wanglab/gogpt-training-data huggingface dataset:
Protein: Clusterin-associated protein 1 (Qilin) (Q96AJ1)
Organism: Homo sapiens (Human)
Function: Required for cilia biogenesis. Appears to function within the multiple intraflagellar transport complex B (IFT-B). Key regulator of hedgehog signaling.
Subcellular location: Cell projection, cilium {ECO:0000269|PubMed:15530380}. Nucleus {ECO:0000269|PubMed:15480429}.
Interaction partners:
- Intraflagellar transport protein 80 homolog
- Intraflagellar transport protein 88 homolog
- Intraflagellar transport protein 57 homolog
- TRAF3-interacting protein 1
- Intraflagellar transport protein 52 homolog
- Intraflagellar transport protein 172 homolog
- Intraflagellar transport protein 20 homolog
- Intraflagellar transport protein 46 homolog
- Intraflagellar transport protein 56
- Intraflagellar transport protein 27 homolog
Sequence:
MSFRDLRNFTEMMRALGYPRHISMENFRTPNFGLVSEVLLWLVKRYEPQTDIPPDVDTEQDRVFFIKAIAQFMATKAHIKLNTKKLYQADGYAVKELLKITSVLYNAMKTKGMEGSEIVEEDVNKFKFDLGSKIADLKAARQLASEITSKGASLYDLLGMEVELREMRTEAIARPLEINETEKVMRIAIKEILTQVQKTKDLLNNVASDEANLEAKIEKRKLELERNRKRLETLQSVRPCFMDEYEKTEEELQKQYDTYLEKFQNLTYLEQQLEDHHRMEQERFEEAKNTLCLIQNKLKEEEKRLLKSGSNDDSDIDIQEDDESDSELEERRLPKPQTAMEMLMQGRPGKRIVGTMQGGDSDDNEDSEESEIDMEDDDDEDDDLEDESISLSPTKPNRRVRKSEPLDESDNDF
Protein: Cytokinin hydroxylase (EC 1.14.13.-) (Cytochrome P450 35A2) (Q9ZW95)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Cytokinin hydroxylase that catalyzes the biosynthesis of trans-zeatin via the isopentenyladenine riboside 5'-monophosphate (iPRMP)-dependent pathway. Can use isopentenyladenosine-5'-monophosphate, isopentenyladenosine-5'-diphosphate and isopentenyladenosine-5'-triphosphate as substrate.
Subcellular location: Membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}.
Interaction partners:
- Adenylate isopentenyltransferase 3, chloroplastic
- Adenylate isopentenyltransferase 5, chloroplastic
- Adenylate isopentenyltransferase 4
- Adenylate isopentenyltransferase 1, chloroplastic
- Adenylate isopentenyltransferase 7, mitochondrial
- Adenylate isopentenyltransferase 6, chloroplastic
- Adenylate isopentenyltransferase 8, chloroplastic
- Cytokinin hydroxylase
- ABC transporter G family member 14
- Cytokinin dehydrogenase 5
Sequence:
MMVTLVLKYVLVIVMTLILRVLYDSICCYFLTPRRIKKFMERQGITGPKPRLLTGNIIDISKMLSHSASNDCSSIHHNIVPRLLPHYVSWSKQYGKRFIMWNGTEPRLCLTETEMIKELLTKHNPVTGKSWLQQQGTKGFIGRGLLMANGEAWHHQRHMAAPAFTRDRLKGYAKHMVECTKMMAERLRKEVGEEVEIGEEMRRLTADIISRTEFGSSCDKGKELFSLLTVLQRLCAQATRHLCFPGSRFLPSKYNREIKSLKTEVERLLMEIIDSRKDSVEIGRSSSYGDDLLGLLLNQMDSNKNNLNVQMIMDECKTFFFTGHETTSLLLTWTLMLLAHNPTWQDNVRDEVRQVCGQDGVPSVEQLSSLTSLNKVINESLRLYPPATLLPRMAFEDIKLGDLIIPKGLSIWIPVLAIHHSNELWGEDANEFNPERFTTRSFASSRHFMPFAAGPRNCIGQTFAMMEAKIILAMLVSKFSFAISENYRHAPIVVLTIKPKYGVQLVLKPLDL
