wanglab/gogpt-training-data huggingface dataset:
Protein: Polypeptide N-acetylgalactosaminyltransferase 3 (EC 2.4.1.41) (Polypeptide GalNAc transferase 3) (GalNAc-T3) (pp-GaNTase 3) (Protein-UDP acetylgalactosaminyltransferase 3) (UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 3) (P70419)
Organism: Mus musculus (Mouse)
Function: Catalyzes the initial reaction in O-linked oligosaccharide biosynthesis, the transfer of an N-acetyl-D-galactosamine residue to a serine or threonine residue on the protein receptor. Has activity toward HIV envelope glycoprotein gp120 (By similarity). Has activity towards EA2, MUC2 and MUC5. Probably glycosylates fibronectin in vivo (By similarity). Glycosylates FGF23 (By similarity).
Subcellular location: Golgi apparatus, Golgi stack membrane {ECO:0000250|UniProtKB:Q14435}; Single-pass type II membrane protein {ECO:0000250|UniProtKB:Q14435}. Note=Resides preferentially in the trans and medial parts of the Golgi stack. {ECO:0000250|UniProtKB:Q14435}.
Interaction partners:
- Fibroblast growth factor 23
- Beta-1,3-galactosyl-O-glycosyl-glycoprotein beta-1,6-N-acetylglucosaminyltransferase
- Acetylgalactosaminyl-O-glycosyl-glycoprotein beta-1,3-N-acetylglucosaminyltransferase
- Alpha-N-acetylgalactosaminide alpha-2,6-sialyltransferase 1
- Glycoprotein-N-acetylgalactosamine 3-beta-galactosyltransferase 1
- C1GALT1-specific chaperone 1
- Chondroitin sulfate synthase 3
- Klotho
- Phosphate-regulating neutral endopeptidase PHEX
- Mucin-2
Sequence:
MAHLKRLVKLHIKRHYHRKFWKLGAVIFFFLVVLILMQREVSVQYSKEESKMERNLKNKNKMLDFMLEAVNNIKDAMPKMQIGAPIKENIDVRERPCLQGYYTAAELKPVFDRPPQDSNAPGASGKPFKITHLSPEEQKEKERGETKHCFNAFASDRISLHRDLGPDTRPPECIEQKFKRCPPLPTTSVIIVFHNEAWSTLLRTVHSVLYSSPAILLKEIILVDDASVDDYLHEKLEEYIKQFSIVKIVRQQERKGLITARLLGAAVATAETLTFLDAHCECFYGWLEPLLARIAENYTAVVSPDIASIDLNTFEFNKPSPYGSNHNRGNFDWSLSFGWESLPDHEKQRRKDETYPIKTPTFAGGLFSISKKYFEHIGSYDEEMEIWGGENIEMSFRVWQCGGQLEIMPCSVVGHVFRSKSPHTFPKGTQVIARNQVRLAEVWMDEYKEIFYRRNTDAAKIVKQKSFGDLSKRFEIKKRLQCKNFTWYLNTIYPEAYVPDLNPVISGYIKSVGQPLCLDVGENNQGGKPLILYTCHGLGGNQYFEYSAQREIRHNIQKELCLHATQGVVQLKACVYKGHRTIAPGEQIWEIRKDQLLYNPLFKMCLSSNGEHPNLVPCDATDLLQKWIFSQND
Protein: AlkB homolog 4, lysine demthylase (Alpha-ketoglutarate-dependent dioxygenase alkB homolog 4 isoform 2 (EC 1.14.11.51)) (A0A2R8RZS3)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
Sequence:
MDQDVWRESQSGRRKQDFGPKVNFKKRRVHVGSFSGLPAISRRLLVRMSDLPQLSSFKPVEQCNLDYDSLRGSAIDPHLDDSWLWGENLVTVNLLSDTVLTLSLDQGWGDMEQGEVRVAVRLPRRSLVVLYGDARHRWKHAIHRKDIHGRRVCSTFRELSAEFLPGGQQEKLGSELLDIALSFQGAPL
Protein: Chaperone DnaJ C-terminal domain-containing protein (H7C2Y5)
Organism: Homo sapiens (Human)
Interaction partners:
- Endoplasmin
Sequence:
XLVNEERTLEVEIEPGVRDGMEYPFIGEGEPHVDGEPGDLRFRIKVVKHPIFERRGDDLYTNVTISLVESLVGFEMDITHLDGHKVHISRDKITRPGAKLWKKGEGLPNFDNNNIKGSLIITFDVDFPKEQLTEEAREGIKQLLKQGSVQKAEWFEDDVIQRKRELW
Protein: ABO glycosyltransferase (B antigen) (Bel antigen) (Bw glycosyltransferases) (Transferase B, alpha 1-3-galactosyltransferase) (B0B1U2)
Organism: Homo sapiens (Human)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004606}; Single-pass type II membrane protein {ECO:0000256|ARBA:ARBA00004606}.
