wanglab/gogpt-training-data huggingface dataset:
Protein: Proton-coupled folate transporter (rPCFT) (Heme carrier protein 1) (PCFT/HCP1) (Solute carrier family 46 member 1) (Q5EBA8)
Organism: Rattus norvegicus (Rat)
Function: Proton-coupled folate symporter that mediates folate absorption using an H(+) gradient as a driving force. Involved in the intestinal absorption of folates at the brush-border membrane of the proximal jejunum, and the transport from blood to cerebrospinal fluid across the choroid plexus. Functions at acidic pH via alternate outward- and inward-open conformation states (By similarity). Protonation of residues in the outward open state primes the protein for transport (By similarity). Binding of folate promotes breaking of salt bridge network and subsequent closure of the extracellular gate, leading to the inward-open state and release of protons and folate (By similarity). Also able to transport antifolate drugs, such as methotrexate and pemetrexed. Involved in FOLR1-mediated endocytosis by serving as a route of export of folates from acidified endosomes (By similarity). Also acts as a lower-affinity, pH-independent heme carrier protein and constitutes the main importer of heme in the intestine (By similarity). Imports heme in the retina and retinal pigment epithelium, in neurons of the hippocampus, in hepatocytes and in the renal epithelial cells (By similarity). Hence, participates in the trafficking of heme and increases intracellular iron content (By similarity).
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:Q96NT5}; Multi-pass membrane protein {ECO:0000255}. Apical cell membrane {ECO:0000250|UniProtKB:Q96NT5}; Multi-pass membrane protein {ECO:0000255}. Basolateral cell membrane {ECO:0000250|UniProtKB:Q96NT5}; Multi-pass membrane protein {ECO:0000255}. Endosome membrane {ECO:0000250|UniProtKB:Q96NT5}; Multi-pass membrane protein {ECO:0000255}. Cytoplasm {ECO:0000250|UniProtKB:Q6PEM8}. Note=Localizes to the apical membrane of intestinal cells in iron-deficient cells, while it resides in the cytoplasm in iron-replete cells (By similarity). Localizes to the basolateral membrane of choroid plexus (By similarity). {ECO:0000250|UniProtKB:Q6PEM8}.
Interaction partners:
- Reduced folate transporter
- Folate receptor alpha
- Plasma membrane ascorbate-dependent reductase CYBRD1
- Natural resistance-associated macrophage protein 2
Sequence:
MEGRVSPVGSSHRLLTAAVLFRGPVEPLVFLANFALVLQGPLTTQYIWHRISTELGYNGTRHRENCGNQSADPVLKEVETLTSHWTLYMNVGGFLVGLFWSTLLGAWSDRVGRRPLLVLASLGLLLQAVVSIFVVQLQLHIGFFVLGRALCALLGDFNGLLAASFASVADVSSNHSRTFRMALLEACIGVAGTLASLLGGHWLRAQGYANPFWLALAVLIVMTLYAAFCFGETVKEPKSTRLFTLRHHRSIVQLYVVPAPEKSRMHLALYSLAIFVVVTVHFGAQDILTLYELSTPLCWDSKLIGYGSAAQHLPYLTSLLGLRLLQFCLADTWVAEIGLAFNILGMVVFAFATITPLMFTGYGLLFLSLVTTPVIRAKLSKLVSESEQGALFSAVACVNSLAMLMASGIFNSLYPATLNFMKGFPFLLGAGLLFIPAILIGVLEKVNPHPEFQQFPQNS
Protein: alpha-1,2-Mannosidase (EC 3.2.1.-) (M9PG98)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00004240}.
