wanglab/gogpt-training-data huggingface dataset:
Protein: Daphnetin O-methyltransferase 1 (ScOMT1) (EC 2.1.1.-) (Q84XW5)
Organism: Secale cereale (Rye)
Function: O-methyltransferase involved in the biosynthesis of coumarins natural products such as daphnetin derivatives. Catalyzes specifically the methylation of daphnetin (7,8-dihydroxycoumarin) to produce hydrangetin (7-hydroxy-8-methoxycoumarin). Probably involved in acclimation to low temperature conditions.
Interaction partners:
Sequence:
MPSSQAQADLWRHTLYYLTSMGLRCAVKLGIPTAIHNLGGVSSLPDLAAALSIPASKQPFLGRLMRALVTSGVFANGKERLLGGLFRLNPLSRILVEGVVAEEHHSQTSFVLAGTSRHYMEAALGMADWFKKDATGPVPTVFEDVHSASLFDESTAALDPELDALVTEGLAAHDNLGIGTIIREFHDLFKGLVSLTDFCCGDGTTSRAITKAHPHVKFTVLDLPKVIDKTPSDGIVNYFAGDLFHTVPKAQAVMLKLVLHHLSYEDCFKILTQCKDAIPSREEGGKVIVIDIVVAPSLGQVMFKEQTLMDILMLVFTRGRQRSENNWHELFTKAGFSDYKIVKKLGARGVIEVYK
Protein: Fructosyl amine:oxygen oxidoreductase (Q4WIF5)
Organism: Aspergillus fumigatus (strain ATCC MYA-4609 / CBS 101355 / FGSC A1100 / Af293) (Neosartorya fumigata)
Interaction partners:
- N,N-dimethylglycine oxidase, putative
- Glycine cleavage system P protein
- Serine hydroxymethyltransferase
- Serine hydroxymethyltransferase, cytosolic
- alanine--glyoxylate transaminase
- Alanine racemase
- Threonine aldolase, putative
- FAD dependent oxidoreductase superfamily
- D-amino-acid oxidase
- 5-aminolevulinate synthase
Sequence:
MAPSILSTESSIIVIGAGTWGCSTALHLARRGYKDVTVLDPHPVPSPIAAGNDINKIMEHSELKDGSSDPRSAAFSTFTRAALKAWKTDPVFQPYFHETGFIISGHTPALIDHIRKDEVEPSETNFVKLETAEDFRRTMPPGVLTGDFPGWKGWLHKSGAGWIHAKKAMISAFNEAKRLGVRFVTGSPEGNVVSLVYEDGDVVGARTADGRVHKAHRTILSAGAGSDSLLDFKKQLRPTAWTLCHIQMGPEEVKQYRNLPVLFNIAKGFFIEPDEDKLELKICDEHPGYCNFLPDPNRPGQEKSVPFAKHQIPLEAEARARDFLHDTMPHLADRPLSFARICWDADTPDRAFLIDRHPEHPSLLVAVGGSGNGAMQMPTIGGFIADALESKLQKEVKDIVRWRPETAVDRDWRATQNRFGGPDRIMDFQQVGEDQWTKIGESRGP
Protein: Thiosulfate sulfurtransferase RDL2, mitochondrial (EC 2.8.1.1) (Altered inheritance of mitochondria protein 42) (Found in mitochondrial proteome protein 31) (Rhodanese-like protein 2) (Q08742)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Thiosulfate sulfurtransferase which catalyzes the transfer of sulfane sulfur from thiosulfate to cyanide.
Subcellular location: Mitochondrion {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:14576278}.
Interaction partners:
- Small ribosomal subunit protein uS17m
- Small ribosomal subunit protein mS29
- Small ribosomal subunit protein mS43
- Cysteine desulfurase, mitochondrial
- mRNA-binding protein PUF3
- Large ribosomal subunit protein uL15m
- CDC25-like phosphatase YCH1
- Large ribosomal subunit protein uL13m
- Large ribosomal subunit protein bL17m
- Large ribosomal subunit protein uL3m
Sequence:
MFKHSTGILSRTVSARSPTLVLRTFTTKAPKIYTFDQVRNLVEHPNDKKLLVDVREPKEVKDYKMPTTINIPVNSAPGALGLPEKEFHKVFQFAKPPHDKELIFLCAKGVRAKTAEELARSYGYENTGIYPGSITEWLAKGGADVKPKK
Protein: Microcephalin (Q6RAS1)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
EYFAGGLHSSFDDLCGNSGCGNQERKLEGSINDIKSDVCISSLVLKANNIHSSPSFTHLDKSSPQKFLSNLSKEEINLQINIAGKVVTPDQKQAAGMSQETFEEKYRLSPTLSSTKGHLLIHSRPRSSSVKRKRVSHGSHSPPKEKCKRKRSTRRSIMPRLQLCRSEGRLQHVAGPALEALSCGESSYDDYFSPDNLKERYSENLPPESQLPSSPAQLSCRSLSKKERTSIFEMSDFSCVGKKTRTVDITNFTAKTISSPRKTGNGEGRATSSCVTSAPEEALRCCRQAGKEDACPEGNGFSYTIEDPALPKGHDDDLTPLEGSLEEMKEAVGLKSTQNKGTTSKISNSSEGEAQSEHEPCFIVDCNMETSTEEKENLPGGYSG
Protein: Probable xyloglucan glycosyltransferase 5 (EC 2.4.1.-) (Cellulose synthase-like protein C5) (AtCslC5) (Q9SB75)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Probable beta-1,4-glucan synthase rather involved in the synthesis of the xyloglucan backbone than cellulose. Seems to work simultaneously with xyloglucan 6-xylosyltransferase. Xyloglucan is a noncellulosic polysaccharides of plant cell wall and consists of a glucan backbone substituted by xylose, galactose and fucose.
