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Q9NS23 (RASF1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 119. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Ras association domain-containing protein 1
Gene names
Name:RASSF1
Synonyms:RDA32
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length344 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.1 Ref.2 Ref.7 Ref.12 Ref.13 Ref.15 Ref.16 Ref.17 Ref.19

Subunit structure

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-RSSF5heterodimer. 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. Ref.1 Ref.8 Ref.10 Ref.11 Ref.12 Ref.13 Ref.14 Ref.15 Ref.16 Ref.17 Ref.19

Subcellular location

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. Ref.12 Ref.17

Isoform C: Nucleus. Note: Predominantly nuclear. Ref.12 Ref.17

Tissue specificity

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. Ref.1 Ref.2

Sequence similarities

Contains 1 phorbol-ester/DAG-type zinc finger.

Contains 1 Ras-associating domain.

Contains 1 SARAH domain.

Sequence caution

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

Ontologies

Keywords
   Biological processCell cycle
   Cellular componentCytoplasm
Cytoskeleton
Microtubule
Nucleus
   Coding sequence diversityAlternative promoter usage
Alternative splicing
Polymorphism
   DiseaseTumor suppressor
   DomainZinc-finger
   LigandMetal-binding
Zinc
   PTMAcetylation
Phosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processRas protein signal transduction

Inferred from direct assay Ref.13. Source: UniProtKB

cell cycle arrest

Inferred from mutant phenotype Ref.7. Source: UniProtKB

cellular response to DNA damage stimulus

Inferred from mutant phenotype Ref.17. Source: UniProtKB

negative regulation of cell cycle arrest

Inferred from direct assay Ref.17. Source: UniProtKB

positive regulation of protein ubiquitination

Inferred from direct assay Ref.17. Source: UniProtKB

protein stabilization

Inferred from direct assay Ref.17. Source: UniProtKB

   Cellular_componentcytoplasm

Inferred from direct assay. Source: HPA

microtubule

Inferred from electronic annotation. Source: UniProtKB-KW

microtubule cytoskeleton

Inferred from direct assay Ref.12Ref.17. Source: UniProtKB

microtubule organizing center

Inferred from electronic annotation. Source: UniProtKB-SubCell

nucleus

Inferred from direct assay Ref.12Ref.17. Source: UniProtKB

plasma membrane

Inferred from direct assay. Source: HPA

spindle pole

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionidentical protein binding

Inferred from physical interaction Ref.8PubMed 20920251. Source: IntAct

protein N-terminus binding

Inferred from physical interaction Ref.17. Source: UniProtKB

zinc ion binding

Traceable author statement Ref.2. Source: UniProtKB

Complete GO annotation...

Alternative products

This entry describes 8 isoforms produced by alternative promoter usage and alternative splicing. [Align] [Select]
Isoform D Ref.2 (identifier: Q9NS23-1)

Also known as: RASSF1D; Cardiac-specific;

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.
Note: Produced by alternative promoter usage.
Isoform A Ref.1 Ref.2 (identifier: Q9NS23-2)

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.
Isoform B Ref.1 (identifier: Q9NS23-3)

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.
Isoform C Ref.1 Ref.2 (identifier: Q9NS23-4)

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.
Isoform E Ref.2 (identifier: Q9NS23-5)

Also known as: RASSF1E; Pancreas-specific;

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.
Isoform F Ref.2 (identifier: Q9NS23-6)

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.
Isoform G Ref.2 (identifier: Q9NS23-7)

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.
Isoform H (identifier: Q9NS23-9)

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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.18
Chain2 – 344343Ras association domain-containing protein 1
PRO_0000068891

Regions

Domain198 – 29295Ras-associating
Domain294 – 34148SARAH
Zinc finger51 – 10555Phorbol-ester/DAG-type
Region2 – 119118Mediates interaction with E4F1
Region315 – 3184MOAP1-binding