Interaction partners:
- alpha-1,2-Mannosidase
- UDP-glucose:glycoprotein glucosyltransferase
- Calnexin 14D
- Calreticulin
- Derlin
- Endoplasmic reticulum lectin 1
- Calreticulin
- X-box-binding protein 1
- Endoplasmic reticulum chaperone BiP
- Homocysteine-induced endoplasmic reticulum protein, isoform A
Sequence:
MQQKPRNNGYPGTLICAVLLVLLSTGVSGQKQYSKARKLELREDVRRMFQHAYDGYLRHASNYDELRPLTCDGHDTWGSYSLTLIDALDTLATMGNFTEFRRAARLLEEKMDFDRDINVSVFETNIRIVGGLLSAHLLSKRAGVELEPGWPCKGPLLRLAEDVARRLLPAFVTNTGMPYGTVNLRYGVPKGETSITCTAGVGTFLIEFGTLSRLTGKTIYEDVAMKAVHALWAYRSPIGLFGNHIDVQSGRWTALDSGIGAGVDSLFEYLVKASVLLNRPELLELFHEARAAIDKYMRKEDWYVWVGMNKGRVTLPVFQSLEAFWPGILSIIGDTEPALRTISRYIGVWKKYGFLPEFYNIAAGEASPNREVYPLRPELIESAMYLYRATGNEYLLEFGEHMLETLEFSAKTKCGYATIRNVVTHEKENRMESFFLAETSKYLYLLFDEENFLHNDGSGGELLSTEDDVCVVQAGAYIFNTEAHPMDMSALHCCHAHNEDIYTSLDLQRFSPRAILERSKKRQVAVQEQWVPQCHPENNEFFNKEDESVQAQDSEKEQEREQSGTSTTMAVDIEVFDEFQQPAGDLLVSNFEQIREERELNESLHRNVVARNQLTVSDLDEFFAQRRESFASASEALNYVKTFMGNYTMDVAFIRGLQLYDTNMSSVLGTGAQKEYESRMRTLWQLYELQQQYVANIRVIQGLGLLTFPADGDRIPSHLTEVLDSLDKSAHLEHMDLQDLETRVSNTSSPQLAHIREVILKARNAYAIAMVNTSAMQEFAIRIYLSGTSEAGVRIHPLLEDGELSEEARKRPLKLAEERALFSYARRIVDFRKRMAETVDRLQTLMQDIPPPKRKEATTDSQAADASTVYTQTKAQMAAPAQQPEPSQEEKQSTQIQKGKLAENGSGLGEEESGCVWSQLVQTILRKTTVQRVKFDEAVLQENTRKALEKYARKELPHHLFACHRPEYIEGFAYRDFYPEALKVRRRCAHDNERLNCRAKRTER
Protein: Growth hormone receptor (Q0R5T2)
Organism: Bos taurus (Bovine)
Interaction partners:
Sequence:
EGKLEEVNTILAIHDNYKHEFYNDDSWVEFIELDIDDPDEKTEGSDTDRLLSNDHEKSLNIFGAKDDDSGRTSCYEPDILEADFHVSDMCDGTSEVAQPQRLKGEADISCLDQKNQNNSPSNDAAPASQQPSVILVEENKPRPLLIGGTESTHQAVHTQLSNPSSLANIDFYAQVSDITPAGNVVLSPGQKNKTGNPQCDTHPEVVTPCQANFIVDNAYFCEVDAKKYIALAPHVEAESHVEPSFNQEDIYITTESLTTTAGRSGTAEHVPSSEIPVPDYTSIHIVQSPQGLVLNATALP
Protein: Prothrombin (EC 3.4.21.5) (Coagulation factor II) (Q7SXH8)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
Sequence:
MGAKLAPLLLFLLFGQVFHLTLCHNVFINNKEASQIIRAKRANTVFEELKPGNLERECVEEICDHEEAREVFERVDKTEIFWAKYLGCEGTTLSRTPQNINSLRICATTEGDCFINIGAKYAGKVSVTKSGKACQYWKSNFPHKIDEFNVTQLKLQENFCRNPDKHKDGPWCFTRDPTVRRETCNVPKCGEAVVPPPKAPLDKFVEEGGGRERTTLDQRKAFFNPRSFGNGELDCGERPLFEKINKADKNEKELLMSYTGSRIVGGDEAEVASAPWQVMLYKRSPQELLCGASLISDEWILTAAHCILYPPWNKNFTINDIIVRLGKHSRTKYERGIEKIVAIDEIIVHPKYNWKENLNRDIALLHMKKPVVFTSEIHPVCLPTKSIAKNLMFAGYKGRVTGWGNLRESWTSNPSNLPAVLQQIHLPIVDQSICRNSTSVIITDNMFCAGYQPDDSKRGDACEGDSGGPFVMKSPSDNRWYQIGIVSWGEGCDRDGKYGFYTHLFRMRRWMKKVIEKTDSGDDE
Protein: Cell wall integrity/stress response component-like protein (Q9SMR9)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
Sequence:
