wanglab/gogpt-training-data huggingface dataset:
Protein: Voltage-dependent L-type calcium channel subunit beta-3 (Calcium channel voltage-dependent subunit beta 3) (A8WHZ5)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
Sequence:
MYDNLYLHGFEDSEAGSADSYTSRPSDSDVSLDEEQGGRQEKEQQATVQLERAKAKAVAFAVRTNVSYCGALDEDVPVAGTAISFDAKDFLHIKEKYNNDWWIGRLVKEGCDIGFIPSPLKLENIRLQQDQKRGRFHGKSSGNSSSSLGEMVSGTFKPNPASAGKQKQKVAEHIPPYDVVPSMRPVVLVGPSLKGYEVTDMMQKALFDFLKHRFEGRISITRVTADISLAKRSVLNNPSKRAIIERSNTRSNLAEVQSEIERIFELARSLQLVVLDADTINHPAQLIKTSLAPIIVHVKVSSPKVLQRLIKSRGKSQSKHLNVQLVAADKLAQCPPEMFDIILDENQLEDACEHLSEYLEAYWRATHTSLSTPLNPLLGRNLGSTALSPYPTAISGLQSQRNKNSNHITDNSPMERRSLMTSDENYHNNERQKKTHNRLSSSSQQSRDHYPLVEEDYHDPYPDAYKPHRNRGSPGGYSNDSRHRL
Protein: RRM domain-containing protein (A0A178W7C6)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
Sequence:
MAESSKLSATTVEAAPAMIKAKDVISPSEKEESDQTEITKVSVLKNLDEKEMIKEFADRLQRLEAKVDLLVTKADLLAIKADIQELLISAKGEKVPAMKTSAKASSESDDSYMDTSSEDESSSAEEPVNKPAASAAKPATKDSLFSAGFKPAAKDSLFSAGFKPDSLFSAGFEPAAKDSLFSAGFKPGSLFSAGFEPAAKDSLFSAGFKPDSLFSVGVKPAAKDSLFSVGVNGRSFSVTGFDASLPVDDIKSALSKYFSSFGEITRVFVPPSHGTGGSLGYAYIDLKEGAEKALELGRHDVGGWDLVVGKAEPIRSGSTWPFPGRCGNQGRCTFC
Protein: Jacalin-related lectin Calsepa (Agglutinin) (Mannose/maltose-specific lectin) (P93114)
Organism: Calystegia sepium (Hedge bindweed) (Convolvulus sepium)
Function: Mannose-binding lectin. Preferentially binds mannose at concentrations ranging between 5 and 25 mM, but binds also glucose. Has a marked preference for methylated sugar derivatives, such as alpha-MeMan and alpha-MeGlc, at concentration down to 5 mM. Binds to N-glycans, but not to glycolipid-type or other type of glycans. Binds N-linked high-mannose-type glycans. Has a preference for smaller (Man(2)-Man(6)) high-mannose-type glycans to larger (Man(7)-Man(9)) ones. Recognizes both alpha1-6 extended and alpha1-3 extended monoantennary glycans. The addition of alpha1-2Man to the Man-alpha1-3Man-beta branch results in a significant loss of affinity, but beta1-2GlcNAc has some affinity. Has less affinity for biantennary glycans. However, affinity is significant for the biantennary complex-type N-glycans with bisecting GlcNAc. No affinity is observed for tri- and tetra-antennary glycans. Binds bisected glycans of the mouse brain. Selectively binds to bisecting N-glycans which are in back-fold conformation, and does not favor a glycan with an extend conformation. Has hemagglutinating activity against rabbit erythrocytes at 0.3 ug/ml and against trypsin-treated human erythrocytes at 5 ug/ml. Has mitogenic activity in murine cells.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:10908718}.
Interaction partners:
Sequence:
MAVPMDTISGPWGNNGGNFWSFRPVNKINQIVISYGGGGNNPIALTFSSTKADGSKDTITVGGGGPDSITGTEMVNIGTDEYLTGISGTFGIYLDNNVLRSITFTTNLKAHGPYGQKVGTPFSSANVVGNEIVGFLGRSGYYVDAIGTYNRHK
Protein: 33 kDa chaperonin (Heat shock protein 33) (HSP33) (P0A6Y5)
Organism: Escherichia coli (strain K12)
Function: Redox regulated molecular chaperone. Protects both thermally unfolding and oxidatively damaged proteins from irreversible aggregation. Plays an important role in the bacterial defense system toward oxidative stress.
Subcellular location: Cytoplasm.
