ID SNX29_HUMAN Reviewed; 813 AA. AC Q8TEQ0; B5MDW2; Q8N2X2; Q9HA26; DT 21-AUG-2007, integrated into UniProtKB/Swiss-Prot. DT 19-OCT-2011, sequence version 3. DT 27-MAR-2024, entry version 142. DE RecName: Full=Sorting nexin-29; DE AltName: Full=RUN domain-containing protein 2A; GN Name=SNX29; Synonyms=RUNDC2A; 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 GENOMIC DNA]. RX PubMed=15616553; DOI=10.1038/nature03187; RA Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G., RA Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E., RA Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J., Buckingham J.M., RA Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C., RA Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M., RA Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M., RA Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D., RA Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L., RA Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E., RA Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H., RA Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y., RA Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J., RA Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D., RA Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S., RA Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A., RA Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M., RA Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H., RA Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A., RA Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J., RA DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J., RA Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M., RA Myers R.M., Rubin E.M., Pennacchio L.A.; RT "The sequence and analysis of duplication-rich human chromosome 16."; RL Nature 432:988-994(2004). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-375 (ISOFORM 1). RC TISSUE=Mammary gland; 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 MRNA] OF 441-813 (ISOFORM 1). RC TISSUE=Spleen; RX PubMed=12693554; DOI=10.1093/dnares/10.1.49; RA Jikuya H., Takano J., Kikuno R., Hirosawa M., Nagase T., Nomura N., RA Ohara O.; RT "Characterization of long cDNA clones from human adult spleen. II. The RT complete sequences of 81 cDNA clones."; RL DNA Res. 10:49-57(2003). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 512-813 (ISOFORM 2). RC TISSUE=Brain; 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 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 [6] 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 [7] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Leukemic T-cell; RX PubMed=19690332; DOI=10.1126/scisignal.2000007; RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., RA Rodionov V., Han D.K.; RT "Quantitative phosphoproteomic analysis of T cell receptor signaling RT reveals system-wide modulation of protein-protein interactions."; RL Sci. Signal. 2:RA46-RA46(2009). RN [8] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=20068231; DOI=10.1126/scisignal.2000475; RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.; RT "Quantitative phosphoproteomics reveals widespread full phosphorylation RT site occupancy during mitosis."; RL Sci. Signal. 3:RA3-RA3(2010). RN [9] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-268 AND SER-330, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma, and Erythroleukemia; 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). CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=Q8TEQ0-1; Sequence=Displayed; CC Name=2; CC IsoId=Q8TEQ0-2; Sequence=VSP_027281; CC -!- SIMILARITY: Belongs to the sorting nexin family. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=BAB14033.1; Type=Miscellaneous discrepancy; Note=Probable cloning artifact.; Evidence={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; AC007216; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC007598; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC007601; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC010333; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC092365; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC131391; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AK022425; BAB14033.1; ALT_SEQ; mRNA. DR EMBL; AK074072; BAB84898.1; -; mRNA. DR EMBL; BC029857; AAH29857.1; -; mRNA. DR CCDS; CCDS10553.2; -. [Q8TEQ0-1] DR RefSeq; NP_115543.3; NM_032167.4. [Q8TEQ0-1] DR AlphaFoldDB; Q8TEQ0; -. DR SMR; Q8TEQ0; -. DR BioGRID; 124903; 45. DR IntAct; Q8TEQ0; 10. DR STRING; 9606.ENSP00000456480; -. DR TCDB; 3.A.34.1.1; the sorting nexins of the escrt complexes (sn-escrt). DR GlyCosmos; Q8TEQ0; 1 site, 1 glycan. DR GlyGen; Q8TEQ0; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; Q8TEQ0; -. DR PhosphoSitePlus; Q8TEQ0; -. DR BioMuta; SNX29; -. DR DMDM; 353526314; -. DR EPD; Q8TEQ0; -. DR jPOST; Q8TEQ0; -. DR MassIVE; Q8TEQ0; -. DR MaxQB; Q8TEQ0; -. DR PaxDb; 9606-ENSP00000456480; -. DR