PLOD2_HUMAN
ID PLOD2_HUMAN Reviewed; 737 AA.
AC O00469; B3KWS3; Q59ED2; Q8N170;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 26-APR-2005, sequence version 2.
DT 03-AUG-2022, entry version 195.
DE RecName: Full=Procollagen-lysine,2-oxoglutarate 5-dioxygenase 2 {ECO:0000305};
DE EC=1.14.11.4 {ECO:0000250|UniProtKB:P24802};
DE AltName: Full=Lysyl hydroxylase 2;
DE Short=LH2;
DE Flags: Precursor;
GN Name=PLOD2 {ECO:0000312|HGNC:HGNC:9082};
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).
RC TISSUE=Kidney;
RX PubMed=9054364; DOI=10.1074/jbc.272.11.6831;
RA Valtavaara M., Papponen H., Pirttila A.M., Hiltunen K., Helander H.,
RA Myllylae R.;
RT "Cloning and characterization of a novel human lysyl hydroxylase isoform
RT highly expressed in pancreas and muscle.";
RL J. Biol. Chem. 272:6831-6834(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC TISSUE=Esophagus;
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 MRNA] (ISOFORM 1).
RC TISSUE=Aortic endothelium;
RA Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.,
RA Ohara O., Nagase T., Kikuno R.F.;
RT "Homo sapiens protein coding cDNA.";
RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16641997; DOI=10.1038/nature04728;
RA Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J.,
RA Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P.,
RA Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A.,
RA Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L.,
RA Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G.,
RA Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W.,
RA Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M.,
RA Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P.,
RA Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H.,
RA Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J.,
RA Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W.,
RA Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B.,
RA Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O.,
RA Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B.,
RA Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H.,
RA Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J.,
RA Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X.,
RA Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R.,
RA Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.;
RT "The DNA sequence, annotation and analysis of human chromosome 3.";
RL Nature 440:1194-1198(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND TISSUE SPECIFICITY.
RC TISSUE=Skin fibroblast;
RX PubMed=10372558; DOI=10.1016/s0945-053x(99)00013-x;
RA Yeowell H.N., Walker L.C.;
RT "Tissue specificity of a new splice form of the human lysyl hydroxylase 2
RT gene.";
RL Matrix Biol. 18:179-187(1999).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
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 project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-320 AND TYR-323, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Platelet;
RX PubMed=18088087; DOI=10.1021/pr0704130;
RA Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J.,
RA Schuetz C., Walter U., Gambaryan S., Sickmann A.;
RT "Phosphoproteome of resting human platelets.";
RL J. Proteome Res. 7:526-534(2008).
RN [8]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-209 AND ASN-522.
RC TISSUE=Liver;
RX PubMed=19159218; DOI=10.1021/pr8008012;
RA Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
RT "Glycoproteomics analysis of human liver tissue by combination of multiple
RT enzyme digestion and hydrazide chemistry.";
RL J. Proteome Res. 8:651-661(2009).
RN [9]
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 [10]
RP VARIANTS BRKS2 VAL-601 AND ILE-608.
RX PubMed=12881513; DOI=10.1074/jbc.m307380200;
RA van der Slot A.J., Zuurmond A.-M., Bardoel A.F.J., Wijmenga C.,
RA Pruijs H.E.H., Sillence D.O., Brinckmann J., Abraham D.J., Black C.M.,
RA Verzijl N., DeGroot J., Hanemaaijer R., TeKoppele J.M., Huizinga T.W.J.,
RA Bank R.A.;
RT "Identification of PLOD2 as telopeptide lysyl hydroxylase, an important
RT enzyme in fibrosis.";
RL J. Biol. Chem. 278:40967-40972(2003).
RN [11]
RP VARIANT BRKS2 HIS-598.
RX PubMed=15523624; DOI=10.1002/ajmg.a.30231;
RA Ha-Vinh R., Alanay Y., Bank R.A., Campos-Xavier A.B., Zankl A.,
RA Superti-Furga A., Bonafe L.;
RT "Phenotypic and molecular characterization of Bruck syndrome (osteogenesis
RT imperfecta with contractures of the large joints) caused by a recessive
RT mutation in PLOD2.";
RL Am. J. Med. Genet. A 131:115-120(2004).
