wanglab/gogpt-training-data huggingface dataset:
Protein: SURP and G-patch domain containing 2 (M0R2Z9)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MSPPRAAAAAGQNNMAARRITQETFDAVLQEKAKRYHMDASGEAVSETLQFKAQDLLRAVPRSRAEMYDDVHSDGRYSLSGSVAHSRDAGREGLRSDVFPGPSFRSSNPSISDDSYFRKECGRDLEFSHSDSRDQVIGHRKLGHFRSQDWKFALRGSWEQDFGHPVSQESSWSQEYSFGPSAVLGDFGSSRLIEKECLEKESRDYDVDHPGEADSVLRGGSQVQARGRALNIVDQEGSLLGKGETQGLLTAKGGVGKLVTLRNVSTKKIPTVNRITPKTQGTNQIQKNTPSPDVTLGTNPGTEDIQFPIQKIPLGLDLKNLRLPRRKMSFDIIDKSDVFSRFGIEIIKWAGFHTIKDDIKFSQLFQTLFELETETCAKMLASFKCSLKPEHRDFCFFTIKFLKHSALKTPRVDNEFLNMLLDKGAVKTKNCFFEIIKPFDKYIMRLQDRLLKSVTPLLMACNAYELSVKMKTLSNPLDLALALETTNSLCRKSLALLGQTFSLASSFRQEKILEAVGLQDIAPSPAAFPNFEDSTLFGREYIDHLKAWLVSSGCPLQVKKAEPEPMREEEKMIPPTKPEIQAKAPSSLSDAVPQRADHRVVGTIDQLVKRVIEGSLSPKERTLLKEDPAYWFLSDENSLEYKYYKLKLAEMQRMSENLRGADQKPTSADCAVRAMLYSRAVRNLKKKLLPWQRRGLLRAQGLRGWKARRATTGTQTLLSSGTRLKHHGRQAPGLSQAKPSLPDRNDAAKDCPPDPVGPSPQDPSLEASGPSPKPAGVDISEAPQTSSPCPSADIDMKTMETAEKLARFVAQVGPEIEQFSIENSTDNPDLWFLHDQNSSAFKFYRKKVFELCPSICFTSSPHNLHTGGGDTTGSQESPVDLMEGEAEFEDEPPPREAELESPEVMPEEEDEDDEDGGEEAPAPGGAGKSEGSTPADGLPGEAAEDDLAGAPALSQASSGTCFPRKRISSKSLKVGMIPAPKRVCLIQEPKVHEPVRIAYDRPRGRPMSKKKKPKDLDFAQQKLTDKNLGFQMLQKMGWKEGHGLGSLGKGIREPVSVGTPSEGEGLGADGQEHKEDTFDVFRQRMMQMYRHKRANK
Protein: Laccase-1 (EC 1.10.3.2) (Benzenediol:oxygen oxidoreductase 1) (Diphenol oxidase 1) (Urishiol oxidase 1) (Q9LMS3)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Lignin degradation and detoxification of lignin-derived products.
Subcellular location: Secreted, extracellular space, apoplast {ECO:0000305}.
Interaction partners:
- Phenylalanine ammonia-lyase 1
- Cinnamoyl-CoA reductase 1
- Cinnamoyl-CoA reductase 2
- Phenylalanine ammonia-lyase 4
- Phenylalanine ammonia-lyase 2
- Phenylalanine ammonia-lyase 3
- Probable caffeoyl-CoA O-methyltransferase At4g26220
- Trans-cinnamate 4-monooxygenase
- Putative caffeoyl-CoA O-methyltransferase At1g67980
- Cytochrome P450 84A1
Sequence:
MENLGFLIISTFLLLFTTLLPYSSASTTRRFHFNVEWKKVTRLCHTKQLLTVNGQYPGPTVAVHEGDIVEIKVTNRIAHNTTIHWHGLRQYRTGWADGPAYITQCPIRSKQSYTYRFKVEDQRGTLLWHAHHSWQRASVYGAFIIYPRQPYPFSGSHIQSEIPIILGEWWNDDVDNVEKAMMKTGAGAKVSDAYTLNGLPGPLYPCSTKDTFTATVDAGKTYILRIINAALNNELFVAVANHTLTVVEVDAVYTKPVHTKAIMIAPGQTTTLLLRADQLSGGEFLIAATPYVTSVFPFNNSTTVGFIRYTGKTKPENSVNTRRRRRLTAMSTVVALPNMLDTKFATKFSDSIKSLGSAKYPCKVPTKIDKRVITTISLNLQDCPLNQTCDGYAGKRFFASMNNISFVRPPISILESYYKKQSKGVFSLDFPEKPPNRFDFTGVDPVSENMNTEFGTKLFEVEFGSRLEIVFQGTSFLNIENHPLHVHGHNFFVVGRGFGNFDPEKDPKRYNLVDPPERNTFAVPTGGWAAIRINADNPGVWFIHCHLEQHTSWGLAMGFIVKDGPLPSQTLLPPPHDLPQC
Protein: Guanylate cyclase soluble subunit beta-1 (GCS-beta-1) (EC 4.6.1.2) (Guanylate cyclase soluble subunit beta-3) (GCS-beta-3) (Soluble guanylate cyclase small subunit) (O54865)
Organism: Mus musculus (Mouse)
Function: Mediates responses to nitric oxide (NO) by catalyzing the biosynthesis of the signaling molecule cGMP.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:P16068}.
