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Q9NS23

- RASF1_HUMAN

UniProt

Q9NS23 - RASF1_HUMAN

Protein

Ras association domain-containing protein 1

Gene

RASSF1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 124 (01 Oct 2014)
      Sequence version 1 (01 Oct 2000)
      Previous versions | rss
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    Functioni

    Potential tumor suppressor. Required for death receptor-dependent apoptosis. Mediates activation of STK3/MST2 and STK4/MST1 during Fas-induced apoptosis by preventing their dephosphorylation. When associated with MOAP1, promotes BAX conformational change and translocation to mitochondrial membranes in response to TNF and TNFSF10 stimulation. Isoform A interacts with CDC20, an activator of the anaphase-promoting complex, APC, resulting in the inhibition of APC activity and mitotic progression. Inhibits proliferation by negatively regulating cell cycle progression at the level of G1/S-phase transition by regulating accumulation of cyclin D1 protein. Isoform C has been shown not to perform these roles, no function has been identified for this isoform. Isoform A disrupts interactions among MDM2, DAXX and USP7, thus contributing to the efficient activation of TP53 by promoting MDM2 self-ubiquitination in cell-cycle checkpoint control in response to DNA damage.9 Publications

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri51 – 10555Phorbol-ester/DAG-typePROSITE-ProRule annotationAdd
    BLAST

    GO - Molecular functioni

    1. identical protein binding Source: IntAct
    2. protein binding Source: IntAct
    3. protein N-terminus binding Source: UniProtKB
    4. zinc ion binding Source: UniProtKB

    GO - Biological processi

    1. cell cycle arrest Source: UniProtKB
    2. cellular response to DNA damage stimulus Source: UniProtKB
    3. negative regulation of cell cycle arrest Source: UniProtKB
    4. positive regulation of protein ubiquitination Source: UniProtKB
    5. protein stabilization Source: UniProtKB
    6. Ras protein signal transduction Source: UniProtKB

    Keywords - Biological processi

    Cell cycle

    Keywords - Ligandi

    Metal-binding, Zinc

    Enzyme and pathway databases

    SignaLinkiQ9NS23.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Ras association domain-containing protein 1
    Gene namesi
    Name:RASSF1Imported
    Synonyms:RDA32Imported
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 3

    Organism-specific databases

    HGNCiHGNC:9882. RASSF1.

    Subcellular locationi

    Isoform A : Cytoplasmcytoskeleton. Cytoplasmcytoskeletonmicrotubule organizing centercentrosome. Cytoplasmcytoskeletonspindle. Cytoplasmcytoskeletonspindle pole. Nucleus
    Note: Localizes to cytoplasmic microtubules during interphase, to bipolar centrosomes associated with microtubules during prophase, to spindle fibers and spindle poles at metaphase and anaphase, to the midzone during early telophase, and to the midbody in late telophase in cells. Colocalizes with MDM2 in the nucleus.
    Isoform C : Nucleus
    Note: Predominantly nuclear.

    GO - Cellular componenti

    1. cytoplasm Source: HPA
    2. microtubule Source: UniProtKB-KW
    3. microtubule cytoskeleton Source: UniProtKB
    4. microtubule organizing center Source: UniProtKB-SubCell
    5. nucleus Source: UniProtKB
    6. plasma membrane Source: HPA
    7. spindle pole Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasm, Cytoskeleton, Microtubule, Nucleus

    Pathology & Biotechi

    Keywords - Diseasei

    Tumor suppressor

    Organism-specific databases

    PharmGKBiPA34245.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 344343Ras association domain-containing protein 1PRO_0000068891Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylserine1 Publication
    Modified residuei2 – 21Phosphoserine1 Publication

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiQ9NS23.
    PaxDbiQ9NS23.
    PRIDEiQ9NS23.

    PTM databases

    PhosphoSiteiQ9NS23.

    Expressioni

    Tissue specificityi

    Isoform A and isoform C are ubiquitously expressed in all tissues tested, however isoform A is absent in many corresponding cancer cell lines. Isoform B is mainly expressed in hematopoietic cells.2 Publications

    Gene expression databases

    ArrayExpressiQ9NS23.
    BgeeiQ9NS23.
    GenevestigatoriQ9NS23.