RN [12]
RP VARIANT BRKS2 CYS-601.
RX PubMed=22689593; DOI=10.1002/humu.22133;
RA Puig-Hervas M.T., Temtamy S., Aglan M., Valencia M., Martinez-Glez V.,
RA Ballesta-Martinez M.J., Lopez-Gonzalez V., Ashour A.M., Amr K., Pulido V.,
RA Guillen-Navarro E., Lapunzina P., Caparros-Martin J.A., Ruiz-Perez V.L.;
RT "Mutations in PLOD2 cause autosomal-recessive connective tissue disorders
RT within the Bruck syndrome--osteogenesis imperfecta phenotypic spectrum.";
RL Hum. Mutat. 33:1444-1449(2012).
RN [13]
RP VARIANTS GLN-473 AND MET-643.
RX PubMed=29983323; DOI=10.1016/j.neuron.2018.06.019;
RA Furey C.G., Choi J., Jin S.C., Zeng X., Timberlake A.T.,
RA Nelson-Williams C., Mansuri M.S., Lu Q., Duran D., Panchagnula S.,
RA Allocco A., Karimy J.K., Khanna A., Gaillard J.R., DeSpenza T., Antwi P.,
RA Loring E., Butler W.E., Smith E.R., Warf B.C., Strahle J.M., Limbrick D.D.,
RA Storm P.B., Heuer G., Jackson E.M., Iskandar B.J., Johnston J.M.,
RA Tikhonova I., Castaldi C., Lopez-Giraldez F., Bjornson R.D., Knight J.R.,
RA Bilguvar K., Mane S., Alper S.L., Haider S., Guclu B., Bayri Y., Sahin Y.,
RA Apuzzo M.L.J., Duncan C.C., DiLuna M.L., Guenel M., Lifton R.P.,
RA Kahle K.T.;
RT "De Novo Mutation in Genes Regulating Neural Stem Cell Fate in Human
RT Congenital Hydrocephalus.";
RL Neuron 99:302-314.e4(2018).
CC -!- FUNCTION: Forms hydroxylysine residues in -Xaa-Lys-Gly- sequences in
CC collagens. These hydroxylysines serve as sites of attachment for
CC carbohydrate units and are essential for the stability of the
CC intermolecular collagen cross-links. {ECO:0000250|UniProtKB:P24802}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-oxoglutarate + L-lysyl-[collagen] + O2 = (5R)-5-hydroxy-L-
CC lysyl-[collagen] + CO2 + succinate; Xref=Rhea:RHEA:16569, Rhea:RHEA-
CC COMP:12751, Rhea:RHEA-COMP:12752, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:16526, ChEBI:CHEBI:16810, ChEBI:CHEBI:29969,
CC ChEBI:CHEBI:30031, ChEBI:CHEBI:133442; EC=1.14.11.4;
CC Evidence={ECO:0000250|UniProtKB:P24802};
CC -!- COFACTOR:
CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC Evidence={ECO:0000250|UniProtKB:P24802};
CC -!- COFACTOR:
CC Name=L-ascorbate; Xref=ChEBI:CHEBI:38290;
CC Evidence={ECO:0000250|UniProtKB:P24802};
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P24802}.
CC -!- SUBCELLULAR LOCATION: Rough endoplasmic reticulum membrane; Peripheral
CC membrane protein; Lumenal side.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1; Synonyms=A;
CC IsoId=O00469-1; Sequence=Displayed;
CC Name=2; Synonyms=B;
CC IsoId=O00469-2; Sequence=VSP_013467;
CC Name=3;
CC IsoId=O00469-3; Sequence=VSP_057221, VSP_057222, VSP_013467;
CC -!- TISSUE SPECIFICITY: Highly expressed in pancreas and muscle. Isoform 1
CC and isoform 2 are expressed in the majority of the examined cell types.
CC Isoform 2 is specifically expressed in skin, lung, dura and aorta.
