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Q96Q80

- DERL3_HUMAN

UniProt

Q96Q80 - DERL3_HUMAN

Protein

Derlin-3

Gene

DERL3

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
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    • History
      Entry version 99 (01 Oct 2014)
      Sequence version 2 (19 Jul 2004)
      Previous versions | rss
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    Functioni

    Functional component of endoplasmic reticulum-associated degradation (ERAD) for misfolded lumenal glycoproteins, but not that of misfolded nonglycoproteins. May act by forming a channel that allows the retrotranslocation of misfolded glycoproteins into the cytosol where they are ubiquitinated and degraded by the proteasome. May mediate the interaction between VCP and the degradation substrate.2 Publications

    GO - Molecular functioni

    1. protein binding Source: UniProtKB

    GO - Biological processi

    1. endoplasmic reticulum unfolded protein response Source: UniProtKB
    2. ER-associated ubiquitin-dependent protein catabolic process Source: UniProtKB
    3. protein N-linked glycosylation via asparagine Source: UniProtKB

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Derlin-3
    Alternative name(s):
    Degradation in endoplasmic reticulum protein 3
    Short name:
    DERtrin-3
    Der1-like protein 3
    Gene namesi
    Name:DERL3
    Synonyms:C22orf14, DER3, LLN2
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 22

    Organism-specific databases

    HGNCiHGNC:14236. DERL3.

    Subcellular locationi

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

    GO - Cellular componenti

    1. integral component of endoplasmic reticulum membrane Source: UniProtKB

    Keywords - Cellular componenti

    Endoplasmic reticulum, Membrane

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA25883.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 235235Derlin-3PRO_0000219048Add
    BLAST

    Proteomic databases

    PaxDbiQ96Q80.
    PRIDEiQ96Q80.

    Expressioni

    Tissue specificityi

    Unlike DERL1 and DERL2, restricted to several tissues. Expressed at high levels in placenta, pancreas, spleen and small intestine.1 Publication

    Inductioni

    Up-regulated in response to endoplasmic reticulum stress via the ERN1-XBP1 pathway of the unfolded protein response (UPR).By similarity

    Gene expression databases

    ArrayExpressiQ96Q80.
    BgeeiQ96Q80.
    CleanExiHS_DERL3.
    GenevestigatoriQ96Q80.

    Organism-specific databases

    HPAiCAB037234.
    HPA049306.

    Interactioni

    Subunit structurei

    Forms homo- and heterooligomers with DERL2 and, to a lesser extent, with DERL1. Interacts with VCP, EDEM1, SELK and VIMP/SELS.2 Publications

    Protein-protein interaction databases

    BioGridi124816. 3 interactions.
    STRINGi9606.ENSP00000384744.

    Structurei

    3D structure databases

    ProteinModelPortaliQ96Q80.
    SMRiQ96Q80. Positions 11-185.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini1 – 2222CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini44 – 5815LumenalSequence AnalysisAdd
    BLAST
    Topological domaini80 – 9819CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini120 – 15738LumenalSequence AnalysisAdd
    BLAST
    Topological domaini179 – 23557CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei23 – 4321Helical; Name=1Sequence AnalysisAdd
    BLAST
    Transmembranei59 – 7921Helical; Name=2Sequence AnalysisAdd
    BLAST
    Transmembranei99 – 11921Helical; Name=3Sequence AnalysisAdd
    BLAST
    Transmembranei158 – 17821Helical; Name=4Sequence AnalysisAdd
    BLAST

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the derlin family.Curated

    Keywords - Domaini

    Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiCOG5291.
    HOGENOMiHOG000200948.
    HOVERGENiHBG051338.
    KOiK13989.
    OrthoDBiEOG73RBC2.
    PhylomeDBiQ96Q80.
    TreeFamiTF314715.

    Family and domain databases

    InterProiIPR007599. DER1.
    [Graphical view]
    PANTHERiPTHR11009. PTHR11009. 1 hit.
    PfamiPF04511. DER1. 1 hit.
    [Graphical view]

    Sequences (5)i

    Sequence statusi: Complete.

    This entry describes 5 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q96Q80-1) [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

    MAWQGLAAEF LQVPAVTRAY TAACVLTTAA VQLELLSPFQ LYFNPHLVFR    50
    KFQVWRLVTN FLFFGPLGFS FFFNMLFVFR YCRMLEEGSF RGRTADFVFM 100
    FLFGGVLMTL LGLLGSLFFL GQALMAMLVY VWSRRSPRVR VNFFGLLTFQ 150
    APFLPWALMG FSLLLGNSIL VDLLGIAVGH IYYFLEDVFP NQPGGKRLLQ 200
    TPGFLKLLLD APAEDPNYLP LPEEQPGPHL PPPQQ 235
    Length:235
    Mass (Da):26,679
    Last modified:July 19, 2004 - v2
    Checksum:i2DC5F02487C4B824
    GO
    Isoform 2 (identifier: Q96Q80-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         206-235: KLLLDAPAEDPNYLPLPEEQPGPHLPPPQQ → GLQSSKAPAGSSLTIWTQQSQGGPGTAGELAAPS

    Note: No experimental confirmation available.

