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Q6P1A2

- MBOA5_HUMAN

UniProt

Q6P1A2 - MBOA5_HUMAN

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Protein
Lysophospholipid acyltransferase 5
Gene
LPCAT3, MBOAT5, OACT5
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Acyltransferase which mediates the conversion of lysophosphatidylcholine (1-acyl-sn-glycero-3-phosphocholine or LPC) into phosphatidylcholine (1,2-diacyl-sn-glycero-3-phosphocholine or PC) (LPCAT activity). Catalyzes also the conversion of lysophosphatidylserine (1-acyl-2-hydroxy-sn-glycero-3-phospho-L-serine or LPS) into phosphatidylserine (1,2-diacyl-sn-glycero-3-phospho-L-serine or PS) (LPSAT activity). Has also weak lysophosphatidylethanolamine acyltransferase activity (LPEAT activity). Favors polyunsaturated fatty acyl-CoAs as acyl donors compared to saturated fatty acyl-CoAs. Seems to be the major enzyme contributing to LPCAT activity in the liver. Lysophospholipid acyltransferases (LPLATs) catalyze the reacylation step of the phospholipid remodeling pathway also known as the Lands cycle.2 Publications

Catalytic activityi

Acyl-CoA + 1-acyl-sn-glycero-3-phosphocholine = CoA + 1,2-diacyl-sn-glycero-3-phosphocholine.
Acyl-CoA + 1-acyl-sn-glycero-3-phosphatidylserine = CoA + 1,2-diacyl-sn-glycero-3-phosphatidylserine.

Enzyme regulationi

Activity is inhibited by thimerosal.

Kineticsi

  1. KM=41.29 µM for palmitoyl-CoA1 Publication
  2. KM=36.65 µM for stearoyl-CoA
  3. KM=72.68 µM for oleoyl-CoA
  4. KM=201.4 µM for linoleoyl-CoA
  5. KM=71.56 µM for arachidonoyl-CoA
  6. KM=72.19 µM for 1-palmitoyl-lysophosphatidylcholine

Vmax=1782 nmol/min/mg enzyme with palmitoyl-CoA and 1-palmitoyl-lysophosphatidylcholine as substrates

Vmax=996 nmol/min/mg enzyme with stearoyl-CoA and 1-palmitoyl-lysophosphatidylcholine as substrates

Vmax=4698 nmol/min/mg enzyme with oleoyl-CoA and 1-palmitoyl-lysophosphatidylcholine as substrates

Vmax=18148 nmol/min/mg enzyme with linoleoyl-CoA and 1-palmitoyl-lysophosphatidylcholine as substrates

Vmax=6247 nmol/min/mg enzyme with arachidonoyl-CoA and 1-palmitoyl-lysophosphatidylcholine as substrates

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei338 – 3381 By similarity
Active sitei374 – 3741 By similarity

GO - Molecular functioni

  1. 1-acylglycerophosphocholine O-acyltransferase activity Source: MGI

GO - Biological processi

  1. glycerophospholipid biosynthetic process Source: Reactome
  2. phosphatidylcholine acyl-chain remodeling Source: Reactome
  3. phosphatidylethanolamine acyl-chain remodeling Source: Reactome
  4. phosphatidylserine acyl-chain remodeling Source: Reactome
  5. phospholipid metabolic process Source: Reactome
  6. regulation of plasma lipoprotein particle levels Source: Ensembl
  7. small molecule metabolic process Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Acyltransferase, Transferase

Keywords - Biological processi

Lipid biosynthesis, Lipid metabolism, Phospholipid biosynthesis, Phospholipid metabolism

Enzyme and pathway databases

ReactomeiREACT_120829. Acyl chain remodelling of PC.
REACT_121369. Acyl chain remodelling of PE.
REACT_121384. Acyl chain remodelling of PS.
UniPathwayiUPA00085.

Names & Taxonomyi

Protein namesi
Recommended name:
Lysophospholipid acyltransferase 5 (EC:2.3.1.-)
Short name:
LPLAT 5
Alternative name(s):
1-acylglycerophosphocholine O-acyltransferase (EC:2.3.1.23)
1-acylglycerophosphoserine O-acyltransferase (EC:2.3.1.n6)
Lysophosphatidylcholine acyltransferase
Short name:
LPCAT
Short name:
Lyso-PC acyltransferase
Lysophosphatidylcholine acyltransferase 3
Short name:
Lyso-PC acyltransferase 3
Lysophosphatidylserine acyltransferase
Short name:
LPSAT
Short name:
Lyso-PS acyltransferase
Membrane-bound O-acyltransferase domain-containing protein 5
Short name:
O-acyltransferase domain-containing protein 5
Gene namesi
Name:LPCAT3
Synonyms:MBOAT5, OACT5
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 12

Organism-specific databases

HGNCiHGNC:30244. LPCAT3.

