wanglab/gogpt-training-data huggingface dataset:
Protein: Transcription elongation factor (A0A384MTX4)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|PROSITE-ProRule:PRU00649, ECO:0000256|RuleBase:RU368078}.
Interaction partners:
Sequence:
MEDEVVRFAKKMDKMVQKKNAAGALDLLKELKNIPMTLELLQSTRIGMSVNAIRKQSTDEEVTSLAKSLIKSWKKLLDGPSTEKDLDEKKKEPAITSQNSPEAREESTSSGNVSNRKDETNARDTYVSSFPRAPSTSDSVRLKCREMLAAALRTGDDYIAIGADEEELGSQIEEAIYQEIRNTDMKYKNRVRSRISNLKDAKNPNLRKNVLCGNIPPDLFARMTAEEMASDELKEMRKNLTKEAIREHQMAKTGGTQTDLFTCGKCKKKNCTYTQVQTRSADEPMTTFVVCNECGNRWKFC
Protein: F-box/LRR-repeat protein 18 (F-box and leucine-rich repeat protein 18) (Q96ME1)
Organism: Homo sapiens (Human)
Function: Substrate-recognition component of the SCF (SKP1-CUL1-F-box protein)-type E3 ubiquitin ligase complex.
Interaction partners:
- Cullin-1
- S-phase kinase-associated protein 1
- E3 ubiquitin-protein ligase RBX1
- F-box/LRR-repeat protein 7
Sequence:
MASSGEDISNDDDDMHPAAAGMADGVHLLGFSDEILLHILSHVPSTDLILNVRRTCRKLAALCLDKSLIHTVLLQKDYQASEDKVRQLVKEIGREIQQLSMAGCYWLPGSTVEHVARCRSLVKVNLSGCHLTSLRLSKMLSALQHLRSLAIDVSPGFDASQLSSECKATLSRVRELKQTLFTPSYGVVPCCTSLEKLLLYFEILDRTREGAILSGQLMVGQSNVPHYQNLRVFYARLAPGYINQEVVRLYLAVLSDRTPQNLHAFLISVPGSFAESGATKNLLDSMARNVVLDALQLPKSWLNGSSLLQHMKFNNPFYFSFSRCTLSGGHLIQQVINGGKDLRSLASLNLSGCVHCLSPDSLLRKAEDDIDSSILETLVASCCNLRHLNLSAAHHHSSEGLGRHLCQLLARLRHLRSLSLPVCSVADSAPRADRAPAQPAMHAVPRGFGKKVRVGVQSCPSPFSGQACPQPSSVFWSLLKNLPFLEHLELIGSNFSSAMPRNEPAIRNSLPPCSRAQSVGDSEVAAIGQLAFLRHLTLAQLPSVLTGSGLVNIGLQCQQLRSLSLANLGMMGKVVYMPALSDMLKHCKRLRDLRLEQPYFSANAQFFQALSQCPSLQRLCLVSRSGTLQPDAVLAFMARCLQVVMCHLFTGESLATCKSLQQSLLRSFQAERPALNVVIFPLLHEGLTDVIRDVPLVHLDEITLFKSRVAEEPPNLWW
Protein: Fibrinogen silencer binding protein (A0A8I6AM82)
Organism: Rattus norvegicus (Rat)
Interaction partners:
Sequence:
MVLAFEISTPASVLHLLQLVLLKMRRSAAPSQVRGNSSKKARFVPPGRSTTGVSKEISMSPEAKLVQGAHQSQGDAGVCSSNPWLTEGSPVEMGDGARVDPLSPVHLASKEIIESKAQEEEASSLLKYFSVVWCKASKKKHKKWEGDAILIVKGRSFILKDMEGKDIGRGIGYKFKELENVEEGQTLMLGGKEIEILGTVSAEDFNSGKCFQAGSGSPAVPSSQAARKCFSNPFKSVCQSTQARRDRGNDWQNCKPRYDPYTPNALVMPRPDKSHQWAFNRSCLPTVDVVIDPHLVRHLRPHQKDGVAFLYECVMGMRAVGKCGAILADEMGLGKTLQCISLIWTLQCQGPYGGKPIVKRTLIVTPGSLVNNWRKEFQKWLGSERIKIFTVDQDHKVEEFINSAFHSVLIISYEMLLRSLDRIKTITFGLLICDEGHRLKNSGIKTTAALSSLSCEKRVILTGTPVQNDLQEFFALVDFVNPGILGSLSSYRRIYEEPIVMSREPSASKEERELGERRTTELTRLTGCFILRRTQEVINKYLPPKIENVVFCRPGALQIELYRKLLSSQSVRFCLQGLLGNSAHLICIGALKKLCNHPRLLFSFVKGKEFNSSRDENEERSLCQGLLTVFPAGYNLLQLSESESGKLQVLVKLLAAISELRPTEKVILVSNYRQTLNLLEEVCKCHGYACARLDGQTPVSQRQQIVDNFNSKYSTDFIFLLSSKAGGVGLNLIGGSHLILYDIDWNPATDIQAMARVWRDGQKHPVHVYRLLTTGTIEEKIYQRQISKQGLSGAVVDLTRSSEQIQFSVEELKNLFTLHENSHCVTHDLLDCECTGEKDHSDDASENPVTSRQCQLGPQKSSSSRPLSMSQLKQWKHFSGDHLNLPDPFLERIRENVSFFFQNITNQAPAI
Protein: Fet3 protein (Q9C1Z1)
Organism: Komagataella pastoris (Yeast) (Pichia pastoris)
Interaction partners:
Sequence:
MFVFEPVLLAVLVASTCVTAKTHTWNFTTGFVNANPDGVYERDDVIGLNGQWPLPVLEADKGDRIELYLTNGFEDYNTSLHFHGLFQNGTNSMDGPELITQCPIPPGETMLYNFTVDQVGAYWYHSHTAGQYGDGMRAAFIVHDGSDDDDFPYEYDEEFTFTISEWYHESSVDLIPNFMSRFNPTGAEPIPQNFLFNDTRNFTWNVEPSKTYKVNLINVGGFVSQYLWMEDHTFKVVQVDGVYTQPNETDMIYITVAQRYTVLIETKDDTSRNYALMQRVDDTMLDVIPKDLELNGTNYIVYNESAGLPEEYKVESLDIFLDDFWLEPLEAQEAYPDPDYQIVVDVAMDNLDDGVNYAFFNNLTYVAPKVPVLGTVFSAGEDAINPLVYGSNTNSFVLEKDEVIEIVLNNLDTGKHPFHLHGHVFQTVVRGPDYGEESTPVPYNASEAHDIPENPMRRDTVYVNPQSYFVIRFKADNPGVWFFHCHIEWHLDQGLALVLIEDPLSIQSQQNLDDNWKRMCEVNNMPYVGNAAANTENFLDLTDENVQVKNLPAGFTARGIVALVFSCIAGILGCVAIGLYGLAATDDNPVKLSQDLGIDEEFIQDETSSQLSHNGSKDTTEKTATELLN
Protein: Heparan sulfate 2-O-sulfotransferase 1 (2-O-sulfotransferase) (2OST) (EC 2.8.2.-) (O08889)
Organism: Cricetulus longicaudatus (Long-tailed dwarf hamster)
Function: Catalyzes the transfer of sulfate to the C2-position of selected hexuronic acid residues within the maturing heparan sulfate (HS). 2-O-sulfation within HS, particularly of iduronate residues, is essential for HS to participate in a variety of high-affinity ligand-binding interactions and signaling processes. Mediates 2-O-sulfation of both L-iduronyl and D-glucuronyl residues (By similarity).
Subcellular location: Golgi apparatus membrane {ECO:0000250|UniProtKB:Q8R3H7}; Single-pass type II membrane protein {ECO:0000250|UniProtKB:Q8R3H7}.
Interaction partners:
Sequence:
MGLLRIMMPPKLQLLAVVAFAVAMLFLENQIQKLEESRAKLERAIARHEVREIEQRHTMDGPRQDAAVDEEEDIVIIYNRVPKTASTSFTNIAYDLCAKNRYHVLHINTTKNNPVMSLQDQVRFVKNITTWNEMKPGFYHGHISYLDFAKFGVKKKPIYINVIRDPIERLVSYYYFLRFGDDYRPGLRRRKQGDKKTFDECVAEGGSDCAPEKLWLQIPFFCGHSSECWNVGSRWAMDQAKYNLINEYFLVGVTEELEDFIMLLEAALPRFFRGATDLYRTGKKSHLRKTTEKKLPTKQTIAKLQQSDIWKMENEFYEFALEQFQFIRAHAVREKDGDLYILAQNFFYEKIYPKSN
Protein: Prostaglandin reductase 1 (PRG-1) (15-oxoprostaglandin 13-reductase) (EC 1.3.1.48) (Dithiolethione-inducible gene 1 protein) (D3T-inducible gene 1 protein) (DIG-1) (Leukotriene B4 12-hydroxydehydrogenase) (NAD(P)H-dependent alkenal/one oxidoreductase) (EC 1.3.1.74) (Q29073)
Organism: Sus scrofa (Pig)
Function: NAD(P)H-dependent oxidoreductase involved in metabolic inactivation of pro- and anti-inflammatory eicosanoids: prostaglandins (PG), leukotrienes (LT) and lipoxins (LX). Preferentially uses NADPH over NADH as cofactor. Catalyzes with high efficiency the reduction of the 13,14 double bond of 15-oxoPGs, including 15-oxo-PGE1, 15-oxo-PGE2, 15-oxo-PGF1-alpha and 15-oxo-PGF2-alpha. Catalyzes with lower efficiency the oxidation of the hydroxyl group at C12 of LTB4 and its derivatives, converting them into biologically less active 12-oxo-LTB4 metabolites. Reduces 15-oxo-LXA4 to 13,14 dihydro-15-oxo-LXA4 and may promote neutrophil recruitment at the inflammatory site. Plays a role in metabolic detoxification of alkenals and ketones. Reduces alpha,beta-unsaturated alkenals and ketones, particularly those with medium-chain length, showing highest affinity toward (2E)-decenal and (3E)-3-nonen-2-one (By similarity). May inactivate 4-hydroxy-2-nonenal, a cytotoxic lipid constituent of oxidized low-density lipoprotein particles (By similarity).