Subcellular location: Golgi apparatus membrane {ECO:0000250|UniProtKB:Q9LJP4}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Hyperosmolality-gated Ca2+ permeable channel 1.5
- Hyperosmolality-gated Ca2+ permeable channel 1.6
- Xyloglucan galactosyltransferase XLT2
- Xyloglucan 6-xylosyltransferase 2
- Xyloglucan 6-xylosyltransferase 1
- Xyloglucan galactosyltransferase MUR3
- Cellulose synthase A catalytic subunit 1
- Probable galacturonosyltransferase-like 2
Sequence:
MAPRLDFSDWWAKDTRKGTPVVVKMENPNYSVVEIDGPDSAFRPVEKSRGKNAKQVTWVLLLKAHRAVGCLTWLATVFWSLLGAIKKRLSFTHPLGSEKLGRDRWLFTAIKLFLAVSLVILGFEIVAYFRGWHYFQSPSLHIPTSTLEIQSLFHLVYVGWLTLRADYIAPPIKALSKFCIVLFLIQSVDRLVLCLGCFWIKYKKIKPRFDEEPFRNDDAEGSGSEYPMVLVQIPMCNEREVYEQSISAVCQLDWPKDRILVQVLDDSNDESIQQLIKAEVAKWSQKGVNIIYRHRLVRTGYKAGNLKSAMSCDYVEAYEYVAIFDADFQPTPDFLKLTVPHFKDNPELGLVQARWTFVNKDENLLTRLQNINLCFHFEVEQQVNGVFLNFFGFNGTAGVWRIKALEESGGWLERTTVEDMDIAVRAHLHGWKFIYLNDVKVLCEVPESYEAYKKQQHRWHSGPMQLFRLCLGSILTSKIAIWKKANLILLFFLLRKLILPFYSFTLFCIILPLTMFVPEAELPVWVICYIPVFMSFLNLLPSPKSFPFIVPYLLFENTMSVTKFNAMVSGLFQLGSSYEWIVTKKAGRSSESDLLSITEKETPTKKSQLLRGVSDSELLELSQLEEQKQAVSKKPVKKTNKIYHKELALAFLLLTAALRSLLAAQGVHFYFLLFQGVTFLLVGLDLIGEQMS
Protein: Secreted frizzled-related protein 1 (Q9GUF5)
Organism: Caenorhabditis elegans
Interaction partners:
- Protein Wnt-1
- Protein Wnt
- Protein mom-2
- Frizzled-2
- Frizzled-4
- Frizzled-4
- Protein mom-5
- Protein Wnt-2
- Abnormal cell lineage protein 44
- Inactive tyrosine-protein kinase RYK
Sequence:
MMLFPVLYILFAFSVTNGYLEDSWAMFSSERPVGPKCVDIPSNLSICNGIEYTQMRLPNILEHETVSEAIHASKDWESLLRLNCHPDTQRFLCSLFAPVCLMQMDRLILPCKSLCMAVKQGCENRMANYGFPWPEMLSCEKFEDDDMCIKPMQPAKPPAGSSTTCTACSQVATYENLVDQFCRSHLVLKAKVIRDSPTHIRVRNGRSLKKGERRRGVSDVEIRLSSESDGSCPCNIPVKNQNEKLLVMASRQPDGKYLANLVLPWQKEKNFKRAIHQFQRLNCQSLGREIRESASRRPHYYEMRRHNTGRYQMF
Protein: Phosphomevalonate kinase, peroxisomal (EC 2.7.4.2) (5-phosphomevalonate kinase) (AtPMK) (Q9C6T1)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Peroxisome {ECO:0000269|PubMed:21655959}.
