ID   SYDE1_HUMAN             Reviewed;         735 AA.
AC   Q6ZW31; Q7L2I8; Q8N6J2; Q9H8K4;
DT   04-DEC-2007, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   27-MAR-2024, entry version 159.
DE   RecName: Full=Rho GTPase-activating protein SYDE1;
DE   AltName: Full=Synapse defective protein 1 homolog 1;
DE            Short=Protein syd-1 homolog 1;
GN   Name=SYDE1;
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 [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Placenta;
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   [2]
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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   TISSUE=Cervix, and Muscle;
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   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-231; SER-235; SER-244 AND
RP   SER-683, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA   Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA   Elledge S.J., Gygi S.P.;
RT   "A quantitative atlas of mitotic phosphorylation.";
RL   Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-224 AND SER-575, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=23186163; DOI=10.1021/pr300630k;
RA   Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA   Mohammed S.;
RT   "Toward a comprehensive characterization of a human cancer cell
RT   phosphoproteome.";
RL   J. Proteome Res. 12:260-271(2013).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-683, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA   Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA   Ye M., Zou H.;
RT   "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT   phosphoproteome.";
RL   J. Proteomics 96:253-262(2014).
RN   [7]
RP   FUNCTION, AND TISSUE SPECIFICITY.
RX   PubMed=27917469; DOI=10.1002/path.4835;
RA   Lo H.F., Tsai C.Y., Chen C.P., Wang L.J., Lee Y.S., Chen C.Y., Liang C.T.,
RA   Cheong M.L., Chen H.;
RT   "Association of dysfunctional synapse defective 1 (SYDE1) with restricted
RT   fetal growth - SYDE1 regulates placental cell migration and invasion.";
RL   J. Pathol. 241:324-336(2017).
RN   [8]
RP   VARIANT [LARGE SCALE ANALYSIS] GLN-408.
RX   PubMed=18772397; DOI=10.1126/science.1164368;
RA   Jones S., Zhang X., Parsons D.W., Lin J.C., Leary R.J., Angenendt P.,
RA   Mankoo P., Carter H., Kamiyama H., Jimeno A., Hong S.M., Fu B., Lin M.T.,
RA   Calhoun E.S., Kamiyama M., Walter K., Nikolskaya T., Nikolsky Y.,
RA   Hartigan J., Smith D.R., Hidalgo M., Leach S.D., Klein A.P., Jaffee E.M.,
RA   Goggins M., Maitra A., Iacobuzio-Donahue C., Eshleman J.R., Kern S.E.,
RA   Hruban R.H., Karchin R., Papadopoulos N., Parmigiani G., Vogelstein B.,
RA   Velculescu V.E., Kinzler K.W.;
RT   "Core signaling pathways in human pancreatic cancers revealed by global
RT   genomic analyses.";
RL   Science 321:1801-1806(2008).
CC   -!- FUNCTION: GTPase activator for the Rho-type GTPases. As a GCM1
CC       downstream effector, it is involved in placental development and
CC       positively regulates trophoblast cells migration. It regulates
CC       cytoskeletal remodeling by controlling the activity of Rho GTPases
CC       including RHOA, CDC42 and RAC1 (PubMed:27917469).
CC       {ECO:0000269|PubMed:27917469}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q6ZW31-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q6ZW31-2; Sequence=VSP_029717;
CC   -!- TISSUE SPECIFICITY: Expressed in trophoblast cells of placental villi.
CC       {ECO:0000269|PubMed:27917469}.
CC   -!- PTM: Palmitoylated. Probably palmitoylated by ZDHHC3 and ZDHHC7.
CC       {ECO:0000250|UniProtKB:D3ZZN9}.
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DR   EMBL; AK023573; BAB14612.1; -; mRNA.
DR   EMBL; AK123686; BAC85676.1; -; mRNA.
DR   EMBL; CH471106; EAW84462.1; -; Genomic_DNA.
DR   EMBL; CH471106; EAW84463.1; -; Genomic_DNA.
DR   EMBL; BC018942; AAH18942.2; -; mRNA.
DR   EMBL; BC029926; AAH29926.1; -; mRNA.
DR   CCDS; CCDS12324.1; -. [Q6ZW31-1]
DR   CCDS; CCDS74299.1; -. [Q6ZW31-2]
DR   RefSeq; NP_001287839.1; NM_001300910.1. [Q6ZW31-2]
DR   RefSeq; NP_149014.3; NM_033025.5. [Q6ZW31-1]
DR   AlphaFoldDB; Q6ZW31; -.
