KTAP2_HUMAN
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 03-AUG-2022, entry version 143.
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}.
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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 AlphaFoldDB; Q8N6L1; -.
DR BioGRID; 128307; 45.
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 from 15 providers.
DR DNASU; 200185; -.
DR Ensembl; ENST00000295682.6; ENSP00000295682.5; ENSG00000163463.13. [Q8N6L1-1]
DR GeneID; 200185; -.
DR KEGG; hsa:200185; -.
DR MANE-Select; ENST00000295682.6; ENSP00000295682.5; NM_173852.4; NP_776251.2.
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; -.
DR eggNOG; KOG4615; Eukaryota.
DR GeneTree; ENSGT00390000003552; -.
DR HOGENOM; CLU_109648_2_0_1; -.
DR InParanoid; Q8N6L1; -.
DR OMA; EMVVFGQ; -.
DR OrthoDB; 1561955at2759; -.
DR TreeFam; TF324347; -.
DR PathwayCommons; Q8N6L1; -.
DR SignaLink; Q8N6L1; -.
DR UniPathway; UPA00378; -.
DR BioGRID-ORCS; 200185; 50 hits in 1081 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 107 other tissues.
DR ExpressionAtlas; Q8N6L1; baseline and differential.
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