Interaction partners:
- Heat shock protein 15
- Chaperone protein DnaK
- Chaperone protein DnaJ
- Protein GrpE
- Chaperonin GroEL
- ATP-dependent protease ATPase subunit HslU
- ATP-dependent protease subunit HslV
- Chaperone protein HtpG
- Chaperone protein ClpB
- Small heat shock protein IbpA
Sequence:
MPQHDQLHRYLFENFAVRGELVTVSETLQQILENHDYPQPVKNVLAELLVATSLLTATLKFDGDITVQLQGDGPMNLAVINGNNNQQMRGVARVQGEIPENADLKTLVGNGYVVITITPSEGERYQGVVGLEGDTLAACLEDYFMRSEQLPTRLFIRTGDVDGKPAAGGMLLQVMPAQNAQQDDFDHLATLTETIKTEELLTLPANEVLWRLYHEEEVTVYDPQDVEFKCTCSRERCADALKTLPDEEVDSILAEDGEIDMHCDYCGNHYLFNAMDIAEIRNNASPADPQVH
Protein: Protein amnionless [Cleaved into: Soluble protein amnionless] (Q99JB7)
Organism: Mus musculus (Mouse)
Function: Membrane-bound component of the endocytic receptor formed by AMN and CUBN. Required for normal CUBN glycosylation and trafficking to the cell surface. The complex formed by AMN and CUBN is required for efficient absorption of vitamin B12 (By similarity). Required for normal CUBN-mediated protein transport in the kidney.
Subcellular location: Apical cell membrane {ECO:0000269|PubMed:15342463}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:Q9BXJ7}. Cell membrane {ECO:0000250|UniProtKB:Q9BXJ7}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:Q9BXJ7}. Endosome membrane {ECO:0000250|UniProtKB:Q9BXJ7}. Membrane, coated pit {ECO:0000250|UniProtKB:Q9BXJ7}.
Interaction partners:
- Cubilin
- Low-density lipoprotein receptor-related protein 2
- Cobalamin binding intrinsic factor
Sequence:
MGALGRVLLWLQLCAMTRAAYKLWVPNTSFDTASNWNQNRTPCAGDAVQFPADKMVSVLVRDSHAISDMLLPLDGELVLASGAALSAAGGDSDPACNPGAPLLFRNPDRFSWLDPHLWSSGTQAPGLFSVDAERVPCSYDDVLFPRDGSFRVALGPGPNPVHVRSVSAVGQTFSRDEDLTAFLASREGRLRFHGSGALRVGSQACTDASGCVCGNAEMLPWICASLLQPLGGRCPQAACQDPLLPQGQCCDLCGAIVSLTHDPTFDLERYRARLLDLFLKQPQYQGLQVAVSKVLRDAHTEIQVVLVETEHATGAAGQLGHALLQDAVAQGSVLGIVSATLRQSGKPMTADSELNQSSSGAGLAGGVAALVLLALLGTVLLLLHRSGRLRWRRHEDAEPVSAGLPLGFRNPIFDAIVFKQQPSVELPDSAQKVDILDIDTKFGCFVNPLFAGEAEAEA
Protein: Cis-3,4-dihydrophenanthrene-3,4-diol dehydrogenase (EC 1.3.1.49) (Cis-phenanthrene dihydrodiol dehydrogenase) (PDD dehydrogenase) (Q9WXG7)
Organism: Alcaligenes faecalis
Function: Involved in the degradation of phenanthrene. Catalyzes the oxidation of cis-phenanthrene dihydrodiol (PDD) to yield phenanthrenediol. It can use either NAD or NADP as electron acceptor, however NAD is preferred to NADP.
Interaction partners:
Sequence:
MAWLEGQSVFLTGGVAGLGRALVKRLVEEGANVTVLDRNARGLDELVESFKGRVAGSPGDVRNLADNRKAVELAVERFGKLDTFNRQRRHLGLLCPPCRPAGRCHQRSFDEVIGINLMGYVMGIKAAAPALVRSRGSVILTLSSSAFYAGGGGVLYTVAKHAAVGLIKQAAHELAPYVRVNGVAPGGIASDLRGPKSLGMGEQSITSVPLADLVKDIAPIGRLSDTEEYTGSYVYLASARNSAPATGVIINCDGGMGVRSVLGPASGGKGLLEKFGG
Protein: V-type proton ATPase subunit (Q5M7T6)
Organism: Rattus norvegicus (Rat)
Interaction partners:
- V-type proton ATPase subunit E 1
- V-type proton ATPase 116 kDa subunit a 1
- V-type proton ATPase subunit D
- V-type proton ATPase catalytic subunit A
- V-type proton ATPase subunit B, brain isoform
- V-type proton ATPase 16 kDa proteolipid subunit c
- V-type proton ATPase 21 kDa proteolipid subunit c''
- V-type proton ATPase subunit S1
- Renin receptor
- V-type proton ATPase subunit F
Sequence:
MSFFPELYFNVDNGYLEGLVRGLKAGVLSQADYLNLVQCETLEDLKLHLQSTDYGNFLANEASPLTVSVIDDKLKEKMVVEFRHMRNHAYEPLASFLDFITYSYMIDNVILLITGTLHQRSIAELVPKCHPLGSFEQMEAVNIAQTPAELYNAILVDTPLAAFFQDCISEQDLDEMNIEIIRNTLYKAYLESFYKFCTLLGGTTADAMCPILEFEADRRAFIITINSFGTELSKEDRAKLFPHCGRLYPEGLAQLARADDYEQVKNVADYYPEYKLLFEGAGSNPGDKTLEDRFFEHEVKLNKLAFLNQFHFGVFYAFVKLKEQECRNIVWIAECIAQRHRAKIDNYIPIF
Protein: UDP-glycosyltransferase 71C3 (EC 2.4.1.-) (Q9LML7)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Possesses low quercetin 3-O-glucosyltransferase activity in vitro.
