SNX12_HUMAN
ID SNX12_HUMAN Reviewed; 162 AA.
AC Q9UMY4; F8W8K5; Q8WUG9;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 18-SEP-2019, sequence version 4.
DT 03-AUG-2022, entry version 187.
DE RecName: Full=Sorting nexin-12;
GN Name=SNX12;
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] (ISOFORM 2).
RX PubMed=11485546; DOI=10.1042/0264-6021:3580007;
RA Teasdale R.D., Loci D., Houghton F., Karlsson L., Gleeson P.A.;
RT "A large family of endosome-localized proteins related to sorting nexin
RT 1.";
RL Biochem. J. 358:7-16(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164054; DOI=10.1038/nature02462;
RA Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L.,
RA Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K.,
RA Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L.,
RA Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P.,
RA Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y.,
RA Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N.,
RA Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A.,
RA Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C.,
RA Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D.,
RA Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C.,
RA Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K.,
RA Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A.,
RA Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S.,
RA McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S.,
RA Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V.,
RA Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A.,
RA Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M.,
RA Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A.,
RA Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P.,
RA Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y.,
RA Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D.,
RA Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.;
RT "The DNA sequence and comparative analysis of human chromosome 10.";
RL Nature 429:375-381(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Placenta;
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-23, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=15592455; DOI=10.1038/nbt1046;
RA Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,
RA Zha X.-M., Polakiewicz R.D., Comb M.J.;
RT "Immunoaffinity profiling of tyrosine phosphorylation in cancer cells.";
RL Nat. Biotechnol. 23:94-101(2005).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [7]
RP 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 [8]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [10]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-73, AND IDENTIFICATION BY
RP 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 [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [13]
RP STRUCTURE BY NMR OF 27-160.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of PX domain from human SNX12.";
RL Submitted (NOV-2005) to the PDB data bank.
CC -!- FUNCTION: May be involved in several stages of intracellular
CC trafficking. {ECO:0000250}.
CC -!- INTERACTION:
CC Q9UMY4; P01019: AGT; NbExp=3; IntAct=EBI-1752602, EBI-751728;
CC Q9UMY4; Q15041: ARL6IP1; NbExp=3; IntAct=EBI-1752602, EBI-714543;
CC Q9UMY4; P78371: CCT2; NbExp=3; IntAct=EBI-1752602, EBI-357407;
CC Q9UMY4; P50990: CCT8; NbExp=3; IntAct=EBI-1752602, EBI-356507;
CC Q9UMY4; P42858: HTT; NbExp=3; IntAct=EBI-1752602, EBI-466029;
CC Q9UMY4; P03952: KLKB1; NbExp=3; IntAct=EBI-1752602, EBI-10087153;
CC Q9UMY4; P06858: LPL; NbExp=3; IntAct=EBI-1752602, EBI-715909;
CC Q9UMY4; P16333: NCK1; NbExp=3; IntAct=EBI-1752602, EBI-389883;
CC Q9UMY4; Q9BY11: PACSIN1; NbExp=3; IntAct=EBI-1752602, EBI-721769;
CC Q9UMY4-1; Q15041: ARL6IP1; NbExp=3; IntAct=EBI-22419305, EBI-714543;
CC Q9UMY4-1; Q9Y680: FKBP7; NbExp=3; IntAct=EBI-22419305, EBI-3918971;
CC Q9UMY4-1; Q96HR9-2: REEP6; NbExp=3; IntAct=EBI-22419305, EBI-14065960;
CC Q9UMY4-1; Q9NS64: RPRM; NbExp=3; IntAct=EBI-22419305, EBI-1052363;
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Peripheral membrane
CC protein {ECO:0000305}; Cytoplasmic side {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=2;
CC IsoId=Q9UMY4-2; Sequence=Displayed;
CC Name=1;
CC IsoId=Q9UMY4-1; Sequence=VSP_060253;
CC Name=3;
CC IsoId=Q9UMY4-3; Sequence=VSP_060252;
CC -!- DOMAIN: The PX domain mediates interaction with membranes enriched in
CC phosphatidylinositol 3-phosphate. {ECO:0000250}.
CC -!- MISCELLANEOUS: [Isoform 1]: May be produced at very low levels due to a
CC premature stop codon in the mRNA, leading to nonsense-mediated mRNA
CC decay. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the sorting nexin family. {ECO:0000305}.
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; AF171229; AAD48491.1; -; mRNA.