MSPLKYLCFRKVLLLLLYSSLFLFSSSSFFASSVDDHELQRIDPHFRVRRLLVKDLDSTGDDDETNLPPPPKKKKLLTDSVSSSSSSSGTKKNQTKLLKPISSSSSTKNQTKLAKTTTMGTSHKLNSTKSSSNTTKTSSELKKLNSGTKSTNSTSSIKKSADLSKSSSSKNKTTIKPPSSKLSSPPSEKKSQPSSKPVTKSKQSEKEIKPFWLDDEEDEDFVSEFRDLPTRFQRSLIPDLERISTTSKNYINKANKQITKNFKPYFGNKYAPTIASVVSFVFILVPLLLVSLIFNRFKAYFSLQKILIFIQIYLSIYFSILCLSSLVTGIEPLKFLYATSSSTYVCLQILQTLGYVFYLLLLLMYLVLVFSTDCGLGLKVLGLAQTFVGFAVGLHYYVAVFHRVVLRQPPKTNWKIHGVYATCFLLICLLSNAERRKKEYLEEGGDEGKKN
Protein: Spore-specific protein YSW1 (P38280)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Interaction partners:
- Sporulation-regulated protein 3
- GLC7-interacting protein 1
- Sporulation-regulated protein 28
- Uncharacterized protein YBR197C
- Ribonuclease P protein subunit RPR2
- Cell division control protein 10
- Cell division control protein 3
- Cell division control protein 12
- Cell division control protein 11
Sequence:
MSSLADTVEGSEAKRGRFSNNALTSDTGILQKNSTLRNWFLKPTADLKNSCEDRVEDDVNDVYLNDKNSQKSVEERKLGRKVRSFFKQTNSNKDESVLEDEDDALVWKKTSNKCAKKENSHDIQKGSFTKKIRNSIFKSANDVKEFRNENNLLLPVELSSDDENESHFTDANSHVMQSKSPEKIPSKDQCLTKGAKNKGLKKEYEKSFEEYSDDSDDEFSPATPPENVLEGPYKFVFQTPNTFTSQPNITVENDFHKGGRHVIDYLNKKLATMNIDIDLTSGGKQNVSWEEELDQLSDHVIESITNHISKGRMHAQEKQDELEKLKLENLNLSTLKQENLQHKQEINSLKDNLESISKKNNDLILEMNKLKKKSTNNKTNEYISTDENENEEITKSNMGPGILELNVNETSKKLQQSTFKPSKYLPRETRNNENRLKHLEKRIFGLEKSLEKKKKQVRADSVRLDLNRYTIDQFLTLLKSLSEVLQFHNVYGNDLKENDDNIIKIETCCSALNMKNCFEDSSFRLQENSFKRQLGPLFANINFSLIDQLTMNFRFYERSANFQKETIGGLRMMLQDKDNYIKTLMQHLKKKESTKLIKDSKNGASTLTS
Protein: Radixin (A0A8I6AIS5)
Organism: Rattus norvegicus (Rat)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004413}; Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004413}; Cytoplasmic side {ECO:0000256|ARBA:ARBA00004413}. Cell projection {ECO:0000256|ARBA:ARBA00004316}.
Interaction partners:
Sequence:
APSPGVTTMDAELEFAIQPNTTGKQLFDQVVKTVGLREVWFFGLQYVDSKGYSTWLKLNKKVTQQDVKKENPLQFKFRAKFFPEDVSEELIQEITQRLFFLQVKEAILNDEIYCPPETAVLLASYAVQAKYGDYNKEIHKPGYLANDRLLPQRVLEQHKLTKEQWEERIQNWHEEHRGMLREDSMMEYLKIAQDLEMYGVNYFEIKNKKGTELWLGVDALGLNIYEHDDKINKRILALCMGNHELYMRRRKPDTIEVQQMKAQAREEKHQKQLERAQLENEKKKREIAEKEKERIEREKEELMERLRQIEEQTMKAQKELEEQTRKALELEQERQRAKEEAERLDRERRAAEEAKSAIAKQAADQMKNQEQLAAELAEFTAKIALLEEAKKKKEEEATEWQHKAFAAQEDLEKTKEELKTVMCAPPPPPPPAVVPPTENEHDEQDEHSAEASAELSSEGVTNHRSEEERVTETQKNERVKKQLQALSSELAQARDETKKTQNDVLHAENVKAGRDKYKTLRQIRQGNTKQRIDEFEAM
Protein: Conserved oligomeric Golgi complex subunit 4 (COG complex subunit 4) (Component of oligomeric Golgi complex 4) (Q95TN4)
Organism: Drosophila melanogaster (Fruit fly)
Function: Required for normal Golgi function.
Subcellular location: Golgi apparatus membrane {ECO:0000250|UniProtKB:Q9H9E3}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q9H9E3}; Cytoplasmic side {ECO:0000250|UniProtKB:Q9H9E3}.
