Q8NCG7 (DGLB_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Sn1-specific diacylglycerol lipase beta
Short name=DGL-beta
EC=3.1.1.-

Alternative name(s):
KCCR13L

Gene names

Name:

DAGLB

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	672 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Catalyzes the hydrolysis of diacylglycerol (DAG) to 2-arachidonoyl-glycerol (2-AG), the most abundant endocannabinoid in tissues. Required for axonal growth during development and for retrograde synaptic signaling at mature synapses. Ref.8
Cofactor	Calcium. Ref.8
Enzyme regulation	Inhibited by p-hydroxy-mercuri-benzoate and HgCl2, but not to PMSF. Also inhibited by RHC80267, a drug that blocks 2-AG formation. Ref.8
Subcellular location	Cell membrane; Multi-pass membrane protein Ref.8.
Sequence similarities	Belongs to the AB hydrolase superfamily. Lipase family.
Biophysicochemical properties	Kinetic parameters: KM=74.1 µM for diacylglycerol Ref.8 Vmax=3.45 nmol/min/mg enzyme pH dependence: Optimum pH is 7.0.
Sequence caution	The sequence BAB85017.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
Biological process	Lipid degradation Lipid metabolism
Cellular component	Cell membrane Membrane
Coding sequence diversity	Alternative splicing Polymorphism
Domain	Transmembrane Transmembrane helix
Ligand	Calcium Metal-binding
Molecular function	Hydrolase
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	lipid catabolic process Inferred from electronic annotation. Source: UniProtKB-KW platelet activation Traceable author statement. Source: Reactome
Cellular_component	integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW plasma membrane Traceable author statement. Source: Reactome
Molecular_function	metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW triglyceride lipase activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Alternative products

This entry describes 4 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q8NCG7-1)

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.

Isoform 2 (identifier: Q8NCG7-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-281: Missing.

Note: No experimental confirmation available.

Isoform 3 (identifier: Q8NCG7-3)

The sequence of this isoform differs from the canonical sequence as follows:
     249-267: IRNNQEPAQVVCHAPGSSQ → TRATGNCPRNDGLTLLSLN
     268-672: Missing.

Note: No experimental confirmation available.

Isoform 4 (identifier: Q8NCG7-4)

The sequence of this isoform differs from the canonical sequence as follows:
     140-310: SWIIIAATVV...TGLCRIGGDC → RTQIWCPATL...WSAMPQGAPS

Note: No experimental confirmation available.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 672	672	Sn1-specific diacylglycerol lipase beta		PRO_0000248350
Regions
	Topological domain	1 – 17	17	Cytoplasmic Potential
	Transmembrane	18 – 38	21	Helical; Potential
	Topological domain	39 – 58	20	Extracellular Potential
	Transmembrane	59 – 79	21	Helical; Potential
	Topological domain	80 – 102	23	Cytoplasmic Potential
	Transmembrane	103 – 123	21	Helical; Potential
	Topological domain	124 – 132	9	Extracellular Potential
	Transmembrane	133 – 153	21	Helical; Potential
	Topological domain	154 – 672	519	Cytoplasmic Potential
Sites
	Active site	443	1	Charge relay system
	Active site	495	1	Charge relay system
Amino acid modifications
	Modified residue	570	1	Phosphoserine Ref.9 Ref.11 Ref.12
	Modified residue	574	1	Phosphoserine Ref.11
	Modified residue	579	1	Phosphoserine Ref.12
	Modified residue	584	1	Phosphoserine Ref.10
Natural variations
	Alternative sequence	1 – 281	281	Missing in isoform 2.		VSP_020245
	Alternative sequence	140 – 310	171	SWIII…IGGDC → RTQIWCPATLRRASPCFISN RTISGTTKSLPRWSAMPQGA PS in isoform 4.		VSP_043309
	Alternative sequence	249 – 267	19	IRNNQ…PGSSQ → TRATGNCPRNDGLTLLSLN in isoform 3.		VSP_020246
	Alternative sequence	268 – 672	405	Missing in isoform 3.		VSP_020247
	Natural variant	664	1	Q → R. Ref.2 Ref.7 Corresponds to variant rs2303361 [ dbSNP | Ensembl ].		VAR_027275
Experimental info
	Mutagenesis	443	1	S → A: Loss of activity. Ref.8
	Mutagenesis	495	1	D → A: Loss of activity. Ref.8
	Sequence conflict	270	1	D → Y in BAC11175. Ref.3
	Sequence conflict	456	1	L → V in BAC04258. Ref.2
	Sequence conflict	545	1	T → K in AAH27603. Ref.7

