RSU1_HUMAN
ID RSU1_HUMAN Reviewed; 277 AA.
AC Q15404; A8KA46; D3DRU3; Q6FI17;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 182.
DE RecName: Full=Ras suppressor protein 1;
DE Short=RSP-1;
DE Short=Rsu-1;
GN Name=RSU1; Synonyms=RSP1;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Skin;
RX PubMed=8288261; DOI=10.1006/geno.1993.1503;
RA Tsuda T., Cutler M.L.;
RT "Human RSU1 is highly homologous to mouse Rsu-1 and localizes to human
RT chromosome 10.";
RL Genomics 18:461-462(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Thalamus, and Trachea;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RG NHLBI resequencing and genotyping service (RS&G);
RL Submitted (FEB-2007) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164054; DOI=10.1038/nature02462;
RA Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L.,
RA Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K.,
RA Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L.,
RA Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P.,
RA Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y.,
RA Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N.,
RA Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A.,
RA Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C.,
RA Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D.,
RA Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C.,
RA Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K.,
RA Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A.,
RA Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S.,
RA McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S.,
RA Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V.,
RA Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A.,
RA Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M.,
RA Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A.,
RA Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P.,
RA Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y.,
RA Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D.,
RA Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.;
RT "The DNA sequence and comparative analysis of human chromosome 10.";
RL Nature 429:375-381(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain, and Eye;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [8]
RP PROTEIN SEQUENCE OF 2-13 (ISOFORM 1).
RC TISSUE=Platelet;
RX PubMed=12665801; DOI=10.1038/nbt810;
RA Gevaert K., Goethals M., Martens L., Van Damme J., Staes A., Thomas G.R.,
RA Vandekerckhove J.;
RT "Exploring proteomes and analyzing protein processing by mass spectrometric
RT identification of sorted N-terminal peptides.";
RL Nat. Biotechnol. 21:566-569(2003).
RN [9]
RP PROTEIN SEQUENCE OF 138-155 AND 192-208.
RC TISSUE=Adipocyte;
RX PubMed=15242332; DOI=10.1042/bj20040647;
RA Aboulaich N., Vainonen J.P., Stralfors P., Vener A.V.;
RT "Vectorial proteomics reveal targeting, phosphorylation and specific
RT fragmentation of polymerase I and transcript release factor (PTRF) at the
RT surface of caveolae in human adipocytes.";
RL Biochem. J. 383:237-248(2004).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [11]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
CC -!- FUNCTION: Potentially plays a role in the Ras signal transduction
CC pathway. Capable of suppressing v-Ras transformation in vitro.
CC -!- INTERACTION:
CC Q15404; P48059: LIMS1; NbExp=6; IntAct=EBI-1057132, EBI-306928;
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q15404-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q15404-2; Sequence=VSP_043831;
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DR EMBL; L12535; AAA60292.1; -; mRNA.
DR EMBL; AK292911; BAF85600.1; -; mRNA.
DR EMBL; AK312520; BAG35419.1; -; mRNA.
DR EMBL; CR536521; CAG38758.1; -; mRNA.
DR EMBL; CR541840; CAG46639.1; -; mRNA.
DR EMBL; EF445013; ACA06048.1; -; Genomic_DNA.
DR EMBL; EF445013; ACA06049.1; -; Genomic_DNA.
DR EMBL; EF445013; ACA06050.1; -; Genomic_DNA.
DR EMBL; AC073367; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL365215; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471072; EAW86222.1; -; Genomic_DNA.
DR EMBL; CH471072; EAW86223.1; -; Genomic_DNA.
DR EMBL; CH471072; EAW86224.1; -; Genomic_DNA.
DR EMBL; BC005993; AAH05993.1; -; mRNA.
DR EMBL; BC008691; AAH08691.1; -; mRNA.
DR EMBL; BC015644; AAH15644.1; -; mRNA.
DR CCDS; CCDS31157.1; -. [Q15404-2]
DR CCDS; CCDS7112.1; -. [Q15404-1]
DR PIR; I60122; I60122.
DR RefSeq; NP_036557.1; NM_012425.3. [Q15404-1]
DR RefSeq; NP_689937.2; NM_152724.2. [Q15404-2]
DR PDB; 7D2S; X-ray; 1.65 A; A=1-215.