    Organism-specific databases

    HPAiHPA040735.
    HPA042098.

    Interactioni

    Subunit structurei

    Interacts with MAP1S and XPA. Binds to the N-terminal of CDC20 during prometaphase. Binds to STK3/MST2 and STK4/MST1. Isoform A interacts with MOAP1 and E4F1. Recruited to the TNFRSF1A and TNFRSF10A complexes in response to their respective cognate ligand, after internalization. Can self-associate. Isoform A interacts with RSSF5 and probably associates with HRAS via a RSSF1 isoform A-RSSF5 heterodimer. Part of a complex with MDM2, DAXX, RASSF1 and USP7. Isoform A interacts (via C-terminus) with DAXX (via N-terminus); the interaction is independent of MDM2 and TP53. Isoform C or isoform H interacts (via N-terminus) with DAXX. Isoform A interacts (via N-terminus) with MDM2 (via C-terminus); the interaction is independent of TP53.11 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    CDC20Q128342EBI-438698,EBI-367462
    DAXXQ9UER76EBI-367363,EBI-77321
    E4F1Q66K897EBI-438698,EBI-1227043
    EWSR1Q018443EBI-438698,EBI-739737
    GABARAPO951662EBI-367363,EBI-712001
    GABARAPL2P605202EBI-367363,EBI-720116
    HRASP011122EBI-438698,EBI-350145
    KDM1AO603412EBI-367363,EBI-710124
    MAP1LC3BQ9GZQ82EBI-367363,EBI-373144
    MAP1LC3CQ9BXW42EBI-367363,EBI-2603996
    MDM2Q009875EBI-367363,EBI-389668
    STK3Q131883EBI-438698,EBI-992580
    STK4Q130434EBI-438698,EBI-367376
    SUV39H1O434632EBI-367363,EBI-349968

    Protein-protein interaction databases

    BioGridi116356. 37 interactions.
    DIPiDIP-31270N.
    IntActiQ9NS23. 37 interactions.
    MINTiMINT-146049.

    Structurei

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2KZUNMR-B-[»]
    ProteinModelPortaliQ9NS23.
    SMRiQ9NS23. Positions 49-105, 138-290, 294-338.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ9NS23.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini198 – 29295Ras-associatingPROSITE-ProRule annotationAdd
    BLAST
    Domaini294 – 34148SARAHPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni2 – 119118Mediates interaction with E4F1Add
    BLAST
    Regioni315 – 3184MOAP1-binding

    Sequence similaritiesi

    Contains 1 phorbol-ester/DAG-type zinc finger.PROSITE-ProRule annotation
    Contains 1 Ras-associating domain.PROSITE-ProRule annotation
    Contains 1 SARAH domain.PROSITE-ProRule annotation

    Zinc finger

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri51 – 10555Phorbol-ester/DAG-typePROSITE-ProRule annotationAdd
    BLAST

    Keywords - Domaini

    Zinc-finger

    Phylogenomic databases

    eggNOGiNOG308852.
    HOVERGENiHBG054362.
    InParanoidiQ9NS23.
    KOiK09850.
    OMAiTTSSGYC.
    OrthoDBiEOG7TF796.
    PhylomeDBiQ9NS23.
    TreeFamiTF319243.

    Family and domain databases

    InterProiIPR002219. Prot_Kinase_C-like_PE/DAG-bd.
    IPR000159. Ras-assoc.
    IPR011524. SARAH_dom.
    IPR029071. Ubiquitin-rel_dom.
    [Graphical view]
    PfamiPF00130. C1_1. 1 hit.
    PF00788. RA. 1 hit.
    [Graphical view]
    SMARTiSM00109. C1. 1 hit.
    SM00314. RA. 1 hit.
    [Graphical view]
    SUPFAMiSSF54236. SSF54236. 1 hit.
    PROSITEiPS50200. RA. 1 hit.
    PS50951. SARAH. 1 hit.
    PS50081. ZF_DAG_PE_2. 1 hit.
    [Graphical view]

    Sequences (8)i

    Sequence statusi: Complete.

