Q9NS23 (RASF1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Ras association domain-containing protein 1

Gene names

Name:	RASSF1
Synonyms:	RDA32

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	344 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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 HRAS1 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. 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: Cytoplasm › cytoskeleton. Cytoplasm › cytoskeleton › centrosome. Cytoplasm › cytoskeleton › spindle. Cytoplasm › cytoskeleton › spindle 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 process	Cell cycle
Cellular component	Cytoplasm Cytoskeleton Microtubule Nucleus
Coding sequence diversity	Alternative promoter usage Alternative splicing Polymorphism
Disease	Tumor suppressor
Domain	Zinc-finger
Ligand	Metal-binding Zinc
PTM	Acetylation Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	Ras protein signal transduction Inferred from direct assay Ref.13. Source: UniProtKB cell cycle arrest Inferred from mutant phenotype Ref.7. 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 response to DNA damage stimulus Inferred from mutant phenotype Ref.17. Source: UniProtKB
Cellular_component	cytoplasm 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_function	zinc ion binding Traceable author statement Ref.2. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
CDC20	Q12834	2	EBI-438698,EBI-367462
E4F1	Q66K89	7	EBI-438698,EBI-1227043
EWSR1	Q01844	3	EBI-438698,EBI-739737
GABARAP	O95166	2	EBI-367363,EBI-712001
GABARAPL2	P60520	2	EBI-367363,EBI-720116
HRAS	P01112	2	EBI-438698,EBI-350145
MAP1LC3B	Q9GZQ8	2	EBI-367363,EBI-373144
MAP1LC3C	Q9BXW4	2	EBI-367363,EBI-2603996
STK3	Q13188	3	EBI-438698,EBI-992580
STK4	Q13043	4	EBI-438698,EBI-367376

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 key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Initiator methionine	1	1	Removed Ref.18
	Chain	2 – 344	343	Ras association domain-containing protein 1		PRO_0000068891
Regions
	Domain	198 – 292	95	Ras-associating
	Domain	294 – 341	48	SARAH
	Zinc finger	51 – 105	55	Phorbol-ester/DAG-type
	Region	2 – 119	118	Mediates interaction with E4F1
	Region	315 – 318	4	MOAP1-binding
Amino acid modifications
	Modified residue	2	1	N-acetylserine Ref.18
	Modified residue	2	1	Phosphoserine Ref.18
Natural variations
	Alternative sequence	1 – 155	155	Missing in isoform B. Ref.1		VSP_050770
	Alternative sequence	1 – 74	74	Missing in isoform C and isoform H. Ref.1 Ref.2		VSP_050773
	Alternative sequence	75 – 123	49	VVRKG…RDTNV → MGEAEAPSFEMTWSSTTSSG YCSQEDSDSELEQYFTARTS LARRPRRDQ in isoform C and isoform H. Ref.1 Ref.2		VSP_050774
	Alternative sequence	84 – 149	66	RLSAD…EYNAQ → QQGRFLHRLHQGSAEAGAPC LCALQQEATLLAGCPAGPRT GHKCQAPHFLLPAQGCCQAP ACAVTHKGT in isoform G. Ref.2		VSP_050775
	Alternative sequence	84 – 88	5	RLSAD → H in isoform A and isoform E. Ref.1 Ref.2		VSP_050771
	Alternative sequence	85 – 91	7	LSADCKF → RACGVGD in isoform F. Ref.2		VSP_050776
	Alternative sequence	93 – 344	252	Missing in isoform F. Ref.2		VSP_050777
	Alternative sequence	123	1	V → VPILQ in isoform E. Ref.2		VSP_050772
	Alternative sequence	150 – 344	195	Missing in isoform G and isoform H. Ref.2		VSP_050778
	Natural variant	21	1	K → Q. Ref.1 Ref.2 Corresponds to variant rs4688725 [ dbSNP | Ensembl ].		VAR_019542
	Natural variant	53	1	R → C. Ref.2		VAR_019543
	Natural variant	133	1	D → E. Ref.2		VAR_019544
	Natural variant	135	1	S → F Prevents G1 cell cycle arrest; reduced protein phosphorylation. Ref.7		VAR_019545
	Natural variant	137	1	A → S Prevents G1 cell cycle arrest; reduced protein phosphorylation. Ref.2 Ref.7 Corresponds to variant rs2073498 [ dbSNP | Ensembl ].		VAR_019546
	Natural variant	319	1	H → R. Corresponds to variant rs12488879 [ dbSNP | Ensembl ].		VAR_059794
	Natural variant	329	1	Y → C. Ref.2		VAR_019547

