ID KTAP2_HUMAN Reviewed; 136 AA. AC Q8N6L1; B2R4Q1; Q6PG45; Q86XW2; Q8IWS4; DT 07-MAR-2006, integrated into UniProtKB/Swiss-Prot. DT 13-NOV-2013, sequence version 2. DT 02-JUN-2021, entry version 139. DE RecName: Full=Keratinocyte-associated protein 2; DE Short=KCP-2; DE AltName: Full=Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit KCP2; DE Short=Oligosaccharyl transferase subunit KCP2; GN Name=KRTCAP2; Synonyms=KCP2; 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), AND TISSUE SPECIFICITY. RC TISSUE=Keratinocyte; RX PubMed=12752121; DOI=10.1046/j.1365-2133.2003.05244.x; RA Bonkobara M., Das A., Takao J., Cruz P.D. Jr., Ariizumi K.; RT "Identification of novel genes for secreted and membrane-anchored proteins RT in human keratinocytes."; RL Br. J. Dermatol. 148:654-664(2003). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). RC TISSUE=Testis; 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 GENOMIC DNA]. RX PubMed=16710414; DOI=10.1038/nature04727; RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K., RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.; RT "The DNA sequence and biological annotation of human chromosome 1."; RL Nature 441:315-321(2006). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND VARIANT VAL-4. RC TISSUE=Brain, Colon, Kidney, and Stomach; 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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-124, AND IDENTIFICATION BY RP 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 [6] 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 [7] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-124, 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 [8] 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 [9] RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH PSEN1 AND NCSTN. RX PubMed=21768116; DOI=10.1074/jbc.m111.249748; RA Wilson C.M., Magnaudeix A., Yardin C., Terro F.; RT "DC2 and keratinocyte-associated protein 2 (KCP2), subunits of the RT oligosaccharyltransferase complex, are regulators of the gamma-secretase- RT directed processing of amyloid precursor protein (APP)."; RL J. Biol. Chem. 286:31080-31091(2011). RN [10] RP SUBUNIT, SUBCELLULAR LOCATION, ER RETENTION MOTIF, TOPOLOGY, ALTERNATIVE RP INITIATION, AND INTERACTION WITH STT3A. RX PubMed=22266900; DOI=10.1242/jcs.094599; RA Roboti P., High S.; RT "Keratinocyte-associated protein 2 is a bona fide subunit of the mammalian RT oligosaccharyltransferase."; RL J. Cell Sci. 125:220-232(2012). RN [11] RP FUNCTION. RX PubMed=22467853; DOI=10.1242/jcs.103952; RA Roboti P., High S.; RT "The oligosaccharyltransferase subunits OST48, DAD1 and KCP2 function as RT ubiquitous and selective modulators of mammalian N-glycosylation."; RL J. Cell Sci. 125:3474-3484(2012). RN [12] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-124, AND IDENTIFICATION BY RP 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 -!- FUNCTION: Subunit of the oligosaccharyl transferase (OST) complex that CC catalyzes the initial transfer of a defined glycan CC (Glc(3)Man(9)GlcNAc(2) in eukaryotes) from the lipid carrier dolichol- CC pyrophosphate to an asparagine residue within an Asn-X-Ser/Thr CC consensus motif in nascent polypeptide chains, the first step in CC protein N-glycosylation. N-glycosylation occurs cotranslationally and CC the complex associates with the Sec61 complex at the channel-forming CC translocon complex that mediates protein translocation across the CC endoplasmic reticulum (ER). All subunits are required for a maximal CC enzyme activity (PubMed:22467853). May be involved in N-glycosylation CC of APP (amyloid-beta precursor protein). Can modulate gamma-secretase CC cleavage of APP by enhancing endoprotelysis of PSEN1 (PubMed:21768116). CC {ECO:0000269|PubMed:21768116, ECO:0000269|PubMed:22467853}. CC -!- PATHWAY: Protein modification; protein glycosylation. CC -!- SUBUNIT: Component of the oligosaccharyltransferase (OST) complex. OST CC exists in two different complex forms which contain common core CC subunits RPN1, RPN2, OST48, OST4, DAD1 and TMEM258, either STT3A or CC STT3B as catalytic subunits, and form-specific accessory subunits CC (PubMed:22266900). STT3A complex assembly occurs through the formation CC of 3 subcomplexes. Subcomplex 1 contains RPN1 and TMEM258, subcomplex 2 CC contains the STT3A-specific subunits STT3A, DC2/OSTC, and KCP2 as well CC as the core subunit OST4, and subcomplex 3 contains RPN2, DAD1, and CC OST48. The STT3A complex can form stable complexes with the Sec61 CC complex or with both the Sec61 and TRAP complexes (By similarity). CC Interacts with PSEN1 and NCSTN; indicative for an association with the CC gamma-secretase complex (PubMed:21768116). CC {ECO:0000250|UniProtKB:P86229, ECO:0000269|PubMed:21768116, CC ECO:0000269|PubMed:22266900}. CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum CC {ECO:0000269|PubMed:21768116}. Endoplasmic reticulum membrane CC {ECO:0000269|PubMed:22266900}; Multi-pass membrane protein CC {ECO:0000269|PubMed:22266900}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative initiation; Named isoforms=2; CC Name=1; CC IsoId=Q8N6L1-1; Sequence=Displayed; CC Name=2; CC IsoId=Q8N6L1-2; Sequence=VSP_053439; CC -!