CC {ECO:0000269|PubMed:10372558}.
CC -!- DISEASE: Bruck syndrome 2 (BRKS2) [MIM:609220]: An autosomal recessive
CC disease characterized by generalized osteopenia, congenital joint
CC contractures, fragile bones with onset of fractures in infancy or early
CC childhood, short stature, severe limb deformity, progressive scoliosis,
CC and pterygia. It is distinguished from osteogenesis imperfecta by the
CC absence of hearing loss and dentinogenesis imperfecta, and by the
CC presence of clubfoot and congenital joint limitations.
CC {ECO:0000269|PubMed:12881513, ECO:0000269|PubMed:15523624,
CC ECO:0000269|PubMed:22689593}. Note=The disease is caused by variants
CC affecting the gene represented in this entry. The molecular defect
CC leading to Bruck syndrome is an aberrant cross-linking of bone
CC collagen, due to underhydroxylation of lysine residues within the
CC telopeptides of type I collagen, whereas the lysine residues in the
CC triple helix are normal.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAD93116.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC -!- WEB RESOURCE: Name=Osteogenesis imperfecta variant database;
CC Note=Procollagen-lysine,2-oxoglutarate 5-dioxygenase 2 (PLOD2);
CC URL="http://oi.gene.le.ac.uk/home.php?select_db=PLOD2";
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DR EMBL; U84573; AAB58363.1; -; mRNA.
DR EMBL; AK125700; BAG54235.1; -; mRNA.
DR EMBL; AB209879; BAD93116.1; ALT_INIT; mRNA.
DR EMBL; AC092982; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC107021; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC037169; AAH37169.1; -; mRNA.
DR CCDS; CCDS3131.1; -. [O00469-1]
DR CCDS; CCDS3132.1; -. [O00469-2]
DR PIR; A59144; A59144.
DR RefSeq; NP_000926.2; NM_000935.2. [O00469-1]
DR RefSeq; NP_891988.1; NM_182943.2. [O00469-2]
DR AlphaFoldDB; O00469; -.
DR SMR; O00469; -.
DR BioGRID; 111367; 114.
DR CORUM; O00469; -.
DR IntAct; O00469; 28.
DR MINT; O00469; -.
DR STRING; 9606.ENSP00000282903; -.
DR DrugBank; DB00126; Ascorbic acid.
DR GlyConnect; 746; 8 N-Linked glycans (3 sites).
DR GlyGen; O00469; 8 sites, 9 N-linked glycans (3 sites), 1 O-linked glycan (1 site).
DR iPTMnet; O00469; -.
DR PhosphoSitePlus; O00469; -.
DR SwissPalm; O00469; -.
DR BioMuta; PLOD2; -.
DR CPTAC; CPTAC-568; -.
DR CPTAC; CPTAC-569; -.
DR EPD; O00469; -.
DR jPOST; O00469; -.
DR MassIVE; O00469; -.
DR MaxQB; O00469; -.
DR PaxDb; O00469; -.
DR PeptideAtlas; O00469; -.
DR PRIDE; O00469; -.
DR ProteomicsDB; 3798; -.
DR ProteomicsDB; 47915; -. [O00469-1]
DR ProteomicsDB; 47916; -. [O00469-2]
DR Antibodypedia; 33520; 249 antibodies from 28 providers.
DR DNASU; 5352; -.
DR Ensembl; ENST00000282903.10; ENSP00000282903.5; ENSG00000152952.12. [O00469-2]
DR Ensembl; ENST00000360060.7; ENSP00000353170.3; ENSG00000152952.12. [O00469-1]
DR Ensembl; ENST00000461497.5; ENSP00000419354.1; ENSG00000152952.12. [O00469-3]
DR GeneID; 5352; -.
DR KEGG; hsa:5352; -.
DR MANE-Select; ENST00000282903.10; ENSP00000282903.5; NM_182943.3; NP_891988.1. [O00469-2]
DR UCSC; uc003evq.2; human. [O00469-1]
DR CTD; 5352; -.
DR DisGeNET; 5352; -.