Interaction partners:
- Mucin-like protein
- Hydroxyproline-rich glycoprotein family protein
- At2g35730
- ER membrane protein, putative
- F-box/kelch-repeat protein At1g55270
- Protein RETICULATA-RELATED 3
- Large ribosomal subunit protein eL32y
Sequence:
MKAEAEIIFVTYPSPGHLLVSIEFAKSLIKRDDRIHTITILYWALPLAPQAHLFAKSLVASQPRIRLLALPDVQNPPPLELFFKAPEAYILESTKKTVPLVRDALSTLVSSRKESGSVRVVGLVIDFFCVPMIEVANELNLPSYIFLTCNAGFLSMMKYLPERHRITTSELDLSSGNVEHPIPGYVCSVPTKVLPPGLFVRESYEAWVEIAEKFPGAKGILVNSVTCLEQNAFDYFARLDENYPPVYPVGPVLSLKDRPSPNLDASDRDRIMRWLEDQPESSIVYICFGSLGIIGKLQIEEIAEALELTGHRFLWSIRTNPTEKASPYDLLPEGFLDRTASKGLVCDWAPQVEVLAHKALGGFVSHCGWNSVLESLWFGVPIATWPMYAEQQLNAFSMVKELGLAVELRLDYVSAYGEIVKAEEIAGAIRSLMDGEDTPRKRVKEMAEAARNALMDGGSSFVAVKRFLDELIGGDV
Protein: Thioredoxin-2 (Thioredoxin II) (TR-II) (Thioredoxin-1) (P22803)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Participates as a hydrogen donor in redox reactions through the reversible oxidation of its active center dithiol to a disulfide, accompanied by the transfer of 2 electrons and 2 protons. It is involved in many cellular processes, including deoxyribonucleotide synthesis, repair of oxidatively damaged proteins, protein folding, sulfur metabolism, and redox homeostasis. Thioredoxin-dependent enzymes include phosphoadenosine-phosphosulfate reductase MET16, alkyl-hydroperoxide reductase DOT5, thioredoxin peroxidases TSA1 and TSA2, alkyl hydroperoxide reductase AHP1, and peroxiredoxin HYR1. Thioredoxin is also involved in protection against reducing stress. As part of the LMA1 complex, it is involved in the facilitation of vesicle fusion such as homotypic vacuole and ER-derived COPII vesicle fusion with the Golgi. This activity does not require the redox mechanism. Through its capacity to inactivate the stress response transcription factor YAP1 and its regulator the hydroperoxide stress sensor HYR1, it is involved in feedback regulation of stress response gene expression upon oxidative stress.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:14562095}. Golgi apparatus membrane {ECO:0000269|PubMed:14562095}; Peripheral membrane protein {ECO:0000269|PubMed:14562095}. Nucleus {ECO:0000269|PubMed:14562095}.
Interaction partners:
- Thioredoxin reductase 1
- Peroxiredoxin AHP1
- Thioredoxin-1
- Peptide methionine sulfoxide reductase
- AP-1-like transcription factor YAP1
- Peroxiredoxin TSA1
- Transcription factor SKN7
- Thioredoxin reductase 2, mitochondrial
- Peroxiredoxin PRX1, mitochondrial
- Glutaredoxin-2
Sequence:
MVTQLKSASEYDSALASGDKLVVVDFFATWCGPCKMIAPMIEKFAEQYSDAAFYKLDVDEVSDVAQKAEVSSMPTLIFYKGGKEVTRVVGANPAAIKQAIASNV
Protein: MAX dimerization protein MGA a (Max gene-associated protein) (D2JVK2)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|PROSITE-ProRule:PRU00201}.
