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C42S2_HUMAN
ID   C42S2_HUMAN             Reviewed;          84 AA.
AC   Q9NRR3; B2R622; Q4KMT9;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 150.
DE   RecName: Full=CDC42 small effector protein 2;
DE   AltName: Full=Small effector of CDC42 protein 2;
GN   Name=CDC42SE2; Synonyms=SPEC2;
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], FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION
RP   WITH CDC42.
RX   PubMed=10816584; DOI=10.1074/jbc.m002832200;
RA   Pirone D.M., Fukuhara S., Gutkind J.S., Burbelo P.D.;
RT   "SPECs, small binding proteins for Cdc42.";
RL   J. Biol. Chem. 275:22650-22656(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain;
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 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   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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   [5]
RP   FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND PALMITOYLATION AT
RP   CYS-10 AND CYS-11.
RX   PubMed=15840583; DOI=10.1074/jbc.m500128200;
RA   Ching K.H., Kisailus A.E., Burbelo P.D.;
RT   "The role of SPECs, small Cdc42-binding proteins, in F-actin accumulation
RT   at the immunological synapse.";
RL   J. Biol. Chem. 280:23660-23667(2005).
RN   [6]
RP   SUBCELLULAR LOCATION.
RX   PubMed=17045588; DOI=10.1016/j.yexcr.2006.09.011;
RA   Ching K.H., Kisailus A.E., Burbelo P.D.;
RT   "Biochemical characterization of distinct regions of SPEC molecules and
RT   their role in phagocytosis.";
RL   Exp. Cell Res. 313:10-21(2007).
RN   [7]
RP   POSSIBLE SUSCEPTIBILITY TO SCHIZOPHRENIA.
RX   PubMed=17030554; DOI=10.1093/hmg/ddl409;
RA   Chen X., Wang X., Hossain S., O'Neill F.A., Walsh D., Pless L.,
RA   Chowdari K.V., Nimgaonkar V.L., Schwab S.G., Wildenauer D.B.,
RA   Sullivan P.F., van den Oord E., Kendler K.S.;
RT   "Haplotypes spanning SPEC2, PDZ-GEF2 and ACSL6 genes are associated with
RT   schizophrenia.";
RL   Hum. Mol. Genet. 15:3329-3342(2006).
CC   -!- FUNCTION: Probably involved in the organization of the actin
CC       cytoskeleton by acting downstream of CDC42, inducing actin filament
CC       assembly. Alters CDC42-induced cell shape changes. In activated T-
CC       cells, may play a role in CDC42-mediated F-actin accumulation at the
CC       immunological synapse. May play a role in early contractile events in
CC       phagocytosis in macrophages. {ECO:0000269|PubMed:10816584,
CC       ECO:0000269|PubMed:15840583}.
CC   -!- SUBUNIT: Interacts with CDC42 (in GTP-bound form). Interacts weakly
CC       with RAC1 and not at all with RHOA. {ECO:0000269|PubMed:10816584}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. Cell membrane; Lipid-
CC       anchor. Cell projection, phagocytic cup. Note=Recruited to the
CC       activated TCR prior actin polymerization. Localizes at the phagocytic
CC       cup of macrophages.
CC   -!- TISSUE SPECIFICITY: Widely expressed. Expressed at higher level in T-
CC       lymphocytes. Highly expressed in CCRF-CEM T-lymphocytes, Jurkat T-
CC       lymphocytes, and Raji B-lymphocytes compared (at protein level).
CC       {ECO:0000269|PubMed:15840583}.
CC   -!- DOMAIN: The CRIB domain mediates interaction with CDC42.
CC   -!- MISCELLANEOUS: CDC42SE2 is mapped in the genomic region associated with
CC       schizophrenia.
CC   -!- SIMILARITY: Belongs to the CDC42SE/SPEC family. {ECO:0000305}.
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DR   EMBL; AF189692; AAF87598.1; -; mRNA.
DR   EMBL; AK312406; BAG35319.1; -; mRNA.
DR   EMBL; CH471062; EAW62373.1; -; Genomic_DNA.
DR   EMBL; BC096703; AAH96703.1; -; mRNA.
DR   EMBL; BC096738; AAH96738.1; -; mRNA.
DR   EMBL; BC098349; AAH98349.1; -; mRNA.
DR   CCDS; CCDS34224.1; -.
DR   RefSeq; NP_001033791.1; NM_001038702.1.
DR   RefSeq; NP_064625.1; NM_020240.2.
DR   RefSeq; XP_016865137.1; XM_017009648.1.
DR   RefSeq; XP_016865138.1; XM_017009649.1.
DR   AlphaFoldDB; Q9NRR3; -.
DR   BioGRID; 121306; 49.
DR   IntAct; Q9NRR3; 4.
DR   STRING; 9606.ENSP00000427421; -.
DR   iPTMnet; Q9NRR3; -.
DR   PhosphoSitePlus; Q9NRR3; -.
DR   SwissPalm; Q9NRR3; -.
DR   BioMuta; CDC42SE2; -.
DR   DMDM; 74719133; -.
DR   EPD; Q9NRR3; -.
DR   jPOST; Q9NRR3; -.
