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Protein

Gastric triacylglycerol lipase

Gene

LIPF

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

Functioni

Catalytic activityi

Triacylglycerol + H2O = diacylglycerol + a carboxylate.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei172 – 1721Nucleophile
Active sitei343 – 3431Charge relay system
Active sitei372 – 3721Charge relay system

GO - Molecular functioni

  1. lipid binding Source: UniProtKB
  2. malate dehydrogenase activity Source: Ensembl
  3. triglyceride lipase activity Source: UniProtKB

GO - Biological processi

  1. lipid catabolic process Source: UniProtKB-KW
  2. malate metabolic process Source: Ensembl
  3. triglyceride metabolic process Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Lipid degradation, Lipid metabolism

Names & Taxonomyi

Protein namesi
Recommended name:
Gastric triacylglycerol lipase (EC:3.1.1.3)
Short name:
GL
Short name:
Gastric lipase
Gene namesi
Name:LIPF
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 10

Organism-specific databases

HGNCiHGNC:6622. LIPF.

Subcellular locationi

GO - Cellular componenti

  1. extracellular region Source: UniProtKB-SubCell
  2. mitochondrion Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA30394.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 19191 PublicationAdd
BLAST
Chaini20 – 398379Gastric triacylglycerol lipasePRO_0000017766Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi34 – 341N-linked (GlcNAc...)
Glycosylationi99 – 991N-linked (GlcNAc...)
Disulfide bondi246 ↔ 255
Glycosylationi271 – 2711N-linked (GlcNAc...)
Glycosylationi327 – 3271N-linked (GlcNAc...)

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PaxDbiP07098.
PRIDEiP07098.

PTM databases

PhosphoSiteiP07098.

Miscellaneous databases

PMAP-CutDBP07098.

Expressioni

Gene expression databases

BgeeiP07098.
CleanExiHS_LIPF.
GenevestigatoriP07098.

Organism-specific databases

HPAiHPA045930.

Interactioni

Protein-protein interaction databases

BioGridi114085. 8 interactions.
IntActiP07098. 1 interaction.
STRINGi9606.ENSP00000238983.

Structurei

Secondary structure

1
398
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi29 – 324Combined sources
Helixi35 – 417Combined sources
Beta strandi47 – 526Combined sources
Beta strandi56 – 649Combined sources
Beta strandi79 – 835Combined sources
Helixi90 – 945Combined sources
Helixi102 – 1087Combined sources
Beta strandi112 – 1154Combined sources
Beta strandi127 – 1304Combined sources
Helixi136 – 1383Combined sources
Helixi142 – 1476Combined sources
Helixi149 – 16113Combined sources
Beta strandi166 – 1716Combined sources
Helixi173 – 18412Combined sources
Helixi186 – 1894Combined sources
Beta strandi192 – 1998Combined sources
Helixi210 – 2167Combined sources
Helixi219 – 2268Combined sources
Beta strandi228 – 2303Combined sources
Turni234 – 2396Combined sources
Helixi241 – 2499Combined sources
Helixi252 – 2554Combined sources
Helixi258 – 2636Combined sources
Helixi272 – 2743Combined sources
Helixi275 – 2795Combined sources
Helixi288 – 30013Combined sources
Helixi311 – 3188Combined sources
Beta strandi319 – 3224Combined sources
Helixi328 – 3303Combined sources
Beta strandi335 – 3406Combined sources
Beta strandi344 – 3463Combined sources
Helixi348 – 35710Combined sources
Beta strandi361 – 3677Combined sources
Helixi374 – 3774Combined sources
Helixi381 – 3844Combined sources
Helixi386 – 3938Combined sources
Turni394 – 3974Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1HLGX-ray3.00A/B28-398[»]
ProteinModelPortaliP07098.
SMRiP07098. Positions 28-398.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP07098.

Family & Domainsi

Sequence similaritiesi

Belongs to the AB hydrolase superfamily. Lipase family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiCOG0596.
GeneTreeiENSGT00550000074328.
HOGENOMiHOG000240694.
HOVERGENiHBG006265.
InParanoidiP07098.
KOiK14452.
OMAiWARRNLY.
OrthoDBiEOG71RXJN.
PhylomeDBiP07098.
TreeFamiTF315485.

Family and domain databases

Gene3Di3.40.50.1820. 1 hit.
InterProiIPR029058. AB_hydrolase.
IPR000073. AB_hydrolase_1.
IPR006693. AB_hydrolase_lipase.
IPR025483. Lipase_euk.
[Graphical view]
PfamiPF04083. Abhydro_lipase. 1 hit.
PF00561. Abhydrolase_1. 1 hit.
[Graphical view]
PIRSFiPIRSF000862. Steryl_ester_lip. 1 hit.
SUPFAMiSSF53474. SSF53474. 1 hit.
PROSITEiPS00120. LIPASE_SER. 1 hit.
[Graphical view]

Sequences (4)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 4 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: P07098-1) [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
MWLLLTMASL ISVLGTTHGL FGKLHPGSPE VTMNISQMIT YWGYPNEEYE
60 70 80 90 100
VVTEDGYILE VNRIPYGKKN SGNTGQRPVV FLQHGLLASA TNWISNLPNN
110 120 130 140 150
SLAFILADAG YDVWLGNSRG NTWARRNLYY SPDSVEFWAF SFDEMAKYDL
160 170 180 190 200
PATIDFIVKK TGQKQLHYVG HSQGTTIGFI AFSTNPSLAK RIKTFYALAP
210 220 230 240 250
VATVKYTKSL INKLRFVPQS LFKFIFGDKI FYPHNFFDQF LATEVCSREM
260 270 280 290 300
LNLLCSNALF IICGFDSKNF NTSRLDVYLS HNPAGTSVQN MFHWTQAVKS
310 320 330 340 350
GKFQAYDWGS PVQNRMHYDQ SQPPYYNVTA MNVPIAVWNG GKDLLADPQD
360 370 380 390
VGLLLPKLPN LIYHKEIPFY NHLDFIWAMD APQEVYNDIV SMISEDKK
Length:398
Mass (Da):45,238
Last modified:April 1, 1988 - v1
Checksum:iCD3EE1621C014F0F
GO
Isoform 2 (identifier: P07098-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     75-107: Missing.

Note: No experimental confirmation available.

Show »
Length:365
Mass (Da):41,693
Checksum:i31199D27DA2A3863
GO
Isoform 3 (identifier: P07098-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MFSNANSRSKM

Note: No experimental confirmation available.

Show »
Length:408
Mass (Da):46,361
Checksum:i96E2AFF12E20DF86
GO
Isoform 4 (identifier: P07098-4) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MFSNANSRSKM
     75-107: Missing.

Note: No experimental confirmation available.

Show »
Length:375
Mass (Da):42,816
Checksum:i17FA3CD30823DDCF
GO

Sequence cautioni

The sequence CAA29414.1 differs from that shown. Reason: Erroneous initiation. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti350 – 3501D → N in BAH13459 (PubMed:14702039).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti161 – 1611T → A.2 Publications
Corresponds to variant rs814628 [ dbSNP | Ensembl ].
VAR_011947
Natural varianti224 – 2241F → I.1 Publication
Corresponds to variant rs6586145 [ dbSNP | Ensembl ].
VAR_020565
Natural varianti348 – 3481P → T.1 Publication
Corresponds to variant rs17333991 [ dbSNP | Ensembl ].
VAR_020566

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 11M → MFSNANSRSKM in isoform 3 and isoform 4. 2 PublicationsVSP_047295
Alternative sequencei75 – 10733Missing in isoform 2 and isoform 4. 2 PublicationsVSP_047296Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X05997 mRNA. Translation: CAA29413.1.
X05997 mRNA. Translation: CAA29414.1. Different initiation.
AK301310 mRNA. Translation: BAH13457.1.
AK301320 mRNA. Translation: BAH13459.1.
AK312940 mRNA. Translation: BAG35782.1.
AL833751 mRNA. Translation: CAH56244.1.
AY631869 Genomic DNA. Translation: AAT38115.1.
AL358532 Genomic DNA. Translation: CAH71057.1.
CH471066 Genomic DNA. Translation: EAW50162.1.
BC112272 mRNA. Translation: AAI12273.1.
BC113711 mRNA. Translation: AAI13712.1.
CCDSiCCDS55718.1. [P07098-3]
CCDS55719.1. [P07098-2]
CCDS65896.1. [P07098-4]
CCDS7389.1. [P07098-1]
PIRiS07145.
RefSeqiNP_001185757.1. NM_001198828.1. [P07098-2]
NP_001185758.1. NM_001198829.1. [P07098-3]
NP_001185759.1. NM_001198830.1. [P07098-4]
NP_004181.1. NM_004190.3. [P07098-1]
UniGeneiHs.523130.

Genome annotation databases

EnsembliENST00000238983; ENSP00000238983; ENSG00000182333. [P07098-1]
ENST00000355843; ENSP00000348101; ENSG00000182333. [P07098-4]
ENST00000394375; ENSP00000377900; ENSG00000182333. [P07098-3]
ENST00000608620; ENSP00000477140; ENSG00000182333. [P07098-2]
GeneIDi8513.
KEGGihsa:8513.
UCSCiuc001kfg.2. human. [P07098-1]
uc010qmu.2. human.