Protein: NADPH-dependent oxidoreductase 2-alkenal reductase (AtAER) (EC 1.3.1.-) (EC 1.3.1.74) (NADP-dependent alkenal double bond reductase P1) (DBR1) (NADPH-azodicarbonyl/quinone reductase) (NADPH:2-alkenal/one alpha,beta-hydrogenase) (ALH) (P1-zeta-crystallin protein) (P1-ZCr) (Q39172)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Involved in the detoxification of reactive carbonyls. Acts on lipid peroxide-derived reactive aldehydes. Specific to a double bond activated by an adjacent carbonyl group. Can use both quinones and diamide as substrates, but not menadione, ferricyanide or phylloquinone. Can use 4-hydroxy-(2E)-nonenal (HNE), 4-hydroxy-(2E)-hexenal (HHE), (2E)-nonenal, (2E)-hexenal, (2E)-pentenal, propenal (acrolein), 3-buten-2-one and 3-penten-2-one, but not (R)-(-)-carvone, n-nonanal, n-hexanal, (3Z)-hexanal, cyclohex-2-en-1-one or 12-oxo phytodienoic acid (OPDA) as electron acceptors. Catalyzes the reduction of the alpha,beta-unsaturated bond of 2-alkenals, of lipid peroxide-derived oxenes 9-oxo-10(E),12(Z)-octadecadienoic acid (9-KODE) and 13-oxo-9(Z),11(E)-octadecadienoic acid (13-KODE), as well as 4-oxo-(2E)-nonenal and 4-hydroxynonenal. Can use 12-oxo-10(E) dodecanoate (traumatin), trans-1,3 diphenyl-2-propenone, trans-1,4-diphenyl-2-butene-1,4-dione, 9-oxo-12,13-epoxy-(10E)-octadecenoic acid (trans-EKODE-1b) and 9,13-dihydroxy-10-oxo-11-octadecenoic acid as substrates. Catalyzes the reduction of the 7-8 double bond of phenylpropanal substrates, such as p-coumaryl aldehyde and coniferyl aldehyde (in vitro). Has activity towards toxic substrates, such as 4-hydroxy-(2E)-nonenal (in vitro). May play a distinct role in plant antioxidant defense and is possibly involved in NAD(P)/NAD(P)H homeostasis.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16299173}. Nucleus, nucleoplasm {ECO:0000269|PubMed:16299173}.
Interaction partners:
- NADPH-dependent alkenal/one oxidoreductase, chloroplastic
Sequence:
MTATNKQVILKDYVSGFPTESDFDFTTTTVELRVPEGTNSVLVKNLYLSCDPYMRIRMGKPDPSTAALAQAYTPGQPIQGYGVSRIIESGHPDYKKGDLLWGIVAWEEYSVITPMTHAHFKIQHTDVPLSYYTGLLGMPGMTAYAGFYEVCSPKEGETVYVSAASGAVGQLVGQLAKMMGCYVVGSAGSKEKVDLLKTKFGFDDAFNYKEESDLTAALKRCFPNGIDIYFENVGGKMLDAVLVNMNMHGRIAVCGMISQYNLENQEGVHNLSNIIYKRIRIQGFVVSDFYDKYSKFLEFVLPHIREGKITYVEDVADGLEKAPEALVGLFHGKNVGKQVVVVARE
Protein: Anaphase-promoting complex subunit 16 (Cyclosome subunit 16) (C5H3H2)
Organism: Homo sapiens (Human)
Subcellular location: Chromosome, centromere, kinetochore {ECO:0000256|ARBA:ARBA00004629}. Cytoplasm {ECO:0000256|ARBA:ARBA00004496}. Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MAASSSSSSAGGVSGSSVTGSGFSVSDLAPPRKALFTYPKGAGEMLEDGSERFLCESVFSYQVASTLKQVKHDQQVARMEKLAGLVEELEADEWRFKPIEQLLGFTPSSG
Protein: Exonuclease, putative (Q57YZ1)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- Endo/exonuclease Mre11
- Mismatch repair protein MLH1
- DNA mismatch repair protein, putative
- BRCT domain-containing protein
- Mismatch repair protein MSH8, putative
- Proliferating cell nuclear antigen
- Mismatch repair protein PMS1, putative
- Protein artemis
- DNA 3'-5' helicase
- DNA 3'-5' helicase
Sequence:
MGIKGLWGEVKPVCRDAHLEKFRGSRVGVDMYVWLHRAVSGSVDLSTEANVEMLRAHVESLSDPSVTVSAHPIPLNTKFLHWVMSQVELLLRYGVKPVLVFDGRELPMKREEEEERRRNRIKHLSEALDLLRRNSRPTPSERKDIAGLVERGMDITTELAHAVIMMLQERQLECIVAPYEADAQLAYLCQQRYVDAVITEDSDLLVYWCPRLIAKLDHKGSCQVIEVESVLHCPLFKGLSYNSFLVGCILSGCDYLPNLRHIGVKKAFGIMSEARSVPDVIRLLEENYGFPREQLRKYEAGLQRAIYCFLHHIVFDPVKRALVTRTPLPNGVAFKQSILGELVGDDLAQSMCCQCLYDPTTRSLYKGIYQYCLDNYRKTSRAGQSTLTAFNGFKELRSPRMTLRLASSNSQASATSVSNTPLTPPTKTFFSAPLEKVREAEGYCGPKVVRSKYFVNGQWKVDNWEESSSQGGDSNTKNGNGDDSQSPSGAVTDECDAAGGVRSDGGKCCVKSEPPTPPDRVSCATLSCKASSVCQVAGASDSATADADRAVDPSHGEFRGTELTCSDVCGLTEVPCSNVEGSASALLQECGADAPNDPVGADRASVQDVNEGAEMLCPFGYIQCRRKHSLFEQCFVGKGWTKKANNPNDQNNGSGAQVVPQGDTDGDGGTSPWRTRGSAKRRWSEIESVQPSQSPPLVSSSSSFLHSIASTTASPLTVREANDAKTGGSCGGSVSVPCRMQSNSPKTLTEQCANGLATEDASDEGVNADFSASTSQSSVAAAPKAAALFELLSYTRR
Protein: Dehydrogenase/reductase SDR family member 9 (EC 1.1.1.209) (EC 1.1.1.53) (3-alpha hydroxysteroid dehydrogenase) (3-alpha-HSD) (Retinol dehydrogenase) (EC 1.1.1.105) (Short-chain dehydrogenase/reductase retSDR8) (Q8VD48)
Organism: Rattus norvegicus (Rat)
Function: 3-alpha-hydroxysteroid dehydrogenase that converts 3-alpha-tetrahydroprogesterone (allopregnanolone) to dihydroxyprogesterone and 3-alpha-androstanediol to dihydroxyprogesterone (By similarity). Plays also role in the biosynthesis of retinoic acid from retinaldehyde. Can utilize both NADH and NADPH (By similarity).
Subcellular location: Microsome membrane {ECO:0000250|UniProtKB:Q9BPW9}. Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q9BPW9}.
Interaction partners:
- Retinaldehyde dehydrogenase 3
- Lecithin retinol acyltransferase
- Cytochrome P450 26A1
- Aldehyde dehydrogenase 1A1
- Retinal dehydrogenase 2
- Dehydrogenase/reductase SDR family member 4
- Dehydrogenase/reductase
- Diacylglycerol O-acyltransferase 1
- Beta,beta-carotene 15,15'-dioxygenase
- Aldehyde oxidase 1
Sequence:
MLLWVLALLFLCAFLWNYKGQLKIADIADKYIFITGCDSGFGNLAARTFDRKGFRVIAACLTESGSEALKAKTSERLHTVLLDVTNPENVKETAQWVKSHVGEKGLWGLINNAGVLGVLAPTDWLTVDDYREPIEVNLFGLINVTLNMLPLVKKARGRVINVSSIGGRLAFGGGGYTPSKYAVEGFNDSLRRDMKAFGVHVSCIEPGLFKTGLADPIKTTEKKLAIWKHLSPDIKQQYGEGYIEKSLHRLKSSTSSVNLDLSLVVECMDHALTSLFPKTRYTAGKDAKTFWIPLSHMPAALQDFLLLKEKVELANPQAV
Protein: F-box protein At3g07870 (Q9SFC7)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- F-box protein At2g14290
- Dirigent protein 22
- Probable thimet oligopeptidase
- Methylenetetrahydrofolate reductase 1
- Sulfite exporter TauE/SafE family protein 3
Sequence:
MASEKSFKKRKITDDVDGVGVGGGLESLPEDIIADIFSRLPISSIARLMFVCRSWRSVLTQHGRLSSSSSSPTKPCLLLHCDSPIRNGLHFLDLSEEEKRIKTKKFTLRFASSMPEFDVVGSCNGLLCLSDSLYNDSLYLYNPFTTNSLELPECSNKYHDQELVFGFGFHEMTKEYKVLKIVYFRGSSSNNNGIYRGRGRIQYKQSEVQILTLSSKTTDQSLSWRSLGKAPYKFVKRSSEALVNGRLHFVTRPRRHVPDRKFVSFDLEDEEFKEIPKPDCGGLNRTNHRLVNLKGCLCAVVYGNYGKLDIWVMKTYGVKESWGKEYSIGTYLPKGLKQNLDRPMWIWKNAENGKVVRVLCLLENGEILLEYKSRVLVAYDPKLGKFKDLLFHGLPNWFHTVVHAGTLSWFDTPLDLW
Protein: Protochlorophyllide-dependent translocon component 52, chloroplastic (EC 1.14.15.-) (ACD1-like protein) (Protein TIC 55-IV) (Translocon at the inner envelope membrane of chloroplasts 55-IV) (Q8W496)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Part of a translocon most abundantly expressed in etiolated plants and involved in the protochlorophyllide-dependent import of the precursor NADPH:protochlorophyllide oxidoreductase A (pPORA).