Interaction partners:
Sequence:
MAEVLRTLAGKPKCHALRPMILFLIMLVLVLFGYGVLSPRSLMPGSLERGFCMAVREPDHLQRVSLPRMVYPQPKVLTPCRKDVLVVTPWLAPIVWEGTFNIDILNEQFRLQNTTIGLTVFAIKKYVAFLKLFLETAEKHFMVGHRVHYYVFTDQPAAVPRVTLGTGRQLSVLEVGAYKRWQDVSMRRMEMISDFCERRFLSEVDYLVCVDVDMEFRDHVGVEILTPLFGTLHPSFYGSSREAFTYERRPQSQAYIPKDEGDFYYMGAFFGGSVQEVQRLTRACHQAMMVDQANGIEAVWHDESHLNKYLLRHKPTKVLSPEYLWDQQLLGWPAVLRKLRFTAVPKNHQAVRNP
Protein: Interferon-activable protein 202 (Ifi-202) (Interferon-inducible protein p202) (Lupus susceptibility protein p202) (Q9R002)
Organism: Mus musculus (Mouse)
Function: Inhibits the transcriptional activity of several transcription factors, including NF-kappa-B p50 and p65, FOS, JUN, E2F1, E2F4, MYOD1 and myogenin. Has anti-apoptotic effects due to inhibition of the transcriptional activity of p53. Binds dsDNA in the cytosol. Is involved in innate immune response and has anti-inflammatory activity. Inhibits caspase activation in response to cytosolic DNA and inhibits the activation of the AIM2 inflammasome, probably by sequestering cytoplasmic DNA and preventing its being bound by AIM2.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:19131592, ECO:0000269|PubMed:8454910}. Nucleus {ECO:0000269|PubMed:8454910}. Note=Accumulates first in the cytoplasm, and is translocated to the nucleus after a delay, where it is primarily chromatin-associated. {ECO:0000269|PubMed:8454910}.
Interaction partners:
Sequence:
MSNRNLRSSTNSEFSEGQHQTPSSDSSGHGEDQPQASPGPNKKSHTPKKNISKGAVLHEKPMTVMVLTATEPFNYKEGKENMFHATVATESQYYRVKVFNMDLKEKFTENKFITISKYFNSSGILEINETATVSEAAPNQIIEVPKNIIRSAKETLKISKIKELDSGTLIYGVFAVEKKKVNDKSITFKIKDNEDNIKVVWDKKQHNINYEKGDKLQLFSFHLRKGNGKPILHSGNHSFIKGEKLLKESFEGDGYHKGPKQVVALKATKLFTYDSIKSKKMFHATVATDTEFFRVMVFEENLEKKFIPGNTIALSDYFGMYGSLAIHEYSSVSEVKSQNKEDSSSSDERLIEHLKICDLHLQTKERLVDGEFKVYRKSTGNNCICYGIWDDTGAMKVVVSGQLTSVNCEIGNTIRLVCFELTSNADEWFLRSTRYSYMEVIMPEK
Protein: non-specific serine/threonine protein kinase (EC 2.7.11.1) (Q7KT38)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MKKILSKFERNENSRLENPPNSSSSSSSNEKNSFVGKVFTVGRVTVTVEDVLAEGGFAMVFLARGNGGGSSSATKYALKRMYVNNEHDLNVAKREIQIASNLSGHKNIIGYVDSSITPTGNGVCEVLLLMPYCKHHMLAMMNARLHVGFTEPEVLNIFCDIAEAVSRLHYCQTPIIHRDLKVENILQTDAGNFVLCDFGSATAKTLNPQQHGVTVVQEEIQKYTTLSYRAPEMIDLYGGKSITTKADIWALGCMLYKLCFFSLPFGESTLAIQNGQFSIPDSSKYSKGMHQLIKYMLEPDMEKRPNIWQVCEVAFRLAGKDNPVQNLHKTPIPNFDLLVVPPFESEAKRISAAASKAAKAQNVSVVEAGTSVAPRSRPKGSSSVHGGNPLGLGLPPSPSPRQNITSPQPQPQPVVEQFQANFPAMPPAVPPPPQAVTPAAPAASKLFESSGYPDPFNEPAAAVIPTEFLPAAEEPNKEEVPQDLNVIAGTPTKSMLTPPKPSGGGGHRRNVSDTSAFNKTFANETSQFLAPFNNNLAAMGDGQQTLASAASNPGIYASSTANSAAVSISELMKPGQTAVEKRVEAWNPFEEEQPFSQMTEDHIFEAEFDKIRQRGSQGSITAKSASTTSTLTPTEQIPSAVVAPVTAAPGAVPPPPIAAAVSPYPSQVSEDPFGSAPFSLPPGLREKASSLRKTGGKA
Protein: Cryptic protein (Cryptic family protein 1) (P0CG37)
Organism: Homo sapiens (Human)
Function: NODAL coreceptor involved in the correct establishment of the left-right axis. May play a role in mesoderm and/or neural patterning during gastrulation.