Subcellular location: Cytoplasm {ECO:0000269|PubMed:8394361}.
Interaction partners:
- BPI fold containing family B member 2
- Actin like 7A
Sequence:
MVRAKSWTLKKHFVGYPTPSNFELKTVELPPLKNGEVLLEALFLTVDPYMRIAARKLKEGDMMMGEQVARVIESKNAAFPTGTIVVALLGWTTHSISDGKNLERLLAEWPDTLPLSLTLGTVGMPGLTAYFGLLDICGLKGGETVMVNAAAGAVGSVVGQIAKLKGCKVVGAAGSDEKVACLKKYGFDVAFNYKTIESLEETLKKASPEGYDCYFDNVGGEFSNAVTSQMKKFGRIAICGAISTYNRTGPPPPGPPPEVVIYNELCFQGFIVTRWQGEVRQKALRDLLKWVSEGKIQYHEHITEGFENMPAAFMGMLKGENLGKAIVKA
Protein: Eukaryotic translation initiation factor 4E-1 (eIF4E-1) (eIF-4F 25 kDa subunit) (eIF-4F p26 subunit) (mRNA cap-binding protein) (Q4VQY1)
Organism: Solanum habrochaites (Wild tomato) (Lycopersicon hirsutum)
Function: Component of the protein complex eIF4F, which is involved in the recognition of the mRNA cap, ATP-dependent unwinding of 5'-terminal secondary structure and recruitment of mRNA to the ribosome. Recognizes and binds the 7-methylguanosine-containing mRNA cap during an early step in the initiation of protein synthesis and facilitates ribosome binding by inducing the unwinding of the mRNAs secondary structures. Key component of recessive resistance to potyviruses.
Subcellular location: Nucleus {ECO:0000250|UniProtKB:K0P2S0}. Cytoplasm {ECO:0000250|UniProtKB:K0P2S0}.
Interaction partners:
Sequence:
MAAAEMERTMSFDAAEKLKAADGGGGEVDDELEEGEIVEESNDTASYLGKEITVKHPLEHSWTFWFDNSTTKSRQTAWGSSLRNLYTFSTVEDFWGAYNNIHHPSKLIMGADFHCFKHKIEPQWEDPVCANGGTWKMSFSKGKSDTSWLYTLLAMIGHQFDHGDEICGAVVSVRAKGEKIALWTKNAANETAQVSIGKQWKQFLDYSDSVGFIFHDDAKRLDRSAKNRYTV
Protein: Expressed protein (SWIB/MDM2 domain superfamily protein) (O82326)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Single-stranded DNA-binding protein WHY2, mitochondrial
- Heat shock 70 kDa protein 9, mitochondrial
- Chromatin structure-remodeling complex protein BSH
- Chaperone DnaJ-domain superfamily protein
- Ankyrin repeat family protein
- NADH-cytochrome b5 reductase-like protein
Sequence:
MAVSSGTFSTFLCIKTTSFRNPSTPLSSLRFASHPAAKLRLVRAVTSATESSEPTATNKRVPRGIMKPRPVSPEMQDIVELPEIARTQALKRIWAYIKEHDLQDPQNKREILCDEKLKKIFEGRDRVGFLEIAKLIGPHFL
Protein: Zona pellucida sperm-binding protein 3 (Sperm receptor) (Zona pellucida glycoprotein 3) (Zp-3) (Zona pellucida protein C) [Cleaved into: Processed zona pellucida sperm-binding protein 3] (P10761)
Organism: Mus musculus (Mouse)
Function: Component of the zona pellucida, an extracellular matrix surrounding oocytes which mediates sperm binding, induction of the acrosome reaction and prevents post-fertilization polyspermy. The zona pellucida is composed of 3 to 4 glycoproteins, ZP1, ZP2, ZP3, and ZP4. ZP3 is essential for sperm binding and zona matrix formation.
Subcellular location: [Processed zona pellucida sperm-binding protein 3]: Zona pellucida {ECO:0000269|PubMed:19052627}.; SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:19052627}; Single-pass type I membrane protein {ECO:0000255}.
Interaction partners:
- Zona pellucida sperm-binding protein 2
- Zona pellucida sperm-binding protein 1
- Beta-1,4-galactosyltransferase 1
- Oviduct-specific glycoprotein
- Zona pellucida sperm-binding protein 3 receptor
- Homeobox protein NOBOX
- Growth/differentiation factor 9
- Izumo sperm-egg fusion protein 1
- Factor in the germline alpha
- Disintegrin and metalloproteinase domain-containing protein 2
Sequence:
MASSYFLFLCLLLCGGPELCNSQTLWLLPGGTPTPVGSSSPVKVECLEAELVVTVSRDLFGTGKLVQPGDLTLGSEGCQPRVSVDTDVVRFNAQLHECSSRVQMTKDALVYSTFLLHDPRPVSGLSILRTNRVEVPIECRYPRQGNVSSHPIQPTWVPFRATVSSEEKLAFSLRLMEENWNTEKSAPTFHLGEVAHLQAEVQTGSHLPLQLFVDHCVATPSPLPDPNSSPYHFIVDFHGCLVDGLSESFSAFQVPRPRPETLQFTVDVFHFANSSRNTLYITCHLKVAPANQIPDKLNKACSFNKTSQSWLPVEGDADICDCCSHGNCSNSSSSQFQIHGPRQWSKLVSRNRRHVTDEADVTVGPLIFLGKANDQTVEGWTASAQTSVALGLGLATVAFLTLAAIVLAVTRKCHSSSYLVSLPQ
Protein: tRNA (34-2'-O)-methyltransferase regulator WDR6 (Q86B53)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:Q9NNW5}.
