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Q9C0E8

- LNP_HUMAN

UniProt

Q9C0E8 - LNP_HUMAN

Protein

Protein lunapark

Gene

LNP

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 88 (01 Oct 2014)
      Sequence version 2 (05 Sep 2006)
      Previous versions | rss
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    Functioni

    Plays a role in tubular endoplasmic reticulum network formation and maintenance. May be involved in limb and central nervous system development.By similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri276 – 30126C4-type; plays a role in ER morphologyBy similarityAdd
    BLAST

    GO - Biological processi

    1. blood coagulation Source: Ensembl
    2. embryonic digit morphogenesis Source: Ensembl
    3. embryonic forelimb morphogenesis Source: Ensembl
    4. limb development Source: UniProtKB
    5. regulation of chondrocyte differentiation Source: Ensembl

    Keywords - Molecular functioni

    Developmental protein

    Keywords - Ligandi

    Metal-binding, Zinc

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Protein lunapark
    Gene namesi
    Name:LNP
    Synonyms:KIAA1715
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 2

    Organism-specific databases

    HGNCiHGNC:21610. KIAA1715.

    Subcellular locationi

    Endoplasmic reticulum membrane 1 Publication; Multi-pass membrane protein 1 Publication
    Note: Localizes to three-way ER tubule junctions.

    GO - Cellular componenti

    1. endoplasmic reticulum membrane Source: MGI
    2. integral component of membrane Source: UniProtKB

    Keywords - Cellular componenti

    Endoplasmic reticulum, Membrane

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA134938939.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed
    Chaini2 – 428427Protein lunaparkPRO_0000248310Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Lipidationi2 – 21N-myristoyl glycine1 Publication
    Modified residuei177 – 1771Phosphoserine1 Publication
    Modified residuei182 – 1821Phosphoserine2 Publications
    Modified residuei194 – 1941Phosphoserine2 Publications
    Modified residuei321 – 3211Phosphoserine1 Publication
    Modified residuei414 – 4141PhosphoserineBy similarity

    Keywords - PTMi

    Lipoprotein, Myristate, Phosphoprotein

    Proteomic databases

    MaxQBiQ9C0E8.
    PaxDbiQ9C0E8.
    PRIDEiQ9C0E8.

    PTM databases

    PhosphoSiteiQ9C0E8.

    Miscellaneous databases

    PMAP-CutDBQ9C0E8.

    Expressioni

    Gene expression databases

    ArrayExpressiQ9C0E8.
    BgeeiQ9C0E8.
    CleanExiHS_KIAA1715.
    GenevestigatoriQ9C0E8.

    Organism-specific databases

    HPAiHPA014205.

    Interactioni

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    CHMP1AQ9HD421EBI-1047206,EBI-1057156

    Protein-protein interaction databases

    BioGridi123333. 3 interactions.
    STRINGi9606.ENSP00000272748.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9C0E8.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini2 – 4544CytoplasmicBy similarityAdd
    BLAST
    Topological domaini67 – 7711LumenalBy similarityAdd
    BLAST
    Topological domaini99 – 428330CytoplasmicBy similarityAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei46 – 6621HelicalSequence AnalysisAdd
    BLAST
    Transmembranei78 – 9821HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili16 – 4126Sequence AnalysisAdd
    BLAST
    Coiled coili102 – 12827Sequence AnalysisAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi178 – 25073Pro-richAdd
    BLAST

    Sequence similaritiesi

    Belongs to the lunapark family.Curated

    Zinc finger

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri276 – 30126C4-type; plays a role in ER morphologyBy similarityAdd
    BLAST

    Keywords - Domaini

    Coiled coil, Transmembrane, Transmembrane helix, Zinc-finger

    Phylogenomic databases

    eggNOGiNOG115207.
    HOGENOMiHOG000231891.
    HOVERGENiHBG079498.
    InParanoidiQ9C0E8.
    OrthoDBiEOG7ZSHTN.
    PhylomeDBiQ9C0E8.
    TreeFamiTF315086.