Subcellular location: Cell membrane {ECO:0000269|PubMed:18930707}; Lipid-anchor, GPI-anchor {ECO:0000269|PubMed:18930707}. Secreted {ECO:0000269|PubMed:18930707}. Note=Does not exhibit a typical GPI-signal sequence. The C-ter hydrophilic extension of the GPI-signal sequence reduces the efficiency of processing and could lead to the production of an secreted unprocessed form. This extension is found only in primates.
Interaction partners:
- Activin receptor type-2B
- Nodal homolog
- Left-right determination factor 2
- Embryonic growth/differentiation factor 1
- Formin-like protein 1
- Zinc finger protein ZIC 3
- Activin receptor type-1B
- Left-right determination factor 1
- Mediator of RNA polymerase II transcription subunit 13-like
- Homeobox protein Nkx-2.6
Sequence:
MTWRHHVRLLFTVSLALQIINLGNSYQREKHNGGREEVTKVATQKHRQSPLNWTSSHFGEVTGSAEGWGPEEPLPYSRAFGEGASARPRCCRNGGTCVLGSFCVCPAHFTGRYCEHDQRRSECGALEHGAWTLRACHLCRCIFGALHCLPLQTPDRCDPKDFLASHAHGPSAGGAPSLLLLLPCALLHRLLRPDAPAHPRSLVPSVLQRERRPCGRPGLGHRL
Protein: Receptor-like protein 3 (AtRLP3) (Protein RESISTANCE TO FUSARIUM OXYSPORUM 2) (Q9SHI4)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Involved in the perception of CLV3 and CLV3-like peptides, that act as extracellular signals regulating meristems maintenance (By similarity). Contributes, with WAKL22/RFO1, to resistance to F.oxysporum (f.) matthioli in cv. Columbia relative to cv. Ty-0.
Subcellular location: Cell membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}.
Interaction partners:
- Wall-associated receptor kinase-like 22
- CASP-like protein 2A1
- Wall-associated receptor kinase-like 17
- Receptor-like kinase
- Putative protease Do-like 13
- Wall-associated receptor kinase-like 14
- Putative protease Do-like 11, mitochondrial
Sequence:
MTNEGRFKAKGFVRTSSTTRPIQALSFHMIGILLQCVLFISVLSIAVSEALCNSQDRESLLWFSGNVSSSVSPLNWNPSIDCCSWEGITCDDSPDSHITAISLPFRALYGKLPLSVLRLHHLSQLNLSHNRLSGHLPSGFLSALDQLKVLDLSYNSLDGELPVEQTFRNGSNRCFPIRIVDLSSNFLQGEILPSSIFMQGTFDLISFNVSKNSFTGSIPSFMCKSSPQLSKLDFSYNDFTGNIPQGLGRCLKLSVLQAGFNNISGEIPSDIYNLSELEQLFLPVNHLSGKINDDITHLTKLKSLELYSNHLGGEIPMDIGQLSRLQSLQLHINNITGTVPPSLANCTNLVKLNLRLNRLEGTLSELDFSRFQSLSILDLGNNSFSGDFPWRVHSCKSLSAMRFASNKLTGQISPHVLELESLSILSLSDNKLMNITGALGILQGCRNLSTLLIGKNFYNETFPSDKDLISSDGFPNLQIFASGGSGLRGEIPAWLIKLKSLAVIDLSHNQLVGSIPGWLGTFPHLFYIDLSENLLSGELPKDLFQLKALMSQKAYDATERNYLKLPVFVSPNNVTTHQQYNQLFSLPPGIYIRRNNLKGSIPIEVGQLKVLHVLELSHNYLSGIIPHELSKLTSLERLDLSNNHLSGRIPWSLTSLHYMSYFNVVNNSLDGPIPTGSQFDTFPQANFKGNPLLCGGILLTSCKASTKLPATTTNKADTEDEEELKFIFILGVATGFFVSYCFYWCFFARLDAFISK
Protein: Seminal fluid protein 38D (Seminal fluid protein 38D, isoform B) (C4NAP3)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Seminal fluid protein
- DUF229 domain containing protein
- Uncharacterized protein
- GH23626p
- ACP53C14B
- Accessory gland protein Acp29AB
- Uncharacterized protein, isoform E
- trypsin
- HDC01001