Interaction partners:
- tRNA
- tRNA
- rRNA methyltransferase 2, mitochondrial
- U3 small nucleolar RNA-associated protein 15 homolog
- Histone chaperone asf1
- Nucleolar protein 56
- NHP2-like protein 1 homolog
- Structural maintenance of chromosomes protein
- tRNA
- Phenoloxidase-activating factor 2
Sequence:
MVLISDAFGLEISPNGILVGHGDQAVLYSSEPKVELPVQLREGKVRGFAWSSLRKSQRLLLLYSENEYSLIRCTTSSENDLFQLVYEGETRDWINAALFLEDENESEDRKRFVLHTSHSALLYMEYDLTSNADCTVLELARCTDSSILYYTKLHGSSFNKLAIISGNAFGELLVWQTQFPTESDPKSVMKTYPLLLRIEAHNGVIHSIEFDLQSQLLVTTSDDRSVKFWNIQKSGDWTTAEIKPMFSCYGHSSRVMCVVILKIDDRTFVASGGEDSYVCIWSSSGELILKRRQQFGAPIWRLGFSQDAEILYSTSSTGNLVGQNLKEVLNRPKIESTILSSLGDANEFVRNLKFVNNEIIVGLSSLNRLYYTRISPDSSHENKWLMVNDFPSYKRTVLEVFDDIIATCGHRRITLHRYNTNTNDFEQLFDGIRMKGTIRSFQFLSRDRYLVSDNLGYCLLLQTHQLHIESHIALFNNREPWITAALLISEQYLLLGNREGHVMLYCRSSASDDFQLKDSIRYLHGKMGSNFFKLLSLNADNAHVMSGGHEAFLKYLSVRFSDSTLRVSQREGIPLAWVEASPSDDLILGFNDNHIVAWSRRNDILLQLACGGGHRCWDFRLSDGDSQLSIAYVKQKRVYFYRNSLYNAVDNRLKDIEPNNWHVRNCNTLRLITPRNQSDPFILSAGDDNIIKVTQVTNDSLSQRAEMHSHISTVRSLQAIPYKSNGGDSSTWLVFSVGGRSQLCISQLSIDASNKCWISEISSHTLHNVAASKTSTIEARLMAIDVVQHSDGDLFSIYVAGGDGNISHYIWELETPNQLDLKHFVDIQRCPLGIQWIASKGMLLVSTTNGEVYGFDRTLETTYFQLQLHVTGINTIDIYVDRHLLHILSGGDDESIKYTVLNLNNNNVEQKIEYLGLHNAQVNALAIHCPTKSVAASELFAYTCSIDRQIYRIDLSTHKYKRVGYTCIADVKGMLLDEHQRMYFYGCGLQTMSISNIL
Protein: Dorsal isoform 1-A (Q534Q6)
Organism: Aedes aegypti (Yellowfever mosquito) (Culex aegypti)
Interaction partners:
- AAEL000709-PB
- Defensin-A
- Defensin-C
- Uncharacterized protein
- Uncharacterized protein
- AAEL007624-PA
- Uncharacterized protein
- histone acetyltransferase
Sequence:
MGPNDNNVMEDDPSLPDLPNNLIVTDDILDLIIDIIDQEMPPTAQERPHVVITEQPQSKALRFRYECEGRSAGSIPGVHSTPEQKTFPGIEIRGYKGRAVVVVSCVTKDPPYRPHPHNLVGKEGCKKGVCTVEINSSTMSYTFSNLGIQCVKKKDIEEALRLREEIRVDPFKTGYGHARQPATIDLNAIRLCFQVFLEGQQRGRFTEPLQPVVSDVIYDKKAMSDLVICKLSDVTAPVAGGREIILLCEKVAKEDIAVRFYEEQHGNIVWEEYGEFQHTNVHKQVAICFRTPRYRTLEVEHPVMVNIQLKRPSDGATSEPLPFELTPLDSAKRKKRKPNTWGDTPEHMPEAARHPYYATLGNVPGEAIKTEPRDSPTHPFNFIGNYRQPNESPSPIERSPLYGNTTPVGQTSPYNAGRTSVTPTPGGYQPNVMNPDFLLGGTQQFQNQYAFPTLPPTNGQPMYLQQPQQQQQQQQFQPPANMNNQQQFNVSNLIDPQDQLPQPGPSGVQAVPSFQPSGSIGEINISSPWLTMDSSELKSLMVHTLSDMKQEQQRIQQEAETLSDSFDRLSTNLNNLNKP
Protein: Protein phosphatase 1, regulatory subunit, putative (Q57VV4)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MSQEGGKSEPDANEKEQRNQKLRLGLEAMFCAQEIPSEKRTDIESDGEEVPPSITRDEDRYRQVAEAILRIDTKSKIIEINNIRLFSVAEIELDKLTECTSLSLRKNLLHDLIPFPEDLADRLDELDLFDNKIRKLNDFFETVTVPGDPPTTKTLPNAYKCLTKLDLSYNQIREIGGLDSIGGTLRELYLVENKIKEVKNLDSLVNLELLELGGNRLRAIGSGLEKLTKLKQLWLGKNKISSIGTALHKLVSLEILSLQANRITSVDAENFLGAKANPNLREVYLSENGLTSVGNVRHLSTIKIIDFSFNSICSIDAEEINPQTMPKLEEFWLTDGNIADWEEVGKLSGFTSTLKTVYLERNPIEEDKRYRDKVYMYLPFLVQIDSWPIVNKGNLEADRKRKA
Protein: Regulatory protein alcR (P21228)
Organism: Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Function: Positive regulatory protein for the ethanol regulon, alcA and aldA. It control positively its own expression and possibly in a negative fashion the expression of the gene coding for ADH-II.