Interaction partners:
- Conserved oligomeric Golgi complex subunit 8
- Conserved oligomeric Golgi complex subunit 1
- Conserved oligomeric Golgi complex subunit 7
- Conserved oligomeric Golgi complex subunit 6
- Conserved oligomeric Golgi complex subunit 2
- Conserved oligomeric Golgi complex subunit 3
- Conserved oligomeric Golgi complex subunit 5
- Syntaxin-5
- Vacuolar protein sorting-associated protein 53 homolog
- Syntaxin 16
Sequence:
MSVLEQLGALDIGTNEQVDETLQRIADEEAKVNEKLESLLAKQCQIEAKMSGIGRSLSLLHTVDSDSNKLNDQIVNTAQLAESVSAKVRRLDLARCRASECQQRVHDLIDLHLCSQGVVKAIGEEDYEKSATHIARFLAMDQQLLRRTADDVQGSITSVSDAVKTLEDATEKTRVLIAKRFDEAVKADDLASVERFFKIFPLVGCHRTGIEKFSLYICQKLANKAQKELRNAQDIAKAESRLQLAYADRLTAILENFARVVEVNQPIIEAFYGQASSSLIDMVSILQHECDTEVKNLLMEFNKNRQIQYRSKQVNESTQRSAGGGNLGSNSIQALGHYRKPSGGSVDKLNPKEIDAIIAEITVMHARVELYFRFMRRRLQVHVETCVPEKEQFDIMERYEKIMKNSDLRRQMQEILSTYLLLERYFMEESVLKAIGLDTYESGQQCSSMVDDVFFILRKSIRRALTTQSINGTCAVINNVAACLDGDFVNALKAPLKSGYPSGYIDLAQAYNAIQTSLQQGKLHSSDADRGRANFLVQLNNADISTEYIETLCQTMEQEIAGTFPQTTQVERQMLDSCLTELKAVRDALKATVDFGMQQLRSSVIKPRLNPWINQFLNYSHNLNEEELAAYEAGETFVQFFIVQLDGLLNSFKNSLSPRNYDALVSILATEVTIQLERAIKKISFNRLGGLVLDQEVRALGSYLTGATSWSVRDKMTRISQIATLLNLDKITELSEYWNPENNKEMSSWHLTPNEVRTFLTLRNDFRIEDIKRLQL
Protein: ARM repeat superfamily protein (F4JSY2)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
Sequence:
MFTAAASSSVGRWRTAFLSLRDEISTTPPPPVPLLLEDLLFSQSHSLISAVSHLPLHELTSDCLFLLDLVSKADGPDWIPVSRHTCQLIHDVCARLLFQLNSSSWPLLLHSFASVLEFLLRQPMPSSPYSAAYFSRIEPVIQCFETLRRLAPMHPENIHLVKFLVRVVPLLHQDLVLSYGFSNQDPSPTLLVEKKLPQQNRLWDSMALAFDMFGRAFSLSESLFPTDVSQCTLEVLRKVMDVLASKGQLVEDRFMWRYMPLVLWRLQFTPFFLGSIRLVALLASLRMFFCFGLTGPPQLSVSDVVHNDKHLNVKLSPLISGVSKNAKNTPYRPPHLRKRDDLNTRQPVSSSWRRLSAHDSGSSDVISSDSDFSDSDGSVPDSYFAQSSKVRIAAIVCIQDLCQADSKSFTTQWVTLFPTSDVLKPRKFEATLMTCLLFDPHLKVRIASASALATMMDGPSSIFLQVAEYKESTKYGSFMPLSNSLGLILMQLHTGILHLIHSDNHGRLLIQLFKILLLLISSTPYSRMPGELLPKVIMSLHARINEGFPFKNDKTGLLVAAIGCLSAAFSTFPPQMKVHNMLLDETSAGFNGCEWNSGVLSTLFRFAEQFSDASTCIEALQVLRAVALNYPTLVPAYWERVSILVYKLLQSAVVEDSPTTWKSSVRESVGYNGDKVLTAAIKVLDGCLRAISGFKGTEDLQYDRLMDTPFTSDCIRSIRISSAPSYGFDNTQEPIFQAGCDQWSEAIRKHIVLVLHHGSAVVRSTTVTCFAGITSSIFSAFNKQEKDFITSSIITAALHDKTPSVRSAACRAIGVISCFPETSLSAEIYEKFILAVEANTRDSLTSVRITASWALANLCDALRYRVDDRSFEGLKTTSQVVDALIECALRLTEDGDKVKSNAVRALGSISKYVKLRCMTSIKSVDQDVLPFPHQQSSNSHHLSCAVDTRWLERTVQAFLSCVTTGNVKVQWNVCHALSNLFSNETVKLQDMDWAPSVFSILLLLLRDASNFKIRIQAASALAVPATPLAYGRSFPDVVKGVEHTLQSLHSDRETTPANFKYKRSLENQLTSTMLHLLSLVSSCHFEALSEFLIRKASFLEEWLRGLCVTLKEEDNVSGSSGTSTSGGKQKKELISRAIRSLARSLRAGHSSEMAQKLQELDSNVN
Protein: Photosystem II protein D1 (PSII D1 protein) (EC 1.10.3.9) (Photosystem II Q(B) protein) (Q6ENJ7)
Organism: Oryza nivara (Indian wild rice) (Oryza sativa f. spontanea)
Function: Photosystem II (PSII) is a light-driven water:plastoquinone oxidoreductase that uses light energy to abstract electrons from H(2)O, generating O(2) and a proton gradient subsequently used for ATP formation. It consists of a core antenna complex that captures photons, and an electron transfer chain that converts photonic excitation into a charge separation. The D1/D2 (PsbA/PsbA) reaction center heterodimer binds P680, the primary electron donor of PSII as well as several subsequent electron acceptors.
