SYDE1_HUMAN
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 03-AUG-2022, entry version 151.
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; 103.
DR IntAct; Q6ZW31; 45.
DR STRING; 9606.ENSP00000341489; -.
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; Q6ZW31; -.
DR PeptideAtlas; Q6ZW31; -.
DR PRIDE; Q6ZW31; -.
DR ProteomicsDB; 68453; -. [Q6ZW31-1]
DR ProteomicsDB; 68454; -. [Q6ZW31-2]
DR Antibodypedia; 2829; 107 antibodies from 18 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 CTD; 85360; -.
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; 1300981at2759; -.
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; 11 hits in 1064 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 186 other tissues.
DR ExpressionAtlas; Q6ZW31; baseline and differential.
DR Genevisible; Q6ZW31; HS.
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:0031532; P:actin cytoskeleton reorganization; 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; -; 1.
DR InterPro; IPR000008; C2_dom.
DR InterPro; IPR008936; Rho_GTPase_activation_prot.
DR InterPro; IPR000198; RhoGAP_dom.
DR Pfam; PF00620; RhoGAP; 1.
DR SMART; SM00324; RhoGAP; 1.
DR SUPFAM; SSF48350; SSF48350; 1.
DR PROSITE; PS50004; C2; 1.
DR PROSITE; PS50238; RHOGAP; 1.
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