Subcellular location: Nucleus.
Interaction partners:
- Alcohol dehydrogenase 1
- Aldehyde dehydrogenase
- DNA-binding protein creA
Sequence:
MADTRRRQNHSCDPCRKGKRRCDAPENRNEANENGWVSCSNCKRWNKDCTFNWLSSQRSKAKGAAPRARTKKARTATTTSEPSTSAATIPTPESDNHDAPPVINSHDALPSWTQGLLSHPGDLFDFSHSAIPANAEDAANVQSDAPFPWDLAIPGDFSMGQQLEKPLSPLSFQAVLLPPHSPNTDDLIRELEEQTTDPDSVTDTNSVQQVAQDGSLWSDRQSPLLPENSLCMASDSTARRYARSTMTKNLMRIYHDSMENALSCWLTEHNCPYSDQISYLPPKQRAEWGPNWSNRMCIRVCRLDRVSTSLRGRALSAEEDKAAARALHLAIVAFASQWTQHAQRGAGLNVPADIAADERSIRRNAWNEARHALQHTTGIPSFRVIFANIIFSLTQSVLDDDEQHGMGARLDKLLENDGAPVFLETANRQLYTFRHKFARMQRRGKAFNRLPGGSVASTFAGIFETPTPSSESPQLDPVVASEEHRSTLSLMFWLGIMFDTLSAAMYQRPLVVSDEDSQISSASPPRRGAETPINLDCWEPPRQVPSNQEKSDVWGDLFLRTSDSLPDHESHTQISQPAARWPCTYEQAAAALSSATPVKVLLYRRVTQLQTLLYRGASPARLEAAIQRTLYVYNHWTAKYQPFMQDCVANHELLPSRIQSWYVILDGHWHLAAMLLADVLESIDRDSYSDINHIDLVTKLRLDNALAVSALARSSLRGQELDPGKASPMYRHFHDSLTEVAFLVEPWTVVLIHSFAKAAYILLDCLDLDGQGNALAGYLQLRQNCNYCIRALQFLGRKSDMAALVAKDLERGLNGKVDSFL
Protein: Protein arginine N-methyltransferase 2 (EC 2.1.1.319) (Histone-arginine N-methyltransferase PRMT2) (D9IVE5)
Organism: Xenopus laevis (African clawed frog)
Function: Arginine methyltransferase that methylates the guanidino nitrogens of arginyl residues in proteins such as histones. Involved in growth regulation (By similarity). Involved in embryonic dorsal development.
Subcellular location: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
Interaction partners:
Sequence:
MESSSECSSISDFQDSTEGDDANTLPENLCMREYVVICDYVATDNTQLSLCSGDKVLLLNAVSQDWWWVNHNGTCGYVPASHLHDALNEQEDTEVNDPWQDEEYYGSYKTLKLHLEMLSDVPRTMTYQNVILKNSSSLCGKHILDLGCGTGIISFFCAKFAQPEAVYAVEASKIAEQTCRLVEQNGISSLVHVIRQQAEELDLPTKVDVLVSEWMGTCLLFEFMLESVLQARDRWLKEDGVMWPSTACIHLVPCSAYKEYSNKVLFWDNPYQLDFSLLKPPATKEFFAKPQPDYILQPEDCLSEPCTLFHLNLKTLQVAELERMNCDFTFLVHTNGLLHGFTAWFSVQFENLEEQGHLELNTGPFSPLTHWKHTLFMLDEPLQVQKRDKISGSVVFERNSVWRRHMSVTLSWVISRELKMQKVGCKVFPIWR
Protein: Betaine aldehyde dehydrogenase (BADH) (EC 1.2.1.8) (P17445)
Organism: Escherichia coli (strain K12)
Function: Involved in the biosynthesis of the osmoprotectant glycine betaine. Catalyzes the irreversible oxidation of betaine aldehyde to the corresponding acid. It is highly specific for betaine and has a significantly higher affinity for NAD than for NADP.
