CHSS2_HUMAN
ID CHSS2_HUMAN Reviewed; 775 AA.
AC Q8IZ52; B4DXU0; Q6UXD6; Q7L4G1; Q9H0F8; Q9H618;
DT 01-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT 02-NOV-2010, sequence version 2.
DT 03-AUG-2022, entry version 166.
DE RecName: Full=Chondroitin sulfate synthase 2 {ECO:0000305};
DE EC=2.4.1.175 {ECO:0000269|PubMed:12761225};
DE EC=2.4.1.226 {ECO:0000269|PubMed:12761225};
DE AltName: Full=Chondroitin glucuronyltransferase 2;
DE AltName: Full=Chondroitin-polymerizing factor;
DE Short=ChPF;
DE AltName: Full=Glucuronosyl-N-acetylgalactosaminyl-proteoglycan 4-beta-N-acetylgalactosaminyltransferase II;
DE AltName: Full=N-acetylgalactosaminyl-proteoglycan 3-beta-glucuronosyltransferase II;
DE AltName: Full=N-acetylgalactosaminyltransferase 2;
GN Name=CHPF {ECO:0000312|HGNC:HGNC:24291}; Synonyms=CSS2;
GN ORFNames=UNQ651/PRO1281;
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), TISSUE SPECIFICITY, VARIANT
RP ARG-371, AND FUNCTION.
RX PubMed=12716890; DOI=10.1074/jbc.m302493200;
RA Kitagawa H., Izumikawa T., Uyama T., Sugahara K.;
RT "Molecular cloning of a chondroitin polymerizing factor that cooperates
RT with chondroitin synthase for chondroitin polymerization.";
RL J. Biol. Chem. 278:23666-23671(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, COFACTOR, TISSUE
RP SPECIFICITY, VARIANT ARG-371, AND CATALYTIC ACTIVITY.
RX PubMed=12761225; DOI=10.1074/jbc.m303657200;
RA Yada T., Gotoh M., Sato T., Shionyu M., Go M., Kaseyama H., Iwasaki H.,
RA Kikuchi N., Kwon Y.-D., Togayachi A., Kudo T., Watanabe H., Narimatsu H.,
RA Kimata K.;
RT "Chondroitin sulfate synthase-2. Molecular cloning and characterization of
RT a novel human glycosyltransferase homologous to chondroitin sulfate
RT glucuronyltransferase, which has dual enzymatic activities.";
RL J. Biol. Chem. 278:30235-30247(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT ARG-371.
RX PubMed=12975309; DOI=10.1101/gr.1293003;
RA Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J.,
RA Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P.,
RA Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S., Huang A.,
RA Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D.,
RA Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L.,
RA Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C.,
RA Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J.,
RA Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M.;
RT "The secreted protein discovery initiative (SPDI), a large-scale effort to
RT identify novel human secreted and transmembrane proteins: a bioinformatics
RT assessment.";
RL Genome Res. 13:2265-2270(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3), AND VARIANT
RP ARG-371.
RC TISSUE=Small intestine;
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 GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 4.";
RL Nature 434:724-731(2005).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT ARG-371.
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 [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT ARG-371.
RC TISSUE=Brain, Muscle, and Skin;
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 210-775, AND VARIANT ARG-371.
RC TISSUE=Testis;
RX PubMed=11230166; DOI=10.1101/gr.gr1547r;
RA Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S.,
RA Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H., Lauber J.,
RA Duesterhoeft A., Beyer A., Koehrer K., Strack N., Mewes H.-W.,
RA Ottenwaelder B., Obermaier B., Tampe J., Heubner D., Wambutt R., Korn B.,
RA Klein M., Poustka A.;
RT "Towards a catalog of human genes and proteins: sequencing and analysis of
RT 500 novel complete protein coding human cDNAs.";
RL Genome Res. 11:422-435(2001).
RN [9]
RP ALTERNATIVE SPLICING, FUNCTION (ISOFORM 2), INTERACTION WITH PRKN,
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=22082830; DOI=10.1093/hmg/ddr530;
RA Kuroda Y., Sako W., Goto S., Sawada T., Uchida D., Izumi Y., Takahashi T.,
RA Kagawa N., Matsumoto M., Matsumoto M., Takahashi R., Kaji R., Mitsui T.;
RT "Parkin interacts with Klokin1 for mitochondrial import and maintenance of
RT membrane potential.";
RL Hum. Mol. Genet. 21:991-1003(2012).