Interaction partners:
Sequence:
MADTEKQGAMVLHEEGVTAPTLAPPTTTPPSIFVVLKQLQSSDSGNDKANLMAISEANKMGKSSIGTTVAGIQPTSSTFADTNSTTPSENLPADARCRGITVTLDNNNMWNEFHRCKTEMILTKQGRRMFPYCRFRLSGMEPFQNYVLAMDIKPADNCRYKWSGKGWEPNGKAEPHISRLFVHPESPASGLHWMQYPVSFYRLKLCNTLDQEGHIILHSMHRYLPQIHIIPADKVSKDILILDRPNVVTLSFAQTEFFAVTAYQNLCITQLKIDYNPFAKGFREDAVNARSSKAKNGLSTDETESELKLSKEMTTLNNLKTLFMKRKASVKVNVNQNVPNPTNGENKVVNGAAPAVDTNVQSLCNKKRPSSSAFSDFIKGAHVKVKRLSLENINKTGGATEPSTACTSKQKEAADISSITENSLQVDQKDGNGAGDVLRCESTDTSLKTGVLKANEIKKEIDEHSADKNTLKSSDQNLSCSDEKKMETVSSLSTEAKPDAQMKKTLPHKRPERVPLPLLAKFLKQRRPILPKPVSHSSLSDSEKSCEPAQTSESSSVLMSFIPCVTTNLDSQPAVTSLSQTVTSSTTDANNMTSLSTTLSYSSTTVPLIPSETQLCDRFSASPVGSDPFSAPNTTSPSKPNSNPALDISNNTDAIFTPDHDNTLRSQSDISSDSTCDVVHDSCPPTVNTDTVETPVVPSPTSVFDVPSSTDNDMNSYQDINSMPDVAEGDSISDCLLDSSTGSCPEFFSEEIPQNTLFTNEESLSLPLDDASSPAFSLPSPAPSSPDPFPPSLFCDRSVPPRKALDSFPERLLDCTAASARDPFPLGFFNDGREPPRQIFDLPERPLIGTVASRESLSSSVNNGPEHPMETGDLFSQSHCPDRANSLNDLESAASCETAVSDNSISKPTKPSPHGSSCKKYKGKQKKVGTLKLGEDSEVFDGPVPVPLQPSLEDVEGQLFVSFMSKKALRIHLGDDDDDKPETAQENTDNPDGNNEEKIEKKIEGLEKVLLHDLKFMKNRQVIHPVLQEVGLKLNLLDVTLEIDLQYLGVQLPIPPPALSPEETSSQAQFVSRTGKTSDFTQIKGWRDKFAPSASLSEGVSSTDAGQSNLSAFCSDMLDEYLASEGKLIDERAASLSQADCTPVAYQLPTKSTSYVRTLDSVLKKQVPAILTPTTNKVKPTFKSKVENKSKKPLKPGKGKQTKPVISDAEPLCTKKPQQNKKYKSRKEFKSPEKPDVAEVPASNTTPMAEDSGSTSSTCAGGRSPGLPKTLVKLLDVEDGAVWEGRHRSYITEERAAIALATLVTAEGASTGSADAIRIIRRRAPPCLNVFCRLGCVCASLVHLRRHHHCGKPQCMLGCSCLRRKVVALKTPKQEEGTADDSDPQGMSEENKAKWRKKNKMRKTYVLTDPELAPEPAKRVSTLWDRTRGNFDKEVLYCPPPPRSPQPQLLSQELQHDLESFLSPSKQKRVEERNLSTSEDNIEINLTCARSRPFHSNCHDKPKADDNKHHISQVSTPDIEEGELVPLNLSGPAKRLEMMSERTWTSIDMRNNVMRIVCEHMAQDRLNQPFWMGKYFIKPVSKTLEKEENGSVEIYKVIISQPVEKKTENEKITQKEEELEKHVKTSEVKGLPFLSKCCPAGLLKAEKKSPDAPGQIMVNGKHYPQAKLELGHMGALHPANRLAAYITGRICPTVSAITKPPVTTVPSSTLTTVSKVTCTPASTTTSVSKSLGGSTLTTTTSASSPGLTSPAKKTVYITVASRNTGLSNSGTQIKKIVSPTGPPQTSGQKMLLQVVKTADGNTLYRNPNGQLMQLVPLSQIKALKPNLLSQGQPTIIRLPAPPTVSMNKPQGGSATIVTSSIPTTQTLAKPSGTVPVSTSSSMGGKLISPPSSKSVSLSSLPSTLKVVQGFLGQSGTCTLRILPPTTSTSSTVLSQSGLTLLKSASSMPPTQDSSNSETNVSFSSQSTEKTVVQVLKQSTIDPAKQNSSDNANVKEKHFNKAPDPEEKEIGSDSTELTDDSDLYSDDDQEDASCMSASDREEKIEDTDGMDSEKKGYAEMVVDIETIEESAEQNRIAKFRASALRRNQYRRNQKRIHDEMLEVRVQKVRKERKRRQTLXECFIKLQGTLGMSSKKFEVSRMRILTKANKEVEYLVKLEDYLVEKKAKLQFKKERYIQTLSQLCDKSTESIGLKLNEIISKQKALEAQSKTKETHPKPIQAKSKAKPKPKSKPKSKVVDVCDKPKGLAVQNKVNDVSKVTYSPSKPIDLSIKKQKSPEMTESVPKSTPSVSVPADLDGNKNTLNVLDTNTVTTTSTPIQPSFNSTLVMKPVSIPSPIKHPPITRERMRPNILSRASSQAMQGSPVKESLLTNVCIPQVLPLMNTMVPCNPIITINNSLQPIGITSVGQQSSTPGVASVSIVPTISHPLRVENTLPMLHPQFIKITNSPVNINTKVDSASLPNISNVISLAENLVVPRKVVEDKPVFQAQPTSVDNQQNSSNDKIPDLEQKTDEAPSTNVPKQSVVEDQKGASVPKSNPEVPENKSPDDSDDPEDENLLSLLDELVLLSQQLTNEDEDERIAVPGDVQSCSDKPEDQEPADDRALSPLFLTLDEDLMSPDSKDEIDIPPKVDDLVKVIFGSDSPSVSSESGVAQSTNASSPHASTCNATGDGLTPPPLLHMKAAYEAASRQSANEGTSVTWRPMPKLVPLGLKAQDAGKVINPSIPNLDSSEQDTPQM
Protein: Glypican-5 [Cleaved into: Secreted glypican-5] (Q8CAL5)
Organism: Mus musculus (Mouse)
Function: Cell surface proteoglycan that bears heparan sulfate.
