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Protein

Ras association domain-containing protein 5

Gene

Rassf5

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Potental tumor suppressor. Seems to be involved in lymphocyte adhesion by linking RAP1A activation upon T-cell receptor or chemokine stimulation to integrin activation. Isoform 2 stimulates lymphocyte polarization and the patch-like distribution of ITGAL/LFA-1, resulting in an enhanced adhesion to ICAM1. Together with RAP1A may participate in regulation of microtubule growth. The association of isoform 2 with activated RAP1A is required for directional movement of endothelial cells during wound healing (By similarity). May be involved in regulation of Ras apoptotic function. The RASSF5-STK4/MST1 complex may mediate HRAS and KRAS induced apoptosis.By similarity1 Publication

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri117 – 16549Phorbol-ester/DAG-typePROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

GO - Biological processi

  • apoptotic process Source: UniProtKB-KW
  • intracellular signal transduction Source: InterPro
  • negative regulation of cell proliferation Source: MGI
  • positive regulation of protein ubiquitination Source: MGI
  • regulation of protein localization to nucleus Source: MGI
Complete GO annotation...

Keywords - Biological processi

Apoptosis

Keywords - Ligandi

Metal-binding, Zinc

Names & Taxonomyi

Protein namesi
Recommended name:
Ras association domain-containing protein 5
Alternative name(s):
New ras effector 1
Regulator for cell adhesion and polarization enriched in lymphoid tissues
Short name:
RAPL
Gene namesi
Name:Rassf5
Synonyms:Nore1, Rapl
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 1

Organism-specific databases

MGIiMGI:1926375. Rassf5.

Subcellular locationi

  • Cytoplasm By similarity
  • Cytoplasmcytoskeleton By similarity

  • Note: Isoform 2 is mainly located in the perinuclear region of unstimulated primary T-cells. Upon stimulation translocates to the leading edge and colocalizes with ITGAL/LFA-1 in the peripheral zone of the immunological synapse. Isoform 2 is localized to growing microtubules in vascular endothelial cells and is dissociated from microtubules by activated RAP1A (By similarity).By similarity

GO - Cellular componenti

  • cytoplasm Source: UniProtKB-SubCell
  • microtubule Source: UniProtKB-KW
  • nucleus Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton, Microtubule

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi220 – 2201C → A: Reduced interaction with HRAS. 1 Publication
Mutagenesisi220 – 2201C → D: Strongly reduced interaction with HRAS. 1 Publication
Mutagenesisi221 – 2211L → A or D: Strongly reduced interaction with HRAS. 1 Publication
Mutagenesisi234 – 2341F → A: Reduced interaction with HRAS. 1 Publication
Mutagenesisi236 – 2361K → A: Reduced interaction with HRAS. 1 Publication
Mutagenesisi280 – 2801D → A: Reduced interaction with HRAS. 1 Publication
Mutagenesisi283 – 2831K → A: Very strong reduction of the interaction with HRAS. 1 Publication
Mutagenesisi284 – 2841Q → A: Reduced interaction with HRAS. 1 Publication
Mutagenesisi302 – 3021K → D: Reduced specificity for HRAS and diminished discrimination between HRAS and RAP1A. 1 Publication
Mutagenesisi303 – 3031K → A: Strongly reduced interaction with HRAS. 1 Publication

Keywords - Diseasei

Tumor suppressor

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 413413Ras association domain-containing protein 5PRO_0000240402Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei177 – 1771PhosphoserineCombined sources
Modified residuei347 – 3471PhosphothreonineBy similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiQ5EBH1.
MaxQBiQ5EBH1.
PaxDbiQ5EBH1.
PRIDEiQ5EBH1.

PTM databases

PhosphoSiteiQ5EBH1.
SwissPalmiQ5EBH1.

Expressioni

Gene expression databases

BgeeiQ5EBH1.
ExpressionAtlasiQ5EBH1. baseline and differential.
GenevisibleiQ5EBH1. MM.