Interaction partners:
- Oxygen-dependent choline dehydrogenase
- HTH-type transcriptional regulator BetI
- High-affinity choline transport protein
- Methionyl-tRNA formyltransferase
Sequence:
MSRMAEQQLYIHGGYTSATSGRTFETINPANGNVLATVQAAGREDVDRAVKSAQQGQKIWASMTAMERSRILRRAVDILRERNDELAKLETLDTGKAYSETSTVDIVTGADVLEYYAGLIPALEGSQIPLRETSFVYTRREPLGVVAGIGAWNYPIQIALWKSAPALAAGNAMIFKPSEVTPLTALKLAEIYSEAGLPDGVFNVLPGVGAETGQYLTEHPGIAKVSFTGGVASGKKVMANSAASSLKEVTMELGGKSPLIVFDDADLDLAADIAMMANFFSSGQVCTNGTRVFVPAKCKAAFEQKILARVERIRAGDVFDPQTNFGPLVSFPHRDNVLRYIAKGKEEGARVLCGGDVLKGDGFDNGAWVAPTVFTDCSDDMTIVREEIFGPVMSILTYESEDEVIRRANDTDYGLAAGIVTADLNRAHRVIHQLEAGICWINTWGESPAEMPVGGYKHSGIGRENGVMTLQSYTQVKSIQVEMAKFQSIF
Protein: Procollagen-lysine,2-oxoglutarate 5-dioxygenase 2 (EC 1.14.11.4) (Lysyl hydroxylase 2) (LH2) (Q811A3)
Organism: Rattus norvegicus (Rat)
Function: Forms hydroxylysine residues in -Xaa-Lys-Gly- sequences in collagens. These hydroxylysines serve as sites of attachment for carbohydrate units and are essential for the stability of the intermolecular collagen cross-links.
Subcellular location: Rough endoplasmic reticulum membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Lumenal side {ECO:0000250}.
Interaction partners:
- Procollagen-lysine,2-oxoglutarate 5-dioxygenase 1
- Glycosyltransferase 25 domain containing 1
- Collagen beta
- Multifunctional procollagen lysine hydroxylase and glycosyltransferase LH3
- Calmodulin-lysine N-methyltransferase
- Prolyl 4-hydroxylase subunit alpha-1
- peptidylprolyl isomerase
- Prolyl 4-hydroxylase subunit alpha 2
- Collagen alpha-1
- Collagen alpha-2
Sequence:
MGDRGVRLGLLMPMLALLSWAASLGVAEETPSRIPADKLLVITVATKENDGFHRFMNSAKYFNYTVKVLGQGQEWRGGDGMNSIGGGQKVRLMKEAMEHYAGQDDLVILFTECFDVIFAGGPEELLKKFQKTNHKIVFAADALLWPDKRLADKYPGVHIGKRYLNSGGFIGYAPYISRLVQQWNLQDNDDDQLFYTKVYIDPLKREALNITLDHRCKIFQALNGATDEVVLKFENGKSRVKNTFYETLPVAINGNGPSKILLNYFGNYVPNSWTQENGCALCDFDASDLSTVDVYPKVTLGVFIEQPTPFQPRFLDLLLTLDYPKEALRLFVHNKEVYHEKDIKAFVDKAKHDISSIKIVGPEENLSQAEARNMGMDFCRQDEKCDYYFSVDADVVLTNPRTLKILIEQNRKIIAPLVTRHGKLWSNFWGALSPDGYYARSEDYVDIVQGNRVGIWNVPYMANVYLIQGKTLRSEMSERNYFVRDKLDPDMSLCRNARDMGVFMYISNRHEFGRLISTANYNTSHLNNDLWQIFENPVDWKEKYINRDYSKIFTENIVEQPCPDVFWFPIFSERACDELVEEMEHYGKWSGGKHHDSRISGGYENVPTDDIHMKQIDLENVWLHFIREFIAPVTLKVFAGYYTKGFALLNFVVKYSPERQRSLRPHHDASTFTINIALNNVGEDFQGGGCKFLRYNCSIESPRKGWSFMHPGRLTHLHEGLPVKNGTRYIAVSFIDP
Protein: Glucan endo-1,3-beta-D-glucosidase 1 (Endo-1,3-beta-glucanase 1) (EC 3.2.1.39) (Daughter specific expression protein 4) (Laminarinase) (Q5AIR7)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Function: Cleaves internal linkages in 1,3-beta-glucan. Involved in the cell separation process. Plays no essential role in growth, nor is it involved in hyphal morphogenesis.
Subcellular location: Secreted, cell wall {ECO:0000269|PubMed:21622905, ECO:0000269|PubMed:23136884, ECO:0000269|PubMed:23243062}.
