S35B2_HUMAN
ID S35B2_HUMAN Reviewed; 432 AA.
AC Q8TB61; B4DDM2; B4DDU9; F5H7Y9; Q2VY06; Q53GA3; Q5T9W1; Q5T9W2; Q7Z2G3;
AC Q8NBK6; Q96AR6;
DT 07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 166.
DE RecName: Full=Adenosine 3'-phospho 5'-phosphosulfate transporter 1;
DE AltName: Full=PAPS transporter 1;
DE AltName: Full=Putative MAPK-activating protein PM15;
DE AltName: Full=Putative NF-kappa-B-activating protein 48;
DE AltName: Full=Solute carrier family 35 member B2;
GN Name=SLC35B2; Synonyms=PAPST1; ORFNames=PSEC0149;
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 1), FUNCTION, BIOPHYSICOCHEMICAL
RP PROPERTIES, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RC TISSUE=Colon;
RX PubMed=12716889; DOI=10.1074/jbc.m302439200;
RA Kamiyama S., Suda T., Ueda R., Suzuki M., Okubo R., Kikuchi N., Chiba Y.,
RA Goto S., Toyoda H., Saigo K., Watanabe M., Narimatsu H., Jigami Y.,
RA Nishihara S.;
RT "Molecular cloning and identification of 3'-phosphoadenosine 5'-
RT phosphosulfate transporter.";
RL J. Biol. Chem. 278:25958-25963(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
RA Xu J., Xie Y., Mao Y.;
RT "Identification of a splicing variant of solute carrier family 35, member
RT B2 (SLC35B2).";
RL Submitted (NOV-2003) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Lung fibroblast;
RX PubMed=12761501; DOI=10.1038/sj.onc.1206406;
RA Matsuda A., Suzuki Y., Honda G., Muramatsu S., Matsuzaki O., Nagano Y.,
RA Doi T., Shimotohno K., Harada T., Nishida E., Hayashi H., Sugano S.;
RT "Large-scale identification and characterization of human genes that
RT activate NF-kappaB and MAPK signaling pathways.";
RL Oncogene 22:3307-3318(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 4 AND 5), AND VARIANT
RP VAL-342.
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Placenta;
RX PubMed=16303743; DOI=10.1093/dnares/12.2.117;
RA Otsuki T., Ota T., Nishikawa T., Hayashi K., Suzuki Y., Yamamoto J.,
RA Wakamatsu A., Kimura K., Sakamoto K., Hatano N., Kawai Y., Ishii S.,
RA Saito K., Kojima S., Sugiyama T., Ono T., Okano K., Yoshikawa Y.,
RA Aotsuka S., Sasaki N., Hattori A., Okumura K., Nagai K., Sugano S.,
RA Isogai T.;
RT "Signal sequence and keyword trap in silico for selection of full-length
RT human cDNAs encoding secretion or membrane proteins from oligo-capped cDNA
RT libraries.";
RL DNA Res. 12:117-126(2005).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=14574404; DOI=10.1038/nature02055;
RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R.,
RA Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D.,
RA Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H.,
RA Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J.,
RA Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E.,
RA Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J.,
RA French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J.,
RA Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C.,
RA Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A.,
RA Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R.,
RA Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M.,
RA Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K.,
RA Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R.,
RA Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A.,
RA Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L.,
RA Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I.,
RA Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y.,
RA Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E.,
RA Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A.,
RA Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W.,
RA Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M.,
RA West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J.,
RA Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M.,
RA Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I.,
RA Rogers J., Beck S.;
RT "The DNA sequence and analysis of human chromosome 6.";
RL Nature 425:805-811(2003).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Lung carcinoma, and Neuroblastoma;
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 [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 64-432 (ISOFORMS 1/3).
RC TISSUE=Thyroid;
RA Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y.,
RA Tanaka A., Yokoyama S.;
RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-427, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the
RT kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [10]
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 [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [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 [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-427, AND IDENTIFICATION BY
RP 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 [13]
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 [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-427, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=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).
RN [15]
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).