Interactioni

Subunit structurei

Interacts directly with activated HRAS; a RASSF5-STK4/MST1 complex probably associates with activated HRAS. Interacts with KRAS. Probably interacts with Ras-like GTPases RRAS, RRAS2, MRAS, RAP1B, RAP2A and RALA. Can self-associate. Interacts with RSSF1 isoform A. The RSSF1 isoform A-RSSF5 heterodimer probably mediates the association of RSSF1 with HRAS. Isoform 2 interacts with activated RAP1A and ITGAL/LFA-1. Binds STK4/MST1, inhibiting STK4/MST1 autoactivation (By similarity).By similarity

Binary interactionsi

WithEntry#Exp.IntActNotes
Hipk1O889045EBI-960530,EBI-692945
HRASP0111211EBI-960530,EBI-350145From a different organism.
HrasQ614112EBI-960530,EBI-400273
Mdm2P238043EBI-960530,EBI-641788
RAP1AP628342EBI-960530,EBI-491414From a different organism.
Stk4Q9JI113EBI-960530,EBI-1181352

Protein-protein interaction databases

BioGridi207620. 1 interaction.
DIPiDIP-29107N.
IntActiQ5EBH1. 19 interactions.
MINTiMINT-5177821.
STRINGi10090.ENSMUSP00000027688.

Structurei

Secondary structure

1
413
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi112 – 1143Combined sources
Turni133 – 1353Combined sources
Beta strandi137 – 1393Combined sources
Turni147 – 1493Combined sources
Helixi155 – 1584Combined sources
Helixi203 – 21513Combined sources
Helixi219 – 2213Combined sources
Helixi227 – 2293Combined sources
Beta strandi231 – 24515Combined sources
Beta strandi275 – 28814Combined sources
Helixi293 – 30311Combined sources
Helixi310 – 3123Combined sources
Beta strandi313 – 3219Combined sources
Beta strandi324 – 3296Combined sources
Helixi336 – 3438Combined sources
Turni347 – 3493Combined sources
Beta strandi351 – 3566Combined sources
Helixi370 – 40536Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1RFHNMR-A108-166[»]
2FNFNMR-X95-166[»]
2YMYX-ray1.69A/B370-413[»]
3DDCX-ray1.80B200-357[»]
ProteinModelPortaliQ5EBH1.
SMRiQ5EBH1. Positions 108-166, 200-357, 370-408.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ5EBH1.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini265 – 35995Ras-associatingPROSITE-ProRule annotationAdd
BLAST
Domaini361 – 40848SARAHPROSITE-ProRule annotationAdd
BLAST

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 fingeri117 – 16549Phorbol-ester/DAG-typePROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

Zinc-finger

Phylogenomic databases

eggNOGiENOG410IPAE. Eukaryota.
ENOG4111HS2. LUCA.
GeneTreeiENSGT00390000003367.
HOGENOMiHOG000013025.
HOVERGENiHBG054362.
InParanoidiQ5EBH1.
KOiK08015.
OMAiKFALFKE.
OrthoDBiEOG7TF796.
PhylomeDBiQ5EBH1.
TreeFamiTF319243.

Family and domain databases

InterProiIPR002219. PE/DAG-bd.
IPR000159. RA_dom.
IPR011524. SARAH_dom.
IPR029071. Ubiquitin-rel_dom.
[Graphical view]
PfamiPF00130. C1_1. 1 hit.
PF16517. Nore1-SARAH. 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.
PS00479. ZF_DAG_PE_1. 1 hit.
PS50081. ZF_DAG_PE_2. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q5EBH1-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MASPAIGQRP YPLLLDPEPP RYLQSLGGTE PPPPARPRRC IPTALIPAAG
60 70 80 90 100
ASEDRGGRRS GRRDPEPTPR DCRHARPVRP GLQPRLRLRP GSHRPRDVRS
110 120 130 140 150
IFEQPQDPRV LAERGEGHRF VELALRGGPG WCDLCGREVL RQALRCANCK
160 170 180 190 200
FTCHSECRSL IQLDCRQKGG PALDRRSPES TLTPTLNQNV CKAVEETQHP
210 220 230 240 250
PTIQEIKQKI DSYNSREKHC LGMKLSEDGT YTGFIKVHLK LRRPVTVPAG
260 270 280 290 300
IRPQSIYDAI KEVNPAATTD KRTSFYLPLD AIKQLHISST TTVSEVIQGL
310 320 330 340 350
LKKFMVVDNP QKFALFKRIH KDGQVLFQKL SIADYPLYLR LLAGPDTDVL
360 370 380 390 400
SFVLKENETG EVEWDAFSIP ELQNFLTILE KEEQDKIHQL QKKYNKFRQK
410
LEEALRESQG KPG
Length:413
Mass (Da):46,714
Last modified:March 15, 2005 - v1
Checksum:iE6FF7DDE6BECB180
GO
Isoform 2 (identifier: Q5EBH1-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-142: Missing.
     143-188: ALRCANCKFT...ESTLTPTLNQ → MTVDSSMSSG...RNLQSKQPSK