DR EMBL; BT007203; AAP35867.1; -; mRNA.
DR EMBL; AL590764; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC020559; -; NOT_ANNOTATED_CDS; mRNA.
DR CCDS; CCDS14405.1; -. [Q9UMY4-2]
DR CCDS; CCDS59169.1; -. [Q9UMY4-3]
DR RefSeq; NP_001243114.1; NM_001256185.1. [Q9UMY4-2]
DR RefSeq; NP_001243117.1; NM_001256188.1. [Q9UMY4-3]
DR RefSeq; NP_037478.2; NM_013346.3. [Q9UMY4-2]
DR PDB; 2CSK; NMR; -; A=27-159.
DR PDBsum; 2CSK; -.
DR AlphaFoldDB; Q9UMY4; -.
DR SMR; Q9UMY4; -.
DR BioGRID; 118974; 54.
DR IntAct; Q9UMY4; 17.
DR MINT; Q9UMY4; -.
DR STRING; 9606.ENSP00000481314; -.
DR GlyGen; Q9UMY4; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q9UMY4; -.
DR PhosphoSitePlus; Q9UMY4; -.
DR BioMuta; SNX12; -.
DR DMDM; 50403807; -.
DR UCD-2DPAGE; Q9UMY4; -.
DR EPD; Q9UMY4; -.
DR jPOST; Q9UMY4; -.
DR MassIVE; Q9UMY4; -.
DR MaxQB; Q9UMY4; -.
DR PaxDb; Q9UMY4; -.
DR PeptideAtlas; Q9UMY4; -.
DR PRIDE; Q9UMY4; -.
DR ProteomicsDB; 30165; -.
DR ProteomicsDB; 85230; -. [Q9UMY4-1]
DR ProteomicsDB; 85231; -. [Q9UMY4-2]
DR TopDownProteomics; Q9UMY4-2; -. [Q9UMY4-2]
DR Antibodypedia; 27466; 278 antibodies from 30 providers.
DR DNASU; 29934; -.
DR Ensembl; ENST00000276105.3; ENSP00000276105.3; ENSG00000147164.12. [Q9UMY4-3]
DR Ensembl; ENST00000374274.8; ENSP00000363392.3; ENSG00000147164.12. [Q9UMY4-2]
DR Ensembl; ENST00000622277.4; ENSP00000481314.1; ENSG00000147164.12. [Q9UMY4-2]
DR GeneID; 29934; -.
DR KEGG; hsa:29934; -.
DR MANE-Select; ENST00000374274.8; ENSP00000363392.3; NM_013346.4; NP_037478.2.
DR UCSC; uc004dyq.5; human. [Q9UMY4-2]
DR CTD; 29934; -.
DR DisGeNET; 29934; -.
DR GeneCards; SNX12; -.
DR HGNC; HGNC:14976; SNX12.
DR HPA; ENSG00000147164; Low tissue specificity.
DR MIM; 300883; gene.
DR neXtProt; NX_Q9UMY4; -.
DR OpenTargets; ENSG00000147164; -.
DR PharmGKB; PA37952; -.
DR VEuPathDB; HostDB:ENSG00000147164; -.
DR eggNOG; KOG2527; Eukaryota.
DR GeneTree; ENSGT00940000153609; -.
DR HOGENOM; CLU_057172_2_2_1; -.
DR InParanoid; Q9UMY4; -.
DR OMA; NMYTDYE; -.
DR PhylomeDB; Q9UMY4; -.
DR TreeFam; TF314980; -.
DR PathwayCommons; Q9UMY4; -.
DR SignaLink; Q9UMY4; -.
DR BioGRID-ORCS; 29934; 10 hits in 702 CRISPR screens.
DR ChiTaRS; SNX12; human.
DR EvolutionaryTrace; Q9UMY4; -.
DR GenomeRNAi; 29934; -.
DR Pharos; Q9UMY4; Tbio.
DR PRO; PR:Q9UMY4; -.
DR Proteomes; UP000005640; Chromosome X.
DR RNAct; Q9UMY4; protein.
DR Bgee; ENSG00000147164; Expressed in ileal mucosa and 184 other tissues.
DR ExpressionAtlas; Q9UMY4; baseline and differential.
DR Genevisible; Q9UMY4; HS.
DR GO; GO:0005769; C:early endosome; IDA:UniProtKB.
