SYJ2B_HUMAN
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 03-AUG-2022, entry version 178.
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}.
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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 PDBsum; 2ENO; -.
DR PDBsum; 2JIK; -.
DR PDBsum; 2JIN; -.
DR AlphaFoldDB; P57105; -.
DR SMR; P57105; -.
DR BioGRID; 120614; 161.
DR IntAct; P57105; 28.
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; P57105; -.
DR PeptideAtlas; P57105; -.
DR PRIDE; P57105; -.
DR ProteomicsDB; 57004; -.
DR TopDownProteomics; P57105; -.
DR Antibodypedia; 46; 126 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 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; WILLRYR; -.
DR OrthoDB; 1502481at2759; -.
DR PhylomeDB; P57105; -.
DR TreeFam; TF318964; -.
DR PathwayCommons; P57105; -.
DR SignaLink; P57105; -.
DR BioGRID-ORCS; 55333; 11 hits in 1067 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 207 other tissues.
DR ExpressionAtlas; P57105; baseline and differential.
DR Genevisible; P57105; HS.
DR GO; GO:0016323; C:basolateral plasma membrane; IBA:GO_Central.
DR GO; GO:0030054; C:cell junction; IBA:GO_Central.
DR GO; GO:0031307; C:integral component of mitochondrial outer membrane; IDA:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; IDA:UniProtKB.
DR GO; GO:0031594; C:neuromuscular junction; IBA:GO_Central.
DR GO; GO:0043005; C:neuron projection; IBA:GO_Central.
DR GO; GO:0098839; C:postsynaptic density membrane; IBA:GO_Central.
DR GO; GO:0098609; P:cell-cell adhesion; IBA:GO_Central.
DR GO; GO:0007268; P:chemical synaptic transmission; IBA:GO_Central.
DR GO; GO:0045197; P:establishment or maintenance of epithelial cell apical/basal polarity; IBA:GO_Central.
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:0043113; P:receptor clustering; IBA:GO_Central.
DR GO; GO:0097120; P:receptor localization to synapse; IBA:GO_Central.
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 Gene3D; 2.30.42.10; -; 1.
DR InterPro; IPR001478; PDZ.
DR InterPro; IPR036034; PDZ_sf.
DR Pfam; PF00595; PDZ; 1.
DR SMART; SM00228; PDZ; 1.
DR SUPFAM; SSF50156; SSF50156; 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:2ENO"
FT STRAND 35..38
FT /evidence="ECO:0007829|PDB:2ENO"
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