Subcellular location: Cell membrane {ECO:0000250}; Lipid-anchor, GPI-anchor {ECO:0000250}; Extracellular side {ECO:0000250}.; SUBCELLULAR LOCATION: [Secreted glypican-5]: Secreted, extracellular space {ECO:0000250}.
Interaction partners:
- Sonic hedgehog protein
- Syndecan-3
- Hepatic sodium/bile acid cotransporter
Sequence:
MDARTWRLGWRCLLLLALLGSTRSEGVESCEEVRKLFQWRLGGAVKGLPEAPRAGPDLQVCLSKNPTCCTRKMEERYQIAARQDLQQVLQTSSSTLKLLISRNAAAFQETLETLIRQAENYTSILFCNTYRNMALEAAASIQEFFTDVGLYLFGADVNPEEFVNRFFDSLFPLVYNHLINPGVTDSSLQYSECIRMARQDVSPFGNIPKRVMGQMGRSLLPGRTFLQALNLGIEVINTTDHIHFSKECSRALLKMQYCPHCQSLMLSKPCMGYCLNVIRGCLAHMTELNPHWHAYIRSLEELSDAMHGTYDVEHVLLNFHLLVNDAVLQAHLNGQKLLDQVNTICGHPVRTPTQSPRCTFDPSKEKHGMKISARNGEETLANRRKEFINSLRLHGSFYGGLADQLCVNELAAPEGRPCWNGEEIVKSYAQRVVGNGIKAQSANPEVRVRGTDPVVNQIIDKLKHVIQLLRGRSPKPNKWELLQPGSGGGMLENSSGDCDDEDGCGGSGSGEVKRTLKITNWMPDSMNFSDVKQVHRADHGSTLDTTSTGCASGTESMALPLMGTLMFLPWLW
Protein: Sulfide-quinone reductase (SQR) (EC 1.8.5.4) (Sulfide:quinone oxidoreductase) (O67931)
Organism: Aquifex aeolicus (strain VF5)
Function: Catalyzes the oxidation of hydrogen sulfide, with the help of a quinone. Consecutive reaction cycles lead to the accumulation of a polysulfide product on the active site Cys residues; these products are released when they exceed a critical length, typically as cyclooctasulfur.
Subcellular location: Membrane {ECO:0000269|PubMed:10816041, ECO:0000269|PubMed:19487671}; Peripheral membrane protein {ECO:0000269|PubMed:10816041, ECO:0000269|PubMed:19487671}.
Interaction partners:
- FAD/NAD
- Sulfur oxygenase reductase
- HupD hydrogenase related function
- Cytochrome c
Sequence:
MAKHVVVIGGGVGGIATAYNLRNLMPDLKITLISDRPYFGFTPAFPHLAMGWRKFEDISVPLAPLLPKFNIEFINEKAESIDPDANTVTTQSGKKIEYDYLVIATGPKLVFGAEGQEENSTSICTAEHALETQKKLQELYANPGPVVIGAIPGVSCFGPAYEFALMLHYELKKRGIRYKVPMTFITSEPYLGHFGVGGIGASKRLVEDLFAERNIDWIANVAVKAIEPDKVIYEDLNGNTHEVPAKFTMFMPSFQGPEVVASAGDKVANPANKMVIVNRCFQNPTYKNIFGVGVVTAIPPIEKTPIPTGVPKTGMMIEQMAMAVAHNIVNDIRNNPDKYAPRLSAICIADFGEDAGFFFADPVIPPRERVITKMGKWAHYFKTAFEKYFLWKVRNGNIAPSFEEKVLEIFLKVHPIELCKDCEGAPGSRC
Protein: interstitial collagenase (EC 3.4.24.7) (B5X4P7)
Organism: Salmo salar (Atlantic salmon)
Subcellular location: Secreted, extracellular space, extracellular matrix {ECO:0000256|ARBA:ARBA00004498}.