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified September 5, 2006. Version 2. Checksum: AA953D737E0EFF44	FASTA	672	73,732
	10 20 30 40 50 60 MPGMVLFGRR WAIASDDLVF PGFFELVVRV LWWIGILTLY LMHRGKLDCA GGALLSSYLI 70 80 90 100 110 120 VLMILLAVVI CTVSAIMCVS MRGTICNPGP RKSMSKLLYI RLALFFPEMV WASLGAAWVA 130 140 150 160 170 180 DGVQCDRTVV NGIIATVVVS WIIIAATVVS IIIVFDPLGG KMAPYSSAGP SHLDSHDSSQ 190 200 210 220 230 240 LLNGLKTAAT SVWETRIKLL CCCIGKDDHT RVAFSSTAEL FSTYFSDTDL VPSDIAAGLA 250 260 270 280 290 300 LLHQQQDNIR NNQEPAQVVC HAPGSSQEAD LDAELENCHH YMQFAAAAYG WPLYIYRNPL 310 320 330 340 350 360 TGLCRIGGDC CRSRTTDYDL VGGDQLNCHF GSILHTTGLQ YRDFIHVSFH DKVYELPFLV 370 380 390 400 410 420 ALDHRKESVV VAVRGTMSLQ DVLTDLSAES EVLDVECEVQ DRLAHKGISQ AARYVYQRLI 430 440 450 460 470 480 NDGILSQAFS IAPEYRLVIV GHSLGGGAAA LLATMLRAAY PQVRCYAFSP PRGLWSKALQ 490 500 510 520 530 540 EYSQSFIVSL VLGKDVIPRL SVTNLEDLKR RILRVVAHCN KPKYKILLHG LWYELFGGNP 550 560 570 580 590 600 NNLPTELDGG DQEVLTQPLL GEQSLLTRWS PAYSFSSDSP LDSSPKYPPL YPPGRIIHLQ 610 620 630 640 650 660 EEGASGRFGC CSAAHYSAKW SHEAEFSKIL IGPKMLTDHM PDILMRALDS VVSDRAACVS 670 CPAQGVSSVD VA
	Isoform 2 [UniParc]. Checksum: 4DAEA2A26417EA69	FASTA	391	43,191
	10 20 30 40 50 60 MQFAAAAYGW PLYIYRNPLT GLCRIGGDCC RSRTTDYDLV GGDQLNCHFG SILHTTGLQY 70 80 90 100 110 120 RDFIHVSFHD KVYELPFLVA LDHRKESVVV AVRGTMSLQD VLTDLSAESE VLDVECEVQD 130 140 150 160 170 180 RLAHKGISQA ARYVYQRLIN DGILSQAFSI APEYRLVIVG HSLGGGAAAL LATMLRAAYP 190 200 210 220 230 240 QVRCYAFSPP RGLWSKALQE YSQSFIVSLV LGKDVIPRLS VTNLEDLKRR ILRVVAHCNK 250 260 270 280 290 300 PKYKILLHGL WYELFGGNPN NLPTELDGGD QEVLTQPLLG EQSLLTRWSP AYSFSSDSPL 310 320 330 340 350 360 DSSPKYPPLY PPGRIIHLQE EGASGRFGCC SAAHYSAKWS HEAEFSKILI GPKMLTDHMP 370 380 390 DILMRALDSV VSDRAACVSC PAQGVSSVDV A
	Isoform 3 [UniParc]. Checksum: 661A57D0B8F4CB6A	FASTA	267	28,899
	10 20 30 40 50 60 MPGMVLFGRR WAIASDDLVF PGFFELVVRV LWWIGILTLY LMHRGKLDCA GGALLSSYLI 70 80 90 100 110 120 VLMILLAVVI CTVSAIMCVS MRGTICNPGP RKSMSKLLYI RLALFFPEMV WASLGAAWVA 130 140 150 160 170 180 DGVQCDRTVV NGIIATVVVS WIIIAATVVS IIIVFDPLGG KMAPYSSAGP SHLDSHDSSQ 190 200 210 220 230 240 LLNGLKTAAT SVWETRIKLL CCCIGKDDHT RVAFSSTAEL FSTYFSDTDL VPSDIAAGLA 250 260 LLHQQQDNTR ATGNCPRNDG LTLLSLN
	Isoform 4 [UniParc]. Checksum: BD549DBC7456917F	FASTA	543	59,837
	10 20 30 40 50 60 MPGMVLFGRR WAIASDDLVF PGFFELVVRV LWWIGILTLY LMHRGKLDCA GGALLSSYLI 70 80 90 100 110 120 VLMILLAVVI CTVSAIMCVS MRGTICNPGP RKSMSKLLYI RLALFFPEMV WASLGAAWVA 130 140 150 160 170 180 DGVQCDRTVV NGIIATVVVR TQIWCPATLR RASPCFISNR TISGTTKSLP RWSAMPQGAP 190 200 210 220 230 240 SCRSRTTDYD LVGGDQLNCH FGSILHTTGL QYRDFIHVSF HDKVYELPFL VALDHRKESV 250 260 270 280 290 300 VVAVRGTMSL QDVLTDLSAE SEVLDVECEV QDRLAHKGIS QAARYVYQRL INDGILSQAF 310 320 330 340 350 360 SIAPEYRLVI VGHSLGGGAA ALLATMLRAA YPQVRCYAFS PPRGLWSKAL QEYSQSFIVS 370 380 390 400 410 420 LVLGKDVIPR LSVTNLEDLK RRILRVVAHC NKPKYKILLH GLWYELFGGN PNNLPTELDG 430 440 450 460 470 480 GDQEVLTQPL LGEQSLLTRW SPAYSFSSDS PLDSSPKYPP LYPPGRIIHL QEEGASGRFG 490 500 510 520 530 540 CCSAAHYSAK WSHEAEFSKI LIGPKMLTDH MPDILMRALD SVVSDRAACV SCPAQGVSSV DVA