DR GO; GO:0031901; C:early endosome membrane; IBA:GO_Central.
DR GO; GO:0030904; C:retromer complex; IBA:GO_Central.
DR GO; GO:0019899; F:enzyme binding; IPI:UniProtKB.
DR GO; GO:0035091; F:phosphatidylinositol binding; IDA:UniProtKB.
DR GO; GO:0032266; F:phosphatidylinositol-3-phosphate binding; IBA:GO_Central.
DR GO; GO:0032456; P:endocytic recycling; IBA:GO_Central.
DR GO; GO:0034499; P:late endosome to Golgi transport; IBA:GO_Central.
DR GO; GO:2000642; P:negative regulation of early endosome to late endosome transport; IDA:UniProtKB.
DR GO; GO:0010629; P:negative regulation of gene expression; IMP:UniProtKB.
DR GO; GO:0042177; P:negative regulation of protein catabolic process; IDA:UniProtKB.
DR GO; GO:0010955; P:negative regulation of protein processing; IDA:UniProtKB.
DR GO; GO:0051224; P:negative regulation of protein transport; IDA:UniProtKB.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0030100; P:regulation of endocytosis; IMP:UniProtKB.
DR Gene3D; 3.30.1520.10; -; 1.
DR InterPro; IPR001683; PX_dom.
DR InterPro; IPR036871; PX_dom_sf.
DR Pfam; PF00787; PX; 1.
DR SMART; SM00312; PX; 1.
DR SUPFAM; SSF64268; SSF64268; 1.
DR PROSITE; PS50195; PX; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Lipid-binding; Membrane;
KW Phosphoprotein; Protein transport; Reference proteome; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:22814378"
FT CHAIN 2..162
FT /note="Sorting nexin-12"
FT /id="PRO_0000213858"
FT DOMAIN 28..152
FT /note="PX"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00147"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 71
FT /ligand="a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-
FT inositol-3-phosphate)"
FT /ligand_id="ChEBI:CHEBI:58088"
FT /evidence="ECO:0000250"
FT BINDING 73
FT /ligand="a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-
FT inositol-3-phosphate)"
FT /ligand_id="ChEBI:CHEBI:58088"
FT /evidence="ECO:0000250"
FT BINDING 96
FT /ligand="a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-
FT inositol-3-phosphate)"
FT /ligand_id="ChEBI:CHEBI:58088"
FT /evidence="ECO:0000250"
FT BINDING 119
FT /ligand="a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-
FT inositol-3-phosphate)"
FT /ligand_id="ChEBI:CHEBI:58088"
FT /evidence="ECO:0000250"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:22814378"
FT MOD_RES 23
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:15592455"
FT MOD_RES 73
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT VAR_SEQ 52..55
FT /note="Missing (in isoform 3)"
FT /id="VSP_060252"
FT VAR_SEQ 160..162
FT /note="VRQ -> SLAVSCPGWSAVA (in isoform 1)"
FT /id="VSP_060253"
FT CONFLICT 101
FT /note="Q -> K (in Ref. 1; AAD48491)"
FT /evidence="ECO:0000305"
FT STRAND 31..45
FT /evidence="ECO:0007829|PDB:2CSK"
FT STRAND 47..55
FT /evidence="ECO:0007829|PDB:2CSK"
FT STRAND 59..62
FT /evidence="ECO:0007829|PDB:2CSK"
FT STRAND 64..70
FT /evidence="ECO:0007829|PDB:2CSK"
FT HELIX 72..82
FT /evidence="ECO:0007829|PDB:2CSK"
FT STRAND 83..87
FT /evidence="ECO:0007829|PDB:2CSK"
FT HELIX 113..132
FT /evidence="ECO:0007829|PDB:2CSK"
FT HELIX 134..138
FT /evidence="ECO:0007829|PDB:2CSK"
FT HELIX 140..145
FT /evidence="ECO:0007829|PDB:2CSK"
SQ SEQUENCE 162 AA; 18885 MW; 48CBC16A86AFDB08 CRC64;
MSDTAVADTR RLNSKPQDLT DAYGPPSNFL EIDIFNPQTV GVGRARFTTY EVRMRTNLPI
FKLKESCVRR RYSDFEWLKN ELERDSKIVV PPLPGKALKR QLPFRGDEGI FEESFIEERR
QGLEQFINKI AGHPLAQNER CLHMFLQEEA IDRNYVPGKV RQ