DR PDB; 7D2T; X-ray; 2.20 A; A/C=1-277.
DR PDB; 7D2U; X-ray; 3.15 A; A=1-277.
DR PDB; 7LT8; X-ray; 1.76 A; A=1-277.
DR PDB; 7LT9; X-ray; 3.05 A; A=1-277.
DR PDBsum; 7D2S; -.
DR PDBsum; 7D2T; -.
DR PDBsum; 7D2U; -.
DR PDBsum; 7LT8; -.
DR PDBsum; 7LT9; -.
DR AlphaFoldDB; Q15404; -.
DR SMR; Q15404; -.
DR BioGRID; 112164; 46.
DR IntAct; Q15404; 15.
DR MINT; Q15404; -.
DR STRING; 9606.ENSP00000367154; -.
DR GlyGen; Q15404; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q15404; -.
DR MetOSite; Q15404; -.
DR PhosphoSitePlus; Q15404; -.
DR BioMuta; RSU1; -.
DR DMDM; 2498866; -.
DR OGP; Q15404; -.
DR EPD; Q15404; -.
DR jPOST; Q15404; -.
DR MassIVE; Q15404; -.
DR MaxQB; Q15404; -.
DR PaxDb; Q15404; -.
DR PeptideAtlas; Q15404; -.
DR PRIDE; Q15404; -.
DR ProteomicsDB; 60570; -. [Q15404-1]
DR ProteomicsDB; 60571; -. [Q15404-2]
DR Antibodypedia; 25179; 178 antibodies from 27 providers.
DR DNASU; 6251; -.
DR Ensembl; ENST00000345264.10; ENSP00000339521.5; ENSG00000148484.18. [Q15404-1]
DR Ensembl; ENST00000377921.7; ENSP00000367154.3; ENSG00000148484.18. [Q15404-1]
DR Ensembl; ENST00000602389.1; ENSP00000473588.1; ENSG00000148484.18. [Q15404-2]
DR GeneID; 6251; -.
DR KEGG; hsa:6251; -.
DR MANE-Select; ENST00000345264.10; ENSP00000339521.5; NM_012425.4; NP_036557.1.
DR UCSC; uc001iok.4; human. [Q15404-1]
DR CTD; 6251; -.
DR DisGeNET; 6251; -.
DR GeneCards; RSU1; -.
DR HGNC; HGNC:10464; RSU1.
DR HPA; ENSG00000148484; Low tissue specificity.
DR MIM; 179555; gene.
DR neXtProt; NX_Q15404; -.
DR OpenTargets; ENSG00000148484; -.
DR PharmGKB; PA34876; -.
DR VEuPathDB; HostDB:ENSG00000148484; -.
DR eggNOG; KOG0617; Eukaryota.
DR GeneTree; ENSGT00940000158676; -.
DR HOGENOM; CLU_000288_18_15_1; -.
DR InParanoid; Q15404; -.
DR OMA; RHMQGGR; -.
DR OrthoDB; 1382533at2759; -.
DR PhylomeDB; Q15404; -.
DR TreeFam; TF314790; -.
DR PathwayCommons; Q15404; -.
DR Reactome; R-HSA-446388; Regulation of cytoskeletal remodeling and cell spreading by IPP complex components.
DR SignaLink; Q15404; -.
DR BioGRID-ORCS; 6251; 57 hits in 1074 CRISPR screens.
DR ChiTaRS; RSU1; human.
DR GeneWiki; RSU1; -.
DR GenomeRNAi; 6251; -.
DR Pharos; Q15404; Tbio.
DR PRO; PR:Q15404; -.
DR Proteomes; UP000005640; Chromosome 10.
DR RNAct; Q15404; protein.
DR Bgee; ENSG00000148484; Expressed in popliteal artery and 208 other tissues.
DR Genevisible; Q15404; HS.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005925; C:focal adhesion; IDA:UniProtKB.
DR GO; GO:0010811; P:positive regulation of cell-substrate adhesion; IMP:UniProtKB.
DR GO; GO:0043547; P:positive regulation of GTPase activity; IMP:UniProtKB.
DR GO; GO:0007165; P:signal transduction; IBA:GO_Central.
