wanglab/gogpt-training-data huggingface dataset:
Protein: Fumitremorgin C synthase (EC 1.14.19.71) (Cytochrome P450 monooxygenase ftmP450-2) (Fumitremorgin biosynthesis protein E) (B9WZX4)
Organism: Aspergillus fumigatus (Neosartorya fumigata)
Function: Cytochrome P450 monooxygenase; part of the gene cluster that mediates the biosynthesis of fumitremorgins, indole alkaloids that carry not only intriguing chemical structures, but also interesting biological and pharmacological activities. The biosynthesis of fumitremorgin-type alkaloids begins by condensation of the two amino acids L-tryptophan and L-proline to brevianamide F, catalyzed by the non-ribosomal peptide synthetase ftmA. Brevianamide F is then prenylated by the prenyltransferase ftmPT1/ftmB in the presence of dimethylallyl diphosphate, resulting in the formation of tryprostatin B. The three cytochrome P450 monooxygenases, ftmP450-1/ftmC, ftmP450-2/ftmE and ftmP450-3/FtmG, are responsible for the conversion of tryprostatin B to 6-hydroxytryprostatin B, tryprostatin A to fumitremorgin C and fumitremorgin C to 12,13-dihydroxyfumitremorgin C, respectively. The putative methyltransferase ftmMT/ftmD is expected for the conversion of 6-hydroxytryprostatin B to tryprostatin A (Probable). FtmPT2/FtmH catalyzes the prenylation of 12,13-dihydroxyfumitre-morgin C in the presence of dimethylallyl diphosphate, resulting in the formation of fumitremorgin B. Fumitremorgin B is further converted to verruculogen by ftmOx1/ftmF via the insertion of an endoperoxide bond between the two prenyl moieties. In some fungal species, verruculogen is further converted to fumitremorgin A, but the enzymes involved in this step have not been identified yet (Probable).
Subcellular location: Membrane {ECO:0000255}; Single-pass membrane protein {ECO:0000255}.
Interaction partners:
Sequence:
MERLPLSPAVLFLIIVLPILYLWIRYTAPARPHGKHLSLPPGPPRLPKIGNLHQVPRQIPWKKYKEWSDTYGPIMSVQLADTIAVVFSSWDLIKNHIERRNTIYSSRPSVPFFLHATGGLNASILPYGPEWKLQRAIRSSVLKPSMTVKYRDVQHVETTQLLHELLSTNDFPVCLRRCIASVFLTVAYGERCVDHAGLEAIDRLEELNRAIALHAEALFSGAAGILTQLVLPKALVDRLPVRWKKDADMLHNRLTADLVARTRAALVRPGWNWVKEFSMKDGIGSGDGDGEQGSKVELKRLAYMVGSLYEASMAASQALRVIILAGLLHPDATRRMHDELDAVVGTGRLPDFHDAAQLPYTQAFIKEAMRWRSLTPMGSPRATSDEDECRGYHIPCGATVLVNVWAINHDEAIFLDPFAFQPERWIENPDLPQLMYGMGQRACPGRHMGQDSLFLATARLFWAFDMALPDGADPIDQERFLDSGTTLAAFLPDFEVRFTPRSEKYQEVIENSMAVLPDVLSISATP
Protein: Glutathione S-transferase kappa (EC 2.5.1.18) (Q6FII1)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MGPLPRTVELFYDVLSPYSWLGFEILCRYQNIWNINLQLRPSLITGIMKDSGNKPPGLLPRKGLYMANDLKLLRHHLQIPIHFPKDFLSVMLEKGSLSAMRFLTAVNLEHPEMLEKASRELWMRVWSRNEDITEPQSILAAAEKAGMSAEQAQGLLEKIATPKVKNQLKETTEAACRYGAFGLPITVAHVDGQTHMLFGSDRMELLAHLLGEKWMGPIPPAVNARL
Protein: Uncharacterized protein Rv2886c (P9WL35)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Interaction partners:
- Putative RNA-guided DNA endonuclease Rv2885c
- Possible transposase
- Possible transposase
- Probable transposase
- Probable transposase
- Possible transposase