CC -!- FUNCTION: Has both beta-1,3-glucuronic acid and beta-1,4-N-
CC acetylgalactosamine transferase activity. Transfers glucuronic acid
CC (GlcUA) from UDP-GlcUA and N-acetylgalactosamine (GalNAc) from UDP-
CC GalNAc to the non-reducing end of the elongating chondroitin polymer.
CC Seems to act as a specific activating factor for CHSY1 in chondroitin
CC polymerization (PubMed:12716890). {ECO:0000269|PubMed:12716890,
CC ECO:0000269|PubMed:12761225}.
CC -!- FUNCTION: [Isoform 2]: May facilitate PRKN transport into the
CC mitochondria. In collaboration with PRKN, may enhance cell viability
CC and protect cells from oxidative stress. {ECO:0000269|PubMed:22082830}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3-O-(beta-D-GlcA-(1->3)-beta-D-GalNAc-(1->4)-beta-D-GlcA-
CC (1->3)-beta-D-Gal-(1->3)-beta-D-Gal-(1->4)-beta-D-Xyl)-L-seryl-
CC [protein] + UDP-N-acetyl-alpha-D-galactosamine = 3-O-(beta-D-GalNAc-
CC (1->4)-beta-D-GlcA-(1->3)-beta-D-GalNAc-(1->4)-beta-D-GlcA-(1->3)-
CC beta-D-Gal-(1->3)-beta-D-Gal-(1->4)-beta-D-Xyl)-L-seryl-[protein] +
CC H(+) + UDP; Xref=Rhea:RHEA:20800, Rhea:RHEA-COMP:14058, Rhea:RHEA-
CC COMP:14059, ChEBI:CHEBI:15378, ChEBI:CHEBI:58223, ChEBI:CHEBI:67138,
CC ChEBI:CHEBI:138442, ChEBI:CHEBI:138443; EC=2.4.1.175;
CC Evidence={ECO:0000269|PubMed:12761225};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:20801;
CC Evidence={ECO:0000305|PubMed:12761225};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3-O-(beta-D-GlcA-(1->3)-[beta-D-GalNAc-(1->4)-beta-D-GlcA-
CC (1->3)](n)-beta-D-GalNAc-(1->4)-beta-D-GlcA-(1->3)-beta-D-Gal-(1->3)-
CC beta-D-Gal-(1->4)-beta-D-Xyl)-L-seryl-[protein] + UDP-N-acetyl-alpha-
CC D-galactosamine = 3-O-([beta-D-GalNAc-(1->4)-beta-D-GlcA-
CC (1->3)](n+1)-beta-D-GalNAc-(1->4)-beta-D-GlcA-(1->3)-beta-D-Gal-
CC (1->3)-beta-D-Gal-(1->4)-beta-D-Xyl)-L-seryl-[protein] + H(+) + UDP;
CC Xref=Rhea:RHEA:55000, Rhea:RHEA-COMP:14060, Rhea:RHEA-COMP:14301,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:58223, ChEBI:CHEBI:67138,
CC ChEBI:CHEBI:138444, ChEBI:CHEBI:138445; EC=2.4.1.175;
CC Evidence={ECO:0000269|PubMed:12761225};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:55001;
CC Evidence={ECO:0000305|PubMed:12761225};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3-O-(beta-D-GalNAc-(1->4)-beta-D-GlcA-(1->3)-beta-D-Gal-
CC (1->3)-beta-D-Gal-(1->4)-beta-D-Xyl)-L-seryl-[protein] + UDP-alpha-D-
CC glucuronate = 3-O-(beta-D-GlcA-(1->3)-beta-D-GalNAc-(1->4)-beta-D-
CC GlcA-(1->3)-beta-D-Gal-(1->3)-beta-D-Gal-(1->4)-beta-D-Xyl)-L-seryl-
CC [protein] + H(+) + UDP; Xref=Rhea:RHEA:23428, Rhea:RHEA-COMP:12575,
CC Rhea:RHEA-COMP:14058, ChEBI:CHEBI:15378, ChEBI:CHEBI:58052,
CC ChEBI:CHEBI:58223, ChEBI:CHEBI:132105, ChEBI:CHEBI:138442;
CC EC=2.4.1.226; Evidence={ECO:0000269|PubMed:12761225};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:23429;
CC Evidence={ECO:0000305|PubMed:12761225};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3-O-([beta-D-GalNAc-(1->4)-beta-D-GlcA-(1->3)](n)-beta-D-
CC GalNAc-(1->4)-beta-D-GlcA-(1->3)-beta-D-Gal-(1->3)-beta-D-Gal-(1->4)-
CC beta-D-Xyl)-L-seryl-[protein] + UDP-alpha-D-glucuronate = 3-O-(beta-
CC D-GlcA-(1->3)-[beta-D-GalNAc-(1->4)-beta-D-GlcA-(1->3)](n)-beta-D-
CC GalNAc-(1->4)-beta-D-GlcA-(1->3)-beta-D-Gal-(1->3)-beta-D-Gal-(1->4)-
CC beta-D-Xyl)-L-seryl-[protein] + H(+) + UDP; Xref=Rhea:RHEA:54996,
CC Rhea:RHEA-COMP:14060, Rhea:RHEA-COMP:14061, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:58052, ChEBI:CHEBI:58223, ChEBI:CHEBI:138444,
CC ChEBI:CHEBI:138445; EC=2.4.1.226;
CC Evidence={ECO:0000269|PubMed:12761225};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:54997;
CC Evidence={ECO:0000305|PubMed:12761225};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000269|PubMed:12761225};
CC Name=Co(2+); Xref=ChEBI:CHEBI:48828;
CC Evidence={ECO:0000269|PubMed:12761225};
CC Note=Highest activities are measured with Mn(2+). Can also utilize
CC Co(2+). {ECO:0000269|PubMed:12761225};
CC -!- SUBUNIT: [Isoform 1]: Interacts with PRKN.
CC {ECO:0000269|PubMed:22082830}.
CC -!- SUBUNIT: [Isoform 2]: Interacts with PRKN.
CC {ECO:0000269|PubMed:22082830}.
CC -!- SUBUNIT: [Isoform 3]: Interacts with PRKN.
CC {ECO:0000269|PubMed:22082830}.
CC -!- INTERACTION:
CC Q8IZ52-2; O60260: PRKN; NbExp=5; IntAct=EBI-9029620, EBI-716346;
CC -!- SUBCELLULAR LOCATION: [Isoform 1]: Golgi apparatus, Golgi stack
CC membrane {ECO:0000305}; Single-pass type II membrane protein
CC {ECO:0000305}. Cytoplasm, cytosol {ECO:0000269|PubMed:22082830}.
CC -!- SUBCELLULAR LOCATION: [Isoform 3]: Cytoplasm, cytosol
CC {ECO:0000269|PubMed:22082830}. Mitochondrion
CC {ECO:0000269|PubMed:22082830}.
CC -!- SUBCELLULAR LOCATION: [Isoform 2]: Mitochondrion matrix
CC {ECO:0000269|PubMed:22082830}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q8IZ52-1; Sequence=Displayed;
CC Name=2; Synonyms=Klokin1;
CC IsoId=Q8IZ52-2; Sequence=VSP_053433;
CC Name=3; Synonyms=ChPF(D996);
CC IsoId=Q8IZ52-4; Sequence=VSP_053434;
CC -!- TISSUE SPECIFICITY: Ubiquitous. Highly expressed in pancreas, ovary,
CC brain, heart, skeletal muscle, colon, kidney, liver, stomach, spleen
CC and placenta. {ECO:0000269|PubMed:12716890,
CC ECO:0000269|PubMed:12761225}.
CC -!- TISSUE SPECIFICITY: [Isoform 2]: Expressed in brain, spleen, ovary,
CC testis, lung and peripheral mononuclear cells.
CC {ECO:0000269|PubMed:22082830}.
CC -!- TISSUE SPECIFICITY: [Isoform 3]: Also ubiquitous.
CC {ECO:0000269|PubMed:22082830}.
CC -!- SIMILARITY: Belongs to the chondroitin N-
CC acetylgalactosaminyltransferase family. {ECO:0000305}.