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	Morimura S., Yasumoto S. Submitted (NOV-2001) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). Tissue: Placenta.
[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] (ISOFORMS 2; 3 AND 4), VARIANT ARG-664. Tissue: Trachea.
[3]	"Signal sequence and keyword trap in silico for selection of full-length human cDNAs encoding secretion or membrane proteins from oligo-capped cDNA libraries." Otsuki T., Ota T., Nishikawa T., Hayashi K., Suzuki Y., Yamamoto J., Wakamatsu A., Kimura K., Sakamoto K., Hatano N., Kawai Y., Ishii S., Saito K., Kojima S., Sugiyama T., Ono T., Okano K., Yoshikawa Y. , Aotsuka S., Sasaki N., Hattori A., Okumura K., Nagai K., Sugano S., Isogai T. DNA Res. 12:117-126(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). Tissue: Embryo.
[4]	"The DNA sequence of human chromosome 7." Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H., Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A., Delehaunty K.D., Miner T.L. , Nash W.E., Cordes M., Du H., Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C., Latreille P., Miller N., Johnson D., Murray J., Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E., Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H., Wilson R.K. Nature 424:157-164(2003) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]	"Human chromosome 7: DNA sequence and biology." Scherer S.W., Cheung J., MacDonald J.R., Osborne L.R., Nakabayashi K., Herbrick J.-A., Carson A.R., Parker-Katiraee L., Skaug J., Khaja R., Zhang J., Hudek A.K., Li M., Haddad M., Duggan G.E., Fernandez B.A., Kanematsu E., Gentles S. , Christopoulos C.C., Choufani S., Kwasnicka D., Zheng X.H., Lai Z., Nusskern D.R., Zhang Q., Gu Z., Lu F., Zeesman S., Nowaczyk M.J., Teshima I., Chitayat D., Shuman C., Weksberg R., Zackai E.H., Grebe T.A., Cox S.R., Kirkpatrick S.J., Rahman N., Friedman J.M., Heng H.H.Q., Pelicci P.G., Lo-Coco F., Belloni E., Shaffer L.G., Pober B., Morton C.C., Gusella J.F., Bruns G.A.P., Korf B.R., Quade B.J., Ligon A.H., Ferguson H., Higgins A.W., Leach N.T., Herrick S.R., Lemyre E., Farra C.G., Kim H.-G., Summers A.M., Gripp K.W., Roberts W., Szatmari P., Winsor E.J.T., Grzeschik K.-H., Teebi A., Minassian B.A., Kere J., Armengol L., Pujana M.A., Estivill X., Wilson M.D., Koop B.F., Tosi S., Moore G.E., Boright A.P., Zlotorynski E., Kerem B., Kroisel P.M., Petek E., Oscier D.G., Mould S.J., Doehner H., Doehner K., Rommens J.M., Vincent J.B., Venter J.C., Li P.W., Mural R.J., Adams M.D., Tsui L.-C. Science 300:767-772(2003) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]	"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), VARIANT ARG-664. Tissue: Testis.
[8]	"Cloning of the first sn1-DAG lipases points to the spatial and temporal regulation of endocannabinoid signaling in the brain." Bisogno T., Howell F., Williams G., Minassi A., Cascio M.G., Ligresti A., Matias I., Schiano-Moriello A., Paul P., Williams E.-J., Gangadharan U., Hobbs C., Di Marzo V., Doherty P. J. Cell Biol. 163:463-468(2003) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, ENZYME REGULATION, SUBCELLULAR LOCATION, MUTAGENESIS OF SER-443 AND ASP-495.