    Family and domain databases

    InterProiIPR019273. DUF2296.
    [Graphical view]
    PfamiPF10058. DUF2296. 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. Align

    Isoform 1 (identifier: Q9C0E8-1) [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

    MGGLFSRWRT KPSTVEVLES IDKEIQALEE FREKNQRLQK LWVGRLILYS    50
    SVLYLFTCLI VYLWYLPDEF TARLAMTLPF FAFPLIIWSI RTVIIFFFSK 100
    RTERNNEALD DLKSQRKKIL EEVMEKETYK TAKLILERFD PDSKKAKECE 150
    PPSAGAAVTA RPGQEIRQRT AAQRNLSPTP ASPNQGPPPQ VPVSPGPPKD 200
    SSAPGGPPER TVTPALSSNV LPRHLGSPAT SVPGMGLHPP GPPLARPILP 250
    RERGALDRIV EYLVGDGPQN RYALICQQCF SHNGMALKEE FEYIAFRCAY 300
    CFFLNPARKT RPQAPRLPEF SFEKRQVVEG SSSVGPLPSG SVLSSDNQFN 350
    EESLEHDVLD DNTEQTDDKI PATEQTNQVI EKASDSEEPE EKQETENEEA 400
    SVIETNSTVP GADSIPDPEL SGESLTAE 428
    Length:428
    Mass (Da):47,740
    Last modified:September 5, 2006 - v2
    Checksum:iF5BBA4186C2691BF
    GO
    Isoform 2 (identifier: Q9C0E8-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-9: MGGLFSRWR → MEGK

    Note: No experimental confirmation available.

    Show »
    Length:423
    Mass (Da):47,094
    Checksum:iCAF46E3EB956B8BC
    GO
    Isoform 3 (identifier: Q9C0E8-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-123: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:305
    Mass (Da):33,001
    Checksum:i2FDFED2CFE7C83EC
    GO
    Isoform 4 (identifier: Q9C0E8-4) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         235-235: M → MEMGLPHIAQAGLEHLSSSDLSTSTSQSAGIT

    Note: No experimental confirmation available.

    Show »
    Length:459
    Mass (Da):50,848
    Checksum:i367198608E69DDF1
    GO

    Sequence cautioni

    The sequence BAB21806.1 differs from that shown. Reason: Erroneous initiation.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti262 – 2621Y → H in BAB71207. (PubMed:14702039)Curated
    Sequence conflicti374 – 3741E → G in AAH31530. (PubMed:15489334)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 123123Missing in isoform 3. 1 PublicationVSP_020238Add
    BLAST
    Alternative sequencei1 – 99MGGLFSRWR → MEGK in isoform 2. 1 PublicationVSP_020239
    Alternative sequencei235 – 2351M → MEMGLPHIAQAGLEHLSSSD LSTSTSQSAGIT in isoform 4. 1 PublicationVSP_054427

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB051502 mRNA. Translation: BAB21806.1. Different initiation.
    AK056532 mRNA. Translation: BAB71207.1.
    AC016751 Genomic DNA. No translation available.
    AC016915 Genomic DNA. No translation available.
    BC031530 mRNA. Translation: AAH31530.1.
    BC105132 mRNA. Translation: AAI05133.1.
    BC105134 mRNA. Translation: AAI05135.1.
    BC110329 mRNA. Translation: AAI10330.1.
    BC143681 mRNA. Translation: AAI43682.1.
    AL832947 mRNA. Translation: CAH56306.1.
    CCDSiCCDS33332.1. [Q9C0E8-1]
    RefSeqiNP_085153.1. NM_030650.1. [Q9C0E8-1]
    XP_006712846.1. XM_006712783.1. [Q9C0E8-1]
    UniGeneiHs.209561.

    Genome annotation databases

    EnsembliENST00000272748; ENSP00000272748; ENSG00000144320. [Q9C0E8-1]
    ENST00000409660; ENSP00000386237; ENSG00000144320. [Q9C0E8-3]
    ENST00000544803; ENSP00000440905; ENSG00000144320. [Q9C0E8-4]
    GeneIDi80856.
    KEGGihsa:80856.
    UCSCiuc002ukc.1. human. [Q9C0E8-1]
    uc010fqw.1. human. [Q9C0E8-2]