Subcellular location: Plastid, chloroplast thylakoid membrane {ECO:0000255|HAMAP-Rule:MF_01379}; Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_01379}.
Interaction partners:
- Photosystem II CP47 reaction center protein
- Photosystem II CP43 reaction center protein
- Cytochrome b559 subunit beta
- Cytochrome b559 subunit alpha
- photosystem II
- Uncharacterized protein
- Photosystem II D2 protein
- Photosystem II reaction center protein H
- Photosystem II reaction center protein K
- Photosystem II reaction center protein I
Sequence:
MTAILERRESTSLWGRFCNWITSTENRLYIGWFGVLMIPTLLTATSVFIIAFIAAPPVDIDGIREPVSGSLLYGNNIISGAIIPTSAAIGLHFYPIWEAASVDEWLYNGGPYELIVLHFLLGVACYMGREWELSFRLGMRPWIAVAYSAPVAAATAVFLIYPIGQGSFSDGMPLGISGTFNFMIVFQAEHNILMHPFHMLGVAGVFGGSLFSAMHGSLVTSSLIRETTENESANEGYRFGQEEETYNIVAAHGYFGRLIFQYASFNNSRSLHFFLAAWPVVGIWFTALGISTMAFNLNGFNFNQSVVDSQGRVINTWADIINRANLGMEVMHERNAHNFPLDLAALEVPSLNG
Protein: Ly6/PLAUR domain-containing protein 6 (Q66IA6)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: Acts as an important regulator of embryogenesis through its enhancement of Wnt/beta-catenin signaling. Positively regulates Wnt/beta-catenin signaling by ensuring phosphorylation of lrp6 specifically in plasma membrane rafts and its subsequent internalization into signaling-competent vesicles. Essential for the wnt8-mediated patterning of the mesoderm and neuroectoderm during gastrulation.
Subcellular location: Cell membrane {ECO:0000269|PubMed:23987510}; Lipid-anchor, GPI-anchor {ECO:0000269|PubMed:23987510}. Membrane raft {ECO:0000269|PubMed:23987510}.
Interaction partners:
- Leucine-rich repeat-containing 31.
Sequence:
MEPWPLMAWGLMLTAITGWIKAVQSRDFTEKDIIFLHPSTTPYPGGFKCFTCEDAPDNYECNRWAPDLYCPRESRYCYTHHKMSWDGNTVSVTKRCVPLEDCLQTGCSDIDHEGNRVCTACCEGNICNLPLPRNETDAIFSTTSPINRSAQSTQTLPLLLLSVSITSLMLHSIN
Protein: Cathepsin E (EC 3.4.23.34) [Cleaved into: Cathepsin E form I; Cathepsin E form II] (P14091)
Organism: Homo sapiens (Human)
Function: May have a role in immune function. Probably involved in the processing of antigenic peptides during MHC class II-mediated antigen presentation. May play a role in activation-induced lymphocyte depletion in the thymus, and in neuronal degeneration and glial cell activation in the brain.
Subcellular location: Endosome {ECO:0000269|PubMed:7983070}. Note=The proenzyme is localized to the endoplasmic reticulum and Golgi apparatus, while the mature enzyme is localized to the endosome.
Interaction partners:
- Cathepsin S
Sequence:
MKTLLLLLLVLLELGEAQGSLHRVPLRRHPSLKKKLRARSQLSEFWKSHNLDMIQFTESCSMDQSAKEPLINYLDMEYFGTISIGSPPQNFTVIFDTGSSNLWVPSVYCTSPACKTHSRFQPSQSSTYSQPGQSFSIQYGTGSLSGIIGADQVSVEGLTVVGQQFGESVTEPGQTFVDAEFDGILGLGYPSLAVGGVTPVFDNMMAQNLVDLPMFSVYMSSNPEGGAGSELIFGGYDHSHFSGSLNWVPVTKQAYWQIALDNIQVGGTVMFCSEGCQAIVDTGTSLITGPSDKIKQLQNAIGAAPVDGEYAVECANLNVMPDVTFTINGVPYTLSPTAYTLLDFVDGMQFCSSGFQGLDIHPPAGPLWILGDVFIRQFYSVFDRGNNRVGLAPAVP
Protein: Zinc finger and BTB domain-containing protein 49 (Zinc finger protein 509) (Q6ZSB9)
Organism: Homo sapiens (Human)
Function: Transcription factor. Inhibits cell proliferation by activating either CDKN1A/p21 transcription or RB1 transcription.