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DR EMBL; AB095813; BAC78393.1; -; mRNA.
DR EMBL; AB086063; BAC81536.1; -; mRNA.
DR EMBL; AY358403; AAQ88769.1; -; mRNA.
DR EMBL; AK026331; BAB15449.1; -; mRNA.
DR EMBL; AK302124; BAG63502.1; -; mRNA.
DR EMBL; AC009955; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471063; EAW70768.1; -; Genomic_DNA.
DR EMBL; BC008878; AAH08878.2; -; mRNA.
DR EMBL; BC021223; AAH21223.2; -; mRNA.
DR EMBL; BC023531; AAH23531.1; -; mRNA.
DR EMBL; AL136814; CAB66748.2; -; mRNA.
DR CCDS; CCDS2443.1; -. [Q8IZ52-1]
DR CCDS; CCDS56169.1; -. [Q8IZ52-4]
DR RefSeq; NP_001182660.1; NM_001195731.1. [Q8IZ52-4]
DR RefSeq; NP_078812.2; NM_024536.5. [Q8IZ52-1]
DR AlphaFoldDB; Q8IZ52; -.
DR BioGRID; 122729; 65.
DR IntAct; Q8IZ52; 18.
DR MINT; Q8IZ52; -.
DR STRING; 9606.ENSP00000243776; -.
DR CAZy; GT31; Glycosyltransferase Family 31.
DR CAZy; GT7; Glycosyltransferase Family 7.
DR GlyGen; Q8IZ52; 2 sites.
DR iPTMnet; Q8IZ52; -.
DR PhosphoSitePlus; Q8IZ52; -.
DR BioMuta; CHPF; -.
DR DMDM; 311033361; -.
DR EPD; Q8IZ52; -.
DR jPOST; Q8IZ52; -.
DR MassIVE; Q8IZ52; -.
DR MaxQB; Q8IZ52; -.
DR PaxDb; Q8IZ52; -.
DR PeptideAtlas; Q8IZ52; -.
DR PRIDE; Q8IZ52; -.
DR ProteomicsDB; 71279; -. [Q8IZ52-1]
DR Antibodypedia; 34339; 206 antibodies from 28 providers.
DR DNASU; 79586; -.
DR Ensembl; ENST00000243776.11; ENSP00000243776.6; ENSG00000123989.15. [Q8IZ52-1]
DR Ensembl; ENST00000535926.3; ENSP00000445571.1; ENSG00000123989.15. [Q8IZ52-4]
DR GeneID; 79586; -.
DR KEGG; hsa:79586; -.
DR MANE-Select; ENST00000243776.11; ENSP00000243776.6; NM_024536.6; NP_078812.3.
DR UCSC; uc002vmc.5; human. [Q8IZ52-1]
DR CTD; 79586; -.
DR DisGeNET; 79586; -.
DR GeneCards; CHPF; -.
DR HGNC; HGNC:24291; CHPF.
DR HPA; ENSG00000123989; Low tissue specificity.
DR MIM; 610405; gene.
DR neXtProt; NX_Q8IZ52; -.
DR OpenTargets; ENSG00000123989; -.
DR PharmGKB; PA162382245; -.
DR VEuPathDB; HostDB:ENSG00000123989; -.
DR eggNOG; KOG3708; Eukaryota.
DR GeneTree; ENSGT01050000244857; -.
DR HOGENOM; CLU_016244_1_0_1; -.
DR InParanoid; Q8IZ52; -.
DR OMA; MEGKYCY; -.
DR OrthoDB; 758579at2759; -.
DR PhylomeDB; Q8IZ52; -.
DR TreeFam; TF318303; -.
DR BioCyc; MetaCyc:HS13103-MON; -.
DR BRENDA; 2.4.1.175; 2681.
DR BRENDA; 2.4.1.226; 2681.
DR PathwayCommons; Q8IZ52; -.
DR Reactome; R-HSA-2022870; Chondroitin sulfate biosynthesis.
DR SignaLink; Q8IZ52; -.
DR BioGRID-ORCS; 79586; 16 hits in 1085 CRISPR screens.
DR ChiTaRS; CHPF; human.
DR GeneWiki; CHPF; -.
DR GenomeRNAi; 79586; -.