Interaction partners:
- Chitinase 3
- Glucan endo-1\3-beta-D-glucosidase
- Filamentous growth regulator 41
- Protein DSE1
- Glucan 1,3-beta-glucosidase
Sequence:
MLFKSVLLSTLIAVQALAENSAHQEIVTVTKTTHISNPCLENYAKKLLPNNPTGLTTGIPIVIVYAPQQPDNQVKQSESLQPTQSSKAQQQQQIQGSSVPASIHDTPTPTDHTKITVTSTTICNQKVCTVKTFSTIISHSESPTTTTTTKQNEEKSIADTKSFTHKALPSSNGAVTLKTTSVKTALTTTSTVFSATSLPSTTYTPSTSVSLVSTTKKNPVSSQSVVSTTKTISINTSLITDAVTITKEATTLPNSKHSSIFTNGSISFISTSANKVKSTVTSDISNNSQNGSSLSLTSTINQLASITNSTLTTITKPTSLVPDFSYTNSSRVSSTMRNSSEESSMVLEKSSSKLLSSTSFLNSSSIASTTESSELASATTSDSSLNHSSSSSVELSSSLSSEADSSSSSESVETGSSDETASNYSGDLFKAIDTNAPPTVFARSEIPLTIPAGVDNNGKPIGTNKFYTNLLLGNQDFMVYPLPYGLYWSKTSYYGFAVQHNNVSDRVFGSINTNNKGVASYYFNPTNNAELIFSATSFSKDSMHMKVSQMAELSALVTLSSSSNDESNYLDIPLVQGMGFVTGIYNGNLTPLLNSLFGVKDLSLETSDALLSNVLKYRATLLNNVQWLIYVTLPDKDTDFKLEVEDFYNLKGSKPVDGLIIQVAIAPEDNDNDKYYDAAAGMYVTGATVSGSVSQGTAASYKFSYTTAGKSSSNNPIVFALPHHMDSLTGSALDALTGITVTSTTKGEMTGFLTNELEFSETINQDVEFLPWTENMTGSLTYTKDQLELLASAANKELAANIAATVKNMNSNYFSGKVLDKYAQILLVVSEIIQDEEVTKDALNAMKDAFKVFTQNKQYYPLMYDTKFGGVTSTSAQDGDPNADFGSAYYNDHDFHYGYFIHAAAIVGYVDKKLGGTWAQSNKDWVNSLVRDASNPSADDTYFPVSRMFDWFSGHSWATGLFVTYKNIESSSESLHFAAAIKLWGKVVGDQSMEARGGLMISIMARSFNMYFYYKSDNTVEPKQILPNKVSGIFFENKVDYTTFFGTPADHPEYVHGIHMLPITPSSSLVRKTSYVQEEWKDQIAGFIDNVDSGWTGILRLNQALFDPKSSYEFFASNNWDDKWLDNGQSRTWSLAFAAGALNAS
Protein: Partitioning defective 3 homolog B (Amyotrophic lateral sclerosis 2 chromosomal region candidate gene 19 protein) (PAR3-beta) (Partitioning defective 3-like protein) (PAR3-L protein) (Q8TEW8)
Organism: Homo sapiens (Human)
Function: Putative adapter protein involved in asymmetrical cell division and cell polarization processes. May play a role in the formation of epithelial tight junctions.
Subcellular location: Endomembrane system. Cell junction. Cell junction, tight junction. Note=Partially localized along the cell-cell contact region. Colocalizes with TJP1 to epithelial tight junctions.
Interaction partners:
- G-protein-signaling modulator 2
- Protein inscuteable homolog
- G-protein-signaling modulator 1
- Protein kinase C iota type
- Protein kinase C zeta type
- Partitioning defective 6 homolog beta
- Partitioning defective 6 homolog alpha
- Partitioning defective 6 homolog gamma
Sequence:
MKVTVCFGRTGIVVPCKEGQLRVGELTQQALQRYLKTREKGPGYWVKIHHLEYTDGGILDPDDVLADVVEDKDKLIAVFEEQEPLHKIESPSGNPADRQSPDAFETEVAAQLAAFKPIGGEIEVTPSALKLGTPLLVRRSSDPVPGPPADTQPSASHPGGQSLKLVVPDSTQNLEDREVLNGVQTELLTSPRTKDTLSDMTRTVEISGEGGPLGIHVVPFFSSLSGRILGLFIRGIEDNSRSKREGLFHENECIVKINNVDLVDKTFAQAQDVFRQAMKSPSVLLHVLPPQNREQYEKSVIGSLNIFGNNDGVLKTKVPPPVHGKSGLKTANLTGTDSPETDASASLQQNKSPRVPRLGGKPSSPSLSPLMGFGSNKNAKKIKIDLKKGPEGLGFTVVTRDSSIHGPGPIFVKNILPKGAAIKDGRLQSGDRILEVNGRDVTGRTQEELVAMLRSTKQGETASLVIARQEGHFLPRELKGEPDCCALSLETSEQLTFEIPLNDSGSAGLGVSLKGNKSRETGTDLGIFIKSIIHGGAAFKDGRLRMNDQLIAVNGESLLGKSNHEAMETLRRSMSMEGNIRGMIQLVILRRPERPMEDPAECGAFSKPCFENCQNAVTTSRRNDNSILHPLGTCSPQDKQKGLLLPNDGWAESEVPPSPTPHSALGLGLEDYSHSSGVDSAVYFPDQHINFRSVTPARQPESINLKASKSMDLVPDESKVHSLAGQKSESPSKDFGPTLGLKKSSSLESLQTAVAEVRKNDLPFHRPRPHMVRGRGCNESFRAAIDKSYDGPEEIEADGLSDKSSHSGQGALNCESAPQGNSELEDMENKARKVKKTKEKEKKKEKGKLKVKEKKRKEENEDPERKIKKKGFGAMLRFGKKKEDKGGKAEQKGTLKHGGLREEELEKMKEERERIGAKHQELREKQARGLLDYATGAIGSVYDMDDDEMDPNYARVNHFREPCTSANVFRSPSPPRAGPFGYPRDGHPLSPERDHLEGLYAKVNKPYHPLVPADSGRPTGGSTDRIQKLRKEYYQARREGFPLYEDDEGRARPSEYDLLWVPGRGPDGNAHNLRFEGMERQYASLPRGGPADPVDYLPAAPRGLYKERELPYYPGAHPMHPPKGSYPRPTELRVADLRYPQHYPPPPAPQHKGPFRQDVPPSPPQHQRMPAYQETGRPGPRGGSPDQYPYRTQDSRQKNPMTAAV
Protein: Caffeyl-CoA reductase-Etf complex subunit CarC (EC 1.3.1.108) (Caffeoyl-CoA reductase CarC) (NADH-dependent caffeyl-CoA reduction) (H6LGM6)
Organism: Acetobacterium woodii (strain ATCC 29683 / DSM 1030 / JCM 2381 / KCTC 1655 / WB1)
Function: The Caffeyl-CoA reductase-Etf complex catalyzes the reduction of caffeyl-CoA to yield hydrocaffeyl-CoA. It couples the endergonic ferredoxin reduction with NADH as reductant to the exergonic reduction of caffeoyl-CoA with the same reductant. It uses the mechanism of electron bifurcation to overcome the steep energy barrier in ferredoxin reduction. Also reduces 4-coumaroyl-CoA and feruloyl-CoA.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:23479729}.