    Polymorphism databases

    DMDMi114149979.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB051502 mRNA. Translation: BAB21806.1 . Different initiation.
    AK056532 mRNA. Translation: BAB71207.1 .
    AC016751 Genomic DNA. No translation available.
    AC016915 Genomic DNA. No translation available.
    BC031530 mRNA. Translation: AAH31530.1 .
    BC105132 mRNA. Translation: AAI05133.1 .
    BC105134 mRNA. Translation: AAI05135.1 .
    BC110329 mRNA. Translation: AAI10330.1 .
    BC143681 mRNA. Translation: AAI43682.1 .
    AL832947 mRNA. Translation: CAH56306.1 .
    CCDSi CCDS33332.1. [Q9C0E8-1 ]
    RefSeqi NP_085153.1. NM_030650.1. [Q9C0E8-1 ]
    XP_006712846.1. XM_006712783.1. [Q9C0E8-1 ]
    UniGenei Hs.209561.

    3D structure databases

    ProteinModelPortali Q9C0E8.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 123333. 3 interactions.
    STRINGi 9606.ENSP00000272748.

    PTM databases

    PhosphoSitei Q9C0E8.

    Polymorphism databases

    DMDMi 114149979.

    Proteomic databases

    MaxQBi Q9C0E8.
    PaxDbi Q9C0E8.
    PRIDEi Q9C0E8.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000272748 ; ENSP00000272748 ; ENSG00000144320 . [Q9C0E8-1 ]
    ENST00000409660 ; ENSP00000386237 ; ENSG00000144320 . [Q9C0E8-3 ]
    ENST00000544803 ; ENSP00000440905 ; ENSG00000144320 . [Q9C0E8-4 ]
    GeneIDi 80856.
    KEGGi hsa:80856.
    UCSCi uc002ukc.1. human. [Q9C0E8-1 ]
    uc010fqw.1. human. [Q9C0E8-2 ]

    Organism-specific databases

    CTDi 80856.
    GeneCardsi GC02M176788.
    HGNCi HGNC:21610. KIAA1715.
    HPAi HPA014205.
    MIMi 610236. gene.
    neXtProti NX_Q9C0E8.
    PharmGKBi PA134938939.
    HUGEi Search...
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG115207.
    HOGENOMi HOG000231891.
    HOVERGENi HBG079498.
    InParanoidi Q9C0E8.
    OrthoDBi EOG7ZSHTN.
    PhylomeDBi Q9C0E8.
    TreeFami TF315086.

    Miscellaneous databases

    GenomeRNAii 80856.
    NextBioi 35481258.
    PMAP-CutDB Q9C0E8.
    PROi Q9C0E8.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9C0E8.
    Bgeei Q9C0E8.
    CleanExi HS_KIAA1715.
    Genevestigatori Q9C0E8.

    Family and domain databases

    InterProi IPR019273. DUF2296.
    [Graphical view ]
    Pfami PF10058. DUF2296. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Prediction of the coding sequences of unidentified human genes. XIX. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro."
      Nagase T., Kikuno R., Hattori A., Kondo Y., Okumura K., Ohara O.
      DNA Res. 7:347-355(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
      Tissue: Brain.
    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. "Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
      Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H.
      , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
      Nature 434:724-731(2005) [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] (ISOFORMS 1; 3 AND 4).
      Tissue: Adrenal cortex and Brain.
    5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 31-428.
      Tissue: Stomach.
    6. "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-182; SER-194 AND SER-321, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    7. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    8. "Strategy for comprehensive identification of human N-myristoylated proteins using an insect cell-free protein synthesis system."
      Suzuki T., Moriya K., Nagatoshi K., Ota Y., Ezure T., Ando E., Tsunasawa S., Utsumi T.
      Proteomics 10:1780-1793(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: MYRISTOYLATION AT GLY-2.
    9. "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-177; SER-182 AND SER-194, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    10. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    11. "ER network formation requires a balance of the dynamin-like GTPase Sey1p and the Lunapark family member Lnp1p."
      Chen S., Novick P., Ferro-Novick S.
      Nat. Cell Biol. 14:707-716(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION.

    Entry informationi

    Entry nameiLNP_HUMAN
    AccessioniPrimary (citable) accession number: Q9C0E8
    Secondary accession number(s): B7ZLA8
    , Q2M2V8, Q2YD99, Q658W8, Q8N5V9, Q96MS5
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: September 5, 2006
    Last sequence update: September 5, 2006
    Last modified: October 1, 2014
    This is version 88 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 2
      Human chromosome 2: 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. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3