DR GeneCards; PLOD2; -.
DR HGNC; HGNC:9082; PLOD2.
DR HPA; ENSG00000152952; Low tissue specificity.
DR MalaCards; PLOD2; -.
DR MIM; 601865; gene.
DR MIM; 609220; phenotype.
DR neXtProt; NX_O00469; -.
DR OpenTargets; ENSG00000152952; -.
DR Orphanet; 2771; Bruck syndrome.
DR PharmGKB; PA33412; -.
DR VEuPathDB; HostDB:ENSG00000152952; -.
DR eggNOG; KOG1971; Eukaryota.
DR GeneTree; ENSGT01030000234558; -.
DR HOGENOM; CLU_022320_1_1_1; -.
DR InParanoid; O00469; -.
DR OMA; WDLQDND; -.
DR OrthoDB; 194164at2759; -.
DR PhylomeDB; O00469; -.
DR TreeFam; TF313826; -.
DR BRENDA; 1.14.11.4; 2681.
DR BRENDA; 2.4.1.50; 2681.
DR PathwayCommons; O00469; -.
DR Reactome; R-HSA-1650814; Collagen biosynthesis and modifying enzymes.
DR SignaLink; O00469; -.
DR BioGRID-ORCS; 5352; 5 hits in 1084 CRISPR screens.
DR ChiTaRS; PLOD2; human.
DR GenomeRNAi; 5352; -.
DR Pharos; O00469; Tbio.
DR PRO; PR:O00469; -.
DR Proteomes; UP000005640; Chromosome 3.
DR RNAct; O00469; protein.
DR Bgee; ENSG00000152952; Expressed in tibia and 199 other tissues.
DR ExpressionAtlas; O00469; baseline and differential.
DR Genevisible; O00469; HS.
DR GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; TAS:Reactome.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0030867; C:rough endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR GO; GO:0031418; F:L-ascorbic acid binding; IEA:UniProtKB-KW.
DR GO; GO:0008475; F:procollagen-lysine 5-dioxygenase activity; IDA:CAFA.
DR GO; GO:0046947; P:hydroxylysine biosynthetic process; IDA:CAFA.
DR GO; GO:0017185; P:peptidyl-lysine hydroxylation; IDA:CAFA.
DR GO; GO:0036211; P:protein modification process; TAS:ProtInc.
DR GO; GO:0001666; P:response to hypoxia; IEP:UniProtKB.
DR Gene3D; 3.90.550.10; -; 1.
DR InterPro; IPR044861; IPNS-like_FE2OG_OXY.
DR InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR InterPro; IPR005123; Oxoglu/Fe-dep_dioxygenase.
DR InterPro; IPR006620; Pro_4_hyd_alph.
DR InterPro; IPR001006; Procol_lys_dOase.
DR Pfam; PF03171; 2OG-FeII_Oxy; 1.
DR SMART; SM00702; P4Hc; 1.
DR SUPFAM; SSF53448; SSF53448; 1.
DR PROSITE; PS51471; FE2OG_OXY; 1.
DR PROSITE; PS01325; LYS_HYDROXYLASE; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Dioxygenase; Disease variant; Endoplasmic reticulum;
KW Glycoprotein; Iron; Membrane; Metal-binding; Osteogenesis imperfecta;
KW Oxidoreductase; Phosphoprotein; Reference proteome; Signal; Vitamin C.