Sequence:
MSRILTHVPGRTVNRSYALPALVGSAAGRLSGNHSHGREAYIALPQWACSRQPSTPPLQTPGRINALWSLRPVLPMPGRGCQLLRLGGRWLSVVCCRNGSMNLVVWAEGNGVARVIAYRWLRVGRLPVPARRVGRVILVDEPAGQPGRWGRTAVCARLSSADQKVDLDRQVVGVTAWATAEQIPVGKVVTEVGSALYGRRRTFLTLLGDPTVRRIVMKRRDRLGRFGFECVQAVLAADGRELVVVDSADVDDDVVGDITEILTSICARLYGKRAAGNRAARAVAAAARAGGHEAR
Protein: V-type proton ATPase subunit a (Q91W06)
Organism: Mus musculus (Mouse)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
Sequence:
MGSMFRSEEVALVQLLLPTGSAYNCVSQLGELGLVEFRDLNESVSAFQRRFVVDVQRCEELEKTFTFLREEVQRAGLTLAPPEGTLPAPPPRDLLRIQEETDRLAQELRDVRGNQQALRAQLHQLRLHSAVLGQSHSPPVAADHTEGPFSETTPLLPGTRGPHSDLKVNFVAGAVEPYKAAALERLLWRACRGFLIASFRETEGQLEDPVTGEPATWMTFVISYWGEQIGQKIRKITDCFHCHVFPYLEQEEARFRTLQQLQQQSQELQEVLGETDRFLSQVLGRVQQLLPPWQVQIHKMKAVYLTLNQCSVNTTHKCLIAEVWCAARDLPTVQQALQSGSSEEGVSAVAHRIPCQDMPPTLIRTNRFTSSFQGIVDAYGVGRYREVNPAPYTIITFPFLFAVMFGDVGHGLLMFLFALAMVLTENRPAVKAAQNEIWQTFFGGRYLLLLMGLFSVYTGFIYNECFSRATTIFPSGWSVAAMANQSGWSDEYLSQHSMLTLNPNITGVFLGPYPFGIDPIWSLATNHLSFLNSFKMKMSVILGVTHMAFGVFLSIFNHVHFGQSHRLLLETLPELIFLLGLFGYLVFLIVYKWVNVSAASASSAPSILIHFINMFLFSQNPTNHLLFHGQEVVQYVLVVLALATVPILLLGTPLYLLRQHRHRRNTQRRPAGQQDEDTDKLLASPDASTLENSWSPDEEKAGSPGDEETEFVPSEIFMHQAIHTIEFCLGCISNTASYLRLWALSLAHAQLSEVLWAMVMRIGLGMGREIGVAAVVLVPVFAAFAVLTVAILLVMEGLSAFLHALRLHWVEFQNKFYSGTGYKLSPFTFTVDSD
Protein: CCR4-associated factor 4 (P36130)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Involved in mitochondrial fission. Has a partially redundant function to MDV1 in acting as an adapter protein, binding to FIS1 on the mitochondrial outer membrane and recruiting the dynamin-like GTPase DNM1 to form mitochondrial fission complexes. Plays a key role in determining the polarized localization of those DNM1 clusters that are not immediately involved in the mitochondrial fission process.
Subcellular location: Mitochondrion outer membrane {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:14576278, ECO:0000269|PubMed:16009724, ECO:0000269|PubMed:17998537}; Peripheral membrane protein {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:14576278, ECO:0000269|PubMed:16009724, ECO:0000269|PubMed:17998537}; Cytoplasmic side {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:14576278, ECO:0000269|PubMed:16009724, ECO:0000269|PubMed:17998537}. Note=Uniformly distributed on the cytoplasmic face of the mitochondrial outer membrane. This localization is dependent on FIS1. Reorganizes to punctate structures on mitochondria, corresponding to mitochondrial constriction sites, at a late step in mitochondrial division.
Interaction partners:
- Mitochondrial fission 1 protein
- Mitochondrial division protein 1
- Dynamin-related protein DNM1
- CCR4-associated factor 16
- CCR4-Not complex 3'-5'-exoribonuclease subunit Ccr4
- Nascent polypeptide-associated complex subunit beta-2
- General negative regulator of transcription subunit 3
- Poly
- Protein CAF40
- Mitofusin FZO1
Sequence:
MGSGDTRGESSLVAKPIEIILNKLPHAILAQQQFQKYITSPIYRYLSKLLLFREVAWPESTKDTQKGQVGIFSFQNNYADSATTFRILAHLDEQRYPLPNGAAEKNLPSLFEGFKATVSIIQQRLLLDNVDGATNSDKEKYVQLPDINTGFVNKTYSRIDLTHLLEDVETNVENLSINKTLEMDELTRLDSMINELESRKLKILERVKHIDSKSTNLENDVTLIKDRINFIEEYNLEADREQSLRKQMEEERSSEASSFTQNEEAISSLCDVESKDTRLKDFYKMPHEKSHDKNRQIISETYSRNTTAFRMTIPHGEHGNSITALDFDTPWGTLCSSSYQDRIVKVWDLNHGIQVGELPGHLATVNCMQIDKKNYNMLITGSKDATLKLWDLNLSREIYLDHSPLKEKTEEIVTPCIHNFELHKDEITALSFDSEALVSGSRDKKIFHWDLTTGKCIQQLDLIFTPTHSDIKMPARSLNNGACLLGTEAPMIGALQCYNSALATGTKDGIVRLWDLRVGKPVRLLEGHTDGITSLKFDSEKLVTGSMDNSVRIWDLRTSSILDVIAYDLPVSSLDFDGKLITVGANEGGVNVFNMERDEHWMTPEPPHSLDGDELSRRIAIVKYKDGFLINGHNDGDINVWTL
Protein: 2-hydroxy-3-oxopropionate reductase, putative (EC 1.1.1.31) (Q585Q3)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- DNA-directed RNA polymerase subunit beta
- V-type proton ATPase subunit
- DNA-direcetd RNA polymerase II, subunit 9, putative
- DNA-directed RNA polymerases I, II, and III subunit RPABC3
- Plastid-encoded RNA polymerase subunit alpha
- V-type ATPase, C subunit, putative
- 3-hydroxyisobutyryl-CoA hydrolase
- RNA polymerase-like protein
- DNA-directed RNA polymerase II, putative
- DNA-directed RNA polymerases I, II, and III subunit RPABC5
Sequence:
MSLRVGYIGLGLMGKPMAANILKAGFPLVVFNRTRSKAAELVASGAKEAASPAELAAVVDVVFTNLSDSSDVYEVVFGKNGVYSGVRPGTIFVDNSTIKPSTAREIAERLWKEKQVPCLDAPVSGGDIGARNGTLTIMVGGDPEVLEKVRPVLQAMGKTITHIGVSGAGQVCKAANQIMIAAQMVAMGEMLVFAEKCGVDGQKVIDAVRGGSAQCWALDVKPQRLFVGNREPGFKAALQTKDLNIVMDSAREFGVPMPSTAVNTQLYQSMLQHGEGDLDNSAIIGVLERMANCKIKETKP
Protein: Protein DSF2 (Deletion suppressor of MPT5 mutation protein 2) (P38213)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Interaction partners:
- tRNA modification GTPase MSS1
Sequence:
MNQNLKNTSWADRIGSDDQERKANSSEVSQSPPPNNSFESSMDSQFSYAHSNKSSISFESIQTTERLLDKLDLSLEDELILQEALLEEENASRNSQLSQTSGPTLCMPASEFPSLRYRTNPSPTYIQARDRSLIIDNLKEKDSTLRGKYSSGKVERHLPVKSRYSYIVEEDYDSETFSGMKPQMNRNEKDYKYPNLENGNRSTNSPNPFNFEKYRIENTRLHHLYPTLISDNNTSVDNNANSKNNRTTSNNINTSTKTDRISEKQSCPNEFTTTQKSNCLYRNGSSTSTNTSFSEVGQLSKPKTQSSFESESSSFSKLKLTKSDTTPIKPSPKRSNSSTSTITKTNTMTNDISLPPTPPYKAHKKKTSLNSLKKLFKSPRTRAKNKKDLESEGSSPIRSATNSLDFSGENIQLPSTSSTINNSSPHLARYIFPPNPVFHFKTASTPQSSTDKKKNSKARPNRTHLRTFSDFHTTEKDSKIGELSALTEQSNKPYHPKVRRRTLSLDGMLPNNSTQCMDSFSHKKEGSNATSKCGKLKFHPEPYDNDESSHIGQAITMRHQGKLEESAQRLKKACACGNKTAFLLYGLALRHGCGVDKNLKLSLGYLMAATDIKSFAAEVLDLDINPLNFASMDDIPDIAPEPTAPALYECGMAYLKGLGMDHPDERKGLKFLEKAALLGHVDSMCLSGTIWSKTSNVKKRDLARAAAWFRIADKKGANLLGSDWIYKEKYMKQGPK
Protein: C2 domain-containing protein aex-1 (G5EEU3)
Organism: Caenorhabditis elegans
Function: Involved in retrograde signaling from post-synaptic cells to pre-synaptic neurons, probably by regulating vesicle exocytosis in post-synaptic cells. Acts in muscles, to regulate the localization of synaptic vesicle fusion protein unc-13 likely during vesicle exocytosis and thus regulate retrograde signaling at the neuromuscular junction (NMJ). Regulates anterior body muscle contractions (aBOC) and the expulsion steps during the defecation motor program (DMP). Probably by regulating DMP, plays a homeostatic role in the uptake of triglycerides. Regulates locomotion.