DR Gene3D; 3.80.10.10; -; 2.
DR InterPro; IPR001611; Leu-rich_rpt.
DR InterPro; IPR003591; Leu-rich_rpt_typical-subtyp.
DR InterPro; IPR032675; LRR_dom_sf.
DR Pfam; PF13855; LRR_8; 2.
DR SMART; SM00369; LRR_TYP; 7.
DR PROSITE; PS51450; LRR; 7.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Direct protein sequencing;
KW Leucine-rich repeat; Reference proteome; Repeat.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22814378"
FT CHAIN 2..277
FT /note="Ras suppressor protein 1"
FT /id="PRO_0000097499"
FT REPEAT 41..63
FT /note="LRR 1"
FT REPEAT 64..85
FT /note="LRR 2"
FT REPEAT 87..109
FT /note="LRR 3"
FT REPEAT 110..133
FT /note="LRR 4"
FT REPEAT 135..156
FT /note="LRR 5"
FT REPEAT 158..179
FT /note="LRR 6"
FT REPEAT 181..202
FT /note="LRR 7"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 250..277
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..21
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 255..269
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0007744|PubMed:22814378"
FT VAR_SEQ 1..53
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_043831"
FT HELIX 5..14
FT /evidence="ECO:0007829|PDB:7D2S"
FT STRAND 18..21
FT /evidence="ECO:0007829|PDB:7D2S"
FT HELIX 30..32
FT /evidence="ECO:0007829|PDB:7D2S"
FT HELIX 36..38
FT /evidence="ECO:0007829|PDB:7D2S"
FT STRAND 43..46
FT /evidence="ECO:0007829|PDB:7D2S"
FT HELIX 57..61
FT /evidence="ECO:0007829|PDB:7D2S"
FT STRAND 66..69
FT /evidence="ECO:0007829|PDB:7D2S"
FT HELIX 80..84
FT /evidence="ECO:0007829|PDB:7D2S"
FT STRAND 90..92
FT /evidence="ECO:0007829|PDB:7D2S"
FT HELIX 105..107
FT /evidence="ECO:0007829|PDB:7D2S"
FT STRAND 113..115
FT /evidence="ECO:0007829|PDB:7D2S"
FT STRAND 118..120
FT /evidence="ECO:0007829|PDB:7LT9"
FT HELIX 123..125
FT /evidence="ECO:0007829|PDB:7D2S"
FT HELIX 130..132
FT /evidence="ECO:0007829|PDB:7D2S"
FT STRAND 137..140
FT /evidence="ECO:0007829|PDB:7D2S"
FT HELIX 151..155
FT /evidence="ECO:0007829|PDB:7D2S"
FT STRAND 161..163
FT /evidence="ECO:0007829|PDB:7D2S"
FT HELIX 174..178
FT /evidence="ECO:0007829|PDB:7D2S"
FT STRAND 184..186
FT /evidence="ECO:0007829|PDB:7D2S"
FT HELIX 197..199
FT /evidence="ECO:0007829|PDB:7D2S"
FT STRAND 206..212
FT /evidence="ECO:0007829|PDB:7LT8"
FT HELIX 220..228
FT /evidence="ECO:0007829|PDB:7LT8"
FT HELIX 230..238
FT /evidence="ECO:0007829|PDB:7LT8"
FT HELIX 240..250
FT /evidence="ECO:0007829|PDB:7LT8"
SQ SEQUENCE 277 AA; 31540 MW; 6EDB2E033F417468 CRC64;
MSKSLKKLVE ESREKNQPEV DMSDRGISNM LDVNGLFTLS HITQLVLSHN KLTMVPPNIA
ELKNLEVLNF FNNQIEELPT QISSLQKLKH LNLGMNRLNT LPRGFGSLPA LEVLDLTYNN
LSENSLPGNF FYLTTLRALY LSDNDFEILP PDIGKLTKLQ ILSLRDNDLI SLPKEIGELT
QLKELHIQGN RLTVLPPELG NLDLTGQKQV FKAENNPWVT PIADQFQLGV SHVFEYIRSE
TYKYLYGRHM QANPEPPKKN NDKSKKISRK PLAAKNR
