ID SYJ2B_HUMAN Reviewed; 145 AA. AC P57105; Q49SH3; Q96IA4; DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot. DT 13-AUG-2002, sequence version 2. DT 27-MAR-2024, entry version 187. DE RecName: Full=Synaptojanin-2-binding protein; DE AltName: Full=Mitochondrial outer membrane protein 25; GN Name=SYNJ2BP; Synonyms=OMP25 {ECO:0000303|PubMed:32973005}; 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]. RA Yang Y., Tai G.X., Xu G.Y., Zhang P.Y., Liu Z.H.; RT "Cloning of a novel protein interacting with activin receptor II A."; RL Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. 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 [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 (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Ovary; 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 INTERACTION WITH DLL1. RX PubMed=24025447; DOI=10.1161/circresaha.113.301686; RA Adam M.G., Berger C., Feldner A., Yang W.J., Wuestehube-Lausch J., RA Herberich S.E., Pinder M., Gesierich S., Hammes H.P., Augustin H.G., RA Fischer A.; RT "Synaptojanin-2 binding protein stabilizes the Notch ligands DLL1 and DLL4 RT and inhibits sprouting angiogenesis."; RL Circ. Res. 113:1206-1218(2013). RN [6] RP SUBCELLULAR LOCATION. RX PubMed=32973005; DOI=10.1126/science.abc5809; RA McKenna M.J., Sim S.I., Ordureau A., Wei L., Harper J.W., Shao S., Park E.; RT "The endoplasmic reticulum P5A-ATPase is a transmembrane helix dislocase."; RL Science 369:0-0(2020). RN [7] RP STRUCTURE BY NMR OF 1-113. RG RIKEN structural genomics initiative (RSGI); RT "Solution structure of the PDZ domain from human synaptojanin 2 binding RT protein."; RL Submitted (MAR-2007) to the PDB data bank. RN [8] RP X-RAY CRYSTALLOGRAPHY (1.35 ANGSTROMS) OF 5-101. RA Tickle J., Phillips C., Pike A.C.W., Cooper C., Salah E., Elkins J., RA Turnbull A.P., Edwards A., Arrowsmith C.H., Weigelt J., Sundstrom M., RA Doyle D.; RT "Crystal structure of PDZ domain of synaptojanin-2 binding protein."; RL Submitted (JUN-2007) to the PDB data bank. CC -!- FUNCTION: Regulates endocytosis of activin type 2 receptor kinases CC through the Ral/RALBP1-dependent pathway and may be involved in CC suppression of activin-induced signal transduction. CC {ECO:0000250|UniProtKB:Q9D6K5}. CC -!- SUBUNIT: Binds (via the PDZ domain) to isoform 2A of SYNJ2 (via the CC unique motif in the C-terminus) (By similarity). Interacts (via C- CC terminus) with RALBP1. Interacts (via PDZ domain) with ACVR2A (via C- CC terminus) and ACVR2B (via C-terminus). Forms a ternary complex with CC ACVR2A and RALBP1 (By similarity). Interacts with MAPK12 (By CC similarity). Interacts with DLL1; enhances DLL1 protein stability, and CC promotes notch signaling in endothelial cells (PubMed:24025447). CC {ECO:0000250|UniProtKB:Q9D6K5, ECO:0000250|UniProtKB:Q9WVJ4, CC ECO:0000269|PubMed:24025447}. CC -!- INTERACTION: CC P57105; Q13520: AQP6; NbExp=3; IntAct=EBI-1049004, EBI-13059134; CC P57105; P11912: CD79A; NbExp=3; IntAct=EBI-1049004, EBI-7797864; CC P57105; Q7Z7G2: CPLX4; NbExp=3; IntAct=EBI-1049004, EBI-18013275; CC P57105; Q96BA8: CREB3L1; NbExp=3; IntAct=EBI-1049004, EBI-6942903; CC P57105; P49447: CYB561; NbExp=3; IntAct=EBI-1049004, EBI-8646596; CC P57105; Q9NR61: DLL4; NbExp=3; IntAct=EBI-1049004, EBI-11700027; CC P57105; Q15125: EBP; NbExp=3; IntAct=EBI-1049004, EBI-3915253; CC P57105; Q9NYP7: ELOVL5; NbExp=3; IntAct=EBI-1049004, EBI-11037623; CC P57105; A1L3X0: ELOVL7; NbExp=3; IntAct=EBI-1049004, EBI-10285373; CC P57105; Q9Y282: ERGIC3; NbExp=3; IntAct=EBI-1049004, EBI-781551; CC P57105; Q96KR6: FAM210B; NbExp=3; IntAct=EBI-1049004, EBI-18938272; CC P57105; Q8TAF8: LHFPL5; NbExp=3; IntAct=EBI-1049004, EBI-2820517; CC P57105; Q5VYS4: MEDAG; NbExp=3; IntAct=EBI-1049004, EBI-1050881; CC P57105; Q9H6H4: REEP4; NbExp=3; IntAct=EBI-1049004, EBI-7545592; CC P57105; Q3KNW5: SLC10A6; NbExp=3; IntAct=EBI-1049004, EBI-18159983; CC P57105; Q9UHI5: SLC7A8; NbExp=3; IntAct=EBI-1049004, EBI-13292283; CC P57105; Q8N1Q8: THEM5; NbExp=3; IntAct=EBI-1049004, EBI-10264970; CC P57105; Q96MV1: TLCD4; NbExp=3; IntAct=EBI-1049004, EBI-12947623; CC P57105; Q96IK0: TMEM101; NbExp=3; IntAct=EBI-1049004, EBI-3922699; CC P57105; Q9NUH8: TMEM14B; NbExp=3; IntAct=EBI-1049004, EBI-8638294; CC P57105; Q9NWH2: TMEM242; NbExp=3; IntAct=EBI-1049004, EBI-10315004; CC P57105; Q8N6Y0: USHBP1; NbExp=6; IntAct=EBI-1049004, EBI-739895; CC -!- SUBCELLULAR LOCATION: Mitochondrion outer membrane CC {ECO:0000269|PubMed:32973005}. 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; AY534623; AAT01566.1; -; mRNA. DR EMBL; AK002133; BAA92098.1; -; mRNA. DR EMBL; CH471061; EAW81032.1; -; Genomic_DNA. DR EMBL; BC007704; AAH07704.1; -; mRNA. DR CCDS; CCDS9803.1; -. DR RefSeq; NP_060843.2; NM_018373.2. DR PDB; 2ENO; NMR; -; A=1-107. DR PDB; 2JIK; X-ray; 1.35 A; A/B=6-100. DR PDB; 2JIN; X-ray; 1.50 A; A=4-99. DR PDB; 7P73; X-ray; 1.85 A; A=6-103. DR PDB; 7P74; X-ray; 1.90 A; A=6-103. DR PDB; 7PC9; X-ray; 2.40 A; A/B=6-103. DR PDB; 7R2M; X-ray; 2.40 A; A/D=6-103. DR PDB; 7R2T; X-ray; 2.50 A; A=6-103. DR PDB; 8AEL; X-ray; 2.20 A; A=7-103. DR PDBsum; 2ENO; -. DR PDBsum; 2JIK; -. DR PDBsum; 2JIN; -. DR PDBsum; 7P73; -. DR PDBsum; 7P74; -. DR PDBsum; 7PC9; -. DR PDBsum; 7R2M; -. DR PDBsum; 7R2T; -. DR PDBsum; 8AEL; -. DR AlphaFoldDB; P57105; -. DR SMR; P57105; -. DR BioGRID; 120614; 163. DR IntAct; P57105; 51. DR STRING; 9606.ENSP00000256366; -. DR TCDB; 8.A.24.1.5; the ezrin/radixin/moesin-binding phosphoprotein 50 (ebp50) family. DR iPTMnet; P57105; -. DR PhosphoSitePlus; P57105; -. DR BioMuta; SYNJ2BP; -. DR DMDM; 22261816; -. DR EPD; P57105; -. DR jPOST; P57105; -. DR MassIVE; P57105; -. DR MaxQB; P57105; -. DR PaxDb; 9606-ENSP00000256366; -. DR PeptideAtlas; P57105; -. DR ProteomicsDB; 57004; -. DR Pumba; P57105; -. DR TopDownProteomics; P57105; -. DR Antibodypedia; 46; 139 antibodies from 21 providers. DR DNASU; 55333; -. DR Ensembl; ENST00000256366.6; ENSP00000256366.4; ENSG00000213463.5. DR GeneID; 55333; -. DR KEGG; hsa:55333; -. DR MANE-Select; ENST00000256366.6; ENSP00000256366.4; NM_018373.3; NP_060843.2. DR UCSC; uc001xmc.5; human. DR AGR; HGNC:18955; -. DR CTD; 55333; -. DR DisGeNET; 55333; -. DR GeneCards; SYNJ2BP; -. DR HGNC; HGNC:18955; SYNJ2BP. DR HPA; ENSG00000213463; Low tissue specificity. DR MIM; 609411; gene. DR neXtProt; NX_P57105; -. DR OpenTargets; ENSG00000213463; -. DR PharmGKB; PA38768; -. DR VEuPathDB; HostDB:ENSG00000213463; -. DR eggNOG; KOG3528; Eukaryota. DR GeneTree; ENSGT00830000128402; -. DR HOGENOM; CLU_149433_1_0_1; -. DR