Interaction partners:
- Endoprotease aex-5
- t-SNARE protein aex-4
- PH domain-containing protein
- G-protein coupled receptor aex-2
- Putative syntaxin-3
- Neuropeptide-like peptides nlp-40
- small monomeric GTPase
Sequence:
MREEALESICAALSISFTEDPDHLESIIDRFSEIFKVKDHLNQLRKKCEKFQTFTLEIRPVGSSNCTENVYAYIIESETCRQLELKPTGTTKLEIGSDKNVSLKFGLSQKKDSTTSKKGLSRSASLLKKLKFSDKKNLDELKISIFPLDIAVRKNINLGSGKSTLLEMKLIRNDHRNMIQCLEFDDFLEMTRSFHEWQAQISESELYDGSLGDPTFSMFYSIAFFFEIPSFVLKLTEMTCFLVWDDEMKKLDERALADVSLKMTACESEVDLQHPLLSPALSYLNDCTCNTIRCILVPFSTEPFFPPVSPSRLKSINVALKLIADICVLDVWDEFENLANPSNFLSSELKKLLESSAERYGESLKKQEFNELCRTILNLWMSLSNESQPYYIFFHQFDINYIGAAMLKLDKYLAESIQISLKCQLDLLNLRIPTELENFTKTTMRLFVTLRNLLNMVEAFHLPECQLFHFEEWFTDISVFWTYSWREVTLQMVERTITLDEDGDSVKYGARRPLPAGLYSFLCIQKGISDDLARLEFTFPHHLVVCAASVVNIMCQNINAYARKLFSEAMRNHEEKASRLVRATNGIEQAMCFVEEGYRRFAQFQRLEEYVDVDDLSAVRSTSIRLLKSTRDTCEIQVSTLLSHFVNLKTDIVLKIAKNLCADGKESNSGLKSYMRELASSERIESILECCYGLVDDVRCLLLPNCFKLSTQHFATSLEQQIRKNIRQKQPAEYYSNIYVGFLNILIFKRLKQMYLKFQIALKYIYEFLEIEDRKDIELLSNLHLNSFSTKDLILSYYDSLCEKIDRTRFGNAPHVDVHISYVKMVDEDTISIQIKLIKMSPIEWIDVISDRVDYFVRLELFPKILFPSNKFESPTTNPMPQSTRPQWKQLFEIRVPLECFFLRGACLAISVFDHERFIDRLVGRGFISLHSVPQASEEKPTQRLQVPLLPNDFSDQNNVFYQLLKTRACRDSIAKEFIETRTRRHQRIRALQHYIRINRNRVGHMLLG
Protein: 1,2-dihydroxynaphthalene dioxygenase (1,2-DHN dioxygenase) (DHNDO) (EC 1.13.11.56) (1,2-dihydroxynaphthalene oxygenase) (P11861)
Organism: Pseudomonas putida (Arthrobacter siderocapsulatus)
Function: Involved in the naphthalene catabolic pathway. Catalyzes the meta-cleavage of 1,2-dihydroxynaphthalene (1,2-DHN) to yield 2-hydroxychromene-2-carboxylic acid. Can also cleave 3-methylcatechol and 4-methylcatechol.
Interaction partners:
Sequence:
MSKQAAVIELGYMGISVKDPDAWKSFAMNMLGLQVLDEGEKDRFYLRMDYWHHRIVVHHSAEDDLEYLGWRVAGKPEFEALGQKLIDAGYKIRVCDKVEAQERMVLGLMKTEDPGGNPTEIFWGPRIDMSNPFHPGRPLHGKFVTGDQGLGHCIVRQTDVAAAHKFYSLLGFRGDVEYRIPLPNGMTAELSFMHCNARDHSIAFGAMPAAKRLNHLMLEYTHMEDLGYTHQQFVKNEIDIALQLGIHANDKALTFYGATPSGWLIEPGWRGATAIDEAEYYVGDIFGHGVEAPGYGLDVKLS
Protein: Dilute class unconventional myosin, isoform B (A1Z700)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MSSEEMLYAQGAKIWVPHADLVWESATLEESYRKGAGFLKICTDSGKLKEVKLKADGSDLPPLRNPAILVGQNDLTTLSYLHEPGVLHNLRVRFCERQIIYTYCGIILVAINPYAEMPLYGPSIIRAYRGHAMGDLEPHIFALAEEAYTKLERENCNLSIIVSGESGAGKTVSAKYAMRYFAAVGGSESETQVERKVLASSPIMEAFGNAKTTRNDNSSRFGKFTKLLFRNQMGVMFLQGATMHTYLLEKSRVVYQAQGERNYHIFYQLCAARSKYPELVLDHQDKFQFLNMGGAPEIERVSDAEQFNETVQAMTVLGFSIQQIADIVKILAGILHLGNIQVSKKFNEGSEEEDSDSCDIFHNDIHLQITADLLRVSADDLRRWLLMRKIESVNEYVLIPNSIEAAQAARDALAKHIYAKLFQYIVGVLNKSLNNGSKQCSFIGVLDIYGFETFEVNSFEQFCINYANEKLQQQFNQHVFKLEQEEYLKEGITWTMIDFYDNQPCIDLIESRLGVLDLLDEECRMPKGSDESWAGKLIGKCNKFPHFEKPRFGTTSFFIKHFSDTVEYDVNGFLEKNRDTVSKELTQVLSESNMSLAKQVMTLEEIDTLCVDSAKSSTLGGRVVISAGRKQVVPSKQHRKTVGSQFQESLASLISTLHATTPHYVRCIKPNDDKVAFKWETAKIIQQLRACGVLETVRISAAGFPSRWLYPDFYMRYQLLVYRSKLDKNDMKLSCRNIVMKWIQDEDKYRFGNTQIFFRAGQVAFLEQVRANLRKKYITIVQSVVRRFVYRRQFLRIQKVINGIQKHARGYLARERTQKMREARAGLILSKYARGWLCRRRYLRLRHSISGIQTYARGMLARNKFHAMRDHYRAVQIQRFVRGALARRAYQKRRRNIIICQAAIRRFLARRKFKRMKAEAKTISHMENKYMGLENKIISMQQRIDELNRDNSNLKHKTSEISVLKMKLELKKTLEAEFKNVKAACQDKDKLIEALNKQLEAERDEKMQLLEENGHAQEEWISQKQTWRQENEELRRQIDEIIDMAKNAEVNQRNQEDRMLAEIDNRELNEAYQRAIKDKEVIENENFMLKEELSRLTAGSFSLHARKASNASSQNEDDVGYASAKNTLDINRPPDLLSKNYSYNDSTSLVVKLRSILEEEKQKHKVLQEQYIKLSSRHKPTEDSFRTACRLAGRGT
