ID RAB1A_MOUSE Reviewed; 205 AA. AC P62821; P11476; Q3TX44; Q811M4; Q96N61; Q9Y3T2; DT 16-AUG-2004, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 3. DT 02-SEP-2026, entry version 181. DE RecName: Full=Ras-related protein Rab-1A {ECO:0000305}; DE EC=3.6.5.2 {ECO:0000250|UniProtKB:P62820}; DE AltName: Full=YPT1-related protein; GN Name=Rab1a {ECO:0000312|MGI:MGI:97842}; GN Synonyms=Rab1 {ECO:0000312|MGI:MGI:97842}; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; OC Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RX PubMed=3127202; DOI=10.1002/j.1460-2075.1987.tb02750.x; RA Haubruck H., Disela C., Wagner P., Gallwitz D.; RT "The ras-related ypt protein is an ubiquitous eukaryotic protein: isolation RT and sequence analysis of mouse cDNA clones highly homologous to the yeast RT YPT1 gene."; RL EMBO J. 6:4049-4053(1987). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=2506528; DOI=10.1093/nar/17.16.6737; RA Wichmann H., Disela C., Haubruck H., Gallwitz D.; RT "Nucleotide sequence of the mouse ypt1 gene encoding a ras-related GTP- RT binding protein."; RL Nucleic Acids Res. 17:6737-6738(1989). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA]. RA Wu G., Dorn G.W. II; RT "Mouse Rab1A, member of RAS oncogene family mRNA."; RL Submitted (JAN-2000) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6J; TISSUE=Diencephalon, and Mammary gland; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J., RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=FVB/N; TISSUE=Mammary tumor; 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 [6] RP PROTEIN SEQUENCE OF 14-24; 31-49; 62-72; 75-103; 112-125 AND 132-156, AND RP IDENTIFICATION BY MASS SPECTROMETRY. RC STRAIN=C57BL/6J; TISSUE=Brain; RA Lubec G., Kang S.U.; RL Submitted (APR-2007) to UniProtKB. RN [7] RP REVIEW. RX PubMed=19603039; DOI=10.1038/nrm2728; RA Stenmark H.; RT "Rab GTPases as coordinators of vesicle traffic."; RL Nat. Rev. Mol. Cell Biol. 10:513-525(2009). RN [8] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, RC Pancreas, Spleen, and Testis; RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001; RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R., RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.; RT "A tissue-specific atlas of mouse protein phosphorylation and expression."; RL Cell 143:1174-1189(2010). RN [9] RP FUNCTION. RX PubMed=20639577; DOI=10.1074/jbc.m110.141440; RA Wang C., Yoo Y., Fan H., Kim E., Guan K.L., Guan J.L.; RT "Regulation of integrin beta 1 recycling to lipid rafts by Rab1a to promote RT cell migration."; RL J. Biol. Chem. 285:29398-29405(2010). RN [10] RP FUNCTION, AND SUBCELLULAR LOCATION. RX PubMed=22854043; DOI=10.1242/jcs.109314; RA Ishida M., Ohbayashi N., Maruta Y., Ebata Y., Fukuda M.; RT "Functional involvement of Rab1A in microtubule-dependent anterograde RT melanosome transport in melanocytes."; RL J. Cell Sci. 125:5177-5187(2012). RN [11] RP INTERACTION WITH C9ORF72. RX PubMed=24549040; DOI=10.1093/hmg/ddu068; RA Farg M.A., Sundaramoorthy V., Sultana J.M., Yang S., Atkinson R.A., RA Levina V., Halloran M.A., Gleeson P.A., Blair I.P., Soo K.Y., King A.E., RA Atkin J.D.; RT "C9ORF72, implicated in amytrophic lateral sclerosis and frontotemporal RT dementia, regulates endosomal trafficking."; RL Hum. Mol. Genet. 23:3579-3595(2014). CC -!