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

    This entry describes 8 isoformsi produced by alternative promoter usage and alternative splicing. Align

    Isoform D1 Publication (identifier: Q9NS23-1) [UniParc]FASTAAdd to Basket

    Also known as: RASSF1D, Cardiac-specific1 Publication

    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

    MSGEPELIEL RELAPAGRAG KGRTRLERAN ALRIARGTAC NPTRQLVPGR    50
    GHRFQPAGPA THTWCDLCGD FIWGVVRKGL QCARLSADCK FTCHYRCRAL 100
    VCLDCCGPRD LGWEPAVERD TNVDEPVEWE TPDLSQAEIE QKIKEYNAQI 150
    NSNLFMSLNK DGSYTGFIKV QLKLVRPVSV PSSKKPPSLQ DARRGPGRGT 200
    SVRRRTSFYL PKDAVKHLHV LSRTRAREVI EALLRKFLVV DDPRKFALFE 250
    RAERHGQVYL RKLLDDEQPL RLRLLAGPSD KALSFVLKEN DSGEVNWDAF 300
    SMPELHNFLR ILQREEEEHL RQILQKYSYC RQKIQEALHA CPLG 344

    Note: Produced by alternative promoter usage.

    Length:344
    Mass (Da):39,219
    Last modified:October 1, 2000 - v1
    Checksum:i4071B8D044C1DB2D
    GO
    Isoform A2 Publications (identifier: Q9NS23-2) [UniParc]FASTAAdd to Basket

    Also known as: RASSF1A

    The sequence of this isoform differs from the canonical sequence as follows:
         84-88: RLSAD → H

    Note: Produced by alternative splicing of isoform D.

    Show »
    Length:340
    Mass (Da):38,814
    Checksum:i73FB7C7D87507D9F
    GO
    Isoform B1 Publication (identifier: Q9NS23-3) [UniParc]FASTAAdd to Basket

    Also known as: RASSF1B

    The sequence of this isoform differs from the canonical sequence as follows:
         1-155: Missing.

    Note: Produced by alternative splicing of isoform D.

    Show »
    Length:189
    Mass (Da):21,899
    Checksum:i2D7C1F632EA7A23B
    GO
    Isoform C2 Publications (identifier: Q9NS23-4) [UniParc]FASTAAdd to Basket

    Also known as: RASSF1C

    The sequence of this isoform differs from the canonical sequence as follows:
         1-74: Missing.
         75-123: VVRKGLQCAR...EPAVERDTNV → MGEAEAPSFE...SLARRPRRDQ

    Note: Produced by alternative promoter usage.

    Show »
    Length:270
    Mass (Da):31,226
    Checksum:i2E7006EA16A38D25
    GO
    Isoform E1 Publication (identifier: Q9NS23-5) [UniParc]FASTAAdd to Basket

    Also known as: RASSF1E, Pancreas-specific1 Publication

    The sequence of this isoform differs from the canonical sequence as follows:
         84-88: RLSAD → H
         123-123: V → VPILQ

    Note: Produced by alternative splicing of isoform D.

    Show »
    Length:344
    Mass (Da):39,265
    Checksum:iDB422771EB2AB7B2
    GO
    Isoform F1 Publication (identifier: Q9NS23-6) [UniParc]FASTAAdd to Basket

    Also known as: RASSF1F

    The sequence of this isoform differs from the canonical sequence as follows:
         85-91: LSADCKF → RACGVGD
         93-344: Missing.

    Note: Produced by alternative splicing of isoform D.

    Show »
    Length:92
    Mass (Da):9,937
    Checksum:iC8FEFAAD37425A01
    GO
    Isoform G1 Publication (identifier: Q9NS23-7) [UniParc]FASTAAdd to Basket

    Also known as: RASSF1G

    The sequence of this isoform differs from the canonical sequence as follows:
         84-149: RLSADCKFTC...EQKIKEYNAQ → QQGRFLHRLH...PACAVTHKGT
         150-344: Missing.

    Note: Produced by alternative splicing of isoform D.