Interaction partners:
- Mevalonate kinase
- Diphosphomevalonate decarboxylase MVD2, peroxisomal
- Diphosphomevalonate decarboxylase MVD1, peroxisomal
- Pre-mRNA-processing protein 40C
- Hydroxymethylglutaryl-CoA synthase
- 2-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase, chloroplastic
- 4-diphosphocytidyl-2-C-methyl-D-erythritol kinase, chloroplastic
- Acetyl-CoA acetyltransferase 1
- Acetyl-CoA acetyltransferase 2
- 1-deoxy-D-xylulose-5-phosphate synthase, chloroplastic
Sequence:
MAVVASAPGKVLMTGGYLVLEKPNAGLVLSTNARFYAIVKPINEEVKPESWAWKWTDVKLTSPQLSRESMYKLSLNHLTLQSVSASDSRNPFVEHAIQYAIAAAHLATEKDKESLHKLLLQGLDITILGSNDFYSYRNQIESAGLPLTPESLGTLAPFASITFNAAESNGANSKPEVAKTGLGSSAAMTTAVVAALLHYLGVVDLSDPCKEGKFGCSDLDVIHMIAQTSHCLAQGKVGSGFDVSCAVYGSQRYVRFSPEVLSFAQVAVTGLPLNEVIGTILKGKWDNKRTEFSLPPLMNLFLGEPGSGGSSTPSMVGAVKKWQMSDPEKARENWQNLSDANLELETKLNDLSKLAKDHWDVYLRVIKSCSVLTSEKWVLHATEPINEAIIKELLEAREAMLRIRILMRQMGEAASVPIEPESQTQLLDSTMSAEGVLLAGVPGAGGFDAIFAITLGDSGTKLTQAWSSHNVLALLVREDPHGVCLESGDPRTTCITSGVSSIHLE
Protein: Phospholipid transfer protein (Lipid transfer protein II) (P55058)
Organism: Homo sapiens (Human)
Function: Mediates the transfer of phospholipids and free cholesterol from triglyceride-rich lipoproteins (low density lipoproteins or LDL and very low density lipoproteins or VLDL) into high-density lipoproteins (HDL) as well as the exchange of phospholipids between triglyceride-rich lipoproteins themselves. Facilitates the transfer of a spectrum of different lipid molecules, including diacylglycerol, phosphatidic acid, sphingomyelin, phosphatidylcholine, phosphatidylinositol, phosphatidylglycerol, cerebroside and phosphatidyl ethanolamine. Plays an important role in HDL remodeling which involves modulating the size and composition of HDL. Also plays a key role in the uptake of cholesterol from peripheral cells and tissues that is subsequently transported to the liver for degradation and excretion. Two distinct forms of PLTP exist in plasma: an active form that can transfer phosphatidylcholine from phospholipid vesicles to HDL, and an inactive form that lacks this capability.
Subcellular location: Secreted {ECO:0000269|PubMed:19321130}. Nucleus {ECO:0000269|PubMed:19321130}. Note=Nuclear export is XPO1/CRM1-dependent. {ECO:0000269|PubMed:19321130}.
Interaction partners:
- Apolipoprotein A-I
- Apolipoprotein E
- Apolipoprotein B-100
- Apolipoprotein A-II
- Phosphatidylcholine-sterol acyltransferase
- Hepatic triacylglycerol lipase
- Serum paraoxonase/arylesterase 1
- Clusterin
- Apolipoprotein L1
- Lipoprotein lipase
Sequence:
MALFGALFLALLAGAHAEFPGCKIRVTSKALELVKQEGLRFLEQELETITIPDLRGKEGHFYYNISEVKVTELQLTSSELDFQPQQELMLQITNASLGLRFRRQLLYWFFYDGGYINASAEGVSIRTGLELSRDPAGRMKVSNVSCQASVSRMHAAFGGTFKKVYDFLSTFITSGMRFLLNQQICPVLYHAGTVLLNSLLDTVPVRSSVDELVGIDYSLMKDPVASTSNLDMDFRGAFFPLTERNWSLPNRAVEPQLQEEERMVYVAFSEFFFDSAMESYFRAGALQLLLVGDKVPHDLDMLLRATYFGSIVLLSPAVIDSPLKLELRVLAPPRCTIKPSGTTISVTASVTIALVPPDQPEVQLSSMTMDARLSAKMALRGKALRTQLDLRRFRIYSNHSALESLALIPLQAPLKTMLQIGVMPMLNERTWRGVQIPLPEGINFVHEVVTNHAGFLTIGADLHFAKGLREVIEKNRPADVRASTAPTPSTAAV
Protein: Dedicator of cytokinesis protein 10 (Zizimin-3) (Q8BZN6)
Organism: Mus musculus (Mouse)
Function: Guanine nucleotide-exchange factor (GEF) that activates CDC42 and RAC1 by exchanging bound GDP for free GTP. Essential for dendritic spine morphogenesis in Purkinje cells and in hippocampal neurons, via a CDC42-mediated pathway. Sustains B-cell lymphopoiesis in secondary lymphoid tissues and regulates FCER2/CD23 expression.
Subcellular location: Nucleus {ECO:0000250|UniProtKB:Q96BY6}. Cytoplasm {ECO:0000250|UniProtKB:Q96BY6}. Cell projection, dendritic spine {ECO:0000269|PubMed:25851601}.
