. "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-221, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  8. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
    Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
    Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiLCLT1_HUMAN
AccessioniPrimary (citable) accession number: Q6UWP7
Secondary accession number(s): A6H8Z7, Q8N1Q7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 26, 2007
Last sequence update: July 5, 2004
Last modified: April 29, 2015
This is version 97 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

Caution

PubMed:16620771 does not detect acyl-CoA:lysocardiolipin acyltransferase activity.Curated

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 2
    Human chromosome 2: 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. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  5. SIMILARITY comments
    Index of protein domains and families

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.