Sequences

	Sequence		Length	Mass (Da)
	Isoform D (RASSF1D) (Cardiac-specific) [UniParc]. Last modified October 1, 2000. Version 1. Checksum: 4071B8D044C1DB2D	FASTA	344	39,219
	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
	Isoform A (RASSF1A) [UniParc]. Checksum: 73FB7C7D87507D9F	FASTA	340	38,814
	10 20 30 40 50 60 MSGEPELIEL RELAPAGRAG KGRTRLERAN ALRIARGTAC NPTRQLVPGR GHRFQPAGPA 70 80 90 100 110 120 THTWCDLCGD FIWGVVRKGL QCAHCKFTCH YRCRALVCLD CCGPRDLGWE PAVERDTNVD 130 140 150 160 170 180 EPVEWETPDL SQAEIEQKIK EYNAQINSNL FMSLNKDGSY TGFIKVQLKL VRPVSVPSSK 190 200 210 220 230 240 KPPSLQDARR GPGRGTSVRR RTSFYLPKDA VKHLHVLSRT RAREVIEALL RKFLVVDDPR 250 260 270 280 290 300 KFALFERAER HGQVYLRKLL DDEQPLRLRL LAGPSDKALS FVLKENDSGE VNWDAFSMPE 310 320 330 340 LHNFLRILQR EEEEHLRQIL QKYSYCRQKI QEALHACPLG
	Isoform B (RASSF1B) [UniParc]. Checksum: 2D7C1F632EA7A23B	FASTA	189	21,899
	10 20 30 40 50 60 MSLNKDGSYT GFIKVQLKLV RPVSVPSSKK PPSLQDARRG PGRGTSVRRR TSFYLPKDAV 70 80 90 100 110 120 KHLHVLSRTR AREVIEALLR KFLVVDDPRK FALFERAERH GQVYLRKLLD DEQPLRLRLL 130 140 150 160 170 180 AGPSDKALSF VLKENDSGEV NWDAFSMPEL HNFLRILQRE EEEHLRQILQ KYSYCRQKIQ EALHACPLG
	Isoform C (RASSF1C) [UniParc]. Checksum: 2E7006EA16A38D25	FASTA	270	31,226
	10 20 30 40 50 60 MGEAEAPSFE MTWSSTTSSG YCSQEDSDSE LEQYFTARTS LARRPRRDQD EPVEWETPDL 70 80 90 100 110 120 SQAEIEQKIK EYNAQINSNL FMSLNKDGSY TGFIKVQLKL VRPVSVPSSK KPPSLQDARR 130 140 150 160 170 180 GPGRGTSVRR RTSFYLPKDA VKHLHVLSRT RAREVIEALL RKFLVVDDPR KFALFERAER 190 200 210 220 230 240 HGQVYLRKLL DDEQPLRLRL LAGPSDKALS FVLKENDSGE VNWDAFSMPE LHNFLRILQR 250 260 270 EEEEHLRQIL QKYSYCRQKI QEALHACPLG
	Isoform E (RASSF1E) (Pancreas-specific) [UniParc]. Checksum: DB422771EB2AB7B2	FASTA	344	39,265
	10 20 30 40 50 60 MSGEPELIEL RELAPAGRAG KGRTRLERAN ALRIARGTAC NPTRQLVPGR GHRFQPAGPA 70 80 90 100 110 120 THTWCDLCGD FIWGVVRKGL QCAHCKFTCH YRCRALVCLD CCGPRDLGWE PAVERDTNVP 130 140 150 160 170 180 ILQDEPVEWE 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
	Isoform F (RASSF1F) [UniParc]. Checksum: C8FEFAAD37425A01	FASTA	92	9,937
	10 20 30 40 50 60 MSGEPELIEL RELAPAGRAG KGRTRLERAN ALRIARGTAC NPTRQLVPGR GHRFQPAGPA 70 80 90 THTWCDLCGD FIWGVVRKGL QCARRACGVG DT
	Isoform G (RASSF1G) [UniParc]. Checksum: 18403EEC734C2695	FASTA	152	16,120
	10 20 30 40 50 60 MSGEPELIEL RELAPAGRAG KGRTRLERAN ALRIARGTAC NPTRQLVPGR GHRFQPAGPA 70 80 90 100 110 120 THTWCDLCGD FIWGVVRKGL QCAQQGRFLH RLHQGSAEAG APCLCALQQE ATLLAGCPAG 130 140 150 PRTGHKCQAP HFLLPAQGCC QAPACAVTHK GT
	Isoform H [UniParc]. Checksum: 5B7A6F7C7409E740	FASTA	75	8,656
	10 20 30 40 50 60 MGEAEAPSFE MTWSSTTSSG YCSQEDSDSE LEQYFTARTS LARRPRRDQD EPVEWETPDL 70 SQAEIEQKIK EYNAQ