PeptideAtlas; Q8TEQ0; -. DR ProteomicsDB; 74476; -. [Q8TEQ0-1] DR ProteomicsDB; 74477; -. [Q8TEQ0-2] DR Pumba; Q8TEQ0; -. DR Antibodypedia; 2225; 146 antibodies from 19 providers. DR DNASU; 92017; -. DR Ensembl; ENST00000566228.6; ENSP00000456480.1; ENSG00000048471.14. [Q8TEQ0-1] DR GeneID; 92017; -. DR KEGG; hsa:92017; -. DR MANE-Select; ENST00000566228.6; ENSP00000456480.1; NM_032167.5; NP_115543.3. DR UCSC; uc002dby.6; human. [Q8TEQ0-1] DR AGR; HGNC:30542; -. DR CTD; 92017; -. DR DisGeNET; 92017; -. DR GeneCards; SNX29; -. DR HGNC; HGNC:30542; SNX29. DR HPA; ENSG00000048471; Low tissue specificity. DR neXtProt; NX_Q8TEQ0; -. DR OpenTargets; ENSG00000048471; -. DR PharmGKB; PA162404312; -. DR VEuPathDB; HostDB:ENSG00000048471; -. DR eggNOG; KOG2101; Eukaryota. DR eggNOG; KOG4381; Eukaryota. DR GeneTree; ENSGT00730000110975; -. DR HOGENOM; CLU_020563_1_0_1; -. DR InParanoid; Q8TEQ0; -. DR OMA; TIPHVKL; -. DR OrthoDB; 5481180at2759; -. DR PhylomeDB; Q8TEQ0; -. DR PathwayCommons; Q8TEQ0; -. DR SignaLink; Q8TEQ0; -. DR BioGRID-ORCS; 92017; 11 hits in 1153 CRISPR screens. DR ChiTaRS; SNX29; human. DR GenomeRNAi; 92017; -. DR Pharos; Q8TEQ0; Tbio. DR PRO; PR:Q8TEQ0; -. DR Proteomes; UP000005640; Chromosome 16. DR RNAct; Q8TEQ0; Protein. DR Bgee; ENSG00000048471; Expressed in kidney epithelium and 181 other cell types or tissues. DR ExpressionAtlas; Q8TEQ0; baseline and differential. DR GO; GO:0035091; F:phosphatidylinositol binding; IEA:InterPro. DR CDD; cd07277; PX_RUN; 1. DR CDD; cd17689; RUN_SNX29; 1. DR Gene3D; 1.20.58.900; -; 1. DR Gene3D; 3.30.1520.10; Phox-like domain; 1. DR InterPro; IPR001683; PX_dom. DR InterPro; IPR036871; PX_dom_sf. DR InterPro; IPR004012; Run_dom. DR InterPro; IPR037213; Run_dom_sf. DR InterPro; IPR047329; RUN_SNX29. DR InterPro; IPR037916; SNX29_PX. DR PANTHER; PTHR47194:SF4; SORTING NEXIN-29; 1. DR PANTHER; PTHR47194; SORTING NEXIN-29-RELATED; 1. DR Pfam; PF00787; PX; 1. DR Pfam; PF02759; RUN; 1. DR SMART; SM00312; PX; 1. DR SMART; SM00593; RUN; 1. DR SUPFAM; SSF64268; PX domain; 1. DR SUPFAM; SSF140741; RUN domain-like; 1. DR PROSITE; PS50195; PX; 1. DR PROSITE; PS50826; RUN; 1. DR Genevisible; Q8TEQ0; HS. PE 1: Evidence at protein level; KW Alternative splicing; Coiled coil; Phosphoprotein; Reference proteome. FT CHAIN 1..813 FT /note="Sorting nexin-29" FT /id="PRO_0000297565" FT DOMAIN 36..180 FT /note="RUN" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00178" FT DOMAIN 656..779 FT /note="PX" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00147" FT REGION 269..299 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 346..378 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 778..813 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COILED 466..545 FT /evidence="ECO:0000255" FT COMPBIAS 357..374 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 268 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 291 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q9D3S3" FT MOD_RES 292 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q9D3S3" FT MOD_RES 330 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 344 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q9D3S3" FT MOD_RES 445 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q9D3S3" FT MOD_RES 450 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q9D3S3" FT MOD_RES 639 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q9D3S3" FT MOD_RES 641 FT /note="Phosphothreonine" FT /evidence="ECO:0000250|UniProtKB:Q9D3S3" FT MOD_RES 642 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q9D3S3" FT MOD_RES 646 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q9D3S3" FT VAR_SEQ 775..813 FT /note="ITPPGEPVNSRPKAASRFPKLSRGQPRETRNVEPQSGDL -> WISLFGNGR FT DSSREEFSSS (in isoform 2)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_027281" FT CONFLICT 183 FT /note="N -> D (in Ref. 2; BAB14033)" FT /evidence="ECO:0000305" FT CONFLICT 344 FT /note="S -> G (in Ref. 2; BAB14033)" FT /evidence="ECO:0000305" SQ SEQUENCE 813 AA; 91254 MW; A1868A682CCFBE0C CRC64; MSGSQNNDKR QFLLERLLDA VKQCQIRFGG RKEIASDSDS RVTCLCAQFE AVLQHGLKRS RGLALTAAAI KQAAGFASKT ETEPVFWYYV KEVLNKHELQ RFYSLRHIAS DVGRGRAWLR CALNEHSLER YLHMLLADRC RLSTFYEDWS FVMDEERSSM LPTMAAGLNS ILFAINIDNK DLNGQSKFAP TVSDLLKEST QNVTSLLKES TQGVSSLFRE ITASSAVSIL IKPEQETDPL PVVSRNVSAD AKCKKERKKK KKVTNIISFD DEEDEQNSGD VFKKTPGAGE SSEDNSDRSS VNIMSAFESP FGPNSNGSQS SNSWKIDSLS LNGEFGYQKL DVKSIDDEDV DENEDDVYGN SSGRKHRGHS ESPEKPLEGN TCLSQMHSWA PLKVLHNDSD ILFPVSGVGS YSPADAPLGS LENGTGPEDH VLPDPGLRYS VEASSPGHGS PLSSLLPSAS VPESMTISEL RQATVAMMNR KDELEEENRS LRNLLDGEME HSAALRQEVD TLKRKVAEQE ERQGMKVQAL ARENEVLKVQ LKKYVGAVQM LKREGQTAEV PNLWSVDGEV TVAEQKPGEI AEELASSYER KLIEVAEMHG ELIEFNERLH RALVAKEALV SQMRQELIDL RGPVPGDLSQ TSEDQSLSDF EISNRALINV WIPSVFLRGK AANAFHVYQV YIRIKDDEWN IYRRYTEFRS LHHKLQNKYP QVRAYNFPPK KAIGNKDAKF VEERRKQLQN YLRSVMNKVI QMVPEFAASP KKETLIQLMP FFVDITPPGE PVNSRPKAAS RFPKLSRGQP RETRNVEPQS GDL //