- Seminal metalloprotease 1
Sequence:
MKFMAICLLANIGYILGTTIGQLNDEATIRLKGLVEKYKLQALSNPEFSQWIGKLEKTSKSRRLEDKMKVKAEFKNYDERRLQLENKIRERITAIDDLISDIMAKVPIKDKGCLKYYQRQKRSLKLAHNFSNLTKQTNLIRNSKQCETTKVQSSELSESSENPDEYSYY
Protein: Glucoamylase S1 (EC 3.2.1.3) (1,4-alpha-D-glucan glucohydrolase) (GAI) (Glucan 1,4-alpha-glucosidase) (P04065)
Organism: Saccharomyces cerevisiae (Baker's yeast)
Interaction partners:
Sequence:
MQRPFLLAYLVLSLLFNSALGFPTALVPRGSSSSNITSSGPSSTPFSSATESFSTGTTVTPSSSKYPGSKTETSVSSTTETTIVPTTTTTSVITPSTTTITTTVCSTGTNSAGETTSGCSPKTITTTVPCSTSPSETASESTTTSPTTPVTTVVSTTVVTTEYSTSTKQGGEITTTFVTKNIPTTYLTTIAPTSSVTTVTNFTPTTITTTVCSTGTNSAGETTSGCSPKTVTTTVPCSTGTGEYTTEATAPVTTAVTTTVVTTESSTGTNSAGKTTTSYTTKSVPTTYVFDFGKGILDQSCGGVFSNNGSSQVQLRDVVLMNGTVVYDSNGAWDSSALEEWLQRQKKVSIERIFENIGPSAVYPSILPGVVIASPSQTHPDYFYQWIRDSALTINSIVSHSADPAIETLLQYLNVSFHLQRTNNTLGAGIGYTNDTVALGDPKWNVDNTAFTEPWGRPQNDGPALRSIAILKIIDYIKQSGTDLGAKYPFQSTADIFDDIVRWDLRFIIDHWNSSGFDLWEEVNGMHFFTLLVQLSAVDRSLSYFNASERSSPFVEELRQTRRDISKFLVDPANGFINGKYNYIVETPMIADTLRSGLDISTLLAANTVHDAPSASHLPFDINDPAVLNTLHHLMLHMRSIYPINDSSKNATGIALGRYPEDVYDGYGVGEGNPWVLATCAASTTLYQLIYRHISEQHDLVVPMNNDCSNAFWSELVFSNLTTLGNDEGYLILEFNTPAFNQTIQKIFQLADSFLVKLKATWEQTGN
Protein: Probable E3 ubiquitin-protein ligase HIP1 (EC 2.3.2.27) (HAL3-interacting protein 1) (OsHIP1) (RING-H2 finger HIP1) (RING-type E3 ubiquitin transferase HIP1) (Q7XTV7)
Organism: Oryza sativa subsp. japonica (Rice)
Function: Probable E3 ubiquitin-protein ligase that functions downstream of HAL3 and is required for HAL3-regulated plant growth. Activation of HIP1 by HAL3 may lead to the degradation of cell cycle suppressors, resulting in enhancement of cell division and plant growth.
Interaction partners:
Sequence:
MQGQKNSVEQLADVFGFDHASSSGNPVMDQQGYWNNILGSVESHNLQGYQVNRSDGTIPYGNGVHQNGTFLGFWESGEASASGSSLHFGGSNEIKAEQRNIGGGLRIGERRLVAERNLSLDNVDIGLNINGNDLSGENSNVNGASQGSELHGGCSHTGSNGQASELRLHPYRTFILGADQPEPFNSLNGSENPLGDFSLMPEGIDQRPGSSLDGRRLACKRKNIEGVNGQCSAGASTSFSHRNDSIFHNIASSSHNPSPSTNLPSPNCLLVPSTLDEQLPRYGATTAGLSSSSYDPSGGNNNSGGSQRSFRPRTSLAQHIGPYGVWPSSSTIRHSNSWNHQPPPFQSSFDEPPEVIPVVSSLNFQYQHPMNVVPGIPQMSHRFTGPGASSSRTGNLENRIIGSEEFSARNVVATSFPDAVPPAALDMRHLIPEPSSWNVDGRATTIPGNVPSSSRANTNSMVNPPAGSPFIAHQNLHRRNPRNLSEEISRLSGALRGHQHPRLRSGFLLERQGDGVWGVPLSTRSREGRRLIEIRNALEMIHRGENVRFESIFYGGVDIHDRHRDMRLDIDNMSYEELLALEERIGNVSTGLSEEEVTKLLKQRKFSSWRLEASVEEEPCCICQEEYVDGDDLGTLDCGHDFHVGCVRQWLVVKNTCPICKNTALKS
Protein: D-galactonate dehydratase family member RspA (EC 4.2.1.-) (D-mannonate dehydratase) (EC 4.2.1.8) (Starvation sensing protein RspA homolog) (Q8FHC7)
Organism: Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC)
Function: Has low D-mannonate dehydratase activity (in vitro), suggesting that this is not a physiological substrate and that it has no significant role in D-mannonate degradation in vivo. Has no detectable activity with a panel of 70 other acid sugars (in vitro).