Subcellular location: [Isoform 1]: Cytoplasm {ECO:0000269|PubMed:25245946}. Nucleus {ECO:0000269|PubMed:25245946}. Note=Predominantly located in the nucleus. {ECO:0000269|PubMed:25245946}.; SUBCELLULAR LOCATION: [Isoform 3]: Cytoplasm {ECO:0000269|PubMed:25245946}. Nucleus {ECO:0000269|PubMed:25245946}.
Interaction partners:
Sequence:
MDPVATHSCHLLQQLHEQRIQGLLCDCMLVVKGVCFKAHKNVLAAFSQYFRSLFQNSSSQKNDVFHLDVKNVSGIGQILDFMYTSHLDLNQDNIQVMLDTAQCLQVQNVLSLCHTFLKSATVVQPPGMPCNSTLSLQSTLTPDATCVISENYPPHLLQECSADAQQNKTLDESHPHASPSVNRHHSAGEISKQAPDTSDGSCTELPFKQPNYYYKLRNFYSKQYHKHAAGPSQERVVEQPFAFSTSTDLTTVESQPCAVSHSECILESPEHLPSNFLAQPVNDSAPHPESDATCQQPVKQMRLKKAIHLKKLNFLKSQKYAEQVSEPKSDDGLTKRLESASKNTLEKASSQSAEEKESEEVVSCENFNCISETERPEDPAALEDQSQTLQSQRQYACELCGKPFKHPSNLELHKRSHTGEKPFECNICGKHFSQAGNLQTHLRRHSGEKPYICEICGKRFAASGDVQRHIIIHSGEKPHLCDICGRGFSNFSNLKEHKKTHTADKVFTCDECGKSFNMQRKLVKHRIRHTGERPYSCSACGKCFGGSGDLRRHVRTHTGEKPYTCEICNKCFTRSAVLRRHKKMHCKAGDESPDVLEELSQAIETSDLEKSQSSDSFSQDTSVTLMPVSVKLPVHPVENSVAEFDSHSGGSYCKLRSMIQPHGVSDQEKLSLDPGKLAKPQMQQTQPQAYAYSDVDTPAGGEPLQADGMAMIRSSLAALDNHGGDPLGSRASSTTYRNSEGQFFSSMTLWGLAMKTLQNENELDQ
Protein: Inositol phosphoceramide mannosyltransferase 3 (EC 2.4.-.-) (IPC mannosyltransferase 3) (Q10323)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: With imt1 and imt2, is required for the synthesis of mannosylinositol phosphoceramide (MIPC). Catalyzes the addition of mannosyl to inositol phosphoceramide (IPC). MIPC is essential for cell morphology, cell-surface distribution of ergosterol, localization for plasma-membrane transporters, and lipid-raft-mediated endocytosis of plasma membrane proteins to the vacuole.
Subcellular location: Endoplasmic reticulum membrane; Multi-pass membrane protein. Golgi apparatus, cis-Golgi network membrane; Multi-pass membrane protein. Golgi apparatus, trans-Golgi network membrane; Multi-pass membrane protein.
Interaction partners:
- Uncharacterized kinase C24B10.02c
- Glutathione S-transferase omega-like 2
- General alpha-glucoside permease
Sequence:
MNKILFYFFFFLTLILSATVYLFGGPMMLFFINYKTDLLKVDDVYNHEIYSNQSAAIPKIIHQTWKTNEIPEKWVGAQKSCIDLHPDYEYVLWTDESMREFIATDYPWFLTQYDSYPYNIERADVVRYFILYKYGGIYLDLDVGCNRTLDPLLHYPAWVRRTSPSGISNNVMGFAKGHPFLLQVVRNLPRFAFNYHFPYLTVMYSTGPLFLSIIWSAWRKLPDAEAWHHIWVMVPELYEKSHHAFFEIYEGSSWHDSDAGFVFYMLHHWAIFTFLGFLTFFIVVYFIFGYALKPAARVSRTGRRVFSSPFSKTSPSRWKIFHRFTSSNEKYDQTRSDSLPFMSDYDLESQTQSHSP
Protein: Fumarate hydratase class I, anaerobic (EC 4.2.1.2) (D-tartrate dehydratase) (EC 4.2.1.81) (Fumarase B) (P14407)
Organism: Escherichia coli (strain K12)
Function: Catalyzes the reversible hydration of fumarate to (S)-malate. Functions in the generation of fumarate for use as an anaerobic electron acceptor. To a lesser extent, also displays D-tartrate dehydratase activity, but is not able to convert (R)-malate, L-tartrate or meso-tartrate. Is required for anaerobic growth on D-tartrate.