Interaction partners:
- Caffeyl-CoA reductase-Etf complex subunit CarD
- Caffeyl-CoA reductase-Etf complex subunit CarE
- Lactate dehydrogenase
- Lactate dehydrogenase
- Acyl-CoA synthetase
- Caffeyl-CoA-synthetase CarB2
- CoA transferase CarA2
- Carbamoyl phosphate synthase large chain
- Iron hydrogenase HydB
- Pyruvate:ferredoxin oxidoreductase
Sequence:
MYFSEQNKMIRKLARDFAEKELTTEILDEVEESGEFPQEILDKMAKFGFFGIKIPKSLGGSGGDHMSYVICMEEFARVSGVASVYLSSPNSLAGGPLLLSGTEEQIEKYLKPIITGKKKLAFALTEPGAGSDAGGMSTTAVDMGDYYLLNGRKTFITMAPLCDDAVIYAKTDMSKGTRGISAFIVDLKSEGVSMGKNEHKMGLIGCATSDIIMEDVKVPKENRLGEVNKGFSNAMKTLDVGRLGVASQSIGVAQGALDEAIKYAKERKQFGKRIADFQAIAFMIADMATKLEAAKLLVYNAASLMDNKKNATKEASMAKFYASEICNEICAKAVQIHGGYGYIKEYKVERMYRDCRVFTIYEGTSQVQQMVISGMLLKK
Protein: Methylenetetrahydrofolate reductase (EC 1.5.1.53) (A0A8I6A5Q6)
Organism: Rattus norvegicus (Rat)
Interaction partners:
Sequence:
MSNEARRSGSPSPRSEGSSSGSESSKDSSRCSTPSLDPDRHERLREKMRRRMDSGDKWFSLEFFPPRTAEGAVNLISRFDRMAAGGPLFVDVTWHPAGDPGSDKETSSMMIASTALNYCGLETILHMTCCQQRQEEISGHLHRAKQLGLKNIMALRGDPVGDHWEAEEGGFSYATDLVKHIRNEFGDYFDICVAGYPKGHPDAESFEDDLKHLKEKVSAGADFIITQLFFEASSFFSFVKACEDIGISCPILPGIFPIQGYTSLRQLVKLSKLEVPQTIKDVIEPIKDNDAAIRNYGIELAVNLCRELLDSGLVPGLHFYTLNREVATMEVLKQLGMWTEDPRRPLPWAVSAHPKRREEDVRPIFWASRPKSYIYRTQGWDEFPNGRWGNSSSPAFGELKDYYLFYLKSKSPREELLKMWGEELTSEESVFEVFEHYLSGEPNRHGYRVTCLPWNDEPLAAETSLMKEELLRVNRLGILTINSQPNINGKPSSDPVVGWGPSGGYVFQKAYLEFFTSRETVEALLQVLKTYELRVNYHIVDVKGENITNAPELQPNAVTWGIFPGREIVQPTVVDPISFMFWKDEAFALWIEQWGKLYEEESPSRMIIQYIHDNYFLVNLVDNEFLLDNCLWQVVEDTFELLNRHTTKKEAQAP
Protein: Fgr24p (A0A1D8PFZ2)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Interaction partners:
- Reverse transcriptase domain-containing protein
- Fgr13p
- 37S ribosomal protein MRP2
Sequence:
MNTILEKYDIIFLQDISPNNTTTLQILTTRLPITVIQSHSNDKTAIAINHKIENLIKIIETNTLNLTEQVSQYVNDVIIQIQNTRIILVSVYYPIADKAPMQVTLTQQLNNELPKTYPIIMGGNFNHILNLATDRQTYGCDKQGEDKSRQESLDLYNNHKLVDVFREFYPNKIWATNKNPQNNRRIDRFHVSSQLMVQIPRFQQIKIPKLKSTHNAITFSYNLEKTQLIGYWSRKGYR