Interaction partners:
- Cell division control protein 42 homolog
- Ras-related C3 botulinum toxin substrate 3
- E3 ubiquitin-protein ligase HERC2
- Ras-related C3 botulinum toxin substrate 1
- Ras-related C3 botulinum toxin substrate 2
Sequence:
MAGERTRRFTRSLLRPGQAAELRHSAASAAAVAVSSRQQQRQEKPRLLDPLDYETVIEELEKTYRDDPLQDLLFFPSDDFSTATVSWDIRTLYSTVPEEAEHRAESLLVKEACKFYSSQWYVVNYKYEQYSGDIRQLPRAEHKPEKLPSHSFEVDHEDADKDEDTTSHSSSKGGGGAGGTGVFKSGWLYKGNFNSTVNNTVTVRSFKKRYFQLTQLPDNSYIMNFYKDEKISKEPKGCIFLDSCTGVVQNNRLRKYAFELKMNDLTYFVLAAETESDMDEWIHTLNRILQISPEGPLQGRKSAELAELGLDPLDNCVTCECTLEETDSSENSLHPDFAKYLTETEDTVKTTRNMGRLNLFSLDPDIDTLKLQKRDSFENELMIKPFEEKAAKRIMIICRALNFNLQGCVTENEYDPVTNIEPFFVSVALYDLRDNRKISADFHVDLNHPAVRQMLSGTPPALENGNIDTGTPRQSEEPHIKGLPEEWLKFPKQAVFSVSDPHSEIVLVAKVEKVLMGNIGSGAEPYIKNPDSNKFAQKILKSNRQFCSKLGKYRMPFAWAVRSVFKDNQGNVDRDSRFSPLYRQESSKMSSEDLLKLVSDYRRADRISKMQSIPGSLDIAVDNIPLEHPNCVTSSFIPVKPFNVSAQSEPTVEVEEFIYDSTKYCRPYRVYKNQIYVYPKHLKYDSQKCFNKARNITVCIEFKNSDDDGAKPMKCIYGKPGGPLFTSSAYTAVLHHSQNPDFSDEVKIELPTQLHGKHHLLFSFYHITCDINAKANAKKKEALETSVGYAWLPLMKHDQIASQEYNIPIATTLPPNYLSIQDPTSAKHGGSDIKWVDGGKPLFKVSTFVVSTVNTQDPHVNAFFRQCQKREKDMSQSPTSSFVRACKNLLNVDKIHSIMSFLPIILNQLFKILVQNEEDEITATVTRVLADIVAKCHEEQLDHSVQSYIKFVFKTKSYKERTIHEELAKNLSDLLKSNDSTIVKHVLEHSWFFFAIILKSMAQHLIDTNKIQLPRAQRFPESYQSELDNLVMGLCDHVIWKCKEAPEETKRANHSVARFLKRCFTFMDRGFVFKMVNNYISMFSSGEFKTLCQYKFDFLQEVCQHEHFIPLCLPIRSANIPDPLTPSESIRELHASDMPEYSVTNEFCRKHFLIGILLREVGFALQEDQDIRHLALAVLKNLMAKHSFDDRYREPRKQAQIASLYMPLYGMLLDNMPRIYLKDLYPFTVNTSNQGSRDDLSTNGGFQTQTSMKHATSVDTSFSKDVLNSIAAFSSIAISTVNHADSRASLASLDSNPSTTEKSSEKTDNCEKIPRPLSLIGSTLRFDKLDQAETRSLLMCFLHIMKTISDETLIAYWQRAPSPEVSDFFSILDVCLQNFRYLGKRNIIRKIAAAFKFVQSTQNNGTLKGSNPSCQTSGLLSQWMHTTSGHEGHKQHRSQTLPIIRGKNALSNPKLLQMLDNSMNSNSNEIDIVHHVDTEANIATEVCLTILDLLSLFTQVHQRQLQQSDCQNSLMKRVFDTYMLFFQVNQSASALKHVFASLRLFVCKFPSAFFQGPADLCGSFCYEVLKCCNHRSRLTQMEASALLYFFMRKNFEFNKQKSIVRSHLQLIKAVSQLIADAGIGGSRFQHSLAITNNFANGDKQMKNSNFPAEVKDLTKRIRTVLMATAQMKEHEKDPEMLVDLQYSLANSYASTPELRRTWLESMAKIHARNGDLSEAAMCYIHIAALIAEYLKRKGYWKMEKICTPPLLPEDTQPCDSNLLLTTPGGGSMFSMGWPAFLSITPNIKEEGAMKEDSGMQDTPYNENILVEQLYMCVEFLWKSERYELIADVNKPIIAVFEKQRDFKKLSDLYYDIHRSYLKVAEVVNSEKRLFGRYYRVAFYGQGFFEEEEGKEYIYKEPKLTGLSEISQRLLKLYADKFGADNVKIIQDSNKVNPKDLDPKYAYIQVTYVTPFFEEKEIEDRKTDFEMHHNINRFVFETPFTLSGKKHGGVAEQCKRRTVLTTSHLFPYVKKRIQVISQSSTELNPIEVAIDEMSRKVSELNQLCTTEEVDMIRLQLKLQGSVSVKVNAGPMAYARAFLEETNAKKYPDNQVKLLKEIFRQFADACGQALDVNERLIKEDQLEYQEELRSHYKDMLSELSAIMNEQITGRDDPAKCGVERPYTTRVTSKGTAAVPVVSISSSAEV