CC -!- FUNCTION: Mediates the transport of adenosine 3'-phospho 5'-
CC phosphosulfate (PAPS), from cytosol into Golgi. PAPS is a universal
CC sulfuryl donor for sulfation events that take place in the Golgi. May
CC indirectly participate in activation of the NF-kappa-B and MAPK
CC pathways. {ECO:0000269|PubMed:12716889}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.8 uM for PAPS {ECO:0000269|PubMed:12716889};
CC -!- INTERACTION:
CC Q8TB61; Q13520: AQP6; NbExp=3; IntAct=EBI-1054782, EBI-13059134;
CC Q8TB61; P07307-3: ASGR2; NbExp=3; IntAct=EBI-1054782, EBI-12808270;
CC Q8TB61; Q07108: CD69; NbExp=3; IntAct=EBI-1054782, EBI-2836595;
CC Q8TB61; Q96FX9: CLDN15; NbExp=3; IntAct=EBI-1054782, EBI-12867518;
CC Q8TB61; Q96BA8: CREB3L1; NbExp=5; IntAct=EBI-1054782, EBI-6942903;
CC Q8TB61; P00387: CYB5R3; NbExp=3; IntAct=EBI-1054782, EBI-1046040;
CC Q8TB61; Q9Y282: ERGIC3; NbExp=3; IntAct=EBI-1054782, EBI-781551;
CC Q8TB61; Q8NBJ4: GOLM1; NbExp=3; IntAct=EBI-1054782, EBI-712073;
CC Q8TB61; Q96K19-5: RNF170; NbExp=3; IntAct=EBI-1054782, EBI-12055631;
CC Q8TB61; Q3SXP7: SHISAL1; NbExp=3; IntAct=EBI-1054782, EBI-18037857;
CC Q8TB61; Q8N6K0: TEX29; NbExp=3; IntAct=EBI-1054782, EBI-19027521;
CC Q8TB61; Q96Q45-2: TMEM237; NbExp=3; IntAct=EBI-1054782, EBI-10982110;
CC Q8TB61; Q9NWD8: TMEM248; NbExp=3; IntAct=EBI-1054782, EBI-10314986;
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane
CC {ECO:0000269|PubMed:12716889}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:12716889}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Name=1;
CC IsoId=Q8TB61-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8TB61-2; Sequence=VSP_014084;
CC Name=3;
CC IsoId=Q8TB61-3; Sequence=VSP_026949;
CC Name=4;
CC IsoId=Q8TB61-4; Sequence=VSP_054696, VSP_054697;
CC Name=5;
CC IsoId=Q8TB61-5; Sequence=VSP_057436;
CC -!- TISSUE SPECIFICITY: Highly expressed in the placenta, pancreas, mammary
CC gland and skeletal muscle. Weakly or not expressed in colon, heart and
CC prostate. {ECO:0000269|PubMed:12716889}.
CC -!- SIMILARITY: Belongs to the nucleotide-sugar transporter family. SLC35B
CC subfamily. {ECO:0000305}.
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DR EMBL; AB106538; BAC79117.1; -; mRNA.
DR EMBL; AY491520; AAS79661.1; -; mRNA.
DR EMBL; AB097021; BAC77374.1; -; mRNA.
DR EMBL; AB097039; BAC77392.1; -; mRNA.
DR EMBL; AK293251; BAG56783.1; -; mRNA.
DR EMBL; AK293344; BAG56860.1; -; mRNA.
DR EMBL; AK075456; BAC11631.1; -; mRNA.
DR EMBL; AL139392; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC016839; AAH16839.1; -; mRNA.
DR EMBL; BC024288; AAH24288.1; -; mRNA.
DR EMBL; AK223028; BAD96748.1; -; mRNA.
DR CCDS; CCDS34462.1; -. [Q8TB61-1]
DR CCDS; CCDS69127.1; -. [Q8TB61-4]
DR CCDS; CCDS75462.1; -. [Q8TB61-5]
DR CCDS; CCDS75463.1; -. [Q8TB61-3]
DR RefSeq; NP_001273438.1; NM_001286509.1.
DR RefSeq; NP_001273439.1; NM_001286510.1.
DR RefSeq; NP_001273440.1; NM_001286511.1. [Q8TB61-3]
DR RefSeq; NP_001273441.1; NM_001286512.1. [Q8TB61-3]
DR RefSeq; NP_001273442.1; NM_001286513.1. [Q8TB61-4]
DR RefSeq; NP_001273446.1; NM_001286517.1.