References

	« Hide 'large scale' referencesShow '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. , 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. , 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 HRAS1.
[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, MASS SPECTROMETRY, CLEAVAGE OF INITIATOR METHIONINE.
[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.

Web resources

Atlas of Genetics and Cytogenetics in Oncology and Haematology

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.

IPI

IPI00172514.
IPI00172661.
IPI00221057.
IPI00395780.
IPI00426162.
IPI00426164.
IPI00426165.
IPI00455193.

RefSeq

NP_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.

UniGene

Hs.476270.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2KZU	NMR	-	B	-	[»]

ProteinModelPortal

Q9NS23.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-31270N.

IntAct

Q9NS23. 20 interactions.

MINT

MINT-146049.

PTM databases

PhosphoSite

Q9NS23.

Polymorphism databases

DMDM

50401686.

Proteomic databases

PaxDb

Q9NS23.

PRIDE

Q9NS23.

Protocols and materials databases

DNASU

11186.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000327761; ENSP00000333327; ENSG00000068028.
ENST00000357043; ENSP00000349547; ENSG00000068028.
ENST00000359365; ENSP00000352323; ENSG00000068028.
ENST00000395117; ENSP00000378549; ENSG00000068028.
ENST00000395126; ENSP00000378558; ENSG00000068028.
ENST00000482447; ENSP00000433000; ENSG00000068028.
ENST00000571713; ENSP00000460113; ENSG00000263005.
ENST00000573573; ENSP00000458429; ENSG00000263005.
ENST00000574064; ENSP00000460844; ENSG00000263005.
ENST00000575029; ENSP00000458147; ENSG00000263005.
ENST00000575676; ENSP00000461709; ENSG00000263005.
ENST00000576813; ENSP00000460729; ENSG00000263005.

GeneID

11186.

KEGG

hsa:11186.

UCSC

uc003daa.1. human.
uc003dab.1. human.
uc003dae.1. human.

Organism-specific databases

CTD

11186.

GeneCards

GC03M050369.

HGNC

HGNC:9882. RASSF1.

HPA

HPA040735.

MIM

605082. gene.

neXtProt

NX_Q9NS23.

PharmGKB

PA34245.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG308852.

HOVERGEN

HBG054362.

InParanoid

Q9NS23.

KO

K09850.

OMA

PRRDQDE.

Enzyme and pathway databases

SignaLink

Q9NS23.

Gene expression databases

ArrayExpress

Q9NS23.

Bgee

Q9NS23.

Genevestigator

Q9NS23.

GermOnline

ENSG00000068028. Homo sapiens.

Family and domain databases

InterPro

IPR002219. Prot_Kinase_C-like_PE/DAG-bd.
IPR000159. Ras-assoc.
IPR011524. SARAH_dom.
[Graphical view]

Pfam

PF00130. C1_1. 1 hit.
PF00788. RA. 1 hit.
[Graphical view]

SMART

SM00109. C1. 1 hit.
SM00314. RA. 1 hit.
[Graphical view]

PROSITE

PS50200. RA. 1 hit.
PS50951. SARAH. 1 hit.
PS00479. ZF_DAG_PE_1. False negative.
PS50081. ZF_DAG_PE_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

Q9NS23.

GenomeRNAi

11186.

NextBio

42571.

SOURCE

Search...

Entry information

Entry name

RASF1_HUMAN

Accession

Primary (citable) accession number: Q9NS23
Secondary accession number(s): B7ZLL1 , 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:	May 29, 2013
This is version 110 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.