    Show »
    Length:239
    Mass (Da):26,605
    Checksum:i7297772E29193957
    GO
    Isoform 3 (identifier: Q96Q80-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         206-235: KLLLDAPAEDPNYLPLPEEQPGPHLPPPQQ → LATAQQCPHRTGPSAGDFRAARPQLAVA

    Note: No experimental confirmation available.

    Show »
    Length:233
    Mass (Da):26,255
    Checksum:i98A860411ED2C73B
    GO
    Isoform 4 (identifier: Q96Q80-4) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-74: Missing.
         110-205: LLGLLGSLFF...KRLLQTPGFL → VSFPQALEPR...LCSTRAPPHR

    Note: No experimental confirmation available.

    Show »
    Length:225
    Mass (Da):23,859
    Checksum:i30576E135EC94D48
    GO
    Isoform 5 (identifier: Q96Q80-5) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         206-235: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:205
    Mass (Da):23,382
    Checksum:iE125D7D2EDBB8031
    GO

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti149 – 1491F → L.1 Publication
    Corresponds to variant rs3177243 [ dbSNP | Ensembl ].
    VAR_048897
    Natural varianti211 – 2111A → V.1 Publication
    Corresponds to variant rs1128127 [ dbSNP | Ensembl ].
    VAR_019517

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 7474Missing in isoform 4. 1 PublicationVSP_011086Add
    BLAST
    Alternative sequencei110 – 20596LLGLL…TPGFL → VSFPQALEPRARAPRRPACV GPGANTAMPERDTVAVSSLV CVEGPLCAQLQGSGLDLQCC MQNTKPRTKEPGTVPALGAH GLLAAAGQLHPRGPAGDCGG PYLLLPGGRLPQPAWRQEAP ADPWLPVSVESPPSLSPPSE GSPPMGTCAGLCSTRAPPHR in isoform 4. 1 PublicationVSP_011087Add
    BLAST
    Alternative sequencei206 – 23530KLLLD…PPPQQ → GLQSSKAPAGSSLTIWTQQS QGGPGTAGELAAPS in isoform 2. 1 PublicationVSP_011088Add
    BLAST
    Alternative sequencei206 – 23530KLLLD…PPPQQ → LATAQQCPHRTGPSAGDFRA ARPQLAVA in isoform 3. CuratedVSP_011089Add
    BLAST
    Alternative sequencei206 – 23530Missing in isoform 5. 1 PublicationVSP_046330Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB049213 Genomic DNA. Translation: BAB68409.1.
    AL389876 mRNA. No translation available.
    AK125830 mRNA. Translation: BAC86311.1.
    CR456372 mRNA. Translation: CAG30258.1.
    AP000350 Genomic DNA. No translation available.
    BC057830 mRNA. Translation: AAH57830.1.
    CCDSiCCDS33615.1. [Q96Q80-1]
    CCDS42986.1. [Q96Q80-5]
    CCDS46672.1. [Q96Q80-2]
    RefSeqiNP_001002862.1. NM_001002862.2. [Q96Q80-1]
    NP_001129223.1. NM_001135751.1. [Q96Q80-2]
    NP_940842.2. NM_198440.3. [Q96Q80-5]
    UniGeneiHs.593679.

    Genome annotation databases

    EnsembliENST00000318109; ENSP00000315303; ENSG00000099958. [Q96Q80-1]
    ENST00000406855; ENSP00000384744; ENSG00000099958. [Q96Q80-2]
    ENST00000476077; ENSP00000419399; ENSG00000099958. [Q96Q80-5]
    GeneIDi91319.
    KEGGihsa:91319.
    UCSCiuc002zyh.3. human. [Q96Q80-1]
    uc002zyj.3. human. [Q96Q80-4]
    uc002zyk.4. human. [Q96Q80-2]

    Polymorphism databases

    DMDMi50400613.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB049213 Genomic DNA. Translation: BAB68409.1 .
    AL389876 mRNA. No translation available.
    AK125830 mRNA. Translation: BAC86311.1 .
    CR456372 mRNA. Translation: CAG30258.1 .
    AP000350 Genomic DNA. No translation available.
    BC057830 mRNA. Translation: AAH57830.1 .
    CCDSi CCDS33615.1. [Q96Q80-1 ]
    CCDS42986.1. [Q96Q80-5 ]
    CCDS46672.1. [Q96Q80-2 ]
    RefSeqi NP_001002862.1. NM_001002862.2. [Q96Q80-1 ]
    NP_001129223.1. NM_001135751.1. [Q96Q80-2 ]
    NP_940842.2. NM_198440.3. [Q96Q80-5 ]
    UniGenei Hs.593679.