Interaction partners:
- Matrix metalloproteinase-9
- Metalloproteinase inhibitor 2
Sequence:
MKTFNLCLLLINLAIVVYSLPISPPSKEDEALAETYLKRFFNLTEETGPAFKRGPSQRSRKVSEMQSFFGLQVTGTLDAETVTMMKKPRCGVPDVQVSRFTTFDNRKWQTNRVTYRIENYTPDMSVAEVDNSIERALQVWAKVSPLRFTRIYSGIADIMISFGTRNHGDSYPFDGPDGTLAHAFSPGADIGGDAHFDDDESFSFSSTRGYNLFLVAAHEFGHSLGLSHSTDPGALMFPVYSYTNPSTFSLPRDDVNGIQYIYGPNTDVNPNPDKPDPTPPSTPNACDPTLVLDAVTTLRGEKMFFKGRFFWRIHSQSSKPEQNLIKNYWPELPDNINAAYESQLSDRVFLFKDSQVWALYGYDIVPGYPRNLNSLGLPSTVKKVDAALYDVDSRKTLFFVDDKYYSYDEEMKRMDKGFPKRVDEGFPGMTGKVTAAFQVRGFTYLYSGSFMFEYSMRTRRQLRVLGNSYFLPC
Protein: Ecdysone 20-monooxygenase (E20MO) (EC 1.14.99.22) (CYPCCCXIVA1) (Cytochrome P450 314a1, mitochondrial) (Protein shade) (Q9VUF8)
Organism: Drosophila melanogaster (Fruit fly)
Function: Required for CNS development; midline glial cells. Involved in the metabolism of insect hormones; responsible for all ecdysone 20-monooxygenase activity during embryonic, larval and adult stages. May be involved in the breakdown of synthetic insecticides.
Subcellular location: Mitochondrion membrane {ECO:0000269|PubMed:14610274}.
Interaction partners:
- Ecdysone oxidase
- Cytochrome P450 18a1
- Cytochrome P450 315a1, mitochondrial
- Cholesterol 7-desaturase nvd
- Probable cytochrome P450 6t3
- Short-chain dehydrogenase/reductase)
- Probable cytochrome P450 303a1
- Cytochrome P450 6g1
- Ecdysone receptor
- Probable cytochrome P450 305a1
Sequence:
MAVILLLALALVLGCYCALHRHKLADIYLRPLLKNTLLEDFYHAELIQPEAPKRRRRGIWDIPGPKRIPFLGTKWIFLLFFRRYKMTKLHEVYADLNRQYGDIVLEVMPSNVPIVHLYNRDDLEKVLKYPSKYPFRPPTEIIVMYRQSRPDRYASVGIVNEQGPMWQRLRSSLTSSITSPRVLQNFLPALNAVCDDFIELLRARRDPDTLVVPNFEELANLMGLEAVCTLMLGRRMGFLAIDTKQPQKISQLAAAVKQLFISQRDSYYGLGLWKYFPTKTYRDFARAEDLIYDVISEIIDHELEELKKSAACEDDEAAGLRSIFLNILELKDLDIRDKKSAIIDFIAAGIETLANTLLFVLSSVTGDPGAMPRILSEFCEYRDTNILQDALTNATYTKACIQESYRLRPTAFCLARILEEDMELSGYSLNAGTVVLCQNMIACHKDSNFQGAKQFTPERWIDPATENFTVNVDNASIVVPFGVGRRSCPGKRFVEMEVVLLLAKMVLAFDVSFVKPLETEFEFLLAPKTPLSLRLSDRVF
Protein: Phytanoyl-CoA hydroxylase-interacting protein (Phytanoyl-CoA hydroxylase-associated protein 1) (PAHX-AP1) (PAHXAP1) (Q8K0S0)
Organism: Mus musculus (Mouse)
Function: Its interaction with PHYH suggests a role in the development of the central system.
Interaction partners:
- Phytanoyl-CoA dioxygenase, peroxisomal
Sequence:
MELLSTPHSIEINNITCDSFRISWAMEDSDLERVTHYFIDLNKKENKNSNKFKHRDVPTKLVAKAVPLPMTVRGHWFLSPRTEYSVAVQTAVKQSDGEYLVSGWSETVEFCTGDYAKEHLAQLQEKAEQIAGRMLRFSVFYRNHHKEYFQHARTHCGNVLQPYLKDNSGSHGSPTSGMLHGVFFSCNTEFNTGQPPQDSPYGRWRFQIPAQRLFNPSTNLYFADFYCMYTAYHYAILVLAPKGSLGDRFCRDRLPLLDIACNKFLTCSVEDGELIFRHAQDLILEIIYTEPVDLSLGTLGEISGHQLMSLSTADAKKDPSCKTCNISVGR
Protein: Small proline-rich protein 3 (22 kDa pancornulin) (Cornifin beta) (Esophagin) (Q9UBC9)
Organism: Homo sapiens (Human)
Function: Cross-linked envelope protein of keratinocytes.