Amino acid modifications

Modified residue21N-acetylserine Ref.18
Modified residue21Phosphoserine Ref.18

Natural variations

Alternative sequence1 – 155155Missing in isoform B. Ref.1
VSP_050770
Alternative sequence1 – 7474Missing in isoform C and isoform H. Ref.1 Ref.2
VSP_050773
Alternative sequence75 – 12349VVRKG…RDTNV → MGEAEAPSFEMTWSSTTSSG YCSQEDSDSELEQYFTARTS LARRPRRDQ in isoform C and isoform H. Ref.1 Ref.2
VSP_050774
Alternative sequence84 – 14966RLSAD…EYNAQ → QQGRFLHRLHQGSAEAGAPC LCALQQEATLLAGCPAGPRT GHKCQAPHFLLPAQGCCQAP ACAVTHKGT in isoform G. Ref.2
VSP_050775
Alternative sequence84 – 885RLSAD → H in isoform A and isoform E. Ref.1 Ref.2
VSP_050771
Alternative sequence85 – 917LSADCKF → RACGVGD in isoform F. Ref.2
VSP_050776
Alternative sequence93 – 344252Missing in isoform F. Ref.2
VSP_050777
Alternative sequence1231V → VPILQ in isoform E. Ref.2
VSP_050772
Alternative sequence150 – 344195Missing in isoform G and isoform H. Ref.2
VSP_050778
Natural variant211K → Q. Ref.1 Ref.2
Corresponds to variant rs4688725 [ dbSNP | Ensembl ].
VAR_019542
Natural variant531R → C. Ref.2
Corresponds to variant rs201618726 [ dbSNP | Ensembl ].
VAR_019543
Natural variant1331D → E. Ref.2
Corresponds to variant rs76335415 [ dbSNP | Ensembl ].
VAR_019544
Natural variant1351S → F Prevents G1 cell cycle arrest; reduced protein phosphorylation. Ref.7
VAR_019545
Natural variant1371A → S Prevents G1 cell cycle arrest; reduced protein phosphorylation. Ref.2 Ref.7
Corresponds to variant rs2073498 [ dbSNP | Ensembl ].
VAR_019546
Natural variant3191H → R.
Corresponds to variant rs12488879 [ dbSNP | Ensembl ].
VAR_059794
Natural variant3291Y → C. Ref.2
VAR_019547

Sequences

Sequence LengthMass (Da)Tools
Isoform D (RASSF1D) (Cardiac-specific) [UniParc].

Last modified October 1, 2000. Version 1.
Checksum: 4071B8D044C1DB2D

FASTA34439,219
        10         20         30         40         50         60 
MSGEPELIEL RELAPAGRAG KGRTRLERAN ALRIARGTAC NPTRQLVPGR GHRFQPAGPA 

        70         80         90        100        110        120 
THTWCDLCGD FIWGVVRKGL QCARLSADCK FTCHYRCRAL VCLDCCGPRD LGWEPAVERD 

       130        140        150        160        170        180 
TNVDEPVEWE TPDLSQAEIE QKIKEYNAQI NSNLFMSLNK DGSYTGFIKV QLKLVRPVSV 

       190        200        210        220        230        240 
PSSKKPPSLQ DARRGPGRGT SVRRRTSFYL PKDAVKHLHV LSRTRAREVI EALLRKFLVV 

       250        260        270        280        290        300 
DDPRKFALFE RAERHGQVYL RKLLDDEQPL RLRLLAGPSD KALSFVLKEN DSGEVNWDAF 

       310        320        330        340 
SMPELHNFLR ILQREEEEHL RQILQKYSYC RQKIQEALHA CPLG 

« Hide

Isoform A (RASSF1A) [UniParc].

Checksum: 73FB7C7D87507D9F
Show »

FASTA34038,814
Isoform B (RASSF1B) [UniParc].

Checksum: 2D7C1F632EA7A23B
Show »

FASTA18921,899
Isoform C (RASSF1C) [UniParc].

Checksum: 2E7006EA16A38D25
Show »

FASTA27031,226
Isoform E (RASSF1E) (Pancreas-specific) [UniParc].

Checksum: DB422771EB2AB7B2
Show »

FASTA34439,265
Isoform F (RASSF1F) [UniParc].

Checksum: C8FEFAAD37425A01
Show »

FASTA929,937
Isoform G (RASSF1G) [UniParc].

Checksum: 18403EEC734C2695
Show »

FASTA15216,120
Isoform H [UniParc].

Checksum: 5B7A6F7C7409E740
Show »