Subcellular location: Plastid, chloroplast inner membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
- Rieske
- Short-chain dehydrogenase TIC 32, chloroplastic
- Protein TIC 62, chloroplastic
- Choline monooxygenase, chloroplastic
- Splicing factor SF3a60 homolog
- Protein TIC110, chloroplastic
- Protein TIC 22, chloroplastic
- IQ-domain 21
- Translocase of chloroplast 120, chloroplastic
- Ferredoxin C 1, chloroplastic
Sequence:
MEAALAACALPSLRILNTKPRFRCSFSNPSLPISPNSLITRKSSRFTTAVSSPPSSSAATSTNSPPEPEALFEPGSDKFDWYANWYPVMPICDLDKKVPHGKKVMGIDLVVWWDRNEKQWKVMDDTCPHRLAPLSDGRIDQWGRLQCVYHGWCFNGSGDCKLIPQAPPDGPPVHTFKQACVAVYPSTVQHEIIWFWPNSDPKYKNIIETNKPPYIPELEDPSFTKLMGNRDIPYGYDVLVENLMDPAHVPYAHYGLMRFPKPKGKYIICISNSCFNPFTNLQILLAEKIDREGGKPLEINVKKLDNKGFFSKQEWGYSNFIAPCVYRSSTDPLPEQEHEYPAPAASDKAALSKRRLSLIFICIPVSPGRSRLIWTFPRNFGVFIDKIVPRWVFHIGQNTILDSDLHLLHVEERKILERGPENWQKACFIPTKSDANVVTFRRWFNKYSEARVDWRGKFDPFLLPPTPPREQLFDRYWSHVENCSSCKKAHKYLNALEVILQIASVAMIGVMAVLKQTTMSNVARIAVLVAAVLSFAASKWLSHFIYKTFHYHDYNHAVV
Protein: Uncharacterized protein YfjW (P52138)
Organism: Escherichia coli (strain K12)
Subcellular location: Cell membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
Sequence:
MAFVSEREIVRKIFSKKIDFTILAFFYISSIFFLLCSGVLFQYFTAAFTKGNCYECSMKLDYIKQFYFSLETAWYLISAVAVFIASVFIQHRIKAYLTLLAITWIVLTITDVALIHALDNIAMNNILLNILYNLFGAILLSLFMCLSNSLLFHLNKIKHIPMILSAMIPLVSAIIIAILITAVIYLLFARQAVEIEMDISEGSDIAYVGVKDNEESFGFLNDKKTDTPTYLDVIKNGSLIYNDTQGLSGADIYIVSGCYALPDLLRNVPLDAKKSFLNVKKLEITQKLPMMGFIQGESADVMPKAASRLSLSKQDDKFMLASSVTDSQIKFKSNNAQLMVAFAFMPITTNGILHDYTYDIIINDKKYKIENHVAPLSRLDKNKKMKCEYQQISDLTNTYNINANYLTGFLLVLKPDDIINYNNSPSVLLKTDFAFYKKTYQKLDKIYDDISNGKLSSLRATGISQFSINGKHLSLRPESEIIISEGSLYGLVNKSKKIKIYGTADLVFVDNKIMNLRKITYLQSKLEIFGSSIMDILKYIFGLGLLAISIKFIHSYFKNDVNENLFL
Protein: Sec20p (A0A1D8PPX8)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Subcellular location: Endoplasmic reticulum membrane {ECO:0000256|ARBA:ARBA00004163}; Single-pass type IV membrane protein {ECO:0000256|ARBA:ARBA00004163}.
Interaction partners:
- SNAP receptor
- Tip20p
- Ufe1p
- Protein transport protein SEC22
- Dsl1p
- Sec39 domain-containing protein
- Vesicular-fusion protein SEC18
- Uncharacterized protein
- t-SNARE syntaxin
- V-SNARE protein
Sequence:
MSTVYYKKLDKLQFQIYDLFSSLLQLSETEDESVYKASFDDTVQEIDSLLIAFKDLLRLLRPKDKSNKFDTYELKFHSLKHKLRELQVFINDQQQDKLHEYRIKHFHLQDSPVDTINNEFARDQLFADRSTKKTKKETEASINQQIVSQNKQITKSLQASRQLLSAGILQSELNIDNIDQQTKDLYKLNEGFIQFNDLLNRSKKIVKFIEKQDKADRQRIYLSMGFFILCCSWVVYRRILRRPLKIFLWSFFKIFNIFNWLLGGGRSKGLSASDMIVSSVIAATTEIVDYEATKTLLDTLSHAVDSNTAIDTLAMVVESLTRSSMEHIVDEL
