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Q9H8S9

- MOB1A_HUMAN

UniProt

Q9H8S9 - MOB1A_HUMAN

Protein

MOB kinase activator 1A

Gene

MOB1A

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 118 (01 Oct 2014)
      Sequence version 4 (23 Jan 2007)
      Previous versions | rss
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    Functioni

    Activator of LATS1/2 in the Hippo signaling pathway which plays a pivotal role in organ size control and tumor suppression by restricting proliferation and promoting apoptosis. The core of this pathway is composed of a kinase cascade wherein STK3/MST2 and STK4/MST1, in complex with its regulatory protein SAV1, phosphorylates and activates LATS1/2 in complex with its regulatory protein MOB1, which in turn phosphorylates and inactivates YAP1 oncoprotein and WWTR1/TAZ. Phosphorylation of YAP1 by LATS1/2 inhibits its translocation into the nucleus to regulate cellular genes important for cell proliferation, cell death, and cell migration. Stimulates the kinase activity of STK38 and STK38L. Acts cooperatively with STK3/MST2 to activate STK38.3 Publications

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi79 – 791Zinc
    Metal bindingi84 – 841Zinc
    Metal bindingi161 – 1611Zinc
    Metal bindingi166 – 1661Zinc

    GO - Molecular functioni

    1. metal ion binding Source: UniProtKB-KW
    2. protein binding Source: UniProtKB

    GO - Biological processi

    1. hippo signaling Source: UniProtKB

    Keywords - Ligandi

    Metal-binding, Zinc

    Enzyme and pathway databases

    ReactomeiREACT_118607. Signaling by Hippo.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    MOB kinase activator 1A
    Alternative name(s):
    Mob1 alpha
    Short name:
    Mob1A
    Mob1 homolog 1B
    Mps one binder kinase activator-like 1B
    Gene namesi
    Name:MOB1A
    Synonyms:C2orf6, MOB4B, MOBK1B, MOBKL1B
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 2

    Organism-specific databases

    HGNCiHGNC:16015. MOB1A.

    Subcellular locationi

    GO - Cellular componenti

    1. cytosol Source: Reactome
    2. extracellular vesicular exosome Source: UniProt

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA25894.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed2 Publications
    Chaini2 – 216215MOB kinase activator 1APRO_0000193566Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylserine2 Publications
    Modified residuei12 – 121Phosphothreonine2 Publications
    Modified residuei35 – 351Phosphothreonine2 Publications
    Modified residuei74 – 741Phosphothreonine; by STK3/MST22 Publications
    Modified residuei181 – 1811Phosphothreonine2 Publications

    Post-translational modificationi

    Phosphorylated by STK3/MST2 and STK4/MST1 and this phosphorylation enhances its binding to LATS1.3 Publications

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiQ9H8S9.
    PaxDbiQ9H8S9.
    PRIDEiQ9H8S9.

    2D gel databases

    OGPiQ9H8S9.

    PTM databases

    PhosphoSiteiQ9H8S9.

    Expressioni

    Tissue specificityi

    Adrenal gland, bone marrow, brain, placenta, prostate, salivary gland, skeletal muscle, testis, thymus, thyroid gland, heart, spinal cord, fetal brain and fetal liver.1 Publication

    Gene expression databases

    ArrayExpressiQ9H8S9.
    BgeeiQ9H8S9.
    CleanExiHS_MOBKL1B.
    GenevestigatoriQ9H8S9.

    Interactioni

    Subunit structurei

    Binds STK38 and STK38L. Interacts with LATS1 and LATS2. Forms a tripartite complex with STK38 and STK3/MST2.3 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    Q9WMX22EBI-748229,EBI-6863748From a different organism.
    LATS1O958359EBI-748229,EBI-444209
    LATS2Q9NRM74EBI-748229,EBI-3506895
    STK38Q152082EBI-748229,EBI-458376
    STK38LQ9Y2H13EBI-748229,EBI-991501

    Protein-protein interaction databases

    BioGridi120527. 46 interactions.
    DIPiDIP-36594N.
    IntActiQ9H8S9. 39 interactions.
    MINTiMINT-197366.
    STRINGi9606.ENSP00000379364.