Protein: Copper ion transmembrane transporter (Q8LG21)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
Sequence:
MAATMIGINLSCFKSTSFFSPDLNSLQSKLSLLSLKPSPTQPRKSTVIRMGGGPRTFPGGVSKWQWKRMQAKKQKQLLKARLCRERQIYEMRKRAELKAAVAELERPWEPIHKPPNLFSVCADEQVKVLADRFQKPGGFDLWTDRDGPQLFESVDDLPSARFFPKGVVHSVKPYGRLSSSSVVDDGDESEVKDEEIGKKLRGRRVRKRGDDGGKRRTENRGNGGRLRNGGSSSSQVYDMTLQNDGRYEIGS
Protein: AMP deaminase 1 (EC 3.5.4.6) (AMP deaminase isoform M) (Myoadenylate deaminase) (P23109)
Organism: Homo sapiens (Human)
Function: AMP deaminase plays a critical role in energy metabolism.
Interaction partners:
- Adenylosuccinate synthetase isozyme 2
- Adenine phosphoribosyltransferase
- Adenosine kinase
- Adenylosuccinate lyase
- Bifunctional purine biosynthesis protein ATIC
- Inosine-5'-monophosphate dehydrogenase 2
- Inosine triphosphate pyrophosphatase
- Hypoxanthine-guanine phosphoribosyltransferase
- Inosine-5'-monophosphate dehydrogenase 1
- Adenylosuccinate synthetase isozyme 1
Sequence:
MPLFKLPAEEKQIDDAMRNFAEKVFASEVKDEGGRQEISPFDVDEICPISHHEMQAHIFHLETLSTSTEARRKKRFQGRKTVNLSIPLSETSSTKLSHIDEYISSSPTYQTVPDFQRVQITGDYASGVTVEDFEIVCKGLYRALCIREKYMQKSFQRFPKTPSKYLRNIDGEAWVANESFYPVFTPPVKKGEDPFRTDNLPENLGYHLKMKDGVVYVYPNEAAVSKDEPKPLPYPNLDTFLDDMNFLLALIAQGPVKTYTHRRLKFLSSKFQVHQMLNEMDELKELKNNPHRDFYNCRKVDTHIHAAACMNQKHLLRFIKKSYQIDADRVVYSTKEKNLTLKELFAKLKMHPYDLTVDSLDVHAGRQTFQRFDKFNDKYNPVGASELRDLYLKTDNYINGEYFATIIKEVGADLVEAKYQHAEPRLSIYGRSPDEWSKLSSWFVCNRIHCPNMTWMIQVPRIYDVFRSKNFLPHFGKMLENIFMPVFEATINPQADPELSVFLKHITGFDSVDDESKHSGHMFSSKSPKPQEWTLEKNPSYTYYAYYMYANIMVLNSLRKERGMNTFLFRPHCGEAGALTHLMTAFMIADDISHGLNLKKSPVLQYLFFLAQIPIAMSPLSNNSLFLEYAKNPFLDFLQKGLMISLSTDDPMQFHFTKEPLMEEYAIAAQVFKLSTCDMCEVARNSVLQCGISHEEKVKFLGDNYLEEGPAGNDIRRTNVAQIRMAYRYETWCYELNLIAEGLKSTE
Protein: phosphatidylinositol-3,4,5-trisphosphate 5-phosphatase (EC 3.1.3.86) (A0A0C5AMM3)
Organism: Ictalurus punctatus (Channel catfish) (Silurus punctatus)
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000256|ARBA:ARBA00004245}. Membrane {ECO:0000256|ARBA:ARBA00004170}; Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004170}.