DR   MassIVE; Q9NRR3; -.
DR   MaxQB; Q9NRR3; -.
DR   PaxDb; Q9NRR3; -.
DR   PeptideAtlas; Q9NRR3; -.
DR   PRIDE; Q9NRR3; -.
DR   ProteomicsDB; 82408; -.
DR   TopDownProteomics; Q9NRR3; -.
DR   Antibodypedia; 25863; 97 antibodies from 14 providers.
DR   DNASU; 56990; -.
DR   Ensembl; ENST00000360515.7; ENSP00000353706.3; ENSG00000158985.14.
DR   Ensembl; ENST00000395246.5; ENSP00000378667.1; ENSG00000158985.14.
DR   Ensembl; ENST00000505065.2; ENSP00000427421.1; ENSG00000158985.14.
DR   GeneID; 56990; -.
DR   KEGG; hsa:56990; -.
DR   MANE-Select; ENST00000505065.2; ENSP00000427421.1; NM_001375635.1; NP_001362564.1.
DR   UCSC; uc003kvh.4; human.
DR   CTD; 56990; -.
DR   DisGeNET; 56990; -.
DR   GeneCards; CDC42SE2; -.
DR   HGNC; HGNC:18547; CDC42SE2.
DR   HPA; ENSG00000158985; Low tissue specificity.
DR   MIM; 619457; gene.
DR   neXtProt; NX_Q9NRR3; -.
DR   OpenTargets; ENSG00000158985; -.
DR   PharmGKB; PA133787056; -.
DR   VEuPathDB; HostDB:ENSG00000158985; -.
DR   eggNOG; ENOG502S22R; Eukaryota.
DR   GeneTree; ENSGT00940000158245; -.
DR   HOGENOM; CLU_173417_1_0_1; -.
DR   InParanoid; Q9NRR3; -.
DR   OMA; IGVPTNF; -.
DR   OrthoDB; 1646014at2759; -.
DR   PhylomeDB; Q9NRR3; -.
DR   TreeFam; TF323815; -.
DR   PathwayCommons; Q9NRR3; -.
DR   Reactome; R-HSA-9013148; CDC42 GTPase cycle.
DR   SignaLink; Q9NRR3; -.
DR   BioGRID-ORCS; 56990; 10 hits in 1081 CRISPR screens.
DR   ChiTaRS; CDC42SE2; human.
DR   GenomeRNAi; 56990; -.
DR   Pharos; Q9NRR3; Tbio.
DR   PRO; PR:Q9NRR3; -.
DR   Proteomes; UP000005640; Chromosome 5.
DR   RNAct; Q9NRR3; protein.
DR   Bgee; ENSG00000158985; Expressed in ileal mucosa and 193 other tissues.
DR   ExpressionAtlas; Q9NRR3; baseline and differential.
DR   Genevisible; Q9NRR3; HS.
DR   GO; GO:0042995; C:cell projection; IEA:UniProtKB-KW.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR   GO; GO:0001891; C:phagocytic cup; IEA:UniProtKB-SubCell.
DR   GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR   GO; GO:0035591; F:signaling adaptor activity; IDA:UniProtKB.
DR   GO; GO:0031267; F:small GTPase binding; IEA:InterPro.
DR   GO; GO:0006909; P:phagocytosis; IEA:UniProtKB-KW.
DR   GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW.
DR   GO; GO:0035023; P:regulation of Rho protein signal transduction; IEA:InterPro.
DR   GO; GO:0009966; P:regulation of signal transduction; IDA:UniProtKB.
DR   Gene3D; 3.90.810.10; -; 1.
DR   InterPro; IPR000095; CRIB_dom.
DR   InterPro; IPR036936; CRIB_dom_sf.
DR   InterPro; IPR039056; SPEC.
DR   PANTHER; PTHR13502; PTHR13502; 1.
DR   Pfam; PF00786; PBD; 1.
DR   PROSITE; PS50108; CRIB; 1.
PE   1: Evidence at protein level;
KW   Cell membrane; Cell projection; Cell shape; Cytoplasm; Cytoskeleton;
KW   Lipoprotein; Membrane; Palmitate; Phagocytosis; Phosphoprotein;
KW   Reference proteome.
FT   CHAIN           1..84
FT                   /note="CDC42 small effector protein 2"
FT                   /id="PRO_0000334639"
FT   DOMAIN          29..42
FT                   /note="CRIB"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00057"
FT   MOD_RES         43
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8BGH7"
FT   MOD_RES         52
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8BGH7"
FT   LIPID           10
FT                   /note="S-palmitoyl cysteine"
FT                   /evidence="ECO:0000269|PubMed:15840583"
FT   LIPID           11
FT                   /note="S-palmitoyl cysteine"
FT                   /evidence="ECO:0000269|PubMed:15840583"
SQ   SEQUENCE   84 AA;  9223 MW;  98C5E82176DA990A CRC64;
     MSEFWLCFNC CIAEQPQPKR RRRIDRSMIG EPTNFVHTAH VGSGDLFSGM NSVSSIQNQM
     QSKGGYGGGM PANVQMQLVD TKAG
 
 
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