DR   SMR; Q6ZW31; -.
DR   BioGRID; 124489; 113.
DR   IntAct; Q6ZW31; 50.
DR   STRING; 9606.ENSP00000341489; -.
DR   GlyGen; Q6ZW31; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; Q6ZW31; -.
DR   PhosphoSitePlus; Q6ZW31; -.
DR   BioMuta; SYDE1; -.
DR   DMDM; 74723056; -.
DR   EPD; Q6ZW31; -.
DR   jPOST; Q6ZW31; -.
DR   MassIVE; Q6ZW31; -.
DR   MaxQB; Q6ZW31; -.
DR   PaxDb; 9606-ENSP00000341489; -.
DR   PeptideAtlas; Q6ZW31; -.
DR   ProteomicsDB; 68453; -. [Q6ZW31-1]
DR   ProteomicsDB; 68454; -. [Q6ZW31-2]
DR   Pumba; Q6ZW31; -.
DR   Antibodypedia; 2829; 117 antibodies from 19 providers.
DR   DNASU; 85360; -.
DR   Ensembl; ENST00000342784.7; ENSP00000341489.1; ENSG00000105137.13. [Q6ZW31-1]
DR   Ensembl; ENST00000600440.5; ENSP00000470733.1; ENSG00000105137.13. [Q6ZW31-2]
DR   GeneID; 85360; -.
DR   KEGG; hsa:85360; -.
DR   MANE-Select; ENST00000342784.7; ENSP00000341489.1; NM_033025.6; NP_149014.3.
DR   UCSC; uc002nah.2; human. [Q6ZW31-1]
DR   AGR; HGNC:25824; -.
DR   DisGeNET; 85360; -.
DR   GeneCards; SYDE1; -.
DR   HGNC; HGNC:25824; SYDE1.
DR   HPA; ENSG00000105137; Low tissue specificity.
DR   MIM; 617377; gene.
DR   neXtProt; NX_Q6ZW31; -.
DR   OpenTargets; ENSG00000105137; -.
DR   PharmGKB; PA142670851; -.
DR   VEuPathDB; HostDB:ENSG00000105137; -.
DR   eggNOG; KOG1452; Eukaryota.
DR   GeneTree; ENSGT01030000234635; -.
DR   HOGENOM; CLU_005764_1_1_1; -.
DR   InParanoid; Q6ZW31; -.
DR   OMA; FLQLDHT; -.
DR   OrthoDB; 2905108at2759; -.
DR   PhylomeDB; Q6ZW31; -.
DR   TreeFam; TF323458; -.
DR   PathwayCommons; Q6ZW31; -.
DR   Reactome; R-HSA-9013148; CDC42 GTPase cycle.
DR   Reactome; R-HSA-9013404; RAC2 GTPase cycle.
DR   Reactome; R-HSA-9013406; RHOQ GTPase cycle.
DR   Reactome; R-HSA-9013409; RHOJ GTPase cycle.
DR   Reactome; R-HSA-9013423; RAC3 GTPase cycle.
DR   Reactome; R-HSA-9035034; RHOF GTPase cycle.
DR   SignaLink; Q6ZW31; -.
DR   BioGRID-ORCS; 85360; 13 hits in 1142 CRISPR screens.
DR   ChiTaRS; SYDE1; human.
DR   GenomeRNAi; 85360; -.
DR   Pharos; Q6ZW31; Tbio.
DR   PRO; PR:Q6ZW31; -.
DR   Proteomes; UP000005640; Chromosome 19.
DR   RNAct; Q6ZW31; Protein.
DR   Bgee; ENSG00000105137; Expressed in decidua and 187 other cell types or tissues.
DR   ExpressionAtlas; Q6ZW31; baseline and differential.
DR   GO; GO:0097060; C:synaptic membrane; IBA:GO_Central.
DR   GO; GO:0005096; F:GTPase activator activity; IDA:MGI.
DR   GO; GO:0030695; F:GTPase regulator activity; IDA:MGI.
DR   GO; GO:0030036; P:actin cytoskeleton organization; IDA:MGI.
DR   GO; GO:0090630; P:activation of GTPase activity; ISS:UniProtKB.
DR   GO; GO:0016477; P:cell migration; IDA:MGI.