Protein: Similar to jumonji domain containing 2B (Q4KM27)
Organism: Rattus norvegicus (Rat)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MKRVSGACIQCSYEHCSTSFHVTCAHAAGVLMEPDDWPYVVSITCLKHRASGAGGQLLRTVSLGQIVITKNRNGLYYRCRVIGTTAQTFYEVNFDDGSYSDNLYPESITSRDCLRLGPPPEGELVELRWTDGNLYRARFISMATSLIYQVEFEDGSQLTVKRADIFTLEEELPKRVRSRLSLSTGTPQEPSFSGDGVKAAKRPRVATVLATTTEDTGRSPEYLAFMESLLQAQGQPGAPF
Protein: Germacrene A hydroxylase (EC 1.14.14.95) (Germacrene A oxidase) (SlGAO) (D5JBW9)
Organism: Saussurea costus (Costus) (Aucklandia costus)
Function: Involved in the biosynthesis of germacrene-derived sesquiterpene lactones. Catalyzes three consecutive oxidations of germacrene A to produce germacrene A acid. Could also catalyze the three-step oxidation of non-natural substrate amorphadiene to artemisinic acid.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:D5JBW8}; Single-pass type II membrane protein {ECO:0000250|UniProtKB:D5JBW8}.
Interaction partners:
Sequence:
MELSFTTSIAVATIVFVLFKLATRPKSNKKLLPEPWRLPIIGHMHHLIGTMPHRGVMDLARKYGSLMHLQLGEVSTIVVSSPKWAKEILTTHDITFANRPETLTGEIIAYHNTDIVLAPYGEYWRQLRKLCTLELLSVKKVKSFQSLREEECWNLVQEVKESGSGRPVDLSENIFKMIATILSRAAFGKGIKDQKEFTEIVKEILRQTGGFDVADIFPSKKFLHHLSGKRARLTSIHKKLDNLINNIVAEHPGNNSSKSNETLLDVMLRLKDSVEFPLTADNVKAIILDMFGAGTDTSSATVEWAISELIRCPRAMEKVQAELRQALKGKDKVKEEDIQDLSYLDLVIKETLRLHPPLPLVMPRECRQPVNLAGYDIANKTKLIVNVFAINRDPEYWKDAESFIPERFENSPITVMGAEYEYLPFGAGRRMCPGAALGLANVQLPLANILYHFNWKLPNGASHDQLDMTESFGATVQRKTHLVLVPSF
Protein: Beta-3 adrenergic receptor (Beta-3 adrenoreceptor) (Beta-3 adrenoceptor) (P25962)
Organism: Mus musculus (Mouse)
Function: Beta-adrenergic receptors mediate the catecholamine-induced activation of adenylate cyclase through the action of G proteins. Beta-3 is involved in the regulation of lipolysis and thermogenesis.
Subcellular location: Cell membrane; Multi-pass membrane protein.
Interaction partners:
- Beta-2 adrenergic receptor
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein G
- Beta-1 adrenergic receptor
- Mitochondrial brown fat uncoupling protein 1
- Hormone-sensitive lipase
- Adiponectin
- Fibroblast growth factor 21
Sequence:
MAPWPHRNGSLALWSDAPTLDPSAANTSGLPGVPWAAALAGALLALATVGGNLLVIIAIARTPRLQTITNVFVTSLAAADLVVGLLVMPPGATLALTGHWPLGETGCELWTSVDVLCVTASIETLCALAVDRYLAVTNPLRYGTLVTKRRARAAVVLVWIVSAAVSFAPIMSQWWRVGADAEAQECHSNPRCCSFASNMPYALLSSSVSFYLPLLVMLFVYARVFVVAKRQRHLLRRELGRFSPEESPPSPSRSPSPATGGTPAAPDGVPPCGRRPARLLPLREHRALRTLGLIMGIFSLCWLPFFLANVLRALAGPSLVPSGVFIALNWLGYANSAFNPVIYCRSPDFRDAFRRLLCSYGGRGPEEPRAVTFPASPVEARQSPPLNRFDGYEGARPFPT
Protein: Beta-casein (P05814)
Organism: Homo sapiens (Human)
Function: Important role in determination of the surface properties of the casein micelles.
Subcellular location: Secreted.