- TISSUE SPECIFICITY: Expressed in skin, heart, placental, liver, CC skeletal muscle, kidney, pancreas, keratinocytes and dermal CC fibroblasts. {ECO:0000269|PubMed:12752121}. CC -!- MISCELLANEOUS: [Isoform 2]: Produced at low levels due to suboptimal CC Kozak context. {ECO:0000305}. CC -!- SIMILARITY: Belongs to the KRTCAP2 family. {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; AY157577; AAO13161.2; -; mRNA. DR EMBL; AK311907; BAG34848.1; -; mRNA. DR EMBL; AL607067; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC029806; AAH29806.1; -; mRNA. DR EMBL; BC048205; AAH48205.1; -; mRNA. DR EMBL; BC057233; AAH57233.1; -; mRNA. DR CCDS; CCDS1096.1; -. [Q8N6L1-1] DR RefSeq; NP_776251.1; NM_173852.3. [Q8N6L1-1] DR BioGRID; 128307; 13. DR IntAct; Q8N6L1; 10. DR MINT; Q8N6L1; -. DR STRING; 9606.ENSP00000295682; -. DR iPTMnet; Q8N6L1; -. DR PhosphoSitePlus; Q8N6L1; -. DR SwissPalm; Q8N6L1; -. DR BioMuta; KRTCAP2; -. DR DMDM; 557952588; -. DR EPD; Q8N6L1; -. DR jPOST; Q8N6L1; -. DR MassIVE; Q8N6L1; -. DR MaxQB; Q8N6L1; -. DR PaxDb; Q8N6L1; -. DR PeptideAtlas; Q8N6L1; -. DR PRIDE; Q8N6L1; -. DR ProteomicsDB; 72188; -. [Q8N6L1-1] DR TopDownProteomics; Q8N6L1-2; -. [Q8N6L1-2] DR Antibodypedia; 56363; 67 antibodies. DR DNASU; 200185; -. DR Ensembl; ENST00000295682; ENSP00000295682; ENSG00000163463. [Q8N6L1-1] DR GeneID; 200185; -. DR KEGG; hsa:200185; -. DR UCSC; uc001fho.4; human. [Q8N6L1-1] DR CTD; 200185; -. DR DisGeNET; 200185; -. DR GeneCards; KRTCAP2; -. DR HGNC; HGNC:28942; KRTCAP2. DR HPA; ENSG00000163463; Low tissue specificity. DR MIM; 619029; gene. DR neXtProt; NX_Q8N6L1; -. DR OpenTargets; ENSG00000163463; -. DR PharmGKB; PA134967679; -. DR VEuPathDB; HostDB:ENSG00000163463.11; -. DR eggNOG; KOG4615; Eukaryota. DR GeneTree; ENSGT00390000003552; -. DR HOGENOM; CLU_109648_2_0_1; -. DR InParanoid; Q8N6L1; -. DR OMA; LTCVSNA; -. DR OrthoDB; 1561955at2759; -. DR TreeFam; TF324347; -. DR PathwayCommons; Q8N6L1; -. DR UniPathway; UPA00378; -. DR BioGRID-ORCS; 200185; 43 hits in 998 CRISPR screens. DR ChiTaRS; KRTCAP2; human. DR GenomeRNAi; 200185; -. DR Pharos; Q8N6L1; Tbio. DR PRO; PR:Q8N6L1; -. DR Proteomes; UP000005640; Chromosome 1. DR RNAct; Q8N6L1; protein. DR Bgee; ENSG00000163463; Expressed in right testis and 155 other tissues. DR Genevisible; Q8N6L1; HS. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0008250; C:oligosaccharyltransferase complex; IDA:ARUK-UCL. DR GO; GO:0008047; F:enzyme activator activity; IMP:ARUK-UCL. DR GO; GO:0006487; P:protein N-linked glycosylation; IMP:ARUK-UCL. DR GO; GO:0042543; P:protein N-linked glycosylation via arginine; IMP:UniProtKB. DR InterPro; IPR018614; KRTCAP2. DR PANTHER; PTHR32001; PTHR32001; 1. DR Pfam; PF09775; Keratin_assoc; 1. PE 1: Evidence at protein level; KW Alternative initiation; Endoplasmic reticulum; Membrane; Phosphoprotein; KW Reference proteome; Transmembrane; Transmembrane helix. FT CHAIN 1..136 FT /note="Keratinocyte-associated protein 2" FT /id="PRO_0000226992" FT TOPO_DOM 1..5 FT /note="Lumenal" FT /evidence="ECO:0000255" FT TRANSMEM 6..23 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 24..34 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 35..55 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 56..75 FT /note="Lumenal" FT /evidence="ECO:0000255" FT TRANSMEM 76..108 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 109..136 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT MOTIF 133..136 FT /note="Prevents secretion from ER" FT /evidence="ECO:0000255" FT MOD_RES 124 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163" FT VAR_SEQ 1 FT /note="M -> MRIANRTRFSSPFLARGAGWTHGRGMM (in isoform 2)" FT /evidence="ECO:0000303|PubMed:14702039, FT ECO:0000303|PubMed:15489334" FT /id="VSP_053439" FT VARIANT 4 FT /note="G -> V (in dbSNP:rs17854920)" FT /evidence="ECO:0000269|PubMed:15489334" FT /id="VAR_025531" FT CONFLICT 87 FT /note="G -> S (in Ref. 4; AAO13161)" FT /evidence="ECO:0000305" SQ SEQUENCE 136 AA; 14679 MW; 090926F115D7532B CRC64; MVVGTGTSLA LSSLLSLLLF AGMQMYSRQL ASTEWLTIQG GLLGSGLFVF SLTAFNNLEN LVFGKGFQAK IFPEILLCLL LALFASGLIH RVCVTTCFIF SMVGLYYINK ISSTLYQAAA PVLTPAKVTG KSKKRN //