Protein: Alpha-galactosidase (EC 3.2.1.-) (Q21801)
Organism: Caenorhabditis elegans
Interaction partners:
- Beta-hexosaminidase A
- Glycosyltransferase family 92 protein R07B7.12
- Alpha-
- Alpha-
- beta-N-acetylhexosaminidase
- beta-N-acetylhexosaminidase
- Alpha-
- Galactokinase
- beta-N-acetylhexosaminidase
- Nuclear receptor
Sequence:
MRLLLPLLFCVGAFCLDNGLGRTPPMGWMSWTAFYCEIDCVKHPTGCINEQLYKDMADQLVSGGYDKVGYKSVHIDDCWSEMERDSHGILVANKTRFPSGMKALAKYMHDRGLKFGIYEDYGTKTCGGYPGSYKHEKVDAQTFAAWDVDYLKLDGCNIDQAMMPIGYPLFEKELNETGRPIMYSCSWPAYLIDHPELVNYNLIGKYCNTWRNFDDINSSWKSIISIISYYDKMQDKHIPTHGPGKWHDPDMLVIGNKGITLDMSISQFTVWCIWSAPLIMSNDLRIIGDSFKDVLKNKEAIKINQDPLGIMGRLIKNSTDIGVYVKQITPSKGDKKSFAFAYLNRNEKEGYKRIEIQLASIGLTDPAGYYVHDIWSHVDLGLLRSGDSIVVSIAPAGSVFFRADLASLHQPKGKRRYKFDNSNVVYEFEREQSQLGRFDFGDYLRTNRVQF
Protein: Fragile X mental retardation 1, isoform CRA_e (Fragile X messenger ribonucleoprotein 1) (G3V0J0)
Organism: Homo sapiens (Human)
Subcellular location: Cell projection, dendrite {ECO:0000256|ARBA:ARBA00004279}. Cell projection, dendritic spine {ECO:0000256|ARBA:ARBA00004552}. Cell projection, filopodium tip {ECO:0000256|ARBA:ARBA00004495}. Cell projection, growth cone {ECO:0000256|ARBA:ARBA00004624}. Chromosome, centromere {ECO:0000256|ARBA:ARBA00004584}. Cytoplasm, Stress granule {ECO:0000256|ARBA:ARBA00004210}. Cytoplasm, perinuclear region {ECO:0000256|ARBA:ARBA00004556}. Nucleus, nucleolus {ECO:0000256|ARBA:ARBA00004604}. Perikaryon {ECO:0000256|ARBA:ARBA00004484}. Presynaptic cell membrane {ECO:0000256|ARBA:ARBA00034111}. Synapse, synaptosome {ECO:0000256|ARBA:ARBA00034102}.
Interaction partners:
Sequence:
MEELVVEVRGSNGAFYKAFVKDVHEDSITVAFENNWQPDRQIPFHDVRFPPPVGYNKDINESDEVEVYSRANEKEPCCWWLAKVRMIKGEFYVIEYAACDATYNEIVTIERLRSVNPNKPATKDTFHKIKLDVPEDLRQMCAKEAAHKDFKKAVGAFSVTYDPENYQLVILSINEVTSKRAHMLIDMHFRSLRTKLSLIMRNEEASKQLESSRQLASRFHEQFIVREDLMGLAIGTHGANIQQARKVPGVTAIDLDEDTCTFHIYGEDQDAVKKARSFLEFAEDVIQVPRNLVVIGKNGKLIQEIVDKSGVVRVRIEAENEKNVPQEEEIMPPNSLPSNNSRVGPNAPEEKKHLDIKENSTHFSQPNSTKVQRGMVPFVFVGTKDSIANATVLLDYHLNYLKEVDQLRLERLQIDEQLRQIGASSRPPPNRTDKEKSYVTDDGQGMGRGSRPYRNRGHGRRGPGYTSGTNSEASNASETESDHRDELSDWSLAPTEEERESFLRRGDGRRRGGGGRGQGGRGRGGGFKGNDDHSRTDNRPRNPREAKGRTTDGSLQNTSSEGSRLRTGKDRNQKKEKPDSVDGQQPLVNGVP
Protein: HEAT repeat-containing protein 1 (Q96ES5)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus, nucleolus {ECO:0000256|ARBA:ARBA00004604, ECO:0000256|RuleBase:RU367065}.