DR   GO; GO:1901165; P:positive regulation of trophoblast cell migration; IMP:UniProtKB.
DR   GO; GO:0051493; P:regulation of cytoskeleton organization; IMP:UniProtKB.
DR   GO; GO:0046578; P:regulation of Ras protein signal transduction; IBA:GO_Central.
DR   GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR   Gene3D; 1.10.555.10; Rho GTPase activation protein; 1.
DR   InterPro; IPR000008; C2_dom.
DR   InterPro; IPR008936; Rho_GTPase_activation_prot.
DR   InterPro; IPR000198; RhoGAP_dom.
DR   PANTHER; PTHR46150; RHO GTPASE-ACTIVATING PROTEIN 100F; 1.
DR   PANTHER; PTHR46150:SF2; RHO GTPASE-ACTIVATING PROTEIN SYDE1; 1.
DR   Pfam; PF00620; RhoGAP; 1.
DR   SMART; SM00324; RhoGAP; 1.
DR   SUPFAM; SSF48350; GTPase activation domain, GAP; 1.
DR   PROSITE; PS50004; C2; 1.
DR   PROSITE; PS50238; RHOGAP; 1.
DR   Genevisible; Q6ZW31; HS.
PE   1: Evidence at protein level;
KW   Alternative splicing; GTPase activation; Lipoprotein; Palmitate;
KW   Phosphoprotein; Reference proteome.
FT   CHAIN           1..735
FT                   /note="Rho GTPase-activating protein SYDE1"
FT                   /id="PRO_0000312158"
FT   DOMAIN          249..366
FT                   /note="C2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT   DOMAIN          398..604
FT                   /note="Rho-GAP"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00172"
FT   REGION          1..253
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          608..651
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          674..696
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        9..35
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        116..132
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        168..193
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        680..695
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         224
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   MOD_RES         231
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18669648"
FT   MOD_RES         235
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18669648"
FT   MOD_RES         244
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18669648"
FT   MOD_RES         575
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   MOD_RES         681
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9DBZ9"
FT   MOD_RES         683
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18669648,
FT                   ECO:0007744|PubMed:24275569"
FT   VAR_SEQ         30..96
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_029717"
FT   VARIANT         408
FT                   /note="R -> Q (in a pancreatic ductal adenocarcinoma
FT                   sample; somatic mutation; dbSNP:rs772906202)"
FT                   /evidence="ECO:0000269|PubMed:18772397"
FT                   /id="VAR_062661"
SQ   SEQUENCE   735 AA;  79793 MW;  87310623E756EB31 CRC64;
     MAEPLLRKTF SRLRGREKLP RKKSDAKERG HPAQRPEPSP PEPEPQAPEG SQAGAEGPSS
     PEASRSPARG AYLQSLEPSS RRWVLGGAKP AEDTSLGPGV PGTGEPAGEI WYNPIPEEDP
     RPPAPEPPGP QPGSAESEGL APQGAAPASP PTKASRTKSP GPARRLSIKM KKLPELRRRL
     SLRGPRAGRE RERAAPAGSV ISRYHLDSSV GGPGPAAGPG GTRSPRAGYL SDGDSPERPA
     GPPSPTSFRP YEVGPAARAP PAALWGRLSL HLYGLGGLRP APGATPRDLC CLLQVDGEAR
     ARTGPLRGGP DFLRLDHTFH LELEAARLLR ALVLAWDPGV RRHRPCAQGT VLLPTVFRGC
     QAQQLAVRLE PQGLLYAKLT LSEQQEAPAT AEPRVFGLPL PLLVERERPP GQVPLIIQKC
     VGQIERRGLR VVGLYRLCGS AAVKKELRDA FERDSAAVCL SEDLYPDINV ITGILKDYLR
     ELPTPLITQP LYKVVLEAMA RDPPNRVPPT TEGTRGLLSC LPDVERATLT LLLDHLRLVS
     SFHAYNRMTP QNLAVCFGPV LLPARQAPTR PRARSSGPGL ASAVDFKHHI EVLHYLLQSW
     PDPRLPRQSP DVAPYLRPKR QPPLHLPLAD PEVVTRPRGR GGPESPPSNR YAGDWSVCGR
     DFLPCGRDFL SGPDYDHVTG SDSEDEDEEV GEPRVTGDFE DDFDAPFNPH LNLKDFDALI
     LDLERELSKQ INVCL
//