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P16233

- LIPP_HUMAN

UniProt

P16233 - LIPP_HUMAN

Protein

Pancreatic triacylglycerol lipase

Gene

PNLIP

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 156 (01 Oct 2014)
      Sequence version 1 (01 Apr 1990)
      Previous versions | rss
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    Functioni

    Catalytic activityi

    Triacylglycerol + H2O = diacylglycerol + a carboxylate.1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei169 – 1691Nucleophile
    Active sitei193 – 1931Charge relay system
    Metal bindingi204 – 2041Calcium; via carbonyl oxygen
    Metal bindingi207 – 2071Calcium; via carbonyl oxygen
    Metal bindingi209 – 2091Calcium
    Metal bindingi212 – 2121Calcium
    Active sitei280 – 2801Charge relay system

    GO - Molecular functioni

    1. metal ion binding Source: UniProtKB-KW
    2. triglyceride lipase activity Source: ProtInc

    GO - Biological processi

    1. intestinal cholesterol absorption Source: Ensembl
    2. lipid catabolic process Source: UniProtKB-KW
    3. lipid digestion Source: Reactome
    4. phototransduction, visible light Source: Reactome
    5. retinoid metabolic process Source: Reactome
    6. small molecule metabolic process Source: Reactome

    Keywords - Molecular functioni

    Hydrolase

    Keywords - Biological processi

    Lipid degradation, Lipid metabolism

    Keywords - Ligandi

    Calcium, Metal-binding

    Enzyme and pathway databases

    BioCyciMetaCyc:HS10947-MONOMER.
    ReactomeiREACT_24968. Retinoid metabolism and transport.
    REACT_9518. Digestion of dietary lipid.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Pancreatic triacylglycerol lipase (EC:3.1.1.3)
    Short name:
    PL
    Short name:
    PTL
    Short name:
    Pancreatic lipase
    Gene namesi
    Name:PNLIP
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 10

    Organism-specific databases

    HGNCiHGNC:9155. PNLIP.

    Subcellular locationi

    GO - Cellular componenti

    1. extracellular region Source: Reactome

    Keywords - Cellular componenti

    Secreted

    Pathology & Biotechi

    Organism-specific databases

    MIMi246600. gene+phenotype.
    PharmGKBiPA33478.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 1616Add
    BLAST
    Chaini17 – 465449Pancreatic triacylglycerol lipasePRO_0000017785Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi20 ↔ 26
    Disulfide bondi107 ↔ 118
    Glycosylationi183 – 1831N-linked (GlcNAc...)
    Disulfide bondi254 ↔ 278
    Disulfide bondi302 ↔ 313
    Disulfide bondi316 ↔ 321
    Disulfide bondi449 ↔ 465

    Keywords - PTMi

    Disulfide bond, Glycoprotein

    Proteomic databases

    PaxDbiP16233.
    PRIDEiP16233.

    PTM databases

    PhosphoSiteiP16233.

    Expressioni

    Inductioni

    By colipase/CLPS in the presence of bile salts.

    Gene expression databases

    BgeeiP16233.
    CleanExiHS_PNLIP.
    GenevestigatoriP16233.

    Interactioni

    Protein-protein interaction databases

    BioGridi111407. 2 interactions.
    IntActiP16233. 1 interaction.
    MINTiMINT-1179407.
    STRINGi9606.ENSP00000358223.

    Structurei

    Secondary structure

    1
    465
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi18 – 214
    Turni22 – 243
    Beta strandi25 – 284
    Turni31 – 333
    Beta strandi34 – 385
    Helixi48 – 514
    Beta strandi54 – 585
    Beta strandi60 – 656
    Beta strandi67 – 693
    Helixi73 – 786
    Beta strandi87 – 915
    Helixi101 – 11010
    Turni111 – 1133
    Beta strandi117 – 1226
    Helixi124 – 1274
    Helixi131 – 15626
    Helixi160 – 1623
    Beta strandi163 – 1686
    Helixi170 – 18011
    Turni181 – 1844
    Beta strandi186 – 1938
    Turni197 – 2015
    Turni204 – 2063
    Helixi210 – 2123
    Beta strandi216 – 2194
    Turni227 – 2293
    Beta strandi239 – 2457
    Beta strandi248 – 2503
    Helixi258 – 2625
    Helixi268 – 29124
    Turni294 – 2974
    Helixi305 – 3095
    Beta strandi323 – 3253
    Helixi328 – 3303
    Turni332 – 3354
    Beta strandi336 – 3449
    Beta strandi348 – 3514
    Beta strandi355 – 36511
    Beta strandi368 – 37811
    Beta strandi386 – 3938
    Beta strandi398 – 40710
    Beta strandi411 – 42010
    Beta strandi431 – 44010
    Beta strandi445 – 4495
    Beta strandi460 – 4645

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1LPAX-ray3.04B17-465[»]
    1LPBX-ray2.46B17-465[»]
    1N8SX-ray3.04A17-465[»]
    ProteinModelPortaliP16233.
    SMRiP16233. Positions 17-465.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP16233.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini355 – 465111PLATPROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

    Belongs to the AB hydrolase superfamily. Lipase family.Curated
    Contains 1 PLAT domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Signal

    Phylogenomic databases

    eggNOGiNOG40923.
    HOGENOMiHOG000038552.
    HOVERGENiHBG003243.
    InParanoidiP16233.
    KOiK14073.
    OMAiVKFIWYN.
    OrthoDBiEOG7KSX8B.
    PhylomeDBiP16233.
    TreeFamiTF324997.

    Family and domain databases

    Gene3Di2.60.60.20. 1 hit.
    3.40.50.1820. 1 hit.
    InterProiIPR029058. AB_hydrolase.
    IPR000734. Lipase.
    IPR008976. Lipase_LipOase.
    IPR013818. Lipase_N.
    IPR002331. Lipase_panc.
    IPR016272. Lipoprotein_lipase_LIPH.
    IPR001024. PLAT/LH2_dom.
    [Graphical view]
    PANTHERiPTHR11610. PTHR11610. 1 hit.
    PfamiPF00151. Lipase. 1 hit.
    PF01477. PLAT. 1 hit.
    [Graphical view]
    PIRSFiPIRSF000865. Lipoprotein_lipase_LIPH. 1 hit.
    PRINTSiPR00823. PANCLIPASE.
    PR00821. TAGLIPASE.
    SMARTiSM00308. LH2. 1 hit.
    [Graphical view]
    SUPFAMiSSF49723. SSF49723. 1 hit.
    SSF53474. SSF53474. 1 hit.
    PROSITEiPS00120. LIPASE_SER. 1 hit.
    PS50095. PLAT. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    P16233-1 [UniParc]FASTAAdd to Basket

    « Hide

    MLPLWTLSLL LGAVAGKEVC YERLGCFSDD SPWSGITERP LHILPWSPKD    50
    VNTRFLLYTN ENPNNFQEVA ADSSSISGSN FKTNRKTRFI IHGFIDKGEE 100
    NWLANVCKNL FKVESVNCIC VDWKGGSRTG YTQASQNIRI VGAEVAYFVE 150
    FLQSAFGYSP SNVHVIGHSL GAHAAGEAGR RTNGTIGRIT GLDPAEPCFQ 200
    GTPELVRLDP SDAKFVDVIH TDGAPIVPNL GFGMSQVVGH LDFFPNGGVE 250
    MPGCKKNILS QIVDIDGIWE GTRDFAACNH LRSYKYYTDS IVNPDGFAGF 300
    PCASYNVFTA NKCFPCPSGG CPQMGHYADR YPGKTNDVGQ KFYLDTGDAS 350
    NFARWRYKVS VTLSGKKVTG HILVSLFGNK GNSKQYEIFK GTLKPDSTHS 400
    NEFDSDVDVG DLQMVKFIWY NNVINPTLPR VGASKIIVET NVGKQFNFCS 450
    PETVREEVLL TLTPC 465
    Length:465
    Mass (Da):51,157
    Last modified:April 1, 1990 - v1
    Checksum:i2BC49CC7F0E2DF52
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    J05125 mRNA. Translation: AAA36740.1.
    M93285 mRNA. Translation: AAA60129.1.
    L24529
    , L11242, L24502, L24522, L24523, L24525, L24526, L24527, L24528 Genomic DNA. Translation: AAA99053.1.
    AK313941 mRNA. Translation: BAG36659.1.
    AL731653 Genomic DNA. Translation: CAH72667.1.
    CH471066 Genomic DNA. Translation: EAW49451.1.
    BC014309 mRNA. Translation: AAH14309.1.
    CCDSiCCDS7594.1.
    PIRiC43357.
    RefSeqiNP_000927.1. NM_000936.2.
    UniGeneiHs.501135.

    Genome annotation databases

    EnsembliENST00000369221; ENSP00000358223; ENSG00000175535.
    GeneIDi5406.
    KEGGihsa:5406.
    UCSCiuc001lcm.3. human.

    Polymorphism databases

    DMDMi126318.

    Cross-referencesi

    Web resourcesi

    Wikipedia

    Pancreatic lipase entry

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    J05125 mRNA. Translation: AAA36740.1 .
    M93285 mRNA. Translation: AAA60129.1 .
    L24529
    , L11242 , L24502 , L24522 , L24523 , L24525 , L24526 , L24527 , L24528 Genomic DNA. Translation: AAA99053.1 .
    AK313941 mRNA. Translation: BAG36659.1 .
    AL731653 Genomic DNA. Translation: CAH72667.1 .
    CH471066 Genomic DNA. Translation: EAW49451.1 .
    BC014309 mRNA. Translation: AAH14309.1 .
    CCDSi CCDS7594.1.
    PIRi C43357.
    RefSeqi NP_000927.1. NM_000936.2.
    UniGenei Hs.501135.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1LPA X-ray 3.04 B 17-465 [» ]
    1LPB X-ray 2.46 B 17-465 [» ]
    1N8S X-ray 3.04 A 17-465 [» ]
    ProteinModelPortali P16233.
    SMRi P16233. Positions 17-465.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 111407. 2 interactions.
    IntActi P16233. 1 interaction.
    MINTi MINT-1179407.
    STRINGi 9606.ENSP00000358223.