[9]	"Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle." Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M. Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-570, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[10]	"A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-584, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[11]	"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions." Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K. Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-570 AND SER-574, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[12]	"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis." Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M. Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-570 AND SER-579, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF450090 mRNA. Translation: AAL47020.1. AK093958 mRNA. Translation: BAC04258.1. AK074210 mRNA. Translation: BAB85017.1. Different initiation. AK122748 mRNA. Translation: BAG53702.1. AK298955 mRNA. Translation: BAG61052.1. AK074584 mRNA. Translation: BAC11073.1. AK074744 mRNA. Translation: BAC11175.1. AK075128 mRNA. Translation: BAC11420.1. AC009412 Genomic DNA. No translation available. AC072052 Genomic DNA. No translation available. CH878731 Genomic DNA. Translation: EAW55033.1. CH878731 Genomic DNA. Translation: EAW55035.1. CH236963 Genomic DNA. Translation: EAL23721.1. BC027603 mRNA. Translation: AAH27603.1.
IPI	IPI00385987. IPI00785012. IPI00926351. IPI00927759.
RefSeq	NP_001136408.1. NM_001142936.1. NP_631918.3. NM_139179.3.
UniGene	Hs.487498.
3D structure databases
ProteinModelPortal	Q8NCG7.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q8NCG7. 2 interactions.
MINT	MINT-1386028.
STRING	9606.ENSP00000297056.
PTM databases
PhosphoSite	Q8NCG7.
Polymorphism databases
DMDM	114149272.
Proteomic databases
PaxDb	Q8NCG7.
PRIDE	Q8NCG7.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000297056; ENSP00000297056; ENSG00000164535. ENST00000425398; ENSP00000391171; ENSG00000164535.
GeneID	221955.
KEGG	hsa:221955.
UCSC	uc003sqa.3. human.
Organism-specific databases
CTD	221955.
GeneCards	GC07M006416.
H-InvDB	HIX0006466.
HGNC	HGNC:28923. DAGLB.
MIM	614016. gene.
neXtProt	NX_Q8NCG7.
PharmGKB	PA162383203.
GenAtlas	Search...
Phylogenomic databases
eggNOG	NOG324741.
HOGENOM	HOG000246993.
HOVERGEN	HBG055573.
InParanoid	Q8NCG7.
KO	K13806.
OMA	LYLMHRG.
OrthoDB	EOG428216.
PhylomeDB	Q8NCG7.
Enzyme and pathway databases
Reactome	REACT_111102. Signal Transduction. REACT_604. Hemostasis.
Gene expression databases
ArrayExpress	Q8NCG7.
Bgee	Q8NCG7.
CleanEx	HS_DAGLB.
Genevestigator	Q8NCG7.
GermOnline	ENSG00000164535. Homo sapiens.
Family and domain databases
InterPro	IPR002921. Lipase_3. [Graphical view]
Pfam	PF01764. Lipase_3. 1 hit. [Graphical view]
PROSITE	PS00120. LIPASE_SER. 1 hit. [Graphical view]
ProtoNet	Search...
Other
BindingDB	Q8NCG7.
ChEMBL	CHEMBL5521.
ChiTaRS	DAGLB. human.
GenomeRNAi	221955.
NextBio	91515.
SOURCE	Search...

Entry information

Entry name

DGLB_HUMAN

Accession

Primary (citable) accession number: Q8NCG7
Secondary accession number(s): A4D2P3 , B3KV90, B4DQU0, Q6PIX3, Q8N2N2, Q8N9S1, Q8TED3, Q8WXE6

Entry history

Integrated into UniProtKB/Swiss-Prot:	September 5, 2006
Last sequence update:	September 5, 2006
Last modified:	May 1, 2013
This is version 80 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.