Subcellular location: Cytoplasm.
Interaction partners:
- Involucrin
- Loricrin
- Small proline-rich protein 2A
- Cornifin-A
- Cornifin-B
- Trichohyalin
- Late cornified envelope protein 3D
- Small proline-rich protein 2D
- Small proline-rich protein 2E
- Small proline-rich protein 2G
Sequence:
MSSYQQKQTFTPPPQLQQQQVKQPSQPPPQEIFVPTTKEPCHSKVPQPGNTKIPEPGCTKVPEPGCTKVPEPGCTKVPEPGCTKVPEPGCTKVPEPGCTKVPEPGYTKVPEPGSIKVPDQGFIKFPEPGAIKVPEQGYTKVPVPGYTKLPEPCPSTVTPGPAQQKTKQK
Protein: Carbonic anhydrase Xa (Q3B739)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
Sequence:
MNIIWEIFIILQANLIVCSSAQPNPPKIHEGWWAYKEVVQGSFVPVPSFWGLVNSAWNLCSVGKRQSPVNIETSHMIFDPFLTPLRLNTGGRKVGGTMYNTGRHVSLRLDKEHLVNISGGPMTYSHRLEEIRLHFGSEDGQGSEHLLNGQAFSGEVQLIHYNHELYTNYTEAAKSPNGLVIVSIFMKISETSNSFLNRMLNRDTITRITYKNDAYLLSGLNIEEVYPETASFITYEGSMTIPPCYETATWILMNKPIYVTKMQMHSMRLLSQNQPSQIFLSMSDNVRPVQPLNNRCIRTNINFSMQGKDCPNNRAQKLQYRVNEWLLK
Protein: Protocadherin gamma B6 (Q8K4A0)
Organism: Mus musculus (Mouse)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004167}; Single-pass membrane protein {ECO:0000256|ARBA:ARBA00004167}.
Interaction partners:
Sequence:
VAVGTRIPLEPATDPDINLNSVKDYQISSNPYFSLMVRVNPDGGKTPELSLEKLLDREEQRSHRLILTALDGGDPPRSATTQIEISVKDNNDNPPVFSKEEYWVSVSENLSPGSSVLQVTATDEDEGVNAEILYYFRSTAQSTRHVFSL
Protein: Serine/threonine-protein kinase STY17 (EC 2.7.11.1) (Serine/threonine/tyrosine-protein kinase 17) (Q8RWL6)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Serine/threonine protein kinase that specifically phosphorylates chloroplast precursor proteins in the cytosol within the cleavable presequences (transit peptides). May be part of a cytosolic regulatory network involved in chloroplast protein import. Does not phosphorylate mitochondrion precursor proteins. Specific for ATP and does not utilize other NTPs. Plays a role in chloroplast biogenesis and differentiation in cotyledons, possibly through phosphorylation of chloroplast preproteins.
Subcellular location: Cytoplasm, cytosol {ECO:0000269|PubMed:21799034}.
Interaction partners:
- AT4g30010/F6G3_40
Sequence:
MAIKEETEESCGSRAVVASITKESPRQHRMKLEVYGEVLQRIQESNYEEANFPGFDDLLWLHFNRLPARYALDVNVERAEDVLTHQRLLKLAEDPATRPVFEVRCVQVSPTLNGNSGDVDPSDPAVNEDAQSSYNSRSLAPPTFGSSPNFEALTQAYKDHAQDDDSAVNAQLPNSRPMHEITFSTIDRPKLLSQLTSMLGELGLNIQEAHAFSTADGFSLDVFVVDGWSQEETEGLKDALKKEIRKFKDQPCSKQKSITFFEHDKSTNELLPACVEIPTDGTDEWEIDMKQLKIEKKVACGSYGELFRGTYCSQEVAIKILKPERVNAEMLREFSQEVYIMRKVRHKNVVQFIGACTRSPNLCIVTEFMTRGSIYDFLHKHKGVFKIQSLLKVALDVSKGMNYLHQNNIIHRDLKTANLLMDEHEVVKVADFGVARVQTESGVMTAETGTYRWMAPEVIEHKPYDHRADVFSYAIVLWELLTGELPYSYLTPLQAAVGVVQKGLRPKIPKETHPKLTELLEKCWQQDPALRPNFAEIIEMLNQLIREVGDDERHKDKHGGYFSGLKKGHR
Protein: Cytochrome P450 86A1 (EC 1.14.14.80) (CYPLXXXVI) (P450-dependent fatty acid omega-hydroxylase) (Protein HYDROXYLASE OF ROOT SUBERIZED TISSUE) (P48422)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Catalyzes the omega-hydroxylation of various fatty acids (FA). Acts on saturated and unsaturated fatty acids with chain lengths from C12 to C18 but not on hexadecane.