    Chemistry

    BindingDBi P16233.
    ChEMBLi CHEMBL1812.
    DrugBanki DB00522. Bentiromide.
    DB01083. Orlistat.
    GuidetoPHARMACOLOGYi 2590.

    PTM databases

    PhosphoSitei P16233.

    Polymorphism databases

    DMDMi 126318.

    Proteomic databases

    PaxDbi P16233.
    PRIDEi P16233.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000369221 ; ENSP00000358223 ; ENSG00000175535 .
    GeneIDi 5406.
    KEGGi hsa:5406.
    UCSCi uc001lcm.3. human.

    Organism-specific databases

    CTDi 5406.
    GeneCardsi GC10P118305.
    HGNCi HGNC:9155. PNLIP.
    MIMi 246600. gene+phenotype.
    neXtProti NX_P16233.
    PharmGKBi PA33478.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG40923.
    HOGENOMi HOG000038552.
    HOVERGENi HBG003243.
    InParanoidi P16233.
    KOi K14073.
    OMAi VKFIWYN.
    OrthoDBi EOG7KSX8B.
    PhylomeDBi P16233.
    TreeFami TF324997.

    Enzyme and pathway databases

    BioCyci MetaCyc:HS10947-MONOMER.
    Reactomei REACT_24968. Retinoid metabolism and transport.
    REACT_9518. Digestion of dietary lipid.

    Miscellaneous databases

    ChiTaRSi PNLIP. human.
    EvolutionaryTracei P16233.
    GeneWikii Pancreatic_lipase.
    GenomeRNAii 5406.
    NextBioi 20931.
    PROi P16233.
    SOURCEi Search...

    Gene expression databases

    Bgeei P16233.
    CleanExi HS_PNLIP.
    Genevestigatori P16233.

    Family and domain databases

    Gene3Di 2.60.60.20. 1 hit.
    3.40.50.1820. 1 hit.
    InterProi IPR029058. AB_hydrolase.
    IPR000734. Lipase.
    IPR008976. Lipase_LipOase.
    IPR013818. Lipase_N.
    IPR002331. Lipase_panc.
    IPR016272. Lipoprotein_lipase_LIPH.
    IPR001024. PLAT/LH2_dom.
    [Graphical view ]
    PANTHERi PTHR11610. PTHR11610. 1 hit.
    Pfami PF00151. Lipase. 1 hit.
    PF01477. PLAT. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF000865. Lipoprotein_lipase_LIPH. 1 hit.
    PRINTSi PR00823. PANCLIPASE.
    PR00821. TAGLIPASE.
    SMARTi SM00308. LH2. 1 hit.
    [Graphical view ]
    SUPFAMi SSF49723. SSF49723. 1 hit.
    SSF53474. SSF53474. 1 hit.
    PROSITEi PS00120. LIPASE_SER. 1 hit.
    PS50095. PLAT. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Cloning and characterization of human pancreatic lipase cDNA."
      Lowe M.E., Rosenblum J.L., Strauss A.W.
      J. Biol. Chem. 264:20042-20048(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    2. "Two novel human pancreatic lipase related proteins, hPLRP1 and hPLRP2. Differences in colipase dependence and in lipase activity."
      Giller T., Buchwald P., Blum-Kaelin D., Hunziker W.
      J. Biol. Chem. 267:16509-16516(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Pancreas.
    3. "The human pancreatic lipase-encoding gene: structure and conservation of an Alu sequence in the lipase gene family."
      Sims H.F., Jennens M.L., Lowe M.E.
      Gene 131:281-285(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    4. "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].
    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(2004) [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(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Lung.
    8. "Hydrolysis of retinyl esters by pancreatic triglyceride lipase."
      van Bennekum A.M., Fisher E.A., Blaner W.S., Harrison E.H.
      Biochemistry 39:4900-4906(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: CATALYTIC ACTIVITY.
    9. Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS).
    10. "Structure of the pancreatic lipase-procolipase complex."
      van Tilbeurgh H., Sarda L., Verger R., Cambillau C.
      Nature 359:159-162(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) IN COMPLEX WITH CLPS.
    11. "Interfacial activation of the lipase-procolipase complex by mixed micelles revealed by X-ray crystallography."
      van Tilbeurgh H., Egloff M.-P., Martinez C., Rugani N., Verger R., Cambillau C.
      Nature 362:814-820(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) IN COMPLEX WITH CLPS.
    12. "Structure-function relationships in naturally occurring mutants of pancreatic lipase."
      Carriere F., Thirstrup K., Boel E., Verger R., Thim L.
      Protein Eng. 7:563-569(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 354-465.

    Entry informationi

    Entry nameiLIPP_HUMAN
    AccessioniPrimary (citable) accession number: P16233
    Secondary accession number(s): Q5VSQ2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 1, 1990
    Last sequence update: April 1, 1990
    Last modified: October 1, 2014
    This is version 156 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, Reference proteome

    Documents

    1. Human chromosome 10
      Human chromosome 10: entries, gene names and cross-references to MIM
    2. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    3. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    4. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3