- FUNCTION: The small GTPases Rab are key regulators of intracellular CC membrane trafficking, from the formation of transport vesicles to their CC fusion with membranes (PubMed:20639577, PubMed:22854043). Rabs cycle CC between an inactive GDP-bound form and an active GTP-bound form that is CC able to recruit to membranes different sets of downstream effectors CC directly responsible for vesicle formation, movement, tethering and CC fusion (PubMed:20639577, PubMed:22854043). RAB1A regulates vesicular CC protein transport from the endoplasmic reticulum (ER) to the Golgi CC compartment and on to the cell surface, and plays a role in IL-8 and CC growth hormone secretion (By similarity). Required to modulate the CC compacted morphology of the Golgi. Regulates the level of CASR present CC at the cell membrane (By similarity). Plays a role in cell adhesion and CC cell migration, via its role in protein trafficking (PubMed:20639577). CC Plays a role in autophagosome assembly and cellular defense reactions CC against pathogenic bacteria (By similarity). Plays a role in CC microtubule-dependent protein transport by early endosomes and in CC anterograde melanosome transport (PubMed:22854043). CC {ECO:0000250|UniProtKB:P62820, ECO:0000269|PubMed:20639577, CC ECO:0000269|PubMed:22854043}. CC -!- CATALYTIC ACTIVITY: CC Reaction=GTP + H2O = GDP + phosphate + H(+); Xref=Rhea:RHEA:19669, CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:37565, CC ChEBI:CHEBI:43474, ChEBI:CHEBI:58189; EC=3.6.5.2; CC Evidence={ECO:0000250|UniProtKB:P62820}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19670; CC Evidence={ECO:0000250|UniProtKB:P62820}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000250|UniProtKB:P62820}; CC -!- ACTIVITY REGULATION: Regulated by guanine nucleotide exchange factors CC (GEFs) which promote the exchange of bound GDP for free GTP. Regulated CC by GTPase activating proteins (GAPs) which increase the GTP hydrolysis CC activity. Inhibited by GDP dissociation inhibitors (GDIs). CC {ECO:0000250|UniProtKB:P62820}. CC -!- SUBUNIT: May interact with YIPF5 (By similarity). Interacts with CC C9orf72; the interaction mediates recruitment of RAB1A to the ATG1/ULK1 CC kinase complex (PubMed:24549040). Interacts with GDI1; this promotes CC dissociation from membranes (By similarity). CC {ECO:0000250|UniProtKB:P62820, ECO:0000250|UniProtKB:P62822, CC ECO:0000269|PubMed:24549040}. CC -!- SUBCELLULAR LOCATION: Golgi apparatus {ECO:0000250|UniProtKB:P62820}. CC Endoplasmic reticulum {ECO:0000250|UniProtKB:P62820}. Early endosome CC {ECO:0000250|UniProtKB:P62820}. Cytoplasm, cytosol CC {ECO:0000250|UniProtKB:P62820}. Membrane CC {ECO:0000250|UniProtKB:P62820}. Melanosome CC {ECO:0000269|PubMed:22854043}. Note=Alternates between membrane- CC associated and cytosolic forms. {ECO:0000250|UniProtKB:P62820}. CC -!- DOMAIN: Switch I, switch II and the interswitch regions are CC characteristic of Rab GTPases and mediate the interactions with Rab CC downstream effectors. The switch regions undergo conformational changes CC upon nucleotide binding which drive interaction with specific sets of CC effector proteins, with most effectors only binding to GTP-bound Rab. CC {ECO:0000250|UniProtKB:P62820}. CC -!- PTM: Phosphorylated by CDK1 kinase during mitosis. CC {ECO:0000250|UniProtKB:P62820}. CC -!- PTM: Ubiquitinated via 'Lys-11'-linked ubiquitination on Lys-49 and CC Lys-61; impairing the recruitment of guanosine diphosphate (GDP) CC dissociation inhibitor 1/GDI1. {ECO:0000250|UniProtKB:P51153}. CC -!- SIMILARITY: Belongs to the small GTPase superfamily. Rab family. CC {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; Y00094; CAA68284.1; -; mRNA. DR EMBL; X15744; CAA33760.1; -; Genomic_DNA. DR EMBL; X15745; CAA33760.1; JOINED; Genomic_DNA. DR EMBL; X15746; CAA33760.1; JOINED; Genomic_DNA. DR EMBL; X15747; CAA33760.1; JOINED; Genomic_DNA. DR EMBL; AF226873; AAF33844.1; -; mRNA. DR EMBL; AK034408; BAC28697.1; -; mRNA. DR EMBL; AK159425; BAE35072.1; -; mRNA. DR EMBL; AK166249; BAE38660.1; -; mRNA. DR EMBL; AK167150; BAE39292.1; -; mRNA. DR EMBL; BC002077; AAH02077.3; -; mRNA. DR CCDS; CCDS36115.1; -. DR PIR; S05551; TVMSYP. DR RefSeq; NP_033022.1; NM_008996.4. DR AlphaFoldDB; P62821; -. DR SMR; P62821; -. DR BioGRID; 