Interaction partners:
- Malate dehydrogenase
- Fumarate hydratase class II
- Anaerobic C4-dicarboxylate transporter DcuB
- Citrate synthase
- NAD-dependent malic enzyme
- NADP-dependent malic enzyme
- Fumarase D
- Malate:quinone oxidoreductase
- Fumarate hydratase class I, aerobic
- Malate synthase A
Sequence:
MSNKPFIYQAPFPMGKDNTEYYLLTSDYVSVADFDGETILKVEPEALTLLAQQAFHDASFMLRPAHQKQVAAILHDPEASENDKYVALQFLRNSEIAAKGVLPTCQDTGTAIIVGKKGQRVWTGGGDEETLSKGVYNTYIEDNLRYSQNAALDMYKEVNTGTNLPAQIDLYAVDGDEYKFLCVAKGGGSANKTYLYQETKALLTPGKLKNFLVEKMRTLGTAACPPYHIAFVIGGTSAETNLKTVKLASAHYYDELPTEGNEHGQAFRDVQLEQELLEEAQKLGLGAQFGGKYFAHDIRVIRLPRHGASCPVGMGVSCSADRNIKAKINREGIWIEKLEHNPGQYIPQELRQAGEGEAVKVDLNRPMKEILAQLSQYPVSTRLSLTGTIIVGRDIAHAKLKELIDAGKELPQYIKDHPIYYAGPAKTPAGYPSGSLGPTTAGRMDSYVDLLQSHGGSMIMLAKGNRSQQVTDACHKHGGFYLGSIGGPAAVLAQQSIKHLECVAYPELGMEAIWKIEVEDFPAFILVDDKGNDFFQQIVNKQCANCTK
Protein: Acyl-CoA thioesterase-like N-terminal HotDog domain-containing protein (Q57U21)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Leucine-rich repeat protein
Sequence:
MDYNEISPSTERRIEDFFAATTQCTRDVALRHASLNVKDVRMTFVGSGAMAASTSLGGDASDLNGSVVEWPMKASKTLASHDSLNKTGDVYVDQGVLSFLIDALTSAHLALLVKMKHVSVSLTIDFVRPLLSERPFILVSRLLRSGRRICSLSAEVRQEQNGKTVLCARADHTKVFNDTKSPNKTRRAAISKL
Protein: Ras-related GTP-binding protein, putative (Q382P0)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Geranylgeranyl transferase type-2 subunit beta
- Golgi reassembly stacking protein
Sequence:
MPSHTTSDGSPTTGGDKSGPRIKIVSLGSVGVGKSCLIKQYCEGRFVSKYIPTIGIDYGVKRVDVRVPAHLAPSGKISTRVNFWDMSGCEEYLEIRNEFYRATEGVLLVYDVTDAESFFALNQWVKEMEAHVNTKGNDTYVARVDASVPCKVVVCANKIDEVSEGGGRKKRAVSSETGRQWAKEHDYKYFETSACTGAGVEEALETLFKDVVAAFF
Protein: RAC-like G-protein Rac1 (Q9SWE8)
Organism: Gossypium hirsutum (Upland cotton) (Gossypium mexicanum)
Interaction partners:
Sequence:
MSASRFIKCVTVGDGAVGKTCLLISYTSNTFPTDYVPTVFDNFSANVVVDGNTVNLGLWDTAGQEDYNRLRPLSYRGADVFLLAFSLISKASYENVAKKWIPELRHYAPGVPIILVGTKLDLREDKQFFIDHPGAVPITTAQGEELRKLIGAHFYIECSSKTQQNVKAVFDAAIKVVLQPPKKKKKKKRKAQKACSIL
Protein: Spindle assembly checkpoint serine/threonine-protein kinase BUB1 (EC 2.7.11.1) (Checkpoint serine/threonine-protein kinase BUB1) (P41695)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Involved in cell cycle checkpoint enforcement. The formation of a MAD1-BUB1-BUB3 complex seems to be required for the spindle checkpoint mechanism. Catalyzes the phosphorylation of BUB3 and its autophosphorylation. Associates with centromere (CEN) DNA via interaction with SKP1. The association with SKP1 is required for the mitotic delay induced by kinetochore tension defects, but not for the arrest induced by spindle depolymerization or kinetochore assembly defects.
Subcellular location: Nucleus {ECO:0000269|PubMed:12769845, ECO:0000269|PubMed:24066227, ECO:0000269|PubMed:7969164}. Chromosome, centromere, kinetochore {ECO:0000269|PubMed:12769845, ECO:0000269|PubMed:24066227}.