DR RefSeq; NP_001273448.1; NM_001286519.1. [Q8TB61-5]
DR RefSeq; NP_001273449.1; NM_001286520.1. [Q8TB61-5]
DR RefSeq; NP_835361.1; NM_178148.3. [Q8TB61-1]
DR AlphaFoldDB; Q8TB61; -.
DR BioGRID; 131484; 88.
DR IntAct; Q8TB61; 37.
DR MINT; Q8TB61; -.
DR STRING; 9606.ENSP00000377401; -.
DR BindingDB; Q8TB61; -.
DR TCDB; 2.A.7.11.3; the drug/metabolite transporter (dmt) superfamily.
DR GlyGen; Q8TB61; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q8TB61; -.
DR PhosphoSitePlus; Q8TB61; -.
DR SwissPalm; Q8TB61; -.
DR BioMuta; SLC35B2; -.
DR DMDM; 67461576; -.
DR EPD; Q8TB61; -.
DR jPOST; Q8TB61; -.
DR MassIVE; Q8TB61; -.
DR MaxQB; Q8TB61; -.
DR PaxDb; Q8TB61; -.
DR PeptideAtlas; Q8TB61; -.
DR PRIDE; Q8TB61; -.
DR ProteomicsDB; 27631; -.
DR ProteomicsDB; 3871; -.
DR ProteomicsDB; 73963; -. [Q8TB61-1]
DR ProteomicsDB; 73964; -. [Q8TB61-2]
DR ProteomicsDB; 73965; -. [Q8TB61-3]
DR Antibodypedia; 30649; 101 antibodies from 24 providers.
DR DNASU; 347734; -.
DR Ensembl; ENST00000393812.4; ENSP00000377401.3; ENSG00000157593.19. [Q8TB61-1]
DR Ensembl; ENST00000537814.2; ENSP00000440340.1; ENSG00000157593.19. [Q8TB61-5]
DR Ensembl; ENST00000538577.5; ENSP00000443845.1; ENSG00000157593.19. [Q8TB61-4]
DR Ensembl; ENST00000615337.4; ENSP00000480681.1; ENSG00000157593.19. [Q8TB61-3]
DR Ensembl; ENST00000619636.4; ENSP00000483181.1; ENSG00000157593.19. [Q8TB61-3]
DR GeneID; 347734; -.
DR KEGG; hsa:347734; -.
DR MANE-Select; ENST00000393812.4; ENSP00000377401.3; NM_178148.4; NP_835361.1.
DR UCSC; uc003oxd.5; human. [Q8TB61-1]
DR UCSC; uc011dvu.4; human.
DR CTD; 347734; -.
DR DisGeNET; 347734; -.
DR GeneCards; SLC35B2; -.
DR HGNC; HGNC:16872; SLC35B2.
DR HPA; ENSG00000157593; Low tissue specificity.
DR MalaCards; SLC35B2; -.
DR MIM; 610788; gene.
DR neXtProt; NX_Q8TB61; -.
DR OpenTargets; ENSG00000157593; -.
DR PharmGKB; PA134927864; -.
DR VEuPathDB; HostDB:ENSG00000157593; -.
DR eggNOG; KOG1581; Eukaryota.
DR GeneTree; ENSGT00940000157927; -.
DR HOGENOM; CLU_036019_3_1_1; -.
DR OMA; CGAIGQV; -.
DR OrthoDB; 820879at2759; -.
DR PhylomeDB; Q8TB61; -.
DR TreeFam; TF105926; -.
DR PathwayCommons; Q8TB61; -.
DR Reactome; R-HSA-174362; Transport and synthesis of PAPS.
DR Reactome; R-HSA-727802; Transport of nucleotide sugars.
DR SABIO-RK; Q8TB61; -.
DR SignaLink; Q8TB61; -.
DR BioGRID-ORCS; 347734; 109 hits in 1083 CRISPR screens.
DR ChiTaRS; SLC35B2; human.
DR GeneWiki; SLC35B2; -.