Interaction partners:
- Starvation sensing protein rspB
- D-mannonate oxidoreductase
- Altronate hydrolase
- Mannonate dehydratase
- 2-dehydro-3-deoxy-D-gluconate 5-dehydrogenase
- Starvation sensing protein rspA
- 2-dehydro-3-deoxygluconokinase
- Ribose 5-phosphate isomerase B
- Ribulose-phosphate 3-epimerase
- 6-phosphogluconate dehydrogenase, decarboxylating
Sequence:
MHHDKRCKESNMKIVKAEVFVTCPGRNFVTLKITTEDGITGLGDATLNGRELSVASYLQDHLCPQLIGRDAHRIEDIWQFFYKGAYWRRGPVTMSAISAVDMALWDIKAKAANMPLYQLLGGASREGVMVYCHTTGHSIDEALDDYARHQELGFKAIRVQCGIPGMKTTYGMSKGKGLAYEPATKGQWPEEQLWSTEKYLDFMPKLFDAVRNKFGFDEHLLHDMHHRLTPIEAARFGKSIEDYRMFWMEDPTPAENQECFRLIRQHTVTPIAVGEVFNSIWDCKQLIEEQLIDYIRTTLTHAGGITGMRRIADFASLYQVRTGSHGPSDLSPVCMAAALHFDLWVPNFGVQEYMGYSEQMLEVFPHNWTFDNGYMHPGEKPGLGIEFDEKLAAKYPYEPAYLPVARLEDGTLWNW
Protein: Thioredoxin superfamily protein (Q8L5Y8)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
Sequence:
MILVSESPMAILSLRSSSSLPLICSTISPLCSKPMLSQLPSNFSSSIASVPVTKLKSSYSSSVSPISRPRVVSARAATESFTDYREDIGEILGDVSIFTASGQRVQFSDLWDQKDGIAAVVLLRHFGCVCCWELATALKEAKPRFDAAGVKLIAVGVGTPDKARILATRLPFPMECLYADPERKAYDVLGLYFGLGRTFFNPASTKVFSRFSEIREATKNYTIEATPEDRSSVLQQGGTFVFRGKKLLYGRKDEGTGDHPSLDDVINVCCKATVA
Protein: 60S ribosomal protein L37a, putative (60S ribosomal proteins L37, putative) (Q38AW9)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- 60S ribosomal subunit protein L31, putative
- 40S ribosomal protein S5, putative
- Ribosomal protein L37
- 40S ribosomal protein S15a, putative
- 40S ribosomal protein S4
- 60S ribosomal protein L2, putative
- 60S ribosomal protein L35A, putative
- Ribosomal protein
- Large ribosomal subunit protein uL5
- 60S ribosomal protein L18a
Sequence:
MAKRTVKMGVMGRYGARYGSNPRKRAKKLEVSQHAKHFCSFCGKFAFRRKAVGIWRCDGCSKTVAGGAYTLSTPNNTTVRSTVRRLRELKQSN
Protein: Hexokinase-2 (EC 2.7.1.1) (P50521)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Catalyzes the phosphorylation of hexose (six-carbon sugars) to hexose 6-phosphate. Phosphorylates D-glucose, D-fructose and D-mannose. Compared to hxk1, has a much higher affinity for D-glucose. Constitutes the initial enzyme of glycolysis by catalyzing the phosphorylation of glucose to D-glucose 6-phosphate (Probable).
Interaction partners:
- Glucose-6-phosphate isomerase
- ATP-dependent 6-phosphofructokinase
- Hexokinase-1
- Phosphoglucomutase
- Invertase
- Putative invertase
- Mannose-6-phosphate isomerase
- Phosphomannomutase
- Fructose-1,6-bisphosphatase
- Glucosamine 6-phosphate N-acetyltransferase
Sequence:
MEANFQQAVKKLVNDFEYPTESLREAVKEFDELRQKGLQKNGEVLAMAPAFISTLPTGAETGDFLALDFGGTNLRVCWIQLLGDGKYEMKHSKSVLPRECVRNESVKPIIDFMSDHVELFIKEHFPSKFGCPEEEYLPMGFTFSYPANQVSITESYLLRWTKGLNIPEAINKDFAQFLTEGFKARNLPIRIEAVINDTVGTLVTRAYTSKESDTFMGIIFGTGTNGAYVEQMNQIPKLAGKCTGDHMLINMEWGATDFSCLHSTRYDLLLDHDTPNAGRQIFEKRVGGMYLGELFRRALFHLIKVYNFNEGIFPPSITDAWSLETSVLSRMMVERSAENVRNVLSTFKFRFRSDEEALYLWDAAHAIGRRAARMSAVPIASLYLSTGRAGKKSDVGVDGSLVEHYPHFVDMLREALRELIGDNEKLISIGIAKDGSGIGAALCALQAVKEKKGLA
Protein: Y-box protein ZONAB-B (Q9N1Q2)
Organism: Canis lupus familiaris (Dog) (Canis familiaris)
Interaction partners:
Sequence:
MSEAGEATGTTSSSSSSLPQAPAEAAPAAPQDPAPKSPGGSGAPQAAAPPPAALAAGNPGGDAAPAATGTAAPASSAPAGGEDAEKKVLATKVLGTVKWFNVRNGYGFINRNDTKEDVFVHHTAIKKNNPRKYLRSVGDGETVEFDVVEGEKGAEAANVTGPDGVPVEGSRYAADRRRYRRGYYGRRRGPPRNYAGEEEEEGSGSSEGFDPPATDGQFSGARSQLRRPQYRPQYRRRFPPYHVGQTFDRRSRVFPHPNRMQAGEIGEMKEGVPEGTQLQGPVHRNPTYRPRYRRGPPRPRPAPAVGEAEDKENQQAANGPNQPSARRGYRRPYNYRRRPRPPNAPSQDGKETKAPEVPSENPAPATEQSSAE
Protein: Asp/Glu-specific dipeptidyl-peptidase (EC 3.4.14.-) (Dipeptidyl-peptidase 11) (DPP11) (A6GWM2)
Organism: Flavobacterium psychrophilum (strain ATCC 49511 / DSM 21280 / CIP 103535 / JIP02/86)
Function: Catalyzes the removal of dipeptides from the N-terminus of oligopeptides. Shows a strict specificity for acidic residues (Asp or Glu) in the P1 position, and has probably a hydrophobic residue preference at the P2 position. Preferentially cleaves the synthetic substrate Leu-Asp-methylcoumaryl-7-amide (Leu-Asp-MCA) as compared to Leu-Glu-MCA.