Interaction partners:
- Guanylate cyclase soluble subunit alpha-1
- Guanylate cyclase soluble subunit alpha-2
- cGMP-dependent protein kinase 1
- cGMP-dependent protein kinase 2
- Nitric oxide synthase 1
- Inosine triphosphate pyrophosphatase
- Bis
- cGMP-specific 3',5'-cyclic phosphodiesterase
- GTP cyclohydrolase 1
- Molybdenum cofactor biosynthesis protein 1
Sequence:
MYGFVNHALELLVIRNYGPEVWEDIKKEAQLDEEGQFLVRIIYDDSKTYDLVAAASKVLNLNAGEILQMFGKMFFVFCQESGYDTILRVLGSNVREFLQNLDALHDHLATIYPGMRAPSFRCTDAEKGKGLILHYYSEREGLQDIVIGIIKTVAQQIHGTEIDMKVIQQRNEECDHTQFLIEEKESKEEDFYEDLDRFEENGTQESRISPYTFCKAFPFHIIFDRNLVVTQCGNAIYRVLPQLQPGNCSLLSVFSLVRPHIDISFHGILSHINTVFVLRSKEGLLDVEKLECEDELTGAEISCLRLKGQMIYLPEADSILFLCSPSVMNLDDLTRRGLYLSDIPLHDATRDLVLLGEQFREEYKLTQELEILTDRLQLTLRALEDEKKKTDTLLYSVLPPSVANELRHKRPVPAKRYDNVTILFSGIVGFNAFCSKHASGEGAMKIVNLLNDLYTRFDTLTDSRKNPFVYKVETVGDKYMTVSGLPEPCIHHARSICHLALDMMEIAGQVQVDGESVQITIGIHTGEVVTGVIGQRMPRYCLFGNTVNLTSRTETTGEKGKINVSEYTYRCLMSPENSDPLFHLEHRGPVSMKGKKEPMQVWFLSRKNTGTEETNEEDEN
Protein: Gasdermin-B (Gasdermin-like protein) [Cleaved into: Gasdermin-B, N-terminal (GSDMB-NT) (p30); Gasdermin-B, C-terminal (GSDMB-CT) (p16)] (Q8TAX9)
Organism: Homo sapiens (Human)
Function: Precursor of a pore-forming protein that acts as a downstream mediator of granzyme-mediated cell death. This form constitutes the precursor of the pore-forming protein: upon cleavage, the released N-terminal moiety (Gasdermin-B, N-terminal) binds to membranes and forms pores, triggering pyroptosis. Also acts as a regulator of epithelial cell repair independently of programmed cell death: translocates to the plasma membrane and promotes epithelial maintenance and repair by regulating PTK2/FAK-mediated phosphorylation of PDGFA.
Subcellular location: [Gasdermin-B]: Cytoplasm {ECO:0000269|PubMed:18038310}. Note=Vesicular localization in the apical region of gastric chief cells and colonic surface mucous cells, and the basal region of neuroendocrine cells. {ECO:0000269|PubMed:18038310}.; SUBCELLULAR LOCATION: [Gasdermin-B, N-terminal]: Cell membrane {ECO:0000269|PubMed:36157507, ECO:0000269|PubMed:36899106}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q5Y4Y6}.
Interaction partners:
- Gasdermin-C
- ORM1-like protein 3
- Zona pellucida-binding protein 2
- Gasdermin-E
- Zinc finger protein Aiolos
- Pejvakin
- GPI-specific phospholipase A2-like PGAP3
Sequence:
MFSVFEEITRIVVKEMDAGGDMIAVRSLVDADRFRCFHLVGEKRTFFGCRHYTTGLTLMDILDTDGDKWLDELDSGLQGQKAEFQILDNVDSTGELIVRLPKEITISGSFQGFHHQKIKISENRISQQYLATLENRKLKRELPFSFRSINTRENLYLVTETLETVKEETLKSDRQYKFWSQISQGHLSYKHKGQREVTIPPNRVLSYRVKQLVFPNKETMNIHFRGKTKSFPEEKDGASSCLGKSLGSEDSRNMKEKLEDMESVLKDLTEEKRKDVLNSLAKCLGKEDIRQDLEQRVSEVLISGELHMEDPDKPLLSSLFNAAGVLVEARAKAILDFLDALLELSEEQQFVAEALEKGTLPLLKDQVKSVMEQNWDELASSPPDMDYDPEARILCALYVVVSILLELAEGPTSVSS
Protein: Tetratricopeptide repeat domain 21A (A0A0B4J1Y2)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MSSNDSSLMAGIIYYSQEKYFHHVQQAAAVGLEKFSNDPVLKFFKAYGVLKEEHIQDAISDLESIRHHPDVSLCSTMALIYAHKRCEIIDREAIQELEYSLKEIRKTVSGTALYYAGLFLWLIGRHDKAKEYIDRMLKISRGFREAYVLRGWVDLTSDKPHTAKKAIEYLEQGIQDTKDVLGLMGKAMYFMMQQNYSEALEVVNQITVTSGSFLPALVLKMQLFLARQDWEQTVEMGHRILEKDESNIDACQILTVHELAREGNMTTATNHVRNLIKALETREPENPSLHLKKIIVVSRLCGSHQVILGLVCSFIERTFMATPSYVHVATELGYLFILKNQVKEALLWYSEAMKLDKDGMAGLTGIILCHILEGHLEEAEYRLEFLKEVQKSLGKSEVLIFLQALLMSRKHKGEEETTALLKEAVELHFSSMQGIPLGSEYFEKLDPYFLVCIAKEYLLFCPKQPRLPGQIVSPLLKQVAVILNPVVKAAPALIDPLYLMAQVRYYSGELENAQSILQRCLELDPASVDAHLLMCQIYLAQGNFGMCFHCLELGVSHNFQVRDHPLYHLIKARALNKAGDYPEAIKTLKMVIKLPALKKEEGRKFLRPSVQPSQRASILLELVEALRLNGELