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CHSTD_HUMAN
ID   CHSTD_HUMAN             Reviewed;         341 AA.
AC   Q8NET6; Q3SYA3; Q3SYA5;
DT   15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   03-AUG-2022, entry version 144.
DE   RecName: Full=Carbohydrate sulfotransferase 13;
DE            EC=2.8.2.5;
DE   AltName: Full=Chondroitin 4-O-sulfotransferase 3;
DE   AltName: Full=Chondroitin 4-sulfotransferase 3;
DE            Short=C4ST-3;
DE            Short=C4ST3;
GN   Name=CHST13;
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), ENZYME ACTIVITY, AND TISSUE
RP   SPECIFICITY.
RX   PubMed=12080076; DOI=10.1074/jbc.m204907200;
RA   Kang H.-G., Evers M.R., Xia G., Baenziger J.U., Schachner M.;
RT   "Molecular cloning and characterization of chondroitin-4-O-
RT   sulfotransferase-3. A novel member of the HNK-1 family of
RT   sulfotransferases.";
RL   J. Biol. Chem. 277:34766-34772(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2), AND VARIANTS
RP   VAL-271 AND GLN-317.
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   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-139, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA   Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA   Ye M., Zou H.;
RT   "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT   phosphoproteome.";
RL   J. Proteomics 96:253-262(2014).
CC   -!- FUNCTION: Catalyzes the transfer of sulfate to position 4 of the N-
CC       acetylgalactosamine (GalNAc) residue of chondroitin. Chondroitin
CC       sulfate constitutes the predominant proteoglycan present in cartilage
CC       and is distributed on the surfaces of many cells and extracellular
CC       matrices. Transfers sulfate to the C4 hydroxyl of beta1,4-linked GalNAc
CC       that is substituted with a beta-linked glucuronic acid at the C-3
CC       hydroxyl. No activity toward dermatan.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=n 3'-phosphoadenylyl sulfate + chondroitin beta-D-glucuronate
CC         = n adenosine 3',5'-bisphosphate + chondroitin 4'-sulfate + n H(+);
CC         Xref=Rhea:RHEA:16101, Rhea:RHEA-COMP:9827, Rhea:RHEA-COMP:9829,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:57652, ChEBI:CHEBI:58339,
CC         ChEBI:CHEBI:58343, ChEBI:CHEBI:58422; EC=2.8.2.5;
CC         Evidence={ECO:0000269|PubMed:12080076};
CC   -!- INTERACTION:
CC       Q8NET6; Q5BVD1: TTMP; NbExp=3; IntAct=EBI-11599701, EBI-10243654;
CC   -!- SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000250}; Single-
CC       pass type II membrane protein {ECO:0000250}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q8NET6-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q8NET6-2; Sequence=VSP_057175, VSP_057176;
CC   -!- TISSUE SPECIFICITY: Highly expressed in adult liver. Expressed at lower
CC       level in kidney, lymph nodes and fetal kidney.
CC       {ECO:0000269|PubMed:12080076}.
CC   -!- SIMILARITY: Belongs to the sulfotransferase 2 family. {ECO:0000305}.
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DR   EMBL; AY120869; AAM55481.1; -; mRNA.
DR   EMBL; BC103895; AAI03896.1; -; mRNA.
DR   EMBL; BC103896; AAI03897.1; -; mRNA.
DR   EMBL; BC103897; AAI03898.1; -; mRNA.
DR   CCDS; CCDS3039.1; -. [Q8NET6-1]
DR   RefSeq; NP_690849.1; NM_152889.2. [Q8NET6-1]
DR   AlphaFoldDB; Q8NET6; -.
DR   BioGRID; 127923; 5.
DR   IntAct; Q8NET6; 2.
DR   STRING; 9606.ENSP00000317404; -.
DR   GlyGen; Q8NET6; 1 site.
DR   iPTMnet; Q8NET6; -.
DR   PhosphoSitePlus; Q8NET6; -.
DR   BioMuta; CHST13; -.
DR   EPD; Q8NET6; -.
DR   jPOST; Q8NET6; -.
DR   MassIVE; Q8NET6; -.
DR   MaxQB; Q8NET6; -.
DR   PaxDb; Q8NET6; -.
DR   PeptideAtlas; Q8NET6; -.
DR   PRIDE; Q8NET6; -.
DR   ProteomicsDB; 61850; -.
DR   ProteomicsDB; 73215; -. [Q8NET6-1]
DR   Antibodypedia; 33086; 139 antibodies from 26 providers.
DR   DNASU; 166012; -.
DR   Ensembl; ENST00000319340.7; ENSP00000317404.2; ENSG00000180767.11. [Q8NET6-1]
DR   GeneID; 166012; -.
DR   KEGG; hsa:166012; -.
DR   MANE-Select; ENST00000319340.7; ENSP00000317404.2; NM_152889.3; NP_690849.1.
DR   UCSC; uc003eja.4; human. [Q8NET6-1]
DR   CTD; 166012; -.
DR   DisGeNET; 166012; -.
DR   GeneCards; CHST13; -.
DR   HGNC; HGNC:21755; CHST13.
DR   HPA; ENSG00000180767; Group enriched (liver, testis).
DR   MIM; 610124; gene.
DR   neXtProt; NX_Q8NET6; -.
DR   OpenTargets; ENSG00000180767; -.
DR   PharmGKB; PA134976803; -.