Interaction partners:
Sequence:
MKYLKLFLLLFIIQTQAQQGGMWIPSLLSGMNETEMKNLGMKISADDIYSVNHSSLKDAVPHFNGGCTSEVISPKGLILTNHHCGFDAIQNHSSVDHDYLTNGFWAMKMEDELPNENLVVTFIVSINDVTAQVLDGVASITSETEKQNKIQENITKVTASFAKEAWQENKVRTFFEGNQYILFVTEVFKDVRLVGAPPSLIGKFGSDTDNWVWPRHTGDFSMFRVYANKNNHPAAYSKDNVPYIPKHFLPVSLDGVQEDDFTMVMGYPGKTQEYLPSFAVAQIVNETNPAKIEIREAALKVQDGFMRKDNAIKIQYASKYAGVANYWKKWIGESQGLKKSNAIGLKQNFEKDFQQKVIAAGKQNEYGNLLADFQKYYTEITPYAVSRDYFNEVVVKNTELLSLGYKLYQLEQVFITKGEQAFNDRKENLIKSQADFFKDFNATVDEKVFEQLVALYATKAPKEFLPISLLNVEYKKFAPSIYSKSKLVDYANFKALLSGDAKAVLKKISLDKGYAFVKSLADNYSKNIAPRYDEINLKINALQRIYMKAQLELYPNSRIFPDANSTLRVTYGKVKGYSPKDAIYYNPTTYLDGAIEKYIPGDYEFDVPKKLIDLYNNKDYGQYGENGKLPVCFIGTNHTTGGNSGSPAVDAQGNLIGLNFDRVWEGTMSDIHYDPSICRNVMVDMRYVLFIVDKFAGAKHLINEMKLVHPKKK
Protein: ERO1-like protein alpha (ERO1-L) (ERO1-L-alpha) (EC 1.8.4.-) (Endoplasmic oxidoreductin-1-like protein) (Endoplasmic reticulum oxidoreductase alpha) (Oxidoreductin-1-L-alpha) (Q96HE7)
Organism: Homo sapiens (Human)
Function: Oxidoreductase involved in disulfide bond formation in the endoplasmic reticulum. Efficiently reoxidizes P4HB/PDI, the enzyme catalyzing protein disulfide formation, in order to allow P4HB to sustain additional rounds of disulfide formation. Following P4HB reoxidation, passes its electrons to molecular oxygen via FAD, leading to the production of reactive oxygen species (ROS) in the cell. Required for the proper folding of immunoglobulins. Plays an important role in ER stress-induced, CHOP-dependent apoptosis by activating the inositol 1,4,5-trisphosphate receptor IP3R1. Involved in the release of the unfolded cholera toxin from reduced P4HB/PDI in case of infection by V.cholerae, thereby playing a role in retrotranslocation of the toxin.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:10671517, ECO:0000269|PubMed:14517240}; Peripheral membrane protein {ECO:0000269|PubMed:10671517, ECO:0000269|PubMed:14517240}; Lumenal side {ECO:0000269|PubMed:10671517, ECO:0000269|PubMed:14517240}. Golgi apparatus lumen {ECO:0000269|PubMed:29858230}. Secreted {ECO:0000269|PubMed:29858230}. Cell projection, dendrite {ECO:0000250|UniProtKB:Q8R4A1}. Note=The association with ERP44 is essential for its retention in the endoplasmic reticulum (PubMed:29858230). In neurons, it localizes to dendrites (By similarity). {ECO:0000250|UniProtKB:Q8R4A1, ECO:0000269|PubMed:29858230}.