202530; 33. DR FunCoup; P62821; 3651. DR IntAct; P62821; 38. DR STRING; 10090.ENSMUSP00000127330; -. DR GlyGen; P62821; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; P62821; -. DR MetOSite; P62821; -. DR PhosphoSitePlus; P62821; -. DR SwissPalm; P62821; -. DR jPOST; P62821; -. DR PaxDb; 10090-ENSMUSP00000127330; -. DR PeptideAtlas; P62821; -. DR ProteomicsDB; 300373; -. DR Pumba; P62821; -. DR Antibodypedia; 3942; 211 antibodies from 32 providers. DR DNASU; 19324; -. DR Ensembl; ENSMUST00000163483.2; ENSMUSP00000127330.2; ENSMUSG00000020149.18. DR GeneID; 19324; -. DR KEGG; mmu:19324; -. DR UCSC; uc007icv.1; mouse. DR AGR; MGI:97842; -. DR CTD; 5861; -. DR MGI; MGI:97842; Rab1a. DR VEuPathDB; HostDB:ENSMUSG00000020149; -. DR eggNOG; KOG0084; Eukaryota. DR GeneTree; ENSGT00940000154958; -. DR HOGENOM; CLU_041217_23_1_1; -. DR InParanoid; P62821; -. DR OMA; TQMAKDF; -. DR OrthoDB; 9989112at2759; -. DR PhylomeDB; P62821; -. DR Reactome; R-MMU-162658; Golgi Cisternae Pericentriolar Stack Reorganization. DR Reactome; R-MMU-204005; COPII-mediated vesicle transport. DR Reactome; R-MMU-6807878; COPI-mediated anterograde transport. DR Reactome; R-MMU-6811434; COPI-dependent Golgi-to-ER retrograde traffic. DR Reactome; R-MMU-8873719; RAB geranylgeranylation. DR Reactome; R-MMU-8876198; RAB GEFs exchange GTP for GDP on RABs. DR BioGRID-ORCS; 19324; 6 hits in 44 CRISPR screens. DR CD-CODE; CE726F99; Postsynaptic density. DR PRO; PR:P62821; -. DR Proteomes; UP000000589; Chromosome 11. DR RNAct; P62821; protein. DR Bgee; ENSMUSG00000020149; Expressed in vault of skull and 259 other cell types or tissues. DR ExpressionAtlas; P62821; baseline and differential. DR GO; GO:0005829; C:cytosol; ISO:GO_Central. DR GO; GO:0005769; C:early endosome; ISS:UniProtKB. DR GO; GO:0005783; C:endoplasmic reticulum; ISS:UniProtKB. DR GO; GO:0005789; C:endoplasmic reticulum membrane; ISO:GO_Central. DR GO; GO:0005794; C:Golgi apparatus; IDA:MGI. DR GO; GO:0000139; C:Golgi membrane; ISO:GO_Central. DR GO; GO:0042470; C:melanosome; IDA:UniProtKB. DR GO; GO:0016020; C:membrane; ISS:UniProtKB. DR GO; GO:0043025; C:neuronal cell body; ISO:GO_Central. DR GO; GO:0098793; C:presynapse; ISO:GO_Central. DR GO; GO:0045202; C:synapse; ISO:GO_Central. DR GO; GO:0003925; F:G protein activity; ISS:UniProtKB. DR GO; GO:0005525; F:GTP binding; ISO:GO_Central. DR GO; GO:0003924; F:GTPase activity; ISS:UniProtKB. DR GO; GO:0001675; P:acrosome assembly; ISS:UniProtKB. DR GO; GO:0000045; P:autophagosome assembly; ISS:UniProtKB. DR GO; GO:0006914; P:autophagy; ISS:UniProtKB. DR GO; GO:0016477; P:cell migration; IMP:UniProtKB. DR GO; GO:0090110; P:COPII-coated vesicle cargo loading; ISO:GO_Central. DR GO; GO:0042742; P:defense response to bacterium; ISS:UniProtKB. DR GO; GO:0006897; P:endocytosis; ISS:UniProtKB. DR GO; GO:0006888; P:endoplasmic reticulum to Golgi vesicle-mediated transport; ISS:UniProtKB. DR GO; GO:0007030; P:Golgi organization; ISS:UniProtKB. DR GO; GO:0030252; P:growth hormone secretion; ISS:UniProtKB. DR GO; GO:0006886; P:intracellular protein transport; TAS:MGI. DR GO; GO:0032402; P:melanosome transport; IMP:UniProtKB. DR GO; GO:1903020; P:positive regulation of glycoprotein metabolic process; ISO:GO_Central. DR GO; GO:0032757; P:positive regulation of interleukin-8 production; ISS:UniProtKB. DR GO; GO:0034446; P:substrate adhesion-dependent cell spreading; IMP:UniProtKB. DR GO; GO:0047496; P:vesicle transport along microtubule; ISS:UniProtKB. DR GO; GO:0019068; P:virion assembly; ISO:GO_Central. DR CDD; cd01869; Rab1_Ypt1; 1. DR FunFam; 3.40.50.300:FF:000069; Ras GTP-binding protein YPT1; 1. DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR050227; Rab. DR InterPro; IPR057289; Rab1/Ypt1. DR InterPro; IPR005225; Small_GTP-bd. DR InterPro; IPR001806; Small_GTPase. DR