    3D structure databases

    ProteinModelPortali Q96Q80.
    SMRi Q96Q80. Positions 11-185.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 124816. 3 interactions.
    STRINGi 9606.ENSP00000384744.

    Polymorphism databases

    DMDMi 50400613.

    Proteomic databases

    PaxDbi Q96Q80.
    PRIDEi Q96Q80.

    Protocols and materials databases

    DNASUi 91319.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000318109 ; ENSP00000315303 ; ENSG00000099958 . [Q96Q80-1 ]
    ENST00000406855 ; ENSP00000384744 ; ENSG00000099958 . [Q96Q80-2 ]
    ENST00000476077 ; ENSP00000419399 ; ENSG00000099958 . [Q96Q80-5 ]
    GeneIDi 91319.
    KEGGi hsa:91319.
    UCSCi uc002zyh.3. human. [Q96Q80-1 ]
    uc002zyj.3. human. [Q96Q80-4 ]
    uc002zyk.4. human. [Q96Q80-2 ]

    Organism-specific databases

    CTDi 91319.
    GeneCardsi GC22M024176.
    HGNCi HGNC:14236. DERL3.
    HPAi CAB037234.
    HPA049306.
    MIMi 610305. gene.
    neXtProti NX_Q96Q80.
    PharmGKBi PA25883.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG5291.
    HOGENOMi HOG000200948.
    HOVERGENi HBG051338.
    KOi K13989.
    OrthoDBi EOG73RBC2.
    PhylomeDBi Q96Q80.
    TreeFami TF314715.

    Miscellaneous databases

    GeneWikii Derlin-3.
    GenomeRNAii 91319.
    NextBioi 77178.
    PROi Q96Q80.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q96Q80.
    Bgeei Q96Q80.
    CleanExi HS_DERL3.
    Genevestigatori Q96Q80.

    Family and domain databases

    InterProi IPR007599. DER1.
    [Graphical view ]
    PANTHERi PTHR11009. PTHR11009. 1 hit.
    Pfami PF04511. DER1. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Molecular cloning of a novel member of the NADH oxidoreductase complex I subunit homolog."
      Shimizu N., Minosima S., Kawasaki K., Sasaki T.
      Submitted (SEP-2000) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE (ISOFORM 3).
    2. The European IMAGE consortium
      Submitted (JUL-2000) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 5), VARIANT LEU-149.
    3. "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 4), VARIANT VAL-211.
      Tissue: Testis.
    4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
    5. "The DNA sequence of human chromosome 22."
      Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M., Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C., Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E., Bridgeman A.M.
      , Buck D., Burgess J., Burrill W.D., Burton J., Carder C., Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G., Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V., Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M., Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A., Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C., Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E., Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F., Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M., Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A., Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D., Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y., Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S., Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E., Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L., Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L., Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N., Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A., Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L., Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P., Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P., Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q., Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J., Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J., Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D., Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T., Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P., Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K., Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R., Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L., McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J., Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E., Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P., Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y., Wright H.
      Nature 402:489-495(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. "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: Placenta.
    7. "Derlin-2 and Derlin-3 are regulated by the mammalian unfolded protein response and are required for ER-associated degradation."
      Oda Y., Okada T., Yoshida H., Kaufman R.J., Nagata K., Mori K.
      J. Cell Biol. 172:383-393(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, TISSUE SPECIFICITY, SUBCELLULAR LOCATION, MEMBRANE TOPOLOGY, OLIGOMERIZATION, INTERACTION WITH VCP AND EDEM1.
    8. "Selenoprotein K binds multiprotein complexes and is involved in the regulation of endoplasmic reticulum homeostasis."
      Shchedrina V.A., Everley R.A., Zhang Y., Gygi S.P., Hatfield D.L., Gladyshev V.N.
      J. Biol. Chem. 286:42937-42948(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH SELK AND VIMP.
    9. "STT3B-dependent posttranslational N-glycosylation as a surveillance system for secretory protein."
      Sato T., Sako Y., Sho M., Momohara M., Suico M.A., Shuto T., Nishitoh H., Okiyoneda T., Kokame K., Kaneko M., Taura M., Miyata M., Chosa K., Koga T., Morino-Koga S., Wada I., Kai H.
      Mol. Cell 47:99-110(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN ERAD PATHWAY.

    Entry informationi

    Entry nameiDERL3_HUMAN
    AccessioniPrimary (citable) accession number: Q96Q80
    Secondary accession number(s): F2Z3B6
    , Q6ICJ6, Q6PEX0, Q6ZUB5
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 19, 2004
    Last sequence update: July 19, 2004
    Last modified: October 1, 2014
    This is version 99 of the entry and version 2 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 22
      Human chromosome 22: 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. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3