Interaction partners:
- Endoplasmic reticulum resident protein 44
- Protein disulfide-isomerase
- Protein disulfide-isomerase A4
- Thioredoxin domain-containing protein 5
- Protein disulfide-isomerase A6
- ERO1-like protein beta
- Endoplasmic reticulum resident protein 29
- Endoplasmic reticulum chaperone BiP
- Protein disulfide-isomerase A2
- Probable glutathione peroxidase 8
Sequence:
MGRGWGFLFGLLGAVWLLSSGHGEEQPPETAAQRCFCQVSGYLDDCTCDVETIDRFNNYRLFPRLQKLLESDYFRYYKVNLKRPCPFWNDISQCGRRDCAVKPCQSDEVPDGIKSASYKYSEEANNLIEECEQAERLGAVDESLSEETQKAVLQWTKHDDSSDNFCEADDIQSPEAEYVDLLLNPERYTGYKGPDAWKIWNVIYEENCFKPQTIKRPLNPLASGQGTSEENTFYSWLEGLCVEKRAFYRLISGLHASINVHLSARYLLQETWLEKKWGHNITEFQQRFDGILTEGEGPRRLKNLYFLYLIELRALSKVLPFFERPDFQLFTGNKIQDEENKMLLLEILHEIKSFPLHFDENSFFAGDKKEAHKLKEDFRLHFRNISRIMDCVGCFKCRLWGKLQTQGLGTALKILFSEKLIANMPESGPSYEFHLTRQEIVSLFNAFGRISTSVKELENFRNLLQNIH
Protein: Type I inositol polyphosphate 5-phosphatase 12 (At5PTase12) (EC 3.1.3.56) (O80560)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Has phosphatase activity toward Ins(1,4,5)P3. Controls Ins(1,4,5)P3/Ca(2+) levels that is crucial for maintaining pollen dormancy and regulating early germination of pollen.
Interaction partners:
- F21F23.12 protein
- AT4g27020/F10M23_360
- Inositol-1,4,5-trisphosphate 5-phosphatase
- F14J22.5 protein
- Probable phosphoinositide phosphatase SAC9
Sequence:
MDIINNNHRDENDDDEEEALSAMSSVPPPRKIHSYSHQLRATGQKGHHRQRQHSLDDIPKITEIVSGCGISGDSSDDEFYPYATTTNSSSFPFTGGDTGDSDDYLHQPEIGEDFQPLPEFVGSGGGVGMFKVPTRSPLHSARPPCLELRPHPLKETQVGRFLRNIACTETQLWAGQESGVRFWNFDDAFEPGCGLSGRVQRGDEDAAPFQESASTSPTTCLMVDNGNRLVWSGHKDGKIRSWKMDYVLDDGDDSPFKEGLAWQAHKGPVNSVIMSSYGDLWSCSEGGVIKIWTWESMEKSLSLRLEEKHMAALLVERSGIDLRAQVTVNGTCNISSSEVKCLLADNVRSKVWAAQLQTFSLWDGRTKELLKVFNSEGQTENRVDMPLGQDQPAAEDEMKAKIASTSKKEKPHGFLQRSRNAIMGAADAVRRVATRGGGAYEDAKRTEAMVLAGDGMIWTGCTNGLLIQWDGNGNRLQDFRHHQCAVLCFCTFGERIYIGYVSGHIQIIDLEGNLIAGWVAHNNAVIKMAAADGYIFSLATHGGIRGWPVISPGPLDGIIRSELAEKERTYAQTDSVRILTGSWNVGQGKASHDALMSWLGSVASDVGILVVGLQEVEMGAGFLAMSAAKESVGGNEGSTIGQYWIDTIGKTLDEKAVFERMGSRQLAGLLISLWVRKNLRTHVGDIDVAAVPCGFGRAIGNKGGVGLRIRVFDRIMCFINCHLAAHLEAVNRRNADFDHIYKTMSFTRSSNAHNAPAAGVSTGSHTTKSANNANVNTEETKQDLAEADMVVFFGDFNYRLFGISYDEARDFVSQRSFDWLREKDQLRAEMKAGRVFQGMREAIITFPPTYKFERHRPGLGGYDSGEKKRIPAWCDRVIFRDTRTSPESECSLDCPVVASIMLYDACMDVTESDHKPVRCKFHVKIEHVDRSVRRQEFGRIIKTNEKVRALLNDLRYVPETIVSSNSIVLQNQDTFVLRITNKCVKENAVFRILCEGQSTVREDEDTLELHPLGSFGFPRWLEVMPAAGTIKPDSSVEVSVHHEEFHTLEEFVDGIPQNWWCEDTRDKEAILVVNVQGGCSTETVCHRVHVRHCFSAKNLRIDSNPSNSKSQSLKKNEGDSNSKSSKKSDGDSNSKSSKKSDGDSNSKSSKKSDGDSNSKSSKKSDGDSNSKSSKKSDGDSNSKSSKKSDGDSNSKSSKKSDGDSCSKSQKKSDGDTNSKSQKKGDGDSSSKSHKKNDGDSSSKSHKKNDGDSSSKSHKKSDGDSSSKSHKKSEGDSSSKSHKKNDGDSSSSYKSQSGKKNSNSSTVEESRNNHNKR
Protein: Collagen alpha-2(VI) chain isoform X4 (Collagen, type VI, alpha 2) (E7FCV8)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
- Collagen, type VI, alpha 1
- Collagen, type VI, alpha 3.