    Structurei

    Secondary structure

    1
    216
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi41 – 444
    Helixi53 – 7422
    Helixi75 – 784
    Turni81 – 833
    Beta strandi85 – 906
    Beta strandi93 – 953
    Beta strandi100 – 1023
    Helixi111 – 12616
    Turni129 – 1313
    Beta strandi135 – 1373
    Helixi144 – 17229
    Helixi176 – 19318
    Helixi198 – 2047
    Helixi205 – 2106

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1PI1X-ray2.00A33-216[»]
    4JIZX-ray2.10A40-211[»]
    ProteinModelPortaliQ9H8S9.
    SMRiQ9H8S9. Positions 33-216.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ9H8S9.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the MOB1/phocein family.Curated

    Phylogenomic databases

    eggNOGiNOG287143.
    HOGENOMiHOG000164685.
    HOVERGENiHBG052489.
    InParanoidiQ9H8S9.
    KOiK06685.
    OMAiFEYRWAD.
    OrthoDBiEOG7N0C5K.
    PhylomeDBiQ9H8S9.
    TreeFamiTF300789.

    Family and domain databases

    Gene3Di1.20.140.30. 1 hit.
    InterProiIPR005301. Mob1_phocein.
    [Graphical view]
    PANTHERiPTHR22599. PTHR22599. 1 hit.
    PfamiPF03637. Mob1_phocein. 1 hit.
    [Graphical view]
    SUPFAMiSSF101152. SSF101152. 1 hit.

    Sequences (2)i

    Sequence statusi: Complete.

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

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q9H8S9-1) [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

    MSFLFSSRSS KTFKPKKNIP EGSHQYELLK HAEATLGSGN LRQAVMLPEG    50
    EDLNEWIAVN TVDFFNQINM LYGTITEFCT EASCPVMSAG PRYEYHWADG 100
    TNIKKPIKCS APKYIDYLMT WVQDQLDDET LFPSKIGVPF PKNFMSVAKT 150
    ILKRLFRVYA HIYHQHFDSV MQLQEEAHLN TSFKHFIFFV QEFNLIDRRE 200
    LAPLQELIEK LGSKDR 216
    Length:216
    Mass (Da):25,080
    Last modified:January 23, 2007 - v4
    Checksum:i58043AECAD1F5987
    GO
    Isoform 2 (identifier: Q9H8S9-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         138-148: VPFPKNFMSVA → ELTLSKYSFFF
         149-216: Missing.

    Note: May be due to an intron retention.

    Show »
    Length:148
    Mass (Da):16,928
    Checksum:i70F00C42359120F2
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti5 – 51F → L in BAB14525. (PubMed:14702039)Curated
    Sequence conflicti176 – 1761E → G in BAA91810. (PubMed:14702039)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei138 – 14811VPFPKNFMSVA → ELTLSKYSFFF in isoform 2. 1 PublicationVSP_012295Add
    BLAST
    Alternative sequencei149 – 21668Missing in isoform 2. 1 PublicationVSP_012296Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB016839 mRNA. Translation: BAB19058.1.
    AJ577474 mRNA. Translation: CAE12093.1.
    AK001650 mRNA. Translation: BAA91810.1.
    AK021657 mRNA. Translation: BAB13868.1.
    AK023321 mRNA. Translation: BAB14525.1.
    AC073263 Genomic DNA. Translation: AAX93060.1.
    BC003398 mRNA. Translation: AAH03398.1.
    CCDSiCCDS46340.1. [Q9H8S9-1]
    RefSeqiNP_060691.2. NM_018221.3. [Q9H8S9-1]
    UniGeneiHs.602092.

    Genome annotation databases

    EnsembliENST00000396049; ENSP00000379364; ENSG00000114978. [Q9H8S9-1]
    GeneIDi55233.
    KEGGihsa:55233.
    UCSCiuc002skh.4. human. [Q9H8S9-1]
    uc002ski.2. human. [Q9H8S9-2]

    Polymorphism databases

    DMDMi56749356.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB016839 mRNA. Translation: BAB19058.1 .
    AJ577474 mRNA. Translation: CAE12093.1 .
    AK001650 mRNA. Translation: BAA91810.1 .
    AK021657 mRNA. Translation: BAB13868.1 .
    AK023321 mRNA. Translation: BAB14525.1 .
    AC073263 Genomic DNA. Translation: AAX93060.1 .
    BC003398 mRNA. Translation: AAH03398.1 .
    CCDSi CCDS46340.1. [Q9H8S9-1 ]
    RefSeqi NP_060691.2. NM_018221.3. [Q9H8S9-1 ]
    UniGenei Hs.602092.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1PI1 X-ray 2.00 A 33-216 [» ]
    4JIZ X-ray 2.10 A 40-211 [» ]
    ProteinModelPortali Q9H8S9.
    SMRi Q9H8S9. Positions 33-216.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 120527. 46 interactions.
    DIPi DIP-36594N.
    IntActi Q9H8S9. 39 interactions.
    MINTi MINT-197366.
    STRINGi 9606.ENSP00000379364.

    PTM databases

    PhosphoSitei Q9H8S9.

    Polymorphism databases

    DMDMi 56749356.

    2D gel databases

    OGPi Q9H8S9.

    Proteomic databases

    MaxQBi Q9H8S9.
    PaxDbi Q9H8S9.
    PRIDEi Q9H8S9.

    Protocols and materials databases

    DNASUi 55233.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000396049 ; ENSP00000379364 ; ENSG00000114978 . [Q9H8S9-1 ]
    GeneIDi 55233.
    KEGGi hsa:55233.
    UCSCi uc002skh.4. human. [Q9H8S9-1 ]
    uc002ski.2. human. [Q9H8S9-2 ]

    Organism-specific databases

    CTDi 55233.
    GeneCardsi GC02M074382.
    HGNCi HGNC:16015. MOB1A.
    MIMi 609281. gene.
    neXtProti NX_Q9H8S9.
    PharmGKBi PA25894.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG287143.
    HOGENOMi HOG000164685.
    HOVERGENi HBG052489.
    InParanoidi Q9H8S9.
    KOi K06685.
    OMAi FEYRWAD.
    OrthoDBi EOG7N0C5K.
    PhylomeDBi Q9H8S9.
    TreeFami TF300789.

    Enzyme and pathway databases

    Reactomei REACT_118607. Signaling by Hippo.

    Miscellaneous databases

    EvolutionaryTracei Q9H8S9.
    GeneWikii MOBKL1B.
    GenomeRNAii 55233.
    NextBioi 59245.
    PROi Q9H8S9.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9H8S9.
    Bgeei Q9H8S9.
    CleanExi HS_MOBKL1B.
    Genevestigatori Q9H8S9.

    Family and domain databases

    Gene3Di 1.20.140.30. 1 hit.
    InterProi IPR005301. Mob1_phocein.
    [Graphical view ]
    PANTHERi PTHR22599. PTHR22599. 1 hit.
    Pfami PF03637. Mob1_phocein. 1 hit.
    [Graphical view ]
    SUPFAMi SSF101152. SSF101152. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "Human MOB1."
      Kagaya S., Kotani S., Todokoro K.
      Submitted (AUG-1998) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    2. "Characterization of the human Mob-1 like proteins."
      Florindo C.S., Tavares A.A.
      Submitted (JUL-2003) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    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] (ISOFORMS 1 AND 2).
      Tissue: Embryo and Ovary.
    4. "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].
    5. "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.
    6. "Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides."
      Gevaert K., Goethals M., Martens L., Van Damme J., Staes A., Thomas G.R., Vandekerckhove J.
      Nat. Biotechnol. 21:566-569(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 2-8, ACETYLATION AT SER-2.
      Tissue: Platelet.
    7. "Mechanism of activation of NDR (nuclear Dbf2-related) protein kinase by the hMOB1 protein."
      Bichsel S.J., Tamaskovic R., Stegert M.R., Hemmings B.A.
      J. Biol. Chem. 279:35228-35235(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, PHOSPHORYLATION, INTERACTION WITH STK38 AND STK38L.
    8. "MOBKL1A/MOBKL1B phosphorylation by MST1 and MST2 inhibits cell proliferation."
      Praskova M., Xia F., Avruch J.
      Curr. Biol. 18:311-321(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT THR-12 AND THR-35 BY STK3/MST2 AND STK4/MST1.
    9. "Threonine 74 of MOB1 is a putative key phosphorylation site by MST2 to form the scaffold to activate nuclear Dbf2-related kinase 1."
      Hirabayashi S., Nakagawa K., Sumita K., Hidaka S., Kawai T., Ikeda M., Kawata A., Ohno K., Hata Y.
      Oncogene 27:4281-4292(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, PHOSPHORYLATION AT THR-74 AND THR-181, INTERACTION WITH STK38 AND STK3/MST2.
    10. "Molecular characterization of human homologs of yeast MOB1."
      Chow A., Hao Y., Yang X.
      Int. J. Cancer 126:2079-2089(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH LATS1 AND LATS2, TISSUE SPECIFICITY.
    11. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    12. "Crystal structure of a human Mob1 protein: toward understanding Mob-regulated cell cycle pathways."
      Stavridi E.S., Harris K.G., Huyen Y., Bothos J., Verwoerd P.-M., Stayrook S.E., Pavletich N.P., Jeffrey P.D., Luca F.C.
      Structure 11:1163-1170(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 33-216, PARTIAL PROTEIN SEQUENCE, IDENTIFICATION BY MASS SPECTROMETRY, ZINC-BINDING.

    Entry informationi

    Entry nameiMOB1A_HUMAN
    AccessioniPrimary (citable) accession number: Q9H8S9
    Secondary accession number(s): Q53S34
    , Q9H3T5, Q9HAI0, Q9NVE2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 21, 2004
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 118 of the entry and version 4 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 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. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    4. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3