DR GenomeRNAi; 347734; -.
DR Pharos; Q8TB61; Tbio.
DR PRO; PR:Q8TB61; -.
DR Proteomes; UP000005640; Chromosome 6.
DR RNAct; Q8TB61; protein.
DR Bgee; ENSG00000157593; Expressed in stromal cell of endometrium and 95 other tissues.
DR ExpressionAtlas; Q8TB61; baseline and differential.
DR Genevisible; Q8TB61; HS.
DR GO; GO:0005794; C:Golgi apparatus; IDA:UniProtKB.
DR GO; GO:0000139; C:Golgi membrane; TAS:Reactome.
DR GO; GO:0030176; C:integral component of endoplasmic reticulum membrane; IBA:GO_Central.
DR GO; GO:0030173; C:integral component of Golgi membrane; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; NAS:UniProtKB.
DR GO; GO:0016020; C:membrane; IDA:UniProtKB.
DR GO; GO:0046964; F:3'-phosphoadenosine 5'-phosphosulfate transmembrane transporter activity; IDA:UniProtKB.
DR GO; GO:0022857; F:transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0050428; P:3'-phosphoadenosine 5'-phosphosulfate biosynthetic process; TAS:Reactome.
DR GO; GO:0046963; P:3'-phosphoadenosine 5'-phosphosulfate transport; IDA:UniProtKB.
DR GO; GO:0043123; P:positive regulation of I-kappaB kinase/NF-kappaB signaling; HMP:UniProtKB.
DR InterPro; IPR013657; UAA.
DR PANTHER; PTHR10778; PTHR10778; 1.
DR Pfam; PF08449; UAA; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Golgi apparatus; Membrane; Phosphoprotein;
KW Reference proteome; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..432
FT /note="Adenosine 3'-phospho 5'-phosphosulfate transporter
FT 1"
FT /id="PRO_0000213374"
FT TRANSMEM 5..25
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 40..60
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 109..129
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 154..174
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 238..258
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 265..285
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 299..319
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 353..373
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 387..407
FT /note="Helical"
FT /evidence="ECO:0000255"
FT MOD_RES 427
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18691976,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT VAR_SEQ 1..133
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_057436"
FT VAR_SEQ 1..49
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|Ref.2"
FT /id="VSP_026949"
FT VAR_SEQ 1..27
FT /note="MDARWWAVVVLAAFPSLGAGGETPEAP -> MLLAMPALWYLATSWCSTSGG
FT RTTWRP (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_054696"
FT VAR_SEQ 28..120
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_054697"
FT VAR_SEQ 272..311
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:12761501"
FT /id="VSP_014084"
FT VARIANT 342
FT /note="L -> V (in dbSNP:rs3734707)"
FT /evidence="ECO:0000269|PubMed:14702039"
FT /id="VAR_022657"
FT CONFLICT 214
FT /note="L -> P (in Ref. 8; BAD96748)"
FT /evidence="ECO:0000305"
FT CONFLICT 336
FT /note="E -> G (in Ref. 5; BAC11631)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 432 AA; 47515 MW; 7E4E9E87231072FB CRC64;
MDARWWAVVV LAAFPSLGAG GETPEAPPES WTQLWFFRFV VNAAGYASFM VPGYLLVQYF
RRKNYLETGR GLCFPLVKAC VFGNEPKASD EVPLAPRTEA AETTPMWQAL KLLFCATGLQ
VSYLTWGVLQ ERVMTRSYGA TATSPGERFT DSQFLVLMNR VLALIVAGLS CVLCKQPRHG
APMYRYSFAS LSNVLSSWCQ YEALKFVSFP TQVLAKASKV IPVMLMGKLV SRRSYEHWEY
LTATLISIGV SMFLLSSGPE PRSSPATTLS GLILLAGYIA FDSFTSNWQD ALFAYKMSSV
QMMFGVNFFS CLFTVGSLLE QGALLEGTRF MGRHSEFAAH ALLLSICSAC GQLFIFYTIG
QFGAAVFTII MTLRQAFAIL LSCLLYGHTV TVVGGLGVAV VFAALLLRVY ARGRLKQRGK
KAVPVESPVQ KV