InParanoid; P57105; -. DR OMA; FRNAGCD; -. DR OrthoDB; 2998836at2759; -. DR PhylomeDB; P57105; -. DR TreeFam; TF318964; -. DR PathwayCommons; P57105; -. DR SignaLink; P57105; -. DR BioGRID-ORCS; 55333; 12 hits in 1138 CRISPR screens. DR EvolutionaryTrace; P57105; -. DR GeneWiki; SYNJ2BP; -. DR GenomeRNAi; 55333; -. DR Pharos; P57105; Tbio. DR PRO; PR:P57105; -. DR Proteomes; UP000005640; Chromosome 14. DR RNAct; P57105; Protein. DR Bgee; ENSG00000213463; Expressed in renal medulla and 209 other cell types or tissues. DR ExpressionAtlas; P57105; baseline and differential. DR Genevisible; P57105; HS. DR GO; GO:0005741; C:mitochondrial outer membrane; IDA:UniProtKB. DR GO; GO:0005739; C:mitochondrion; IDA:UniProtKB. DR GO; GO:0016525; P:negative regulation of angiogenesis; IMP:UniProtKB. DR GO; GO:0010596; P:negative regulation of endothelial cell migration; IMP:UniProtKB. DR GO; GO:0001937; P:negative regulation of endothelial cell proliferation; IMP:UniProtKB. DR GO; GO:0070373; P:negative regulation of ERK1 and ERK2 cascade; IDA:UniProtKB. DR GO; GO:1903671; P:negative regulation of sprouting angiogenesis; IMP:UniProtKB. DR GO; GO:0006605; P:protein targeting; IEA:Ensembl. DR GO; GO:0030100; P:regulation of endocytosis; IEA:Ensembl. DR GO; GO:0008593; P:regulation of Notch signaling pathway; IMP:UniProtKB. DR GO; GO:0007266; P:Rho protein signal transduction; IEA:Ensembl. DR CDD; cd00992; PDZ_signaling; 1. DR Gene3D; 2.30.42.10; -; 1. DR InterPro; IPR001478; PDZ. DR InterPro; IPR036034; PDZ_sf. DR PANTHER; PTHR23119; DISCS LARGE; 1. DR PANTHER; PTHR23119:SF6; DISKS LARGE HOMOLOG 2; 1. DR Pfam; PF00595; PDZ; 1. DR SMART; SM00228; PDZ; 1. DR SUPFAM; SSF50156; PDZ domain-like; 1. DR PROSITE; PS50106; PDZ; 1. PE 1: Evidence at protein level; KW 3D-structure; Membrane; Mitochondrion; Mitochondrion outer membrane; KW Reference proteome; Transmembrane; Transmembrane helix. FT CHAIN 1..145 FT /note="Synaptojanin-2-binding protein" FT /id="PRO_0000072383" FT TOPO_DOM 1..117 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 118..138 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 139..145 FT /note="Mitochondrial intermembrane" FT /evidence="ECO:0000255" FT DOMAIN 13..100 FT /note="PDZ" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143" FT VARIANT 9 FT /note="V -> I (in dbSNP:rs4356408)" FT /id="VAR_051394" FT CONFLICT 68 FT /note="V -> A (in Ref. 2; BAA92098)" FT /evidence="ECO:0000305" FT HELIX 6..8 FT /evidence="ECO:0007829|PDB:2JIK" FT STRAND 9..17 FT /evidence="ECO:0007829|PDB:2JIK" FT STRAND 20..22 FT /evidence="ECO:0007829|PDB:2ENO" FT STRAND 25..29 FT /evidence="ECO:0007829|PDB:2JIK" FT TURN 31..33 FT /evidence="ECO:0007829|PDB:7PC9" FT STRAND 35..38 FT /evidence="ECO:0007829|PDB:7P73" FT STRAND 42..47 FT /evidence="ECO:0007829|PDB:2JIK" FT STRAND 49..51 FT /evidence="ECO:0007829|PDB:2ENO" FT HELIX 52..56 FT /evidence="ECO:0007829|PDB:2JIK" FT STRAND 64..68 FT /evidence="ECO:0007829|PDB:2JIK" FT HELIX 78..86 FT /evidence="ECO:0007829|PDB:2JIK" FT STRAND 90..100 FT /evidence="ECO:0007829|PDB:2JIK" SQ SEQUENCE 145 AA; 15928 MW; A62A82AC06A64995 CRC64; MNGRVDYLVT EEEINLTRGP SGLGFNIVGG TDQQYVSNDS GIYVSRIKEN GAAALDGRLQ EGDKILSVNG QDLKNLLHQD AVDLFRNAGY AVSLRVQHRL QVQNGPIGHR GEGDPSGIPI FMVLVPVFAL TMVAAWAFMR YRQQL //