Show »
Length:265
Mass (Da):30,339
Checksum:iCF0431ED3B2D23D6
GO

Sequence cautioni

The sequence BAD21397.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti179 – 1791E → G in AAC08580 (PubMed:9488663).Curated
Sequence conflicti251 – 2577IRPQSIY → SGPSPSM in AAC08580 (PubMed:9488663).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 142142Missing in isoform 2. 3 PublicationsVSP_019368Add
BLAST
Alternative sequencei143 – 18846ALRCA…PTLNQ → MTVDSSMSSGYCSLDEELED CFFTAKTTFFRNLQSKQPSK in isoform 2. 3 PublicationsVSP_019369Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF053959 mRNA. Translation: AAC08580.1.
AY261333 mRNA. Translation: AAP83361.1.
AK131147 mRNA. Translation: BAD21397.1. Different initiation.
AK088751 mRNA. Translation: BAC40546.1.
AK155534 mRNA. Translation: BAE33312.1.
AK155869 mRNA. Translation: BAE33472.1.
BC089605 mRNA. Translation: AAH89605.1.
CCDSiCCDS15268.1. [Q5EBH1-1]
CCDS78675.1. [Q5EBH1-2]
RefSeqiNP_001298023.1. NM_001311094.2. [Q5EBH1-2]
NP_061220.2. NM_018750.4. [Q5EBH1-1]
UniGeneiMm.248291.

Genome annotation databases

EnsembliENSMUST00000027688; ENSMUSP00000027688; ENSMUSG00000026430. [Q5EBH1-1]
ENSMUST00000068564; ENSMUSP00000067011; ENSMUSG00000026430. [Q5EBH1-2]
GeneIDi54354.
KEGGimmu:54354.
UCSCiuc007cnc.1. mouse. [Q5EBH1-2]
uc007cnd.1. mouse. [Q5EBH1-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF053959 mRNA. Translation: AAC08580.1.
AY261333 mRNA. Translation: AAP83361.1.
AK131147 mRNA. Translation: BAD21397.1. Different initiation.
AK088751 mRNA. Translation: BAC40546.1.
AK155534 mRNA. Translation: BAE33312.1.
AK155869 mRNA. Translation: BAE33472.1.
BC089605 mRNA. Translation: AAH89605.1.
CCDSiCCDS15268.1. [Q5EBH1-1]
CCDS78675.1. [Q5EBH1-2]
RefSeqiNP_001298023.1. NM_001311094.2. [Q5EBH1-2]
NP_061220.2. NM_018750.4. [Q5EBH1-1]
UniGeneiMm.248291.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1RFHNMR-A108-166[»]
2FNFNMR-X95-166[»]
2YMYX-ray1.69A/B370-413[»]
3DDCX-ray1.80B200-357[»]
ProteinModelPortaliQ5EBH1.
SMRiQ5EBH1. Positions 108-166, 200-357, 370-408.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi207620. 1 interaction.
DIPiDIP-29107N.
IntActiQ5EBH1. 19 interactions.
MINTiMINT-5177821.
STRINGi10090.ENSMUSP00000027688.

PTM databases

PhosphoSiteiQ5EBH1.
SwissPalmiQ5EBH1.