DR   VEuPathDB; HostDB:ENSG00000180767; -.
DR   eggNOG; KOG4651; Eukaryota.
DR   GeneTree; ENSGT00940000161154; -.
DR   HOGENOM; CLU_043398_1_1_1; -.
DR   InParanoid; Q8NET6; -.
DR   OMA; RYFKHIS; -.
DR   OrthoDB; 1330889at2759; -.
DR   PhylomeDB; Q8NET6; -.
DR   TreeFam; TF325581; -.
DR   BioCyc; MetaCyc:HS11524-MON; -.
DR   BRENDA; 2.8.2.5; 2681.
DR   PathwayCommons; Q8NET6; -.
DR   Reactome; R-HSA-2022870; Chondroitin sulfate biosynthesis.
DR   SignaLink; Q8NET6; -.
DR   BioGRID-ORCS; 166012; 14 hits in 1066 CRISPR screens.
DR   ChiTaRS; CHST13; human.
DR   GenomeRNAi; 166012; -.
DR   Pharos; Q8NET6; Tbio.
DR   PRO; PR:Q8NET6; -.
DR   Proteomes; UP000005640; Chromosome 3.
DR   RNAct; Q8NET6; protein.
DR   Bgee; ENSG00000180767; Expressed in right lobe of liver and 87 other tissues.
DR   ExpressionAtlas; Q8NET6; baseline and differential.
DR   Genevisible; Q8NET6; HS.
DR   GO; GO:0000139; C:Golgi membrane; TAS:Reactome.
DR   GO; GO:0016021; C:integral component of membrane; NAS:UniProtKB.
DR   GO; GO:0047756; F:chondroitin 4-sulfotransferase activity; IDA:UniProtKB.
DR   GO; GO:0001537; F:N-acetylgalactosamine 4-O-sulfotransferase activity; IDA:UniProtKB.
DR   GO; GO:0008146; F:sulfotransferase activity; IBA:GO_Central.
DR   GO; GO:0016051; P:carbohydrate biosynthetic process; IEA:InterPro.
DR   GO; GO:0030206; P:chondroitin sulfate biosynthetic process; IDA:UniProtKB.
DR   GO; GO:0030166; P:proteoglycan biosynthetic process; IBA:GO_Central.
DR   InterPro; IPR018011; Carb_sulfotrans_8-10.
DR   InterPro; IPR005331; Sulfotransferase.
DR   PANTHER; PTHR12137; PTHR12137; 1.
DR   Pfam; PF03567; Sulfotransfer_2; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Carbohydrate metabolism; Glycoprotein;
KW   Golgi apparatus; Membrane; Phosphoprotein; Reference proteome;
KW   Signal-anchor; Transferase; Transmembrane; Transmembrane helix.
FT   CHAIN           1..341
FT                   /note="Carbohydrate sulfotransferase 13"
FT                   /id="PRO_0000189671"
FT   TOPO_DOM        1..9
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        10..30
FT                   /note="Helical; Signal-anchor for type II membrane protein"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        31..341
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   MOTIF           132..134
FT                   /note="Cell attachment site"
FT                   /evidence="ECO:0000255"
FT   BINDING         113..119
FT                   /ligand="3'-phosphoadenylyl sulfate"
FT                   /ligand_id="ChEBI:CHEBI:58339"
FT                   /evidence="ECO:0000250"
FT   BINDING         174..182
FT                   /ligand="3'-phosphoadenylyl sulfate"
FT                   /ligand_id="ChEBI:CHEBI:58339"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         139
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:24275569"
FT   CARBOHYD        331
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   VAR_SEQ         191..225
FT                   /note="PYSAAFQRRYGARIVQRLRPRALPDARARGHDVRF -> TRSATRVASATTS
FT                   WASSRRWRRTRPSCWAWRAHPT (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_057175"
FT   VAR_SEQ         226..341
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_057176"
FT   VARIANT         146
FT                   /note="P -> S (in dbSNP:rs34311016)"
FT                   /id="VAR_053698"
FT   VARIANT         271
FT                   /note="A -> V (in dbSNP:rs1056523)"
FT                   /evidence="ECO:0000269|PubMed:15489334"
FT                   /id="VAR_021477"
FT   VARIANT         317
FT                   /note="R -> Q (in dbSNP:rs1056522)"
FT                   /evidence="ECO:0000269|PubMed:15489334"
FT                   /id="VAR_021478"
SQ   SEQUENCE   341 AA;  38920 MW;  A372134675D661F6 CRC64;
     MGRRCCRRRV LAAACLGAAL LLLCAAPRSL RPAFGNRALG SSWLGGEKRS PLQKLYDLDQ
     DPRSTLAKVH RQRRDLLNSA CSRHSRRQRL LQPEDLRHVL VDDAHGLLYC YVPKVACTNW
     KRVLLALSGQ ARGDPRAISA QEAHAPGRLP SLADFSPAEI NRRLRAYLAF LFVREPFERL
     ASAYRNKLAR PYSAAFQRRY GARIVQRLRP RALPDARARG HDVRFAEFLA YLLDPRTRRE
     EPFNEHWERA HALCHPCRLR YDVVGKFETL AEDAAFVLGL AGASDLSFPG PPRPRGAAAS
     RDLAARLFRD ISPFYQRRLF DLYKMDFLLF NYSAPSYLRL L
 
 
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