Interaction partners:
- Alpha-S1-casein
- Kappa-casein
- Alpha-lactalbumin
- Signal transducer and activator of transcription 5A
- Albumin
- Prolactin
- Lactotransferrin
- Receptor tyrosine-protein kinase erbB-4
- Prolactin receptor
- Butyrophilin subfamily 1 member A1
Sequence:
MKVLILACLVALALARETIESLSSSEESITEYKQKVEKVKHEDQQQGEDEHQDKIYPSFQPQPLIYPFVEPIPYGFLPQNILPLAQPAVVLPVPQPEIMEVPKAKDTVYTKGRVMPVLKSPTIPFFDPQIPKLTDLENLHLPLPLLQPLMQQVPQPIPQTLALPPQPLWSVPQPKVLPIPQQVVPYPQRAVPVQALLLNQELLLNPTHQIYPVTQPLAPVHNPISV
Protein: BK channel (H7BRM4)
Organism: Caenorhabditis elegans
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
Sequence:
MGEIYSPSQSKGFNQPYGYPMNCNLSRVFMEMTEEDRKCLEERKYWCFLLSSITTFCASMILVVIWRVVTHLCCQRREKEFVEPIPAPEAVQINMNGSKHAPSETDPFLKQQEEKHLGWMTEAKDWAGELISGQSLTGRFLVLLVFILSIGSLIIYFYDASFQNFQVETCIPWQDSPSQQIDLGFNIFFLVYFFIRFIAASDKVWFLLEMYSWIDFFTIPPSFVAIYLQRNWLGFRFLRALRLMTVPDILQYLNILKTSSSIRLTQLVTIFVAVCLTGAGLVHLLENSGDFFKGFINPHRITYADSVYFVLVTMSTVGYGDIYCTTLCGRLFMIFFILFGLAMFASYVPEIADLIGNRQKYGGEYKGEHGKKHIVVCGHITYDSVSHFLQDFLHEDRDDVDVEVVFLHRVVPDLELEGLFKRHFTKVEFFTGTVMDSLDLSRVKIGDADACLVLANKYSTNPDAEDAANIMRVISIKNYSSDIRVIVQLMQYHNKAYLLNIPSWDWKRGDDVICLAELKLGFIAQSCLAPGFSTMMANLFAMRSFKTSPHTPLWLNDYLRGAGMEMYTESLSPSFANMSFPEAANLLFNRLGLLLLAIELKDEENKECNIAINPGPHIVIQPQTQGFFIAQSADEVKRAFFWCKQCHDDIKDVSLIKKCKCKNLALFRRNTKHSTAARDYSDFDALFYQNDARATDVLQQFQPQAPAGPMGHLGQQVQLRMINQQSSTSDTHLNTKSLRFAYEIKKLMPSSGGRRNSMSIPPDGRGVDFSKDFEQQFQDMKYDSTGMFHWCPSRNLEDCVLERHQAAMTVLNGHVVVCLFADQDSPLIGLRNFIMPLRSSNFHYHELKHVVIVGDLEYLRKEWKTLYNLPKISILNGSPLSRADLRAVNINLCDMCVIISARVPNTEDTTLADKEAILASLNIKAMQFDDTLGFFPMRHQTGDRSPLGSPISMQKKGAKFGTNVPMITELVNDSNVQFLDQDDDDDPDTELYLTQPFACGTAFAISVLDSLMSTTYFNDSALTLIRTLVTGGATPELELILAEGAGLRGGYSTPETLSNRDRCRIAQISLQDNPYDGVVHNTTYGAMFTIALRRYGQLCIGLYRLHDQDNPDSMKRYVITNPPAELRIKNTDYVYVLEQFDPGLEYEPGKRHF
Protein: Ubiquitin carboxyl-terminal hydrolase 42 (EC 3.4.19.12) (Deubiquitinating enzyme 42) (Ubiquitin thioesterase 42) (Ubiquitin-specific-processing protease 42) (B2RQC2)
Organism: Mus musculus (Mouse)
Function: Deubiquitinating enzyme which may play an important role during spermatogenesis.