FT SIGNAL 1..25
FT /evidence="ECO:0000255"
FT CHAIN 26..737
FT /note="Procollagen-lysine,2-oxoglutarate 5-dioxygenase 2"
FT /id="PRO_0000024683"
FT DOMAIN 644..737
FT /note="Fe2OG dioxygenase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT ACT_SITE 728
FT /evidence="ECO:0000255"
FT BINDING 666
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 668
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 718
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT MOD_RES 320
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18088087"
FT MOD_RES 323
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:18088087"
FT MOD_RES 704
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9R0B9"
FT CARBOHYD 63
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 209
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19159218"
FT CARBOHYD 297
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 365
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 522
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19159218"
FT CARBOHYD 696
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 725
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 1..36
FT /note="MGGCTVKPQLLLLALVLHPWNPCLGADSEKPSSIPT -> MLENHILHKRIY
FT ILTFFSQQIFILCHAHFIFFFTVR (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_057221"
FT VAR_SEQ 37..376
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_057222"
FT VAR_SEQ 500
FT /note="M -> MTLQREKDSPTPETFQMLSPPK (in isoform 2 and
FT isoform 3)"
FT /evidence="ECO:0000303|PubMed:10372558,
FT ECO:0000303|PubMed:14702039, ECO:0000303|PubMed:15489334"
FT /id="VSP_013467"
FT VARIANT 473
FT /note="R -> Q (found in a patient with congenital
FT hydrocephalus; unknown pathological significance;
FT dbSNP:rs533478450)"
FT /evidence="ECO:0000269|PubMed:29983323"
FT /id="VAR_083432"
FT VARIANT 598
FT /note="R -> H (in BRKS2; dbSNP:rs121434461)"
FT /evidence="ECO:0000269|PubMed:15523624"
FT /id="VAR_022164"
FT VARIANT 601
FT /note="G -> C (in BRKS2; phenotype characterized by mild to
FT severe osteogenesis imperfecta with or without postnatal
FT contractures; dbSNP:rs762788421)"
FT /evidence="ECO:0000269|PubMed:22689593"
FT /id="VAR_069531"
FT VARIANT 601
FT /note="G -> V (in BRKS2; dbSNP:rs121434460)"
FT /evidence="ECO:0000269|PubMed:12881513"
FT /id="VAR_022165"
FT VARIANT 608
FT /note="T -> I (in BRKS2; dbSNP:rs121434459)"
FT /evidence="ECO:0000269|PubMed:12881513"
FT /id="VAR_022166"
FT VARIANT 643
FT /note="T -> M (found in a patient with congenital
FT hydrocephalus; unknown pathological significance;
FT dbSNP:rs763670371)"
FT /evidence="ECO:0000269|PubMed:29983323"
FT /id="VAR_083433"
FT CONFLICT 624
FT /note="H -> D (in Ref. 1; AAB58363)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 737 AA; 84686 MW; C9AEA79A574D6B66 CRC64;
MGGCTVKPQL LLLALVLHPW NPCLGADSEK PSSIPTDKLL VITVATKESD GFHRFMQSAK
YFNYTVKVLG QGEEWRGGDG INSIGGGQKV RLMKEVMEHY ADQDDLVVMF TECFDVIFAG
GPEEVLKKFQ KANHKVVFAA DGILWPDKRL ADKYPVVHIG KRYLNSGGFI GYAPYVNRIV
QQWNLQDNDD DQLFYTKVYI DPLKREAINI TLDHKCKIFQ TLNGAVDEVV LKFENGKARA
KNTFYETLPV AINGNGPTKI LLNYFGNYVP NSWTQDNGCT LCEFDTVDLS AVDVHPNVSI
GVFIEQPTPF LPRFLDILLT LDYPKEALKL FIHNKEVYHE KDIKVFFDKA KHEIKTIKIV
GPEENLSQAE ARNMGMDFCR QDEKCDYYFS VDADVVLTNP RTLKILIEQN RKIIAPLVTR
HGKLWSNFWG ALSPDGYYAR SEDYVDIVQG NRVGVWNVPY MANVYLIKGK TLRSEMNERN
YFVRDKLDPD MALCRNAREM GVFMYISNRH EFGRLLSTAN YNTSHYNNDL WQIFENPVDW
KEKYINRDYS KIFTENIVEQ PCPDVFWFPI FSEKACDELV EEMEHYGKWS GGKHHDSRIS
GGYENVPTDD IHMKQVDLEN VWLHFIREFI APVTLKVFAG YYTKGFALLN FVVKYSPERQ
RSLRPHHDAS TFTINIALNN VGEDFQGGGC KFLRYNCSIE SPRKGWSFMH PGRLTHLHEG
LPVKNGTRYI AVSFIDP
