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Q9NS23

- RASF1_HUMAN

UniProt

Q9NS23 - RASF1_HUMAN

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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

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 N-terminus binding Source: UniProtKB
  3. 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
Complete GO annotation...

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. nucleus Source: UniProtKB
  5. plasma membrane Source: HPA
Complete GO annotation...

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

BgeeiQ9NS23.
ExpressionAtlasiQ9NS23. baseline and differential.
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. 43 interactions.
DIPiDIP-31270N.
IntActiQ9NS23. 37 interactions.
MINTiMINT-146049.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.
GeneTreeiENSGT00390000003367.
HOVERGENiHBG054362.
InParanoidiQ9NS23.
KOiK09850.
OMAiTTSSGYC.
OrthoDBiEOG7TF796.
PhylomeDBiQ9NS23.
TreeFamiTF319243.

Family and domain databases

InterProiIPR002219. 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

        10         20         30         40         50
MSGEPELIEL RELAPAGRAG KGRTRLERAN ALRIARGTAC NPTRQLVPGR
60 70 80 90 100
GHRFQPAGPA THTWCDLCGD FIWGVVRKGL QCARLSADCK FTCHYRCRAL
110 120 130 140 150
VCLDCCGPRD LGWEPAVERD TNVDEPVEWE TPDLSQAEIE QKIKEYNAQI
160 170 180 190 200
NSNLFMSLNK DGSYTGFIKV QLKLVRPVSV PSSKKPPSLQ DARRGPGRGT
210 220 230 240 250
SVRRRTSFYL PKDAVKHLHV LSRTRAREVI EALLRKFLVV DDPRKFALFE
260 270 280 290 300
RAERHGQVYL RKLLDDEQPL RLRLLAGPSD KALSFVLKEN DSGEVNWDAF
310 320 330 340
SMPELHNFLR ILQREEEEHL RQILQKYSYC RQKIQEALHA CPLG

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. Curated

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:
EMBLi
GenBanki
DDBJi
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]
ENST00000616212; ENSP00000482696; ENSG00000068028. [Q9NS23-3]
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:
EMBLi
GenBanki
DDBJi
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:
PDBei
RCSB PDBi
PDBji
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. 43 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 ]
ENST00000616212 ; ENSP00000482696 ; ENSG00000068028 . [Q9NS23-3 ]
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.
GeneTreei ENSGT00390000003367.
HOVERGENi HBG054362.
InParanoidi Q9NS23.
KOi K09850.
OMAi TTSSGYC.
OrthoDBi EOG7TF796.
PhylomeDBi Q9NS23.
TreeFami TF319243.

Enzyme and pathway databases

SignaLinki Q9NS23.

Miscellaneous databases

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

Gene expression databases

Bgeei Q9NS23.
ExpressionAtlasi Q9NS23. baseline and differential.
Genevestigatori Q9NS23.

Family and domain databases

InterProi IPR002219. 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

« Hide 'large scale' publications
  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: November 26, 2014
This is version 126 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