Interaction partners:
- Cellular tumor antigen p53
Sequence:
MTIVDKTEPSDPSTCQNQPGSCEAVSPEDMDTGSASWGAVSSISDVSSHTLPLGPVPGAVVYSNSSVPEKSKPSPPKDQVLGDGIAPPQKVLFPSEKICLKWQQSHRVGAGLQNLGNTCFANAALQCLTYTPPLANYMLSHEHSKTCHAEGFCMMCTMQTHITQALSNPGDVIKPMFVINEMRRIARHFRFGNQEDAHEFLQYTVDAMQKACLNGSNKLDRHTQATTLVCQIFGGYLRSRVKCLNCKGVSDTFDPYLDITLEIKAAQSVTKALEQFVKPEQLDGENSYKCSKCKKMVPASKRFTIHRSSNVLTISLKRFANFTGGKIAKDVKYPEYLDIRPYMSQPNGEPIIYVLYAVLVHTGFNCHAGHYFCYIKASNGLWYQMNDSIVSTSDIRAVLNQQAYVLFYIRSHDVKNGGESAHPAHSPGQSSPRPGVSQRVVNNKQVAPGFIGPQLPSHVMKNTPHLNGTTPVKDTPSSSVSSPNGNTSVNRASPATASTSVQNWSVTRPSVIPDHPKKQKITISIHNKLPARQGQAPLNNSLHGPCLEAPSKAAPSSTITNPSAIQSTSNVPTTSTSPSEACPKPMVNGKAKVGASVLVPYGAESSEESDEESKGLAKENGVDMMAGTHSDRPEAAADDGAEASSHELQEPVLLNGANSADSDSQENSLAFDSASCQVQPELHTENLFSKLNGLPGKVTPAPLQSVPEDRILETFKLTNQAKGPAGEESWTTTGGSSPKDPVSQLEPISDEPSPLEIPEAVTNGSTQTPSTTSPLEPTISCTKEDSSVVVSAEPVEGLPSVPALCNSTGTILGDTPVPELCDPGDLTANPSQPTEAVKGDTAEKAQDSAMAEVVERLSPAPSVLTGDGCEQKLLLYLSAEGSEETEDSSRSSAVSADTMPPKPDRTTTSSCEGAAEQAAGDRGDGGHVGPKAQEPSPAKEKMSSLRKVDRGHYRSRRERSSSGEHVRDSRPRPEDHHHKKRHCYSRERPKQDRHPTNSYCNGGQHLGHGDRASPERRSLSRYSHHHSRIRSGLEQDWSRYHHLENEHAWVRERFYQDKLRWDKCRYYHDRYTPLYTARDAREWRPLHGREHDRLVQSGRPYKDSYWGRKGWELQSRGKERPHFNSPREAPSLAVPLERHLQEKAALSVQDSSHSLPERFHEHKSVKSRKRRYETLENNDGRLEKKVHKSLEKDTLEEPRVKKHKKSKKKKKSKDKHRDRESRHQQESDFSGAYSDADLHRHRKKKKKKKRHSRKSEDFIKDVEMRLPKLSSYEAGGHFRRTEGSFLLADGLPVEDSGPFREKTKHLRMESRPDRCRLSEYGQGD
Protein: Alpha pinene synthase, chloroplastic (LsPINS) (EC 4.2.3.-) (T1RRL8)
Organism: Lavandula stoechas (Butterfly lavender)
Function: Monoterpene synthase involved in the biosynthesis of volatile compounds widely used in aromatherapy and folk medicine, and present in culinary herbs. Mediates the conversion of (2E)-geranyl diphosphate (GPP) into alpha-pinene and, as minor compounds, into alpha-phellandrene, limonene and alpha-terpinolene (By similarity).
Subcellular location: Plastid, chloroplast {ECO:0000255}.
Interaction partners:
Sequence:
MSSISMHARPLNISAANNHHPSWDRRVSKPRRVAAKHLRLRLSCSLQLDGKPLDETRRSANYQPSAWDFNFIQSLHNQYKEDKYVTRHTELTAQVKMLLEEETDAVQQLDLIEDLKNLGINYLFKDKIQQILNHIYNQHRCFQNNQVEGNDLYFTALGFRLLRQHGFEVSQEVFDRFTNEEGTDFNPSLIDDTKGLLQLYEASFLLREGEDTLELARQFSTKLLQKKVDEDGDREVGDNLLVWIRHSLELPLHWRIHRIEARWFLDAYATRHDMNPIIFELAKLDFNITQATQQEELRDLSRWWNSAGLVEKLSFARDRVVESYFWAIGTLEPRQYGYQRKLVAKIIALISVVDDVYDIYGTLDELKLFTDVMRRWDAESFDQLPYYMKICYLIINNFIFELAYDILKDKGFNSLSYLQRSWLDVVEGYFTEAKWYYSGYTPNLEEYLKNAKITVTCPMILSQIYFTIASSIEKPELESMYKYHDILYLSGLLLRLPDDLGTALHELKRGDVPKAMQCYMKEKNVPEKEAREHVRFLIREASKQMNTVSAADCPFPDDFVAAAANLGRVANFVYVDGDGFGDQHSKMLQQIAALMFEPYD