DR Pharos; Q8IZ52; Tbio.
DR PRO; PR:Q8IZ52; -.
DR Proteomes; UP000005640; Chromosome 2.
DR RNAct; Q8IZ52; protein.
DR Bgee; ENSG00000123989; Expressed in decidua and 160 other tissues.
DR ExpressionAtlas; Q8IZ52; baseline and differential.
DR Genevisible; Q8IZ52; HS.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0032580; C:Golgi cisterna membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0000139; C:Golgi membrane; TAS:Reactome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR GO; GO:0008376; F:acetylgalactosaminyltransferase activity; IBA:GO_Central.
DR GO; GO:0047238; F:glucuronosyl-N-acetylgalactosaminyl-proteoglycan 4-beta-N-acetylgalactosaminyltransferase activity; IDA:FlyBase.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0050510; F:N-acetylgalactosaminyl-proteoglycan 3-beta-glucuronosyltransferase activity; IDA:FlyBase.
DR GO; GO:0030206; P:chondroitin sulfate biosynthetic process; IDA:FlyBase.
DR InterPro; IPR008428; Chond_GalNAc.
DR Pfam; PF05679; CHGN; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cytoplasm; Glycoprotein; Golgi apparatus; Membrane;
KW Metal-binding; Mitochondrion; Reference proteome; Signal-anchor;
KW Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..775
FT /note="Chondroitin sulfate synthase 2"
FT /id="PRO_0000189560"
FT TOPO_DOM 1..15
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 16..34
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 35..775
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT REGION 37..100
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 617
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000255"
FT CARBOHYD 138
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 361
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 1..460
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_053433"
FT VAR_SEQ 1..162
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_053434"
FT VARIANT 371
FT /note="Q -> R (in dbSNP:rs6436155)"
FT /evidence="ECO:0000269|PubMed:11230166,
FT ECO:0000269|PubMed:12716890, ECO:0000269|PubMed:12761225,
FT ECO:0000269|PubMed:12975309, ECO:0000269|PubMed:14702039,
FT ECO:0000269|PubMed:15489334, ECO:0000269|Ref.6"
FT /id="VAR_047394"
FT CONFLICT 650
FT /note="A -> G (in Ref. 3; AAQ88769)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 775 AA; 85467 MW; 94EDDB2481C97B70 CRC64;
MRASLLLSVL RPAGPVAVGI SLGFTLSLLS VTWVEEPCGP GPPQPGDSEL PPRGNTNAAR
RPNSVQPGAE REKPGAGEGA GENWEPRVLP YHPAQPGQAA KKAVRTRYIS TELGIRQRLL
VAVLTSQTTL PTLGVAVNRT LGHRLERVVF LTGARGRRAP PGMAVVTLGE ERPIGHLHLA
LRHLLEQHGD DFDWFFLVPD TTYTEAHGLA RLTGHLSLAS AAHLYLGRPQ DFIGGEPTPG
RYCHGGFGVL LSRMLLQQLR PHLEGCRNDI VSARPDEWLG RCILDATGVG CTGDHEGVHY
SHLELSPGEP VQEGDPHFRS ALTAHPVRDP VHMYQLHKAF ARAELERTYQ EIQELQWEIQ
NTSHLAVDGD QAAAWPVGIP APSRPASRFE VLRWDYFTEQ HAFSCADGSP RCPLRGADRA
DVADVLGTAL EELNRRYHPA LRLQKQQLVN GYRRFDPARG MEYTLDLQLE ALTPQGGRRP
LTRRVQLLRP LSRVEILPVP YVTEASRLTV LLPLAAAERD LAPGFLEAFA TAALEPGDAA
AALTLLLLYE PRQAQRVAHA DVFAPVKAHV AELERRFPGA RVPWLSVQTA APSPLRLMDL
LSKKHPLDTL FLLAGPDTVL TPDFLNRCRM HAISGWQAFF PMHFQAFHPA VAPPQGPGPP
ELGRDTGRFD RQAASEACFY NSDYVAARGR LAAASEQEEE LLESLDVYEL FLHFSSLHVL
RAVEPALLQR YRAQTCSARL SEDLYHRCLQ SVLEGLGSRT QLAMLLFEQE QGNST