NCBIfam; TIGR00231; small_GTP; 1. DR PANTHER; PTHR47977; RAS-RELATED PROTEIN RAB; 1. DR Pfam; PF00071; Ras; 1. DR PRINTS; PR00449; RASTRNSFRMNG. DR SMART; SM00177; ARF; 1. DR SMART; SM00175; RAB; 1. DR SMART; SM00176; RAN; 1. DR SMART; SM00173; RAS; 1. DR SMART; SM00174; RHO; 1. DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1. DR PROSITE; PS51419; RAB; 1. PE 1: Evidence at protein level; KW Acetylation; Autophagy; Cytoplasm; Direct protein sequencing; KW Endoplasmic reticulum; Endosome; ER-Golgi transport; Golgi apparatus; KW GTP-binding; Hydrolase; Isopeptide bond; Lipoprotein; Magnesium; Membrane; KW Metal-binding; Nucleotide-binding; Phosphoprotein; Prenylation; KW Protein transport; Reference proteome; Transport; Ubl conjugation. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0000250|UniProtKB:P62820" FT CHAIN 2..205 FT /note="Ras-related protein Rab-1A" FT /id="PRO_0000121057" FT REGION 38..46 FT /note="Switch-I" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00753" FT REGION 69..85 FT /note="Switch-II" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00753" FT REGION 178..205 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOTIF 34..48 FT /note="Switch 1" FT /evidence="ECO:0000250|UniProtKB:P62820" FT MOTIF 66..83 FT /note="Switch 2" FT /evidence="ECO:0000250|UniProtKB:P62820" FT BINDING 20 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000250|UniProtKB:P62820" FT BINDING 21 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000250|UniProtKB:P62820" FT BINDING 23 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000250|UniProtKB:P62820" FT BINDING 24 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000250|UniProtKB:P62820" FT BINDING 25 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000250|UniProtKB:P62820" FT BINDING 25 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000250|UniProtKB:P62820" FT BINDING 26 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000250|UniProtKB:P62820" FT BINDING 38 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000250|UniProtKB:P62820" FT BINDING 43 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000250|UniProtKB:P62820" FT BINDING 43 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000250|UniProtKB:P62820" FT BINDING 66 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000250|UniProtKB:P62820" FT BINDING 69 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000250|UniProtKB:P62820" FT BINDING 124 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000250|UniProtKB:P62820" FT BINDING 125 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000250|UniProtKB:P62820" FT BINDING 127 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000250|UniProtKB:P62820" FT BINDING 155 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000250|UniProtKB:P62820" FT BINDING 156 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000250|UniProtKB:P62820" FT MOD_RES 2 FT /note="N-acetylserine" FT /evidence="ECO:0000250|UniProtKB:P62820" FT MOD_RES 194 FT /note="Phosphoserine; by CDK1" FT /evidence="ECO:0000250|UniProtKB:P62820" FT LIPID 204 FT /note="S-geranylgeranyl cysteine" FT /evidence="ECO:0000250|UniProtKB:P62820" FT LIPID 205 FT /note="S-geranylgeranyl cysteine" FT /evidence="ECO:0000250|UniProtKB:P62820" FT CROSSLNK 49 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in ubiquitin)" FT /evidence="ECO:0000250|UniProtKB:P51153" FT CROSSLNK 61 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in ubiquitin)" FT /evidence="ECO:0000250|UniProtKB:P51153" SQ SEQUENCE 205 AA; 22678 MW; B2A8F4E3B0FB17D6 CRC64; MSSMNPEYDY LFKLLLIGDS GVGKSCLLLR FADDTYTESY ISTIGVDFKI RTIELDGKTI KLQIWDTAGQ ERFRTITSSY YRGAHGIIVV YDVTDQESFN NVKQWLQEID RYASENVNKL LVGNKCDLTT KKVVDYTTAK EFADSLGIPF LETSAKNATN VEQSFMTMAA EIKKRMGPGA TAGGAEKSNV KIQSTPVKQS GGGCC //