Polymorphism databases

DMDMi126306.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

NIEHS-SNPs

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X05997 mRNA. Translation: CAA29413.1.
X05997 mRNA. Translation: CAA29414.1. Different initiation.
AK301310 mRNA. Translation: BAH13457.1.
AK301320 mRNA. Translation: BAH13459.1.
AK312940 mRNA. Translation: BAG35782.1.
AL833751 mRNA. Translation: CAH56244.1.
AY631869 Genomic DNA. Translation: AAT38115.1.
AL358532 Genomic DNA. Translation: CAH71057.1.
CH471066 Genomic DNA. Translation: EAW50162.1.
BC112272 mRNA. Translation: AAI12273.1.
BC113711 mRNA. Translation: AAI13712.1.
CCDSiCCDS55718.1. [P07098-3]
CCDS55719.1. [P07098-2]
CCDS65896.1. [P07098-4]
CCDS7389.1. [P07098-1]
PIRiS07145.
RefSeqiNP_001185757.1. NM_001198828.1. [P07098-2]
NP_001185758.1. NM_001198829.1. [P07098-3]
NP_001185759.1. NM_001198830.1. [P07098-4]
NP_004181.1. NM_004190.3. [P07098-1]
UniGeneiHs.523130.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1HLGX-ray3.00A/B28-398[»]
ProteinModelPortaliP07098.
SMRiP07098. Positions 28-398.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi114085. 8 interactions.
IntActiP07098. 1 interaction.
STRINGi9606.ENSP00000238983.

Chemistry

ChEMBLiCHEMBL1796.
DrugBankiDB01083. Orlistat.

PTM databases

PhosphoSiteiP07098.

Polymorphism databases

DMDMi126306.

Proteomic databases

PaxDbiP07098.
PRIDEiP07098.

Protocols and materials databases

DNASUi8513.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000238983; ENSP00000238983; ENSG00000182333. [P07098-1]
ENST00000355843; ENSP00000348101; ENSG00000182333. [P07098-4]
ENST00000394375; ENSP00000377900; ENSG00000182333. [P07098-3]
ENST00000608620; ENSP00000477140; ENSG00000182333. [P07098-2]
GeneIDi8513.
KEGGihsa:8513.
UCSCiuc001kfg.2. human. [P07098-1]
uc010qmu.2. human.

Organism-specific databases

CTDi8513.
GeneCardsiGC10P090415.
HGNCiHGNC:6622. LIPF.
HPAiHPA045930.
MIMi601980. gene.
neXtProtiNX_P07098.
PharmGKBiPA30394.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG0596.
GeneTreeiENSGT00550000074328.
HOGENOMiHOG000240694.
HOVERGENiHBG006265.
InParanoidiP07098.
KOiK14452.
OMAiWARRNLY.
OrthoDBiEOG71RXJN.
PhylomeDBiP07098.
TreeFamiTF315485.

Miscellaneous databases

ChiTaRSiLIPF. human.
EvolutionaryTraceiP07098.
GenomeRNAii8513.
NextBioi31864.
PMAP-CutDBP07098.
PROiP07098.
SOURCEiSearch...

Gene expression databases

BgeeiP07098.
CleanExiHS_LIPF.
GenevestigatoriP07098.

Family and domain databases

Gene3Di3.40.50.1820. 1 hit.
InterProiIPR029058. AB_hydrolase.
IPR000073. AB_hydrolase_1.
IPR006693. AB_hydrolase_lipase.
IPR025483. Lipase_euk.
[Graphical view]
PfamiPF04083. Abhydro_lipase. 1 hit.
PF00561. Abhydrolase_1. 1 hit.
[Graphical view]
PIRSFiPIRSF000862. Steryl_ester_lip. 1 hit.
SUPFAMiSSF53474. SSF53474. 1 hit.
PROSITEiPS00120. LIPASE_SER. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Molecular cloning of a human gastric lipase and expression of the enzyme in yeast."
    Bodmer M.W., Angal S., Yarranton G.T., Harris T.J.R., Lyons A., King D.J., Pieroni G., Riviere C., Verger R., Lowe P.A.
    Biochim. Biophys. Acta 909:237-244(1986) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [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(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 3).
    Tissue: Stomach.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
    Tissue: Stomach.
  4. NIEHS SNPs program
    Submitted (APR-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS ALA-161; ILE-224 AND THR-348.
  5. "The DNA sequence and comparative analysis of human chromosome 10."
    Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L., Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K., Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L., Taylor A., Battles J.
    , Bird C.P., Ainscough R., Almeida J.P., Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.
    Nature 429:375-381(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. 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(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), VARIANT ALA-161.
  8. "Human gastric lipase. The N-terminal tetrapeptide is essential for lipid binding and lipase activity."
    Bernbaeck S., Blaeckberg L.
    Eur. J. Biochem. 182:495-499(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 20-45.
  9. "Crystal structure of human gastric lipase and model of lysosomal acid lipase, two lipolytic enzymes of medical interest."
    Roussel A., Canaan S., Egloff M.P., Riviere M., Dupuis L., Verger R., Cambillau C.
    J. Biol. Chem. 274:16995-17002(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS).

Entry informationi

Entry nameiLIPG_HUMAN
AccessioniPrimary (citable) accession number: P07098
Secondary accession number(s): B7Z723
, F5H1P4, Q2M1P6, Q5VXI7, Q5VXI8, Q658L8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1988
Last sequence update: April 1, 1988
Last modified: January 7, 2015
This is version 158 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

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 10
    Human chromosome 10: 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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. 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.