Interaction partners:
Sequence:
MSSHQPWYHGNITRSMAEDLLSKNAKDGSFLLRDSESIQGAYALCVLYQNCVYTYRILPNEEKKLSVQASEGVPIRFFSVVSELVEAYYKENMGLVTHLQYPVQKEEEPEDEPEQFSLPPQLPPRNFTPIESKECHTEPVKTEQKVSILDTYLQRMQLVDMSHISEEHQKAIQDYFSSAVGLDVEQVHNGNLNLPNLKKLLKTICKSLNSEISRTLPSLEALQKIIDQPMSPGAGRLRGQLSLDASQSVSFRLEQLTKLLYSIEDKAKNTVFESAGYDGGHRKSLIPPVTFEVKSDSLGISNKMFLKVDVESGKVYFKKSKDGPEDKYFVHNKILQLVKSKKMHNKLELVVETEKEKTQRKEFVFNDTKKREGFCQLLQQMKNKHSDKAEPDMISLFVGTWNMGNASPPTNITSWFQSKGQGKTRDDTASQIPHDIYVIGTQEDPLGEKDWIDIVRGTLRDITNISFKQIATQTLWNIRIIVLAKPEHENRISHIFCDSVKTGIANALGNKGAVGVSFMFNDTSFGFVNSHLTSGSEKKIRRNQNYVSILRFLNLGDKKLNPFDITHRFTHLFWLGDLNYRIELPTAEAENIVMKIKQQQYQELLCRDQLTMERADGKVFLYYEEEDITFPPTYRLERDTHERYVYTKAKATGTKYNLPSWCDRVLRKSHPQVHVACHSYGCTCDIMTSDHAPVFATFDVGVTSQFVSKNDPIKESQGAIKFMNCVATLKTKSKTRFFIEYHSSCLEKFVKSSEIYNQESTEGSIKVRFEAHVELTPIISDPEYLLDQHILISITSTDSDESYGETCVALRAAEEAYTEFDVPLTHHGEQTGMLSGGIQLRTSEGKLTEKLYDFIKIGDDSGTGKVKSGDLSNKSLALPTDISNPNYMDVGYKSSSQSGWSYTVSNRQGASSGHMAKDTTTGNTSPKKTTYDHSVCSPTGKLSSPTSEEEQPAEMFDNPLYGSMGKSRCGKDQEMSRKEHLVIPEIFAFPKGSESDPDRAPPVPTPRARSFTCSEGKSQNPSPTPSTSSNHSSNSSLQPQSFSKKPVVPSRSEGGGMMSGKPPLPMKSRPEPQSKPRDYRDSSELPGKMRPHARPCQPLPKDVHPEATPSPKTGRL
Protein: Endoplasmic reticulum chaperone BiP (EC 3.6.4.10) (78 kDa glucose-regulated protein) (GRP-78) (Binding-immunoglobulin protein) (BiP) (Heat shock protein 70 family protein 5) (HSP70 family protein 5) (Heat shock protein family A member 5) (Immunoglobulin heavy chain-binding protein) (P07823)
Organism: Mesocricetus auratus (Golden hamster)
Function: Endoplasmic reticulum chaperone that plays a key role in protein folding and quality control in the endoplasmic reticulum lumen (By similarity). Involved in the correct folding of proteins and degradation of misfolded proteins via its interaction with DNAJC10/ERdj5, probably to facilitate the release of DNAJC10/ERdj5 from its substrate (By similarity). Acts as a key repressor of the ERN1/IRE1-mediated unfolded protein response (UPR). In the unstressed endoplasmic reticulum, recruited by DNAJB9/ERdj4 to the luminal region of ERN1/IRE1, leading to disrupt the dimerization of ERN1/IRE1, thereby inactivating ERN1/IRE1. Accumulation of misfolded protein in the endoplasmic reticulum causes release of HSPA5/BiP from ERN1/IRE1, allowing homodimerization and subsequent activation of ERN1/IRE1 (By similarity). Plays an auxiliary role in post-translational transport of small presecretory proteins across endoplasmic reticulum (ER). May function as an allosteric modulator for SEC61 channel-forming translocon complex, likely cooperating with SEC62 to enable the productive insertion of these precursors into SEC61 channel. Appears to specifically regulate translocation of precursors having inhibitory residues in their mature region that weaken channel gating. May also play a role in apoptosis and cell proliferation (By similarity).
Subcellular location: Endoplasmic reticulum lumen {ECO:0000250|UniProtKB:P11021}. Melanosome {ECO:0000250|UniProtKB:P11021}. Cytoplasm {ECO:0000250|UniProtKB:P20029}. Cell surface. Note=Identified by mass spectrometry in melanosome fractions from stage I to stage IV (By similarity). Localizes to the cell surface in epithelial cells; high levels of free iron promotes cell surface localization (By similarity). {ECO:0000250|UniProtKB:P11021}.