Subcellular location: Membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}.
Interaction partners:
- Glycerol-3-phosphate acyltransferase 5
- Peptidyl-prolyl cis-trans isomerase CYP71
- Aldehyde dehydrogenase family 3 member F1
- Protein HOTHEAD
- Cytochrome P450 704B1
- Probable peroxygenase 3
- Probable peroxygenase 7
- Aldehyde dehydrogenase family 3 member I1, chloroplastic
- Aldehyde dehydrogenase family 2 member B7, mitochondrial
- Aldehyde dehydrogenase family 3 member H1
Sequence:
MEALNSILTGYAVAALSVYALWFYFLSRRLTGPKVLPFVGSLPYLIANRSRIHDWIADNLRATGGTYQTCTMVIPFVAKAQGFYTVTCHPKNVEHILKTRFDNYPKGPMWRAAFHDLLGQGIFNSDGDTWLMQRKTAALEFTTRTLRQAMARWVNGTIKNRLWLILDRAVQNNKPVDLQDLFLRLTFDNICGLTFGKDPETLSLDLPDNPFSVAFDTATEATLKRLLYTGFLWRIQKAMGIGSEDKLKKSLEVVETYMNDAIDARKNSPSDDLLSRFLKKRDVNGNVLPTDVLQRIALNFVLAGRDTSSVALSWFFWLVMNNREVETKIVNELSMVLKETRGNDQEKWTEEPLEFDEADRLVYLKAALAETLRLYPSVPQDFKYVVDDDVLPDGTFVPRGSTVTYSIYSIGRMKTIWGEDCLEFRPERWLTADGERFETPKDGYKFVAFNAGPRTCLGKDLAYNQMKSVASAVLLRYRVFPVPGHRVEQKMSLTLFMKNGLRVYLQPRGEVLA
Protein: Mitochondrial glycoprotein family protein (A0A178W169)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Probable diphthine methyl ester synthase
- At4g27620
- At4g12840
- Pentatricopeptide repeat
- Uncharacterized protein At1g27050
- BRISC and BRCA1-A complex member 1
- RNA-binding
- MIF4G domain-containing protein
- F-box protein At1g70590
- Alpha/beta-Hydrolases superfamily protein
Sequence:
MARFVRCLRRTLFSNSSPSIAHRSPRIGLPTNLNPKILISRRCLSSGSYVSEMQKSAFQGNILRLIRNEIEYELDHSPPLQPPNSFGPFTVDERPGEQWISLKRNFGDKEDIKIEATMFDRSVPTSKSTKTEPEYILHITFIVNISKAGATEALEIMCSAWPDTIEISKLCIRRGINTSPSSYGGPEFEELDDQLQDALYQFLEERGISDELAVFLHRYMKNKGKAEYVRWMESVKSYVEQK
Protein: LPS-assembly lipoprotein LptE (Rare lipoprotein B) (P0ADC1)
Organism: Escherichia coli (strain K12)
Function: Together with LptD, is involved in the assembly of lipopolysaccharide (LPS) at the surface of the outer membrane. Required for the proper assembly of LptD. Binds LPS and may serve as the LPS recognition site at the outer membrane.
Subcellular location: Cell outer membrane {ECO:0000255|HAMAP-Rule:MF_01186, ECO:0000269|PubMed:20446753, ECO:0000269|PubMed:21257904, ECO:0000269|PubMed:3316191}; Lipid-anchor {ECO:0000255|HAMAP-Rule:MF_01186, ECO:0000269|PubMed:20446753, ECO:0000269|PubMed:21257904, ECO:0000269|PubMed:3316191}. Note=A substantial portion is found inside the LptD beta-barrel.
Interaction partners:
- LPS-assembly protein LptD
- Lipopolysaccharide export system protein LptC
- Lipopolysaccharide export system ATP-binding protein LptB
- Lipopolysaccharide export system permease protein LptG
- Lipopolysaccharide export system protein LptA
- Lipopolysaccharide export system permease protein LptF
- DNA polymerase III subunit delta
- Leucine--tRNA ligase
- Nicotinate-nucleotide adenylyltransferase
- Adenosylcobalamin/alpha-ribazole phosphatase
Sequence:
MRYLATLLLSLAVLITAGCGWHLRDTTQVPSTMKVMILDSGDPNGPLSRAVRNQLRLNGVELLDKETTRKDVPSLRLGKVSIAKDTASVFRNGQTAEYQMIMTVNATVLIPGRDIYPISAKVFRSFFDNPQMALAKDNEQDMIVKEMYDRAAEQLIRKLPSIRAADIRSDEEQTSTTTDTPATPARVSTTLGN