Interaction partners:
Sequence:
MGSASQANIRLTSLKKTLATTLAPRVLLPAIKKTYKQIEKNWKNHMGPFMSILQEHIGAMKKEELTSHQSQLTAFFLEALDFRAQHSENDLEEVGKTENCIIDCLVAMVVKLSEVTFRPLFFKLFDWAKTEDAPKDRLLTFYNLADCIAEKLKGLFTLFAGHLVKPFADTLDQVNISKTDEAFFDSENDPEKCCLLLQFILNCLYKIFLFDTQHFISKERAGALMMPLVDQLENRLGGEEKFQERVTKHLIPCIAQFSVAMADDSLWKPLNYQILLKTRDSSPKVRFAALITVLALAEKLKENYIVLLPESIPFLAELMEDECEEVEHQCQKTIQQLETVLGEPLQSYF
Protein: Fbxw7 protein (Q0VGT7)
Organism: Mus musculus (Mouse)
Interaction partners:
Sequence:
MNQELLSVGSKRRRTGGSLRGNASSSQVDEGQMNRVVEEDPQQQARHQEEEHTARNGELVGANPRPGDQNDTQQGQVEENNNRFISVDEDSSGNQEEQEEDEEHAGEQEEEEEEEEEEEEMDQESDDFDPSDDSSREDEHTHNSNVTNCSSVSDLPAHQLSSPFYTKTTKMKRKLDHGSEVRSFSLGKKPCKVSDYTSTTGLVPCSATPTTFGDLRAANGQGQQRRRITSVQPPTGLQEWLKMFQSWSGPEKLLALDELIDSCEPTQVKHMMQVIEPQFQRDFISLLPKELALYVLSFLEPKDLLQAAQTCRYWRILAEDNLLWREKCKEEGKFRITHRCVSTLETS
Protein: Polyphenol oxidase I, chloroplastic (PPO-I) (EC 1.10.3.1) (Catechol oxidase I) (Q9ZP19)
Organism: Ipomoea batatas (Sweet potato) (Convolvulus batatas)
Function: Catalyzes the oxidation of mono- and o-diphenols to o-diquinones.
Subcellular location: Plastid, chloroplast thylakoid lumen {ECO:0000250}.
Interaction partners:
Sequence:
APIQAPEISKCVVPPADLPPGAVVDNCCPPVASNIVDYKLPAVTTMKVRPAAHTMDKDAIAKFAKAVELMKALPADDPRNFYQQALVHCAYCNGGYDQVNFPDQEIQVHNSWLFFPFHRWYLYFYERILGKLIGDPSFGLPFWNWDNPGGMVLPDFLNDSTSSLYDSNRNQSHLPPVVVDLGYNGADTDVTDQQRITDNLALMYKQMVTNAGTAELFLGKAYRAGDAPSPGAGSIETSPHIPIHRWVGDPRNTNNEDMGNFYSAGRDIAFYCHHSNVDRMWTIWQQLAGKPRKRDYTDSDWLNATFLFYDENGQAVKVRIGDSLDNQKMGYKYAKTPLPWLDSKPVPTKKKGGYASKSKAPFVASVFPVTLDKVVQVKVARPKKSRSAEEKEAEEEILLIVGIEVEIDKYAKFDVYLNDSDDPSGGKDKAEYAGSFAHLPHKHKGMKKIRTTLSLGLNEPLEDLGAEDDDTILVTLAPKVGGGVVSVDNVKVVYGS
Protein: Interleukin-34 (IL-34) (Q6ZMJ4)
Organism: Homo sapiens (Human)
Function: Cytokine that promotes the proliferation, survival and differentiation of monocytes and macrophages. Promotes the release of pro-inflammatory chemokines, and thereby plays an important role in innate immunity and in inflammatory processes. Plays an important role in the regulation of osteoclast proliferation and differentiation, and in the regulation of bone resorption. Signaling via CSF1R and its downstream effectors stimulates phosphorylation of MAPK1/ERK2 AND MAPK3/ERK1.
Subcellular location: Secreted {ECO:0000269|PubMed:18467591}.
Interaction partners:
- Macrophage colony-stimulating factor 1 receptor
- Macrophage colony-stimulating factor 1
- Syndecan-1
- Receptor-type tyrosine-protein phosphatase zeta
- Immunoglobulin heavy variable 3-43D
- Probable non-functional immunoglobulin heavy variable 3-16
- CX3C chemokine receptor 1
Sequence:
MPRGFTWLRYLGIFLGVALGNEPLEMWPLTQNEECTVTGFLRDKLQYRSRLQYMKHYFPINYKISVPYEGVFRIANVTRLQRAQVSERELRYLWVLVSLSATESVQDVLLEGHPSWKYLQEVETLLLNVQQGLTDVEVSPKVESVLSLLNAPGPNLKLVRPKALLDNCFRVMELLYCSCCKQSSVLNWQDCEVPSPQSCSPEPSLQYAATQLYPPPPWSPSSPPHSTGSVRPVRAQGEGLLP
Protein: Gamma-aminobutyric acid receptor subunit beta-3 (GABA(A) receptor subunit beta-3) (GABAAR subunit beta-3) (P63079)
Organism: Rattus norvegicus (Rat)
Function: Ligand-gated chloride channel which is a component of the heteropentameric receptor for GABA, the major inhibitory neurotransmitter in the brain. Plays an important role in the formation of functional inhibitory GABAergic synapses in addition to mediating synaptic inhibition as a GABA- gated ion channel (By similarity). The gamma2 subunit is necessary but not sufficient for a rapid formation of active synaptic contacts and the synaptogenic effect of this subunit is influenced by the type of alpha and beta subunits present in the receptor pentamer (By similarity). The alpha1/beta3/gamma2 receptor exhibits synatogenic activity whereas the alpha2/beta3/gamma2 receptor shows very little or no synaptogenic activity (By similarity). Functions also as histamine receptor and mediates cellular responses to histamine (By similarity). Plays an important role in somatosensation and in the production of antinociception (By similarity).