Interaction partners:
- Endoplasmin
- Hypoxia up-regulated protein 1
- DnaJ homolog subfamily C member 10
- Mesencephalic astrocyte-derived neurotrophic factor
- DnaJ homolog subfamily B member 11
- Serine/threonine-protein kinase/endoribonuclease IRE1
- Nucleotide exchange factor SIL1
- Derlin
- non-specific serine/threonine protein kinase
- Protein disulfide-isomerase
Sequence:
MKFPMVAAALLLLCAVRAEEEDKKEDVGTVVGIDLGTTYSCVGVFKNGRVEIIANDQGNRITPSYVAFTPEGERLIGDAAKNQLTSNPENTVFDAKRLIGRTWNDPSVQQDIKFLPFKVVEKKTKPYIQVDIGGGQTKTFAPEEISAMVLTKMKETAEAYLGKKVTHAVVTVPAYFNDAQRQATKDAGTIAGLNVMRIINEPTAAAIAYGLDKREGEKNILVFDLGGGTFDVSLLTIDNGVFEVVATNGDTHLGGEDFDQRVMEHFIKLYKKKTGKDVRKDNRAVQKLRREVEKAKRALSSQHQARIEIESFFEGEDFSETLTRAKFEELNMDLFRSTMKPVQKVLEDSDLKKSDIDEIVLVGGSTRIPKIQQLVKEFFNGKEPSRGINPDEAVAYGAAVQAGVLSGDQDTGDLVLLDVCPLTLGIETVGGVMTKLIPRNTVVPTKKSQIFSTASDNQPTVTIKVYEGERPLTKDNHLLGTFDLTGIPPAPRGVPQIEVTFEIDVNGILRVTAEDKGTGNKNKITITNDQNRLTPEEIERMVNDAEKFAEEDKKLKERIDTRNELESYAYSLKNQIGDKEKLGGKLSSEDKETMEKAVEEKIEWLESHQDADIEDFKAKKKELEEIVQPIISKLYGSAGPPPTGEEDTSEKDEL
Protein: SUMO-activating enzyme subunit (Q7KJV6)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MAAAINGVFPPTLQELVKKSKVLVVGAGGIGCEVLKNLVLSGFTDIEIIDLDTIDLSNLNRQFLFHREHVGKSKARVARESALSFNPDAKITAYHDSVTSTDYGVNFFKKFDLVLSALDNRAARNHVNRMCLNADVPLIESGTAGYNGQVELIKRGLTQCYECTPKDKQRSFPGCTIRNTPSEPIHCIVWAKHLFNQLFGESLEDEDISPDAADPDAKEKDGGDGNGEPKGDGKEKGEESKEEKEAKEDTANGNIMRINTRQWAKDSNYDAGKLFNKFFNEDITYLLRMSNLWKTRKAPVPVQWDTLLPEGSSGDQKDVAKQHHKVWSIEECAQVFANSLKELSANFLKLEGDDTLAWDKDDQPAMDFVAACANVRSHIFDIERKSRFEIKSMAGNIIPAIATTNAITAGISVMRAFKVLEAKWEQCKAVYARLRPNARNHFLVPDASLPGPNPNCHVCASDPAITLKIDTKRMRIKELRDEVLVKTLNMLNPDVTVQSNGSILISSEEGETECNDGKLLSELNIVDGVILKCDDFFQNYELSIIISHFDAERDENLFEVVADASQLKPKDEDQKEAVKDKEDEPKSAKKRSTNGEGDSKDDGPSTSKRSRPNEVVEEDDDDCLVIEEDEDQADVVVVATDKLSVQSPPKSGSKRKPCEVIEDEDITEILESSDDEPAGPTKCKRSRLDDSNPVAVISID
Protein: Homeotic protein ultrabithorax (P05048)
Organism: Drosophila funebris (Fruit fly)
Function: Sequence-specific transcription factor which is part of a developmental regulatory system that provides cells with specific positional identities on the anterior-posterior axis. Binds the consensus region 5'-TTAAT[GT][GA]-3'. This homeotic protein controls development of the cells in the posterior thoracic and first abdominal segments. It activates the synthesis of the decapentaplegic (DPP) growth factor (By similarity).
Subcellular location: Nucleus.