- Collagen alpha-2
- Integrin beta
- Uncharacterized protein.
- Collagen, type VI, alpha 3.
- Integrin alpha-2 isoform X1, tandem duplicate 2)
- Integrin beta.
- Integrin, alpha 3a
- Integrin, alpha 1
Sequence:
MMSLSILLLLFVGVHAQGQTPAGSSCSPIKSTECPIDLYFAIDTSETIALQENPPGSLVESIKDFTIRFAEKLQNVNYRGSVNITWAIGGLHFSQLQEFFSTITTKEKFISNLRPIRYLGRGTHIDCAITNMTKQLVRFPSRPDAKRFAVVITDGHVTANPCGGIKVAAERARDENIRIFAVASSRNLEETGLREIANSPAGVYRDKYMAVNLTGTRPVIVTSTIDRIYDTMLHMAYQECYSTKCLETPGPPGPPGHRGQKGAKGDNGGAGLKGERGRPGDPGIEGPIGHPGPKGEPGLKGEKGEIGAQGKKGVAGIAGRDGKDGQKGKFGRIGAPGCKGDPGDKGPDGHPGDVGEPGLPGALGDKGDRGRPGRSGPPGPAGDPGPKGERGSPGSPGIPGTKGGAGTAGGPGPKGDAGRRGDFGPKGSTGPNGAKGEKGEPGAEGPRGLAGEVGGKGSKGDNGLPGPRGPPGAPGDAGRKGSSGDPGDSGPRGDPGPPGPKGDSGRPGFSYPGPRGPTGDRGEKGSPGPRGSRGDCGPKGDPGLKGTPGEPGEPGPAGEPGQRGPRGDGGRDGDPGPEGDPGLTECDVMNYIRETCGCCDCEKRCGALDIVFVIDSSESVGLTNFTLEKNFVINTINRLGSIAKDPSSETGTRVGVVQYSHNGTFQAIRLNDSKIDSMSAFKDAVKKLEWIAGGTWTPSALKFAYDNLIRDSRRSKANVTVVVITDGRYDPRDDDKLLNYLCTDTSIDVNAIGIGDMFDQPEENESLKSIACRKDGRVMGMRRFADLVAEDFIDRIETVLCPDPVVICPDLPCKSEPAVANCIQRPVDLVFMLDGSERMGQENFRYAREFVENVANRLTLAQGDDDERNARVALLQYGDENQHQLAFKLTNNFTVIADGLANMRYLDSTSNVGSGIIYAINNIVTSRGTRLARRNAELSFVFITDGVTSNKNLEEGISAMRRAEGVPTVIAMSNDVDKEILAKISLGDQTAVFRGEDFARLNKASFFERFVRWIC
Protein: (-)-alpha-pinene synthase, chloroplastic (EC 4.2.3.119) ((+)-(3S:5S)-alpha-pinene synthase) (Synthase I) (Q84KL6)
Organism: Pinus taeda (Loblolly pine)
Function: Involved in defensive oleoresin formation in conifers in response to insect attack or other injury. Involved in monoterpene (C10) olefins biosynthesis. Produces mainly (-)-alpha-pinene (79%) and lesser amounts of (-)-beta-pinene (4.2%), nearly racemic mixtures of camphene (2.8% (+)/2.2% (-)) and limonene (2.4% (+)/3.7% (-)), as well as small amounts of (+)-alpha-pinene (3.3%) and (+)-beta-pinene (2.4%).
Subcellular location: Plastid, chloroplast {ECO:0000305}.
Interaction partners:
Sequence:
MSPVSVISLPSDLCLPTSFIDRSGRELIPLHITIPNVAMRRQGKLMTRASMSMNLRTAVSDDAVIRRRGDFHSNLWDDDLIQSLSSPYGEPSYRERAERLIGEVKNSFNSMSNEDGESITPLDDLIQRLWMVDSVERLGIDRHFKKEIKSALDHVYRYWSEKGIGCGRESVVTDLNSTALGLRTLRLHGYDVSADVLNHFKNQSGQFACTLKQTEDQIRTVLNLYRASLIAFPGEKVMDEAESFSAKYLKEALQKIPVSSFSREIGDVLEYGWHTYLPRLEARNYIDVFGQDTENSKSYMKTEKLLELAKLEFNIFHALQKRELEYLVRWWKGSGSPQMTFCRHRHVEYYTLASCIAFEPQHSGFRLGFAKACHIITVLDDMYDTFGTLDELELFTSAIKRWDPSATECLPEYMKGVYMIVYNTVNEMSQEADKAQGRDTLNYCRQAWEEYIDAYMQEAKWIASGEVPTFEEYYENGKVSSGHRVSALQPILTTDIPFPEHVLKEVDIPSQLNDLASAILRLRGDTRCYQADRARGEEASCISCYMKDNPGTTEEDALNHLNAMISDVIKGLNWELLKPNSSVPISAKKHAFDISRAFHCGYKYRDGYSVANIETKSLVKRTVIDPVTL