Subcellular locationi

Endoplasmic reticulum membrane; Multi-pass membrane protein 1 Publication

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei44 – 6421Helical; Reviewed prediction
Add
BLAST
Transmembranei84 – 10421Helical; Reviewed prediction
Add
BLAST
Transmembranei111 – 13121Helical; Reviewed prediction
Add
BLAST
Transmembranei180 – 20021Helical; Reviewed prediction
Add
BLAST
Transmembranei227 – 24721Helical; Reviewed prediction
Add
BLAST
Transmembranei285 – 30521Helical; Reviewed prediction
Add
BLAST
Transmembranei364 – 38421Helical; Reviewed prediction
Add
BLAST
Transmembranei422 – 44221Helical; Reviewed prediction
Add
BLAST
Transmembranei453 – 47321Helical; Reviewed prediction
Add
BLAST

GO - Cellular componenti

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

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA162394266.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 487487Lysophospholipid acyltransferase 5
PRO_0000233382Add
BLAST

Proteomic databases

MaxQBiQ6P1A2.
PaxDbiQ6P1A2.
PRIDEiQ6P1A2.

PTM databases

PhosphoSiteiQ6P1A2.

Expressioni

Tissue specificityi

Highly expressed in liver, pancreas and adipose tissue. Very low expression in skeletal muscle and heart. Detected in neutrophils.2 Publications

Gene expression databases

ArrayExpressiQ6P1A2.
BgeeiQ6P1A2.
CleanExiHS_LPCAT3.
GenevestigatoriQ6P1A2.

Interactioni

Protein-protein interaction databases

BioGridi115464. 2 interactions.
MINTiMINT-3049790.

Structurei

3D structure databases

ProteinModelPortaliQ6P1A2.

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi484 – 4874Di-lysine motif

Domaini

The di-lysine motif confers endoplasmic reticulum localization.

Sequence similaritiesi

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG5202.
HOGENOMiHOG000019529.
HOVERGENiHBG054659.
InParanoidiQ6P1A2.
KOiK13515.
OMAiWLKVYKS.
PhylomeDBiQ6P1A2.
TreeFamiTF106143.

Family and domain databases

InterProiIPR004299. MBOAT_fam.
[Graphical view]
PfamiPF03062. MBOAT. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q6P1A2-1) [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

MASSAEGDEG TVVALAGVLQ SGFQELSLNK LATSLGASEQ ALRLIISIFL    50
GYPFALFYRH YLFYKETYLI HLFHTFTGLS IAYFNFGNQL YHSLLCIVLQ 100
FLILRLMGRT ITAVLTTFCF QMAYLLAGYY YTATGNYDIK WTMPHCVLTL 150
KLIGLAVDYF DGGKDQNSLS SEQQKYAIRG VPSLLEVAGF SYFYGAFLVG 200
PQFSMNHYMK LVQGELIDIP GKIPNSIIPA LKRLSLGLFY LVGYTLLSPH 250
ITEDYLLTED YDNHPFWFRC MYMLIWGKFV LYKYVTCWLV TEGVCILTGL 300
GFNGFEEKGK AKWDACANMK VWLFETNPRF TGTIASFNIN TNAWVARYIF 350
KRLKFLGNKE LSQGLSLLFL ALWHGLHSGY LVCFQMEFLI VIVERQAARL 400
IQESPTLSKL AAITVLQPFY YLVQQTIHWL FMGYSMTAFC LFTWDKWLKV 450
YKSIYFLGHI FFLSLLFILP YIHKAMVPRK EKLKKME 487
Length:487
Mass (Da):56,035
Last modified:July 5, 2004 - v1
Checksum:i429258B54585B4A7
GO
Isoform 2 (identifier: Q6P1A2-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     21-100: Missing.

Note: No experimental confirmation available.

Show »
Length:407
Mass (Da):46,765
Checksum:i61FFE235FB189231
GO

Sequence cautioni

The sequence AAB51326.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.
The sequence AAC51640.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.
The sequence BAG37917.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti63 – 631F → L.
Corresponds to variant rs34196984 [ dbSNP | Ensembl ].
VAR_050027
Natural varianti217 – 2171I → T.
Corresponds to variant rs1984564 [ dbSNP | Ensembl ].
VAR_050028

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei21 – 10080Missing in isoform 2.
VSP_053680Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti387 – 3871E → K in AAH00664. 1 Publication
Sequence conflicti387 – 3871E → K in AAP35646. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
BX648009 mRNA. No translation available.
AK296145 mRNA. Translation: BAH12269.1.
AK315538 mRNA. Translation: BAG37917.1. Different initiation.
AC006512 Genomic DNA. No translation available.
BC000664 mRNA. Translation: AAH00664.2.
BC065194 mRNA. Translation: AAH65194.1.
U47924 Genomic DNA. Translation: AAB51326.1. Different initiation.
U72515 mRNA. Translation: AAC51640.1. Different initiation.
BT007000 mRNA. Translation: AAP35646.1.
CCDSiCCDS8572.1. [Q6P1A2-1]
RefSeqiNP_005759.4. NM_005768.5. [Q6P1A2-1]
UniGeneiHs.655248.