Proteomic databases

EPDiQ5EBH1.
MaxQBiQ5EBH1.
PaxDbiQ5EBH1.
PRIDEiQ5EBH1.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000027688; ENSMUSP00000027688; ENSMUSG00000026430. [Q5EBH1-1]
ENSMUST00000068564; ENSMUSP00000067011; ENSMUSG00000026430. [Q5EBH1-2]
GeneIDi54354.
KEGGimmu:54354.
UCSCiuc007cnc.1. mouse. [Q5EBH1-2]
uc007cnd.1. mouse. [Q5EBH1-1]

Organism-specific databases

CTDi83593.
MGIiMGI:1926375. Rassf5.

Phylogenomic databases

eggNOGiENOG410IPAE. Eukaryota.
ENOG4111HS2. LUCA.
GeneTreeiENSGT00390000003367.
HOGENOMiHOG000013025.
HOVERGENiHBG054362.
InParanoidiQ5EBH1.
KOiK08015.
OMAiKFALFKE.
OrthoDBiEOG7TF796.
PhylomeDBiQ5EBH1.
TreeFamiTF319243.

Miscellaneous databases

EvolutionaryTraceiQ5EBH1.
NextBioi311142.
PROiQ5EBH1.
SOURCEiSearch...

Gene expression databases

BgeeiQ5EBH1.
ExpressionAtlasiQ5EBH1. baseline and differential.
GenevisibleiQ5EBH1. MM.

Family and domain databases

InterProiIPR002219. PE/DAG-bd.
IPR000159. RA_dom.
IPR011524. SARAH_dom.
IPR029071. Ubiquitin-rel_dom.
[Graphical view]
PfamiPF00130. C1_1. 1 hit.
PF16517. Nore1-SARAH. 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.
PS00479. ZF_DAG_PE_1. 1 hit.
PS50081. ZF_DAG_PE_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Identification of Nore1 as a potential Ras effector."
    Vavvas D., Li X., Avruch J., Zhang X.F.
    J. Biol. Chem. 273:5439-5442(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), INTERACTION WITH HRAS.
    Strain: BALB/cJ.
    Tissue: Brain.
  2. "RAPL, a Rap1-binding molecule that mediates Rap1-induced adhesion through spatial regulation of LFA-1."
    Katagiri K., Maeda A., Shimonaka M., Kinashi T.
    Nat. Immunol. 4:741-748(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
    Strain: BALB/cJ.
    Tissue: Spleen.
  3. "Prediction of the coding sequences of mouse homologues of FLJ genes: the complete nucleotide sequences of 110 mouse FLJ-homologous cDNAs identified by screening of terminal sequences of cDNA clones randomly sampled from size-fractionated libraries."
    Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S., Saga Y., Kitamura H., Nakagawa T., Nagase T., Ohara O., Koga H.
    DNA Res. 11:127-135(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
    Tissue: Natural killer cell.
  4. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
    Strain: C57BL/6J and NOD.
    Tissue: Thymus.
  5. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Kidney.
  6. Cited for: FUNCTION IN APOPTOSIS, INTERACTION WITH STK4/MST1; HRAS AND KRAS.
  7. "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 RSSF1; HRAS; KRAS; RRAS; RRAS2; MRAS; RAP1B; RAP2A AND RALA.
  8. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-177, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Kidney, Lung, Spleen and Testis.
  9. "GTP-Ras disrupts the intramolecular complex of C1 and RA domains of Nore1."
    Harjes E., Harjes S., Wohlgemuth S., Mueller K.H., Krieger E., Herrmann C., Bayer P.
    Structure 14:881-888(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 95-166, SUBUNIT.
  10. "Novel type of Ras effector interaction established between tumour suppressor NORE1A and Ras switch II."
    Stieglitz B., Bee C., Schwarz D., Yildiz O., Moshnikova A., Khokhlatchev A., Herrmann C.
    EMBO J. 27:1995-2005(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 200-357 OF MUTANT ASP-302 IN COMPLEX WITH HRAS, MUTAGENESIS OF CYS-220; LEU-221; PHE-234; LYS-236; ASP-280; LYS-283; GLN-284; LYS-302 AND LYS-303, INTERACTION WITH RAP1A.

Entry informationi

Entry nameiRASF5_MOUSE
AccessioniPrimary (citable) accession number: Q5EBH1
Secondary accession number(s): O70407, Q6KAR0, Q8C2E8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 27, 2006
Last sequence update: March 15, 2005
Last modified: March 16, 2016
This is version 109 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.