Interaction partners:
Sequence:
MNSYFEQASGFYGHPHQASGMAMGSGGHHDQTTASAAAAAYRGFTLPLGMSPYANHHLQRTTQDSPYDASITAACNKIYGDAGSAYKQDCLNIKADAVNGYKDIWNTGGANGGGGGGGGGAATAGNTSNGSNAPNAANGQNNAGGGGMPVRPSACTPDSRVGGYLDTSGGSPVSHRGGGSAGGGNGTAGGVPQNSASGVGGGVGAGTAWNANCTISGAAAAQTAAASSLHQPGNHTFYPWMAIAGESTADPIK
Protein: Candida glabrata strain CBS138 chromosome G complete sequence (Q6FTD8)
Organism: Candida glabrata (strain ATCC 2001 / BCRC 20586 / JCM 3761 / NBRC 0622 / NRRL Y-65 / CBS 138) (Yeast) (Nakaseomyces glabratus)
Interaction partners:
- Ribosome-associated molecular chaperone SSB
- Candida glabrata strain CBS138 chromosome H complete sequence
- Candida glabrata strain CBS138 chromosome M complete sequence
- Candida glabrata strain CBS138 chromosome G complete sequence
- Candida glabrata strain CBS138 chromosome G complete sequence
- Candida glabrata strain CBS138 chromosome L complete sequence
- Candida glabrata strain CBS138 chromosome H complete sequence
- Candida glabrata strain CBS138 chromosome H complete sequence
- Transcription factor
- Candida glabrata strain CBS138 chromosome G complete sequence
Sequence:
MSKAVGIDLGTTYSCVAHFANDRVEIIANDQGNRTTPSYVAFTDTERLIGDAAKNQAAINPKNTVFDAKRLIGRKFDDAEVTNDAKHFPFKVINKDSKPAIEVEFKGETKTFTPEEISSMVLGKMKETAEQFLGTTVNDAVVTVPAYFNDSQRQATKDAGTIAGLNVLRIINEPTAAAIAYGLDKKGASEHNVLIFDLGGGTFDVSLLSIDDGVFEVKATAGDTHLGGEDFDNRLVTHLANEFKRKNKKDLTTNQRALRRLRTAAERAKRALSSSSQTSIEIDSLFEGVDFYTSITRARFEELCADLFRSTLEPVEKVLRDSKLDKSQIDEIVLVGGSTRIPKVQKLVSDFFNGKEPNRSINPDEAVAYGAAVQAAILTGDQSSKTQDLLLLDVAPLSLGIETAGGIMTKLIPRNSTIPTKKSEVFSTYADNQPGVLIQVFEGERTKTKDNNLLGKFELSGIPPAPRGVPQIEVTFDIDANGILNVSAVEKGTGKSNKITITNDKGRLSKEDIEKMVAEAEKFKAEDEKEAERVQAKNQLESYAFSLKNTLNEASFKEKVGEEDSKKLETAAQETIDWLDASQAASTDEYKDRQKELEAVANPIMSKFYGAAGGMPGAGGMPGAGGMPGAGAGTGAADSGPTVEEVD
Protein: Low specificity L-threonine aldolase (Low specificity L-TA) (TA) (EC 4.1.2.48) (P37303)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Catalyzes the cleavage of L-allo-threonine and L-threonine to glycine and acetaldehyde.
Interaction partners:
- Alanine--glyoxylate aminotransferase 1
- Serine hydroxymethyltransferase, cytosolic
- Serine hydroxymethyltransferase, mitochondrial
- Glycine dehydrogenase
- Threonine synthase
- Threonine dehydratase, mitochondrial
- Catabolic L-serine/threonine dehydratase
- 5-aminolevulinate synthase, mitochondrial
- NADP-dependent 3-hydroxy acid dehydrogenase
- Homoserine kinase
Sequence:
MTEFELPPKYITAANDLRSDTFTTPTAEMMEAALEASIGDAVYGEDVDTVRLEQTVARMAGKEAGLFCVSGTLSNQIAIRTHLMQPPYSILCDYRAHVYTHEAAGLAILSQAMVVPVVPSNGDYLTLEDIKSHYVPDDGDIHGAPTRLISLENTLHGIVYPLEELVRIKAWCMENGLKLHCDGARIWNAAAQSGVPLKQYGEIFDSISICLSKSMGAPIGSVLVGNLKFVKKATHFRKQQGGGIRQSGMMARMALVNINNDWKSQLLYSHSLAHELAEYCEAKGIPLESPADTNFVFINLKAARMDPDVLVKKGLKYNVKLMGGRVSFHYQVTRDTLEKVKLAISEAFDYAKEHPFDCNGPTQIYRSESTEVDVDGNAIREIKTYKY
Protein: DUF547 domain-containing protein (F4HWD0)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- AP3-complex subunit beta-A
- AP-3 complex subunit delta
- AP-3 complex subunit mu
- AP-4 complex subunit epsilon
- AP-1 complex subunit gamma-1
- Apoptosis inhibitory protein
- AP-1 complex subunit gamma-2
Sequence:
MNLYKQTRKCEKMMGLCSPSPSSHDCSSSSPRNSEKKQNVIVASPSRFSTYTKPSLSIEKRLLTYQDSNCNVTPKSSEDLRKEIASLEFEILRTEQYLLSLYRTAFDEQVSSFSPHTETSLVSNQFLPKSEQSDVTSVFSYHYQASPASECSSLCPPRSFQASLKALSAREKSRYVSSSHTTLGDLLGSTLIVDNIANPSRLSEDILRCICSVYCTLSSKARINSCLQASPSSPSSVSSKATFDSLNSRHEERKEANVPGVVVIESLELHLDDGSFNHAAVMLQNFRSLVQKLEKVDPSRMKREEKLAFWINIHNALTMHAYLAYGTHNRARNTSVLKAAYDVGGYSVNPYIIQSSILGIRPHFSQPLLQTLFSPSRKSKTCNVKHIYALEYPEALAHFALSSGFSTDPPVRVYTADCVFRDLRKSKEEFIRNNVRIHNETKILLPKIVHYYAKDMSLEPSALMETTVKCLPDSTKRTAQKLLKKKSRNIEYSPENSSFRYVIIQEPTTRRHDSTII