ID H6ST2_HUMAN Reviewed; 605 AA. AC Q96MM7; B9WRT4; B9WRT5; Q2TB13; Q4VC07; Q6PIC4; Q86SM9; Q8N3T4; AC Q8NBN4; Q96SJ4; DT 11-OCT-2005, integrated into UniProtKB/Swiss-Prot. DT 11-OCT-2005, sequence version 2. DT 05-OCT-2010, entry version 60. DE RecName: Full=Heparan-sulfate 6-O-sulfotransferase 2; DE Short=HS6ST-2; DE EC=2.8.2.-; GN Name=HS6ST2; ORFNames=PSEC0092; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2 AND 3). RC TISSUE=Brain; RX PubMed=12492399; DOI=10.1042/BJ20021259; RA Habuchi H., Miyake G., Nogami K., Kuroiwa A., Matsuda Y., RA Kusche-Gullberg M., Habuchi O., Tanaka M., Kimata K.; RT "Biosynthesis of heparan sulphate with diverse structures and RT functions: two alternatively spliced forms of human heparan sulphate RT 6-O-sulphotransferase-2 having different expression patterns and RT properties."; RL Biochem. J. 371:131-142(2003). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2). RC TISSUE=Placenta; 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., RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., RA 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., RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., RA Nakai K., Yada T., Nakamura Y., Ohara O., 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 GENOMIC DNA]. RX PubMed=15772651; DOI=10.1038/nature03440; RA Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D., RA Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., RA Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., RA Jones M.C., Hurles M.E., Andrews T.D., Scott C.E., Searle S., RA Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R., RA Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L., RA Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A., RA Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S., RA Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R., RA Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M., RA Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N., RA Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D., RA Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W., RA Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C., RA Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C., RA Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S., RA Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S., RA Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., RA Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., RA Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., RA Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L., RA Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P., RA Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S., RA Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A., RA Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J., RA Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J., RA Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S., RA de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z., RA Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C., RA Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W., RA Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D., RA Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H., RA McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., RA Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., RA Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., RA Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J., RA Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E., RA Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S., RA Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K., RA Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D., RA Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R., RA Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., RA Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., RA Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L., RA Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A., RA Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L., RA Williams G., Williams L., Williamson A., Williamson H., Wilming L., RA Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H., RA Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A., RA Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F., RA Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., RA Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., RA Gibbs R.A., Beck S., Rogers J., Bentley D.R.; RT "The DNA sequence of the human X chromosome."; RL Nature 434:325-337(2005). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND NUCLEOTIDE RP SEQUENCE [LARGE SCALE MRNA] OF 176-605 (ISOFORM 3). 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 RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 136-605. RC TISSUE=Teratocarcinoma; 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- RT length human cDNAs encoding secretion or membrane proteins from oligo- RT capped cDNA libraries."; RL DNA Res. 12:117-126(2005). RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 465-605. RC TISSUE=Amygdala; RX PubMed=17974005; DOI=10.1186/1471-2164-8-399; RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., RA Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., RA Ottenwaelder B., Poustka A., Wiemann S., Schupp I.; RT "The full-ORF clone resource of the German cDNA consortium."; RL BMC Genomics 8:399-399(2007). CC -!- FUNCTION: 6-O-sulfation enzyme which catalyzes the transfer of CC sulfate from 3'-phosphoadenosine 5'-phosphosulfate (PAPS) to CC position 6 of the N-sulfoglucosamine residue (GlcNS) of heparan CC sulfate. CC -!- CATALYTIC ACTIVITY: 3'-phosphoadenylyl sulfate + [heparan CC sulfate]-glucosamine = adenosine 3',5'-bisphosphate + [heparan CC sulfate]-glucosamine 6-sulfate. CC -!- SUBCELLULAR LOCATION: Membrane; Single-pass type II membrane CC protein (Potential). CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=3; CC Name=1; CC IsoId=Q96MM7-1; Sequence=Displayed; CC Name=2; Synonyms=HS6ST-2S; CC IsoId=Q96MM7-2; Sequence=VSP_015846; CC Name=3; Synonyms=HS6ST-2; CC IsoId=Q96MM7-3; Sequence=VSP_015846, VSP_015847; CC Note=No experimental confirmation available; CC -!- SIMILARITY: Belongs to the sulfotransferase 6 family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AB067776; BAC07183.1; -; mRNA. DR EMBL; AB067777; BAC07184.1; -; mRNA. DR EMBL; AK027720; BAB55322.1; -; mRNA. DR EMBL; AK056706; BAB71260.1; -; mRNA. DR EMBL; Z81365; CAX30811.1; -; Genomic_DNA. DR EMBL; Z86064; CAX30811.1; JOINED; Genomic_DNA. DR EMBL; Z81365; CAX30812.1; -; Genomic_DNA. DR EMBL; Z86064; CAX30812.1; JOINED; Genomic_DNA. DR EMBL; AL022309; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AL022159; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; Z82205; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; Z86064; CAI42774.1; -; Genomic_DNA. DR EMBL; Z81365; CAI42774.1; JOINED; Genomic_DNA. DR EMBL; Z86064; CAI42775.1; -; Genomic_DNA. DR EMBL; Z81365; CAI42775.1; JOINED; Genomic_DNA. DR EMBL; BC037325; AAH37325.1; -; mRNA. DR EMBL; BC094718; AAH94718.1; -; mRNA. DR EMBL; BC110620; AAI10621.1; -; mRNA. DR EMBL; BC110621; AAI10622.1; -; mRNA. DR EMBL; AK075402; BAC11597.1; -; mRNA. DR EMBL; AL831923; CAD38583.1; -; mRNA. DR IPI; IPI00157454; -. DR