Protein: alpha-mannosidase (EC 3.2.1.24) (A0A140VJN9)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MAAAPALKHWRTTLERVEKFVSPLYFTDCNLRGRLFGASCPVAVLSSFLTPERLPYQEAVQRDFRPAQVGDSFGPTWWTCWFRVELTIPEAWVGQEVHLCWESDGEGLVWRDGEPVQGLTKEGEKTSYVLTDRLGERDPRSLTLYVEVACNGLLGAGKGSMIAAPDPEKMFQLSRAELAVFHRDVHMLLVDLELLLGIAKGLGKDNQRSFQALYTANQMVNVCDPAQPETFPVAQALASRFFGQHGGESQHTIHATGHCHIDTAWLWPFKETVRKCARSWVTALQLMERNPEFIFACSQAQQLEWVKSRYPGLYSRIQEFACRGQFVPVGGTWVEMDGNLPSGEAMVRQFLQGQNFFLQEFGKMCSEFWLPDTFGYSAQLPQIMHGCGIRRFLTQKLSWNLVNSFPHHTFFWEGLDGSRVLVHFPPGDSYGMQGSVEEVLKTVANNRDKGRANHSAFLFGFGDGGGGPTQTMLDRLKRLSNTDGLPRVQLSSPRQLFSALESDSEQLCTWVGELFLELHNGTYTTHAQIKKGNRECERILHDVELLSSLALARSAQFLYPAAQLQHLWRLLLLNQFHDVVTGSCIQMVAEEAMCHYEDIRSHGNTLLSAAAAALCAGEPGPEGLLIVNTLPWKRIEVMALPKPGGAHSLALVTVPSMGYAPVPPPTSLQPLLPQQPVFVVQETDGSVTLDNGIIRVKLDPTGRLTSLVLVASGREAIAEGAVGNQFVLFDDVPLYWDAWDVMDYHLETRKPVLGQAGTLAVGTEGGLRGSAWFLLQISPNSRLSQEVVLDVGCPYVRFHTEVHWHEAHKFLKVEFPARVRSSQATYEIQFGHLQRPTHYNTSWDWARFEVWAHRWMDLSEHGFGLALLNDCKYGASVRGSILSLSLLRAPKAPDATADTGRHEFTYALMPHKGSFQDAGVIQAAYSLNFPLLALPAPSPAPATSWSAFSVSSPAVVLETVKQAESSPQRRSLVLRLYEAHGSHVDCWLHLSLPVQEAILCDLLERPDPAGHLTLRDNRLKLTFSPFQVLSLLLVLQPPPH
Protein: C-1-tetrahydrofolate synthase, mitochondrial (C1-THF synthase) [Includes: Methylenetetrahydrofolate dehydrogenase (EC 1.5.1.5); Methenyltetrahydrofolate cyclohydrolase (EC 3.5.4.9); Formyltetrahydrofolate synthetase (EC 6.3.4.3)] (P09440)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Mitochondrial isozyme of C-1-tetrahydrofolate synthase. The trifunctional enzyme catalyzes the interconversion of the one-carbon derivatives of tetrahydrofolate (THF) between different oxidation states by the enzymatic activities 10-formyltetrahydrofolate synthetase, 5,lO-methenyltetrahydrofolate cyclohydrolase, and 5,lO-methylenetetrahydrofolate dehydrogenase.
Subcellular location: Mitochondrion {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:14576278, ECO:0000269|PubMed:3528153}.
Interaction partners:
- Serine hydroxymethyltransferase, mitochondrial
- Serine hydroxymethyltransferase, cytosolic
- Methionyl-tRNA formyltransferase, mitochondrial
- Phosphoribosylglycinamide formyltransferase
- Methylenetetrahydrofolate dehydrogenase [NAD
- Aminomethyltransferase, mitochondrial
- 5-formyltetrahydrofolate cyclo-ligase
- Bifunctional purine biosynthesis protein ADE16
- Bifunctional purine biosynthesis protein ADE17
- Dihydrofolate reductase
Sequence:
MLSRLSLLSNSRAFQQARWRIYRLKVSPTVHASQYHILSGRKLAQSIREKANDEIQAIKLKHPNFKPTLKIIQVGARPDSSTYVRMKLKASKDSNVDCIIEKLPAEITEVELLKKISDINDDDSIHGLLIQLPLPRHLDETTITNAVDFKKDVDGFHRYNAGELAKKGGKPYFIPCTPYGCMKLLEEAHVKLDGKNAVVLGRSSIVGNPIASLLKNANATVTVCHSHTRNIAEVVSQADIVIAACGIPQYVKSDWIKEGAVVIDVGINYVPDISKKSGQKLVGDVDFDSVKEKTSYITPVPGGVGPMTVAMLVSNVLLAAKRQFVESEKLPVIKPLPLHLESPVPSDIDISRAQSPKHIKQVAEELGIHSHELELYGHYKAKISPNIFKRLESRENGKYVLVAGITPTPLGEGKSTTTMGLVQALSAHLGKPSIANVRQPSLGPTLGVKGGAAGGGYAQVIPMDEFNLHLTGDIHAISAANNLLAAAIDTRMFHEATQKNDSTFYKRLVPRKKGIRKFTPSMQRRLKRLDIEKEDPDALTPEEVKRFARLNINPDTITIRRVVDINDRMLRQITIGEAATEKGFTRTTGFDITVASELMAILALSKSLHEMKERIGRMVIGADYDNKPVTVEDIGCTGALTALLRDAIKPNLMQTLEGTPVMVHAGPFANISIGASSVIADLMALKLVGSEKNPLNDKNIHEPGYVVTEAGFDFAMGGERFFDIKCRSSGLVPDAVVLVATVRALKSHGGAPNVKPGQSLPKEYTEENIDFVAKGVSNLVKQIENIKTFGIPVVVAINRFETDSQAEIEVIKKAALNAGASHAVTSNHWMEGGKGAVELAHAVVDATKEPKNFNFLYDVNSSIEDKLTSIVQKMYGGAKIEVSPEAQKKIDTYKKQGFGNLPICIAKTQYSLSHDPSLKGVPRGFTFPIRDVRASIGAGYLYALAAEIQTIPGLSTYAGYMAVEVDDDGEIEGLF