Subcellular location: Postsynaptic cell membrane {ECO:0000269|PubMed:9464994}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P28472}. Cell membrane {ECO:0000269|PubMed:2540033, ECO:0000269|PubMed:2548852, ECO:0000269|PubMed:9092594, ECO:0000269|PubMed:9464994}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P28472}. Cytoplasmic vesicle membrane {ECO:0000269|PubMed:25172774}. Note=The beta-3 subunits are present in Golgi synapses and on the extrasynaptic membranes (when coassembled with alpha-1/6 and gamma-2 subunits), and in some of the mossy fiber to granule cell synapses (when coassembled with alpha-6 and gamma-2 subunits) (PubMed:9464994). The beta-3 subunits, when coassembled with alpha-6 and delta subunits, are found only on the extrasynaptic somatic and dendritic membranes (PubMed:9464994). {ECO:0000269|PubMed:9464994}.
Interaction partners:
- Gamma-aminobutyric acid receptor subunit gamma-2
- Gamma-aminobutyric acid receptor subunit beta-2
- Huntingtin-associated protein 1
- Gamma-aminobutyric acid receptor subunit alpha-1
- Gamma-aminobutyric acid receptor subunit beta-1
- Gamma-aminobutyric acid receptor subunit alpha-4
- Vesicle-fusing ATPase
- Trafficking kinesin-binding protein 2
- Inactive phospholipase C-like protein 1
- Gamma-aminobutyric acid receptor subunit delta
Sequence:
MWGFAGGRLFGIFSAPVLVAVVCCAQSVNDPGNMSFVKETVDKLLKGYDIRLRPDFGGPPVCVGMNIDIASIDMVSEVNMDYTLTMYFQQYWRDKRLAYSGIPLNLTLDNRVADQLWVPDTYFLNDKKSFVHGVTVKNRMIRLHPDGTVLYGLRITTTAACMMDLRRYPLDEQNCTLEIESYGYTTDDIEFYWRGGDKAVTGVERIELPQFSIVEHRLVSRNVVFATGAYPRLSLSFRLKRNIGYFILQTYMPSILITILSWVSFWINYDASAARVALGITTVLTMTTINTHLRETLPKIPYVKAIDMYLMGCFVFVFLALLEYAFVNYIFFGRGPQRQKKLAEKTAKAKNDRSKSEINRVDAHGNILLAPMDVHNEMNEVAGSVGDTRNSAISFDNSGIQYRKQSMPKEGHGRYMGDRSIPHKKTHLRRRSSQLKIKIPDLTDVNAIDRWSRIVFPFTFSLFNLVYWLYYVN
Protein: Protein-lysine N-methyltransferase EFM3 (EC 2.1.1.-) (Elongation factor methyltransferase 3) (P47163)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: S-adenosyl-L-methionine-dependent protein-lysine N-methyltransferase that mono-, di- and trimethylates elongation factor 2 (EFT1/EFT2) at 'Lys-509'.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:14562095}.
Interaction partners:
- Protein-lysine N-methyltransferase EFM2
- Protein-lysine N-methyltransferase EFM4
- Elongation factor 2
- Histidine protein methyltransferase 1
- 25S rRNA
- 25S rRNA
- Protein-lysine N-methyltransferase EFM1
- Protein-lysine N-methyltransferase EFM5
- Alpha N-terminal protein methyltransferase 1
- Ribosomal lysine N-methyltransferase 5
Sequence:
MNEDLFYDRLHQRCPGKYLLEELETSKSNDVLHASRFVCEMELVQKTNAYYCKTIVKMLLDHEWIFAKAFTIVNDGEDEIEIYDYLYEKYIKLLSTGKPDPMMKDVVRYRFDEDVKIKIEETPNLISAASTTGFRTWEAALYMGDFLIHKPLQELAPVQGQDDGKKKLNVLEVGAGTGIVSLVILQKYHEFVNKMYVTDGDSNLVETQLKRNFELNNEVRENEPDIKLQRLWWGSDRVPEDIDLVVGADVTYDPTILPDLCECLAECLALDRCKLCLLSATIRSESTVQLFSQECNKLGLKCTIVTSTEYDANNEIRAMKALQFKPLIAPIRIYKITKQ
Protein: Ccna2 protein (A0JPK0)
Organism: Rattus norvegicus (Rat)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MPWLLVPLSLYPEPENHWYLLIIQWMVVLIAGQTHGRQNSCYRQLCRCYDLTVETRDVESPHAMDISIVLEDEKPVNVNEVPDYHEDIHTYLREMEVKCKPKVSYMKRQPDITNSMRAILVDWLVEVGEEYKLQNETLHLAVNYIDRFLSSMSVLRGKLQLVGTAAMLLASKFEEIYPPEVAEFVYITDDTYSKKQVLRMEHLVLKVLAFDLAAPTVNQFLTQYFLHLQPANCKVESLAMFLGELSLIDADPYLKYLPSLIAGAAFHLALYTVTGQSWPESLVQKTGYTLESLKPCLMDLHQTYLKAPQHAQQSIREKYKHSKYHSVSLLNPPETLNV
Protein: Suppression of tumorigenicity 18 protein (C2-HC type zinc finger protein r-MyT3) (Neural zinc finger factor 3) (NZF-3) (Q9QX27)
Organism: Rattus norvegicus (Rat)
Function: Repressor that binds to DNA sequences containing a bipartite element consisting of a direct repeat of the sequence 5'-AAAGTTT-3' separated by 2-9 nucleotides. Represses basal transcription activity from target promoters.