Genome annotation databases

EnsembliENST00000261407; ENSP00000261407; ENSG00000111684. [Q6P1A2-1]
GeneIDi10162.
KEGGihsa:10162.
UCSCiuc001qsi.3. human. [Q6P1A2-1]

Polymorphism databases

DMDMi74737127.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
BX648009 mRNA. No translation available.
AK296145 mRNA. Translation: BAH12269.1 .
AK315538 mRNA. Translation: BAG37917.1 . Different initiation.
AC006512 Genomic DNA. No translation available.
BC000664 mRNA. Translation: AAH00664.2 .
BC065194 mRNA. Translation: AAH65194.1 .
U47924 Genomic DNA. Translation: AAB51326.1 . Different initiation.
U72515 mRNA. Translation: AAC51640.1 . Different initiation.
BT007000 mRNA. Translation: AAP35646.1 .
CCDSi CCDS8572.1. [Q6P1A2-1 ]
RefSeqi NP_005759.4. NM_005768.5. [Q6P1A2-1 ]
UniGenei Hs.655248.

3D structure databases

ProteinModelPortali Q6P1A2.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 115464. 2 interactions.
MINTi MINT-3049790.

PTM databases

PhosphoSitei Q6P1A2.

Polymorphism databases

DMDMi 74737127.

Proteomic databases

MaxQBi Q6P1A2.
PaxDbi Q6P1A2.
PRIDEi Q6P1A2.

Protocols and materials databases

DNASUi 10162.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000261407 ; ENSP00000261407 ; ENSG00000111684 . [Q6P1A2-1 ]
GeneIDi 10162.
KEGGi hsa:10162.
UCSCi uc001qsi.3. human. [Q6P1A2-1 ]

Organism-specific databases

CTDi 10162.
GeneCardsi GC12M007085.
H-InvDB HIX0129675.
HGNCi HGNC:30244. LPCAT3.
MIMi 611950. gene.
neXtProti NX_Q6P1A2.
PharmGKBi PA162394266.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG5202.
HOGENOMi HOG000019529.
HOVERGENi HBG054659.
InParanoidi Q6P1A2.
KOi K13515.
OMAi WLKVYKS.
PhylomeDBi Q6P1A2.
TreeFami TF106143.

Enzyme and pathway databases

UniPathwayi UPA00085 .
Reactomei REACT_120829. Acyl chain remodelling of PC.
REACT_121369. Acyl chain remodelling of PE.
REACT_121384. Acyl chain remodelling of PS.

Miscellaneous databases

ChiTaRSi LPCAT3. human.
GeneWikii MBOAT5.
GenomeRNAii 10162.
NextBioi 35479285.
PROi Q6P1A2.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q6P1A2.
Bgeei Q6P1A2.
CleanExi HS_LPCAT3.
Genevestigatori Q6P1A2.

Family and domain databases

InterProi IPR004299. MBOAT_fam.
[Graphical view ]
Pfami PF03062. MBOAT. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Endometrium.
  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).
  3. "The finished DNA sequence of human chromosome 12."
    Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R.
    , Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K., Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D., Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J., Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A., Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M., Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I., Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A., Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G., Gibbs R.A.
    Nature 440:346-351(2006) [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 1).
    Tissue: Colon and Pancreas.
  5. "Large-scale sequencing in human chromosome 12p13: experimental and computational gene structure determination."
    Ansari-Lari M.A., Shen Y., Muzny D.M., Lee W., Gibbs R.A.
    Genome Res. 7:268-280(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] OF 50-487 (ISOFORM 1).
  6. "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
    Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
    Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 107-487 (ISOFORM 1/2).
  7. "Identification and characterization of a major liver lysophosphatidylcholine acyltransferase."
    Zhao Y., Chen Y.Q., Bonacci T.M., Bredt D.S., Li S., Bensch W.R., Moller D.E., Kowala M., Konrad R.J., Cao G.
    J. Biol. Chem. 283:8258-8265(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION, FUNCTION, SUBCELLULAR LOCATION, BIOPHYSICOCHEMICAL PROPERTIES, TISSUE SPECIFICITY.
  8. "Lysophospholipid acyltransferases and arachidonate recycling in human neutrophils."
    Gijon M.A., Riekhof W.R., Zarini S., Murphy R.C., Voelker D.R.
    J. Biol. Chem. 283:30235-30245(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, TISSUE SPECIFICITY, SUBSTRATE SPECIFICITY.

Entry informationi

Entry nameiMBOA5_HUMAN
AccessioniPrimary (citable) accession number: Q6P1A2
Secondary accession number(s): B2RDH0
, B7Z3N3, Q7KZS1, Q92980, Q9BW40
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 2, 2006
Last sequence update: July 5, 2004
Last modified: September 3, 2014
This is version 96 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, Reference proteome

Documents

  1. Human chromosome 12
    Human chromosome 12: 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

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