FASTA758,656

References

« Hide 'large scale' references
[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]"Epigenetic inactivation of RASSF1A in lung and breast cancers and malignant phenotype suppression."
Burbee D.G., Forgacs E., Zochbauer-Muller S., Shivakumar L., Fong K., Gao B., Randle D., Kondo M., Virmani A., Bader S., Sekido Y., Latif F., Milchgrub S., Toyooka S., Gazdar A.F., Lerman M.I., Zabarovsky E., White M., Minna J.D.
J. Natl. Cancer Inst. 93:691-699(2001) [PubMed] [Europe PMC] [Abstract]
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: Heart, Lung and Pancreas.
[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. expand/collapse author list , 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]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
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]Erratum
Ortiz-Vega S., Khokhlatchev A., Nedwidek M., Zhang X.F., Dammann R., Pfeifer G.P., Avruch J.
Oncogene 21:1943-1943(2002)
[10]"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.
[11]"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.
[12]"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.
[13]"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.
[14]"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.
[15]"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.
[16]"Role of the tumor suppressor RASSF1A in Mst1-mediated apoptosis."
Oh H.J., Lee K.-K., Song S.J., Jin M.S., Song M.S., Lee J.H., Im C.R., Lee J.-O., Yonehara S., Lim D.-S.
Cancer Res. 66:2562-2569(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH STK3/MST2 AND STK4/MST1.
[17]"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.
[18]"Large-scale proteomics analysis of the human kinome."
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G., Mann M., Daub H.
Mol. Cell. Proteomics 8:1751-1764(2009) [PubMed] [Europe PMC] [Abstract]
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].
[19]"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.
[20]"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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
RefSeqNP_001193886.1. NM_001206957.1.
NP_009113.3. NM_007182.4.
NP_733830.1. NM_170712.2.
NP_733831.1. NM_170713.2.
NP_733832.1. NM_170714.1.
UniGeneHs.476270.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2KZUNMR-B-[»]
ProteinModelPortalQ9NS23.
SMRQ9NS23. Positions 49-105, 138-290, 294-338.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid116356. 37 interactions.
DIPDIP-31270N.
IntActQ9NS23. 37 interactions.
MINTMINT-146049.

PTM databases

PhosphoSiteQ9NS23.

Polymorphism databases

DMDM50401686.

Proteomic databases

PaxDbQ9NS23.
PRIDEQ9NS23.

Protocols and materials databases

DNASU11186.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000327761; 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]
ENST00000571713; ENSP00000460113; ENSG00000263005. [Q9NS23-2]
ENST00000573573; ENSP00000458429; ENSG00000263005. [Q9NS23-1]
ENST00000574064; ENSP00000460844; ENSG00000263005. [Q9NS23-3]
ENST00000575029; ENSP00000458147; ENSG00000263005. [Q9NS23-4]
ENST00000575676; ENSP00000461709; ENSG00000263005. [Q9NS23-6]
ENST00000576813; ENSP00000460729; ENSG00000263005. [Q9NS23-7]
GeneID11186.
KEGGhsa:11186.
UCSCuc003daa.1. human. [Q9NS23-1]
uc003dae.1. human. [Q9NS23-2]

Organism-specific databases

CTD11186.
GeneCardsGC03M050369.
HGNCHGNC:9882. RASSF1.
HPAHPA040735.
HPA042098.
MIM605082. gene.
neXtProtNX_Q9NS23.
PharmGKBPA34245.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG308852.
HOVERGENHBG054362.
InParanoidQ9NS23.
KOK09850.
OMATTSSGYC.
OrthoDBEOG7TF796.
PhylomeDBQ9NS23.
TreeFamTF319243.

Enzyme and pathway databases

SignaLinkQ9NS23.

Gene expression databases

ArrayExpressQ9NS23.
BgeeQ9NS23.
GenevestigatorQ9NS23.

Family and domain databases

InterProIPR002219. Prot_Kinase_C-like_PE/DAG-bd.
IPR000159. Ras-assoc.
IPR011524. SARAH_dom.
[Graphical view]
PfamPF00130. C1_1. 1 hit.
PF00788. RA. 1 hit.
[Graphical view]
SMARTSM00109. C1. 1 hit.
SM00314. RA. 1 hit.
[Graphical view]
PROSITEPS50200. RA. 1 hit.
PS50951. SARAH. 1 hit.
PS50081. ZF_DAG_PE_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceQ9NS23.
GeneWikiRASSF1.
GenomeRNAi11186.
NextBio42571.
PROQ9NS23.
SOURCESearch...

Entry information

Entry nameRASF1_HUMAN
AccessionPrimary (citable) accession number: Q9NS23
Secondary accession number(s): B7ZLL1 expand/collapse secondary AC list , O14571, O60539, O60710, Q0VGC6, Q5TZT2, Q9HB04, Q9HB18, Q9NS22, Q9UND4, Q9UND5
Entry history
Integrated into UniProtKB/Swiss-Prot: July 19, 2004
Last sequence update: October 1, 2000
Last modified: April 16, 2014
This is version 119 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 3

Human chromosome 3: entries, gene names and cross-references to MIM