IPI; IPI00160316; -. DR IPI; IPI00937318; -. DR RefSeq; NP_001070656.1; -. DR RefSeq; NP_671704.3; -. DR UniGene; Hs.385956; -. DR ProteinModelPortal; Q96MM7; -. DR STRING; Q96MM7; -. DR PRIDE; Q96MM7; -. DR Ensembl; ENST00000319809; ENSP00000324617; ENSG00000171004. DR Ensembl; ENST00000370833; ENSP00000359870; ENSG00000171004. DR Ensembl; ENST00000370836; ENSP00000359873; ENSG00000171004. DR Ensembl; ENST00000370837; ENSP00000359874; ENSG00000171004. DR Ensembl; ENST00000406696; ENSP00000384013; ENSG00000171004. DR GeneID; 90161; -. DR KEGG; hsa:90161; -. DR UCSC; uc004ewy.1; human. DR UCSC; uc004ewz.1; human. DR CTD; 90161; -. DR GeneCards; GC0XM131760; -. DR HGNC; HGNC:19133; HS6ST2. DR HPA; HPA034625; -. DR MIM; 300545; gene. DR PharmGKB; PA134950831; -. DR eggNOG; prNOG10538; -. DR HOVERGEN; HBG083012; -. DR OrthoDB; EOG9MGVT6; -. DR NextBio; 76561; -. DR ArrayExpress; Q96MM7; -. DR Bgee; Q96MM7; -. DR CleanEx; HS_HS6ST2; -. DR Genevestigator; Q96MM7; -. DR GermOnline; ENSG00000171004; Homo sapiens. DR GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW. DR GO; GO:0008146; F:sulfotransferase activity; IEA:InterPro. DR GO; GO:0016051; P:carbohydrate biosynthetic process; IEA:InterPro. DR InterPro; IPR010635; Heparan_SO4-6-sulfoTrfase. DR InterPro; IPR005331; Sulfotransferase. DR PANTHER; PTHR12812; HS6ST; 1. DR Pfam; PF03567; Sulfotransfer_2; 1. PE 2: Evidence at transcript level; KW Alternative splicing; Complete proteome; Glycoprotein; Membrane; KW Polymorphism; Signal-anchor; Transferase; Transmembrane; KW Transmembrane helix. FT CHAIN 1 605 Heparan-sulfate 6-O-sulfotransferase 2. FT /FTId=PRO_0000190805. FT TOPO_DOM 1 4 Cytoplasmic (Potential). FT TRANSMEM 5 27 Helical; Signal-anchor for type II FT membrane protein; (Potential). FT TOPO_DOM 28 605 Lumenal (Potential). FT REGION 236 242 5'-phosphosulfate-binding (Potential). FT REGION 325 333 3'-phosphate binding (Potential). FT CARBOHYD 209 209 N-linked (GlcNAc...) (Potential). FT CARBOHYD 404 404 N-linked (GlcNAc...) (Potential). FT CARBOHYD 460 460 N-linked (GlcNAc...) (Potential). FT CARBOHYD 544 544 N-linked (GlcNAc...) (Potential). FT CARBOHYD 556 556 N-linked (GlcNAc...) (Potential). FT CARBOHYD 564 564 N-linked (GlcNAc...) (Potential). FT CARBOHYD 589 589 N-linked (GlcNAc...) (Potential). FT CARBOHYD 592 592 N-linked (GlcNAc...) (Potential). FT VAR_SEQ 1 146 Missing (in isoform 2 and isoform 3). FT /FTId=VSP_015846. FT VAR_SEQ 315 316 SR -> SRWRIFQILDAASKDKRGSPNTNAGANSPSSTKTR FT NTSKSGK (in isoform 3). FT /FTId=VSP_015847. FT VARIANT 127 127 K -> N (in dbSNP:rs7053397). FT /FTId=VAR_061828. FT CONFLICT 192 192 D -> G (in Ref. 2; BAB71260). FT CONFLICT 299 299 C -> Y (in Ref. 4; AAH37325). FT CONFLICT 426 426 K -> R (in Ref. 5; BAC11597). FT CONFLICT 568 568 S -> N (in Ref. 2; BAB71260). FT CONFLICT 580 580 Q -> R (in Ref. 5; BAC11597). FT CONFLICT 585 585 E -> G (in Ref. 5; BAC11597). SQ SEQUENCE 605 AA; 69130 MW; 10528AC424935B13 CRC64; MALPACAVRE FEPPRQPERG APVRTTCPRR HSRVEAELAA SRPGSVAASV RAGPPRGVSH GFHTRPLLDK PRKASSSLAG AACAPLFALL SRGRRRRMHV LRRRWDLGSL CRALLTRGLA ALGHSLKHVL GAIFSKIFGP MASVGNMDEK SNKLLLALVM LFLFAVIVLQ YVCPGTECQL LRLQAFSSPV PDPYRSEDES SARFVPRYNF TRGDLLRKVD FDIKGDDLIV FLHIQKTGGT TFGRHLVRNI QLEQPCECRV GQKKCTCHRP GKRETWLFSR FSTGWSCGLH ADWTELTSCV PSVVDGKRDA RLRPSRNFHY ITILRDPVSR YLSEWRHVQR GATWKASLHV CDGRPPTSEE LPSCYTGDDW SGCPLKEFMD CPYNLANNRQ VRMLSDLTLV GCYNLSVMPE KQRNKVLLES AKSNLKHMAF FGLTEFQRKT QYLFEKTFNM NFISPFTQYN TTRASSVEIN EEIQKRIEGL NFLDMELYSY AKDLFLQRYQ FMRQKEHQEA RRKRQEQRKF LKGRLLQTHF QSQGQGQSQN PNQNQSQNPN PNANQNLTQN LMQNLTQSLS QKENRESPKQ NSGKEQNDNT SNGTNDYIGS VEKWR //