Subcellular location: Nucleus {ECO:0000269|PubMed:9478997}.
Interaction partners:
Sequence:
MQRLKIKRCILSQKEPKVAYDCSMAKKRRAEEQALGVPVNKRKSLLMKPRHYSPDMDCKENPDNRNEDDGLETNDHSTADEIVVKPMDKTLHLPAQESSLPKEDQYACYPELMVKSLMHLGKFEESESVQTVGENLNGNGIQSLKAECDEANECFMVHSDDGRDKVHHSQPPFCSSGDSESDSDNTENGWGSGSNSSEDTDTHKGPKRKLTYNRKDLLEVPEIKAEDDKFIPCENRCDSDTSGRDPQNSHMEPLAVKVQPSFPEVEESESLATVIAESAEVEKAKGSLSLLEQAIALQAERGSVFHHTYKELDRFLLDHLARQRRQPKVTDASGRQIFNNKHSPRPERREAKCPIPGCDGTGHVTGLYPHHRSLSGCPHKVRVPLEILAMHENVLKCPTPGCTGRGHVNSNRNTHRSLSGCPIAAAEKLAMTQDKSQLDSSQTGQGPEQAHRVNLVKQIEFNFRSQAITSPRASASKEQEKFGKVPFDYASFDAQVFGKRPLLQTGQGQKAPPFPESKHFSNPVKFSNGLPSAGAHTQSTVRASSYGHGQYSEDTHIAAAAAILNLSTRCREATDILSNKPQSLRAKGAEIEVDENGTLDLSMKKNRILDKSIPPTSSHTTIATPSSSPFKASSLLVNAAFYQALCDQEGWNVPINYSKSHGKTEEEKEKDPVNSLENLEEKKFAGEASIPSPKPKLHTRDLKKELITCPTPGCDGSGHVTGNYASHRSVSGCPLADKTLKSLMAANSQELKCPTPGCDGSGHVTGNYASHRSLSGCPRARKGGIKMTPTKEEKEDSELRCPVIGCDGQGHISGKYTSHRTASGCPLAAKRQKENPLNGTPLSWKLNKQELPHCPLPGCNGLGHVNNVFVTHRSLSGCPLNAQAIKKVKVSEELMTIKLKATGGIEGDEEIRHLDEEIKELNESNLKIEADMMKLQTQITSMESNLKTIEEENKLIEQSNESLLKELAGLSQALISSLADIQLPQMGPINEQNFEAYVNTLTDMYSNLERDYSPECKALLESIKQAVKGIHV
Protein: RING-type E3 ubiquitin transferase (EC 2.3.2.27) (P87662)
Organism: Equid alphaherpesvirus 1 (Equine herpesvirus 1)
Interaction partners:
Sequence:
MATVAERCPICLEDPSNYSMALPCLHAFCYVCITRWIRQNPTCPLCKVPVESVVHTIESDSEFKETKVSVDFDYDSEEDEDSFEGQFLAVDSGDAPANISAWNGPMAFVPLNANGTAGAPRLQPLVDWLVERLDQLFETPELALVMRNIVMDTLCEHGCNEEELTRQFWPMFHEDTVPFVTDLIIQAELCVASRPILPIARGRGVEYIDSSSSSSSSEEETDSDIEVDPNNLTDPEDTSDETSTDNSSAQAPRQEDSRPARARPGPPTRGRRRGRRPAAPGPASRRSARLRRRQPRTNSRTNGGDNGEIIDLTLDSDGPVAVVLVDRSSEGAGLFGGRFAQHVRRRTEDESARRRGNVLLRPRRQSVPPVPYPDIASTSPLIRQGGQRVRDLQRAFQTQPAEPEEMRCPHNCQRYRRNQ