    Show »
    Length:152
    Mass (Da):16,120
    Checksum:i18403EEC734C2695
    GO
    Isoform H (identifier: Q9NS23-9) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-74: Missing.
         75-123: VVRKGLQCAR...EPAVERDTNV → MGEAEAPSFE...SLARRPRRDQ
         150-344: Missing.

    Note: Produced by alternative splicing of isoform C.

    Show »
    Length:75
    Mass (Da):8,656
    Checksum:i5B7A6F7C7409E740
    GO

    Sequence cautioni

    The sequence AAB67312.1 differs from that shown. Reason: Erroneous gene model prediction.

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti21 – 211K → Q.2 Publications
    Corresponds to variant rs4688725 [ dbSNP | Ensembl ].
    VAR_019542
    Natural varianti53 – 531R → C.1 Publication
    Corresponds to variant rs201618726 [ dbSNP | Ensembl ].
    VAR_019543
    Natural varianti133 – 1331D → E.1 Publication
    Corresponds to variant rs76335415 [ dbSNP | Ensembl ].
    VAR_019544
    Natural varianti135 – 1351S → F Prevents G1 cell cycle arrest; reduced protein phosphorylation. 1 Publication
    VAR_019545
    Natural varianti137 – 1371A → S Prevents G1 cell cycle arrest; reduced protein phosphorylation. 1 Publication
    Corresponds to variant rs2073498 [ dbSNP | Ensembl ].
    VAR_019546
    Natural varianti319 – 3191H → R.
    Corresponds to variant rs12488879 [ dbSNP | Ensembl ].
    VAR_059794
    Natural varianti329 – 3291Y → C.1 Publication
    VAR_019547

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 155155Missing in isoform B. 2 PublicationsVSP_050770Add
    BLAST
    Alternative sequencei1 – 7474Missing in isoform C and isoform H. 3 PublicationsVSP_050773Add
    BLAST
    Alternative sequencei75 – 12349VVRKG…RDTNV → MGEAEAPSFEMTWSSTTSSG YCSQEDSDSELEQYFTARTS LARRPRRDQ in isoform C and isoform H. 3 PublicationsVSP_050774Add
    BLAST
    Alternative sequencei84 – 14966RLSAD…EYNAQ → QQGRFLHRLHQGSAEAGAPC LCALQQEATLLAGCPAGPRT GHKCQAPHFLLPAQGCCQAP ACAVTHKGT in isoform G. 1 PublicationVSP_050775Add
    BLAST
    Alternative sequencei84 – 885RLSAD → H in isoform A and isoform E. 3 PublicationsVSP_050771
    Alternative sequencei85 – 917LSADCKF → RACGVGD in isoform F. 1 PublicationVSP_050776
    Alternative sequencei93 – 344252Missing in isoform F. 1 PublicationVSP_050777Add
    BLAST
    Alternative sequencei123 – 1231V → VPILQ in isoform E. 1 PublicationVSP_050772
    Alternative sequencei150 – 344195Missing in isoform G and isoform H. 1 PublicationVSP_050778Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF061836 mRNA. Translation: AAC16001.1.
    AF132675 mRNA. Translation: AAD44174.1.
    AF132676 mRNA. Translation: AAD44175.1.
    AF132677 mRNA. Translation: AAD44176.1.
    AF040703 mRNA. Translation: AAC70910.2.
    AF102770 mRNA. Translation: AAF35127.2.
    AF102771 mRNA. Translation: AAF35128.2.
    AF102772 mRNA. Translation: AAF35129.2.
    BT020047 mRNA. Translation: AAV38850.1.
    BT020048 mRNA. Translation: AAV38851.1.
    AF286217 mRNA. Translation: AAG10038.1.
    AF291719 mRNA. Translation: AAG10064.1.
    AC002455 Genomic DNA. No translation available.
    AC002481 Genomic DNA. Translation: AAB67312.1. Sequence problems.
    CH471055 Genomic DNA. Translation: EAW65098.1.
    CH471055 Genomic DNA. Translation: EAW65101.1.
    CH471055 Genomic DNA. Translation: EAW65102.1.
    BC110412 mRNA. Translation: AAI10413.1.
    BC143879 mRNA. Translation: AAI43880.1.
    CCDSiCCDS2820.1. [Q9NS23-1]
    CCDS2821.1. [Q9NS23-4]
    CCDS2822.1. [Q9NS23-3]
    CCDS43096.1. [Q9NS23-2]
    RefSeqiNP_001193886.1. NM_001206957.1. [Q9NS23-3]
    NP_009113.3. NM_007182.4. [Q9NS23-2]
    NP_733830.1. NM_170712.2. [Q9NS23-3]
    NP_733831.1. NM_170713.2. [Q9NS23-4]
    NP_733832.1. NM_170714.1. [Q9NS23-1]
    UniGeneiHs.476270.