Interaction partners:
- Spindle assembly checkpoint protein BUB3
- Mitotic spindle checkpoint component MAD2
- APC/C activator protein CDC20
- Outer kinetochore KNL1 complex subunit SPC105
- Serine/threonine-protein kinase MPS1
- Spindle assembly checkpoint component MAD1
- S-phase entry cyclin-5
- Regulatory protein SWI6
- Protein SIC1
- Mitotic check point protein BUB2
Sequence:
MNLDLGSTVRGYESDKDTFPQSKGVSSSQKEQHSQLNQTKIAYEQRLLNDLEDMDDPLDLFLDYMIWISTSYIEVDSESGQEVLRSTMERCLIYIQDMETYRNDPRFLKIWIWYINLFLSNNFHESENTFKYMFNKGIGTKLSLFYEEFSKLLENAQFFLEAKVLLELGAENNCRPYNRLLRSLSNYEDRLREMNIVENQNSVPDSRERLKGRLIYRTAPFFIRKFLTSSLMTDDKENRANLNSNVGVGKSAPNVYQDSIVVADFKSETERLNLNSSKQPSNQRLKNGNKKTSIYADQKQSNNPVYKLINTPGRKPERIVFNFNLIYPENDEEFNTEEILAMIKGLYKVQRRGKKHTEDYTSDKNRKKRKLDVLVERRQDLPSSQPPVVPKSTRIEVFKDDDNPSQSTHHKNTQVQVQTTTSILPLKPVVDGNLAHETPVKPSLTSNASRSPTVTAFSKDAINEVFSMFNQHYSTPGALLDGDDTTTSKFNVFENFTQEFTAKNIEDLTEVKDPKQETVSQQTTSTNETNDRYERLSNSSTRPEKADYMTPIKETTETDVVPIIQTPKEQIRTEDKKSGDNTETQTQLTSTTIQSSPFLTQPEPQAEKLLQTAEHSEKSKEHYPTIIPPFTKIKNQPPVIIENPLSNNLRAKFLSEISPPLFQYNTFYNYNQELKMSSLLKKIHRVSRNENKNPIVDFKKTGDLYCIRGELGEGGYATVYLAESSQGHLRALKVEKPASVWEYYIMSQVEFRLRKSTILKSIINASALHLFLDESYLVLNYASQGTVLDLINLQREKAIDGNGIMDEYLCMFITVELMKVLEKIHEVGIIHGDLKPDNCMIRLEKPGEPLGAHYMRNGEDGWENKGIYLIDFGRSFDMTLLPPGTKFKSNWKADQQDCWEMRAGKPWSYEADYYGLAGVIHSMLFGKFIETIQLQNGRCKLKNPFKRYWKKEIWGVIFDLLLNSGQASNQALPMTEKIVEIRNLIESHLEQHAENHLRNVILSIEEELSHFQYKGKPSRRF
Protein: Sorbitol dehydrogenase (A6KWY5)
Organism: Phocaeicola vulgatus (strain ATCC 8482 / DSM 1447 / JCM 5826 / CCUG 4940 / NBRC 14291 / NCTC 11154) (Bacteroides vulgatus)
Interaction partners:
- Amidohydrolase-related domain-containing protein
- Putative oxidoreductase
- L-arabinose isomerase
- Uronate isomerase
- Fucose permease
Sequence:
MKAIQITAPSEMKVVDIEKPVLEPGEVLVKIKYVGFCGSDLNTFLGRNPMVKLPVIPGHEVGAVIEAVGKDVPDSLKPGMSVTVNPYTNCGKCASCRNGRVNACEHNETLGVQRNGAMCEYIALPWSKIIPAHRIPPRDCALIEPMSVGFHAVSRAQVTDIDIVMVIGCGMIGMGAIVRSALRGATVIAVDLDDEKLELAKRIGAHHTINSMTENVHECLTKITEGLGPDVVIEAVGSPATYVMAVNEVGFTGRVVCIGYAKSEVSFQTKYFVQKELDIRGSRNALPTDFRAVIRYMEQGTCPKNELISKVVKPEAAIQAMKEWAAAPGKVFRILVEFD
Protein: Antitoxin DinJ (Q47150)
Organism: Escherichia coli (strain K12)
Function: Antitoxin component of a type II toxin-antitoxin (TA) system. A labile antitoxin that counteracts the effect of cognate toxin YafQ. YafQ and DinJ together bind their own promoter, and repress its expression. There are 2 operators with imperfect inverted repeats (IR) in the dinJ promoter, YafQ-(DinJ)2-YafQ only binds to the first (most upstream) of them to repress transcription; binding to a single IR is sufficient for activity in vivo and in vitro. DinJ alone is as potent a transcriptional repressor as the heterotetramer and also only needs to bind 1 IR to act.
Interaction partners:
- mRNA interferase toxin YafQ
- Antitoxin MqsA
- Endoribonuclease toxin MazF
- mRNA interferase toxin RelE
- Endoribonuclease toxin ChpB
- Antitoxin YefM
- Toxin YoeB
- Antitoxin MazE
- Antitoxin RelB
- mRNA interferase toxin MqsR
Sequence:
MAANAFVRARIDEDLKNQAADVLAGMGLTISDLVRITLTKVAREKALPFDLREPNQLTIQSIKNSEAGIDVHKAKDADDLFDKLGI