    Genome annotation databases

    EnsembliENST00000327761; ENSP00000333327; ENSG00000068028. [Q9NS23-4]
    ENST00000357043; ENSP00000349547; ENSG00000068028. [Q9NS23-1]
    ENST00000359365; ENSP00000352323; ENSG00000068028. [Q9NS23-2]
    ENST00000395117; ENSP00000378549; ENSG00000068028. [Q9NS23-6]
    ENST00000395126; ENSP00000378558; ENSG00000068028. [Q9NS23-3]
    ENST00000482447; ENSP00000433000; ENSG00000068028. [Q9NS23-7]
    GeneIDi11186.
    KEGGihsa:11186.
    UCSCiuc003daa.1. human. [Q9NS23-1]
    uc003dab.1. human.
    uc003dae.1. human. [Q9NS23-2]

    Polymorphism databases

    DMDMi50401686.

    Keywords - Coding sequence diversityi

    Alternative promoter usage, Alternative splicing, Polymorphism

    Cross-referencesi

    Web resourcesi

    Atlas of Genetics and Cytogenetics in Oncology and Haematology

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF061836 mRNA. Translation: AAC16001.1 .
    AF132675 mRNA. Translation: AAD44174.1 .
    AF132676 mRNA. Translation: AAD44175.1 .
    AF132677 mRNA. Translation: AAD44176.1 .
    AF040703 mRNA. Translation: AAC70910.2 .
    AF102770 mRNA. Translation: AAF35127.2 .
    AF102771 mRNA. Translation: AAF35128.2 .
    AF102772 mRNA. Translation: AAF35129.2 .
    BT020047 mRNA. Translation: AAV38850.1 .
    BT020048 mRNA. Translation: AAV38851.1 .
    AF286217 mRNA. Translation: AAG10038.1 .
    AF291719 mRNA. Translation: AAG10064.1 .
    AC002455 Genomic DNA. No translation available.
    AC002481 Genomic DNA. Translation: AAB67312.1 . Sequence problems.
    CH471055 Genomic DNA. Translation: EAW65098.1 .
    CH471055 Genomic DNA. Translation: EAW65101.1 .
    CH471055 Genomic DNA. Translation: EAW65102.1 .
    BC110412 mRNA. Translation: AAI10413.1 .
    BC143879 mRNA. Translation: AAI43880.1 .
    CCDSi CCDS2820.1. [Q9NS23-1 ]
    CCDS2821.1. [Q9NS23-4 ]
    CCDS2822.1. [Q9NS23-3 ]
    CCDS43096.1. [Q9NS23-2 ]
    RefSeqi NP_001193886.1. NM_001206957.1. [Q9NS23-3 ]
    NP_009113.3. NM_007182.4. [Q9NS23-2 ]
    NP_733830.1. NM_170712.2. [Q9NS23-3 ]
    NP_733831.1. NM_170713.2. [Q9NS23-4 ]
    NP_733832.1. NM_170714.1. [Q9NS23-1 ]
    UniGenei Hs.476270.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2KZU NMR - B - [» ]
    ProteinModelPortali Q9NS23.
    SMRi Q9NS23. Positions 49-105, 138-290, 294-338.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 116356. 37 interactions.
    DIPi DIP-31270N.
    IntActi Q9NS23. 37 interactions.
    MINTi MINT-146049.

    PTM databases

    PhosphoSitei Q9NS23.

    Polymorphism databases

    DMDMi 50401686.

    Proteomic databases

    MaxQBi Q9NS23.
    PaxDbi Q9NS23.
    PRIDEi Q9NS23.

    Protocols and materials databases

    DNASUi 11186.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000327761 ; ENSP00000333327 ; ENSG00000068028 . [Q9NS23-4 ]
    ENST00000357043 ; ENSP00000349547 ; ENSG00000068028 . [Q9NS23-1 ]
    ENST00000359365 ; ENSP00000352323 ; ENSG00000068028 . [Q9NS23-2 ]
    ENST00000395117 ; ENSP00000378549 ; ENSG00000068028 . [Q9NS23-6 ]
    ENST00000395126 ; ENSP00000378558 ; ENSG00000068028 . [Q9NS23-3 ]
    ENST00000482447 ; ENSP00000433000 ; ENSG00000068028 . [Q9NS23-7 ]
    GeneIDi 11186.
    KEGGi hsa:11186.
    UCSCi uc003daa.1. human. [Q9NS23-1 ]
    uc003dab.1. human.
    uc003dae.1. human. [Q9NS23-2 ]

    Organism-specific databases

    CTDi 11186.
    GeneCardsi GC03M050369.
    HGNCi HGNC:9882. RASSF1.
    HPAi HPA040735.
    HPA042098.
    MIMi 605082. gene.
    neXtProti NX_Q9NS23.
    PharmGKBi PA34245.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG308852.
    HOVERGENi HBG054362.
    InParanoidi Q9NS23.
    KOi K09850.
    OMAi TTSSGYC.
    OrthoDBi EOG7TF796.
    PhylomeDBi Q9NS23.
    TreeFami TF319243.

    Enzyme and pathway databases

    SignaLinki Q9NS23.

    Miscellaneous databases

    EvolutionaryTracei Q9NS23.
    GeneWikii RASSF1.
    GenomeRNAii 11186.
    NextBioi 42571.
    PROi Q9NS23.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9NS23.
    Bgeei Q9NS23.
    Genevestigatori Q9NS23.

    Family and domain databases

    InterProi IPR002219. Prot_Kinase_C-like_PE/DAG-bd.
    IPR000159. Ras-assoc.
    IPR011524. SARAH_dom.
    IPR029071. Ubiquitin-rel_dom.
    [Graphical view ]
    Pfami PF00130. C1_1. 1 hit.
    PF00788. RA. 1 hit.
    [Graphical view ]
    SMARTi SM00109. C1. 1 hit.
    SM00314. RA. 1 hit.
    [Graphical view ]
    SUPFAMi SSF54236. SSF54236. 1 hit.
    PROSITEi PS50200. RA. 1 hit.
    PS50951. SARAH. 1 hit.
    PS50081. ZF_DAG_PE_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Epigenetic inactivation of a RAS association domain family protein from the lung tumour suppressor locus 3p21.3."
      Dammann R., Li C., Yoon J.-H., Chin P.L., Bates S., Pfeifer G.P.
      Nat. Genet. 25:315-319(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS A; B AND C), FUNCTION, TISSUE SPECIFICITY, VARIANT GLN-21, INTERACTION WITH XPA.
    2. Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS A; C; D; E; F AND G), FUNCTION, TISSUE SPECIFICITY, VARIANTS GLN-21; CYS-53; GLU-133; SER-137 AND CYS-329.
      Tissue: HeartImported, LungImported and PancreasImported.
    3. "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
      Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
      Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM C).
    4. "The DNA sequence, annotation and analysis of human chromosome 3."
      Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J.
      , Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P., Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H., Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B., Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H., Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J., Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X., Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R., Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.
      Nature 440:1194-1198(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. 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] (ISOFORMS A AND B).
      Tissue: Blood and Brain.
    7. "The RASSF1A tumor suppressor blocks cell cycle progression and inhibits cyclin D1 accumulation."
      Shivakumar L., Minna J., Sakamaki T., Pestell R., White M.A.
      Mol. Cell. Biol. 22:4309-4318(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, VARIANT PHE-135, CHARACTERIZATION OF VARIANTS PHE-135 AND SER-137.
    8. "The putative tumor suppressor RASSF1A homodimerizes and heterodimerizes with the Ras-GTP binding protein Nore1."
      Ortiz-Vega S., Khokhlatchev A., Nedwidek M., Zhang X.F., Dammann R., Pfeifer G.P., Avruch J.
      Oncogene 21:1381-1390(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: SELF-ASSOCIATION, INTERACTION WITH RSSF5 AND HRAS.
    9. "Identification of the E1A-regulated transcription factor p120 E4F as an interacting partner of the RASSF1A candidate tumor suppressor gene."
      Fenton S.L., Dallol A., Agathanggelou A., Hesson L., Ahmed-Choudhury J., Baksh S., Sardet C., Dammann R., Minna J.D., Downward J., Maher E.R., Latif F.
      Cancer Res. 64:102-107(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH E4F1.
    10. "RASSF1A interacts with microtubule-associated proteins and modulates microtubule dynamics."
      Dallol A., Agathanggelou A., Fenton S.L., Ahmed-Choudhury J., Hesson L., Vos M.D., Clark G.J., Downward J., Maher E.R., Latif F.
      Cancer Res. 64:4112-4116(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH MAP1S.
    11. "The tumour suppressor RASSF1A regulates mitosis by inhibiting the APC-Cdc20 complex."
      Song M.S., Song S.J., Ayad N.G., Chang J.S., Lee J.H., Hong H.K., Lee H., Choi N., Kim J., Kim H., Kim J.W., Choi E.-J., Kirschner M.W., Lim D.-S.
      Nat. Cell Biol. 6:129-137(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH CDC20.
    12. "Regulation of the MST1 kinase by autophosphorylation, by the growth inhibitory proteins, RASSF1 and NORE1, and by Ras."
      Praskova M., Khoklatchev A., Ortiz-Vega S., Avruch J.
      Biochem. J. 381:453-462(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH STK3/MST2 AND STK4/MST1.
    13. "Specificity of the methylation-suppressed A isoform of candidate tumor suppressor RASSF1 for microtubule hyperstabilization is determined by cell death inducer C19ORF5."
      Liu L., Vo A., McKeehan W.L.
      Cancer Res. 65:1830-1838(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH MAP1S.
    14. "The tumor suppressor RASSF1A and MAP-1 link death receptor signaling to Bax conformational change and cell death."
      Baksh S., Tommasi S., Fenton S., Yu V.C., Martins L.M., Pfeifer G.P., Latif F., Downward J., Neel B.G.
      Mol. Cell 18:637-650(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH MOAP1, FUNCTION.
    15. Cited for: FUNCTION, INTERACTION WITH STK3/MST2 AND STK4/MST1.
    16. "The tumour suppressor RASSF1A promotes MDM2 self-ubiquitination by disrupting the MDM2-DAXX-HAUSP complex."
      Song M.S., Song S.J., Kim S.Y., Oh H.J., Lim D.S.
      EMBO J. 27:1863-1874(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, IDENTIFICATION IN A COMPLEX WITH MDM2; DAXX AND USP7, INTERACTION WITH DAXX AND MDM2, SUBCELLULAR LOCATION.
    17. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
    18. "The tumor suppressor RASSF1A prevents dephosphorylation of the mammalian STE20-like kinases MST1 and MST2."
      Guo C., Zhang X., Pfeifer G.P.
      J. Biol. Chem. 286:6253-6261(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH STK3/MST2 AND STK4/MST1.
    19. "Structural characterization of the DAXX N-terminal helical bundle domain and its complex with Rassf1C."
      Escobar-Cabrera E., Lau D.K., Giovinazzi S., Ishov A.M., McIntosh L.P.
      Structure 18:1642-1653(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR (ISOFORM C/H) IN COMPLEX WITH DAXX.

    Entry informationi

    Entry nameiRASF1_HUMAN
    AccessioniPrimary (citable) accession number: Q9NS23
    Secondary accession number(s): B7ZLL1
    , O14571, O60539, O60710, Q0VGC6, Q5TZT2, Q9HB04, Q9HB18, Q9NS22, Q9UND4, Q9UND5
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 19, 2004
    Last sequence update: October 1, 2000
    Last modified: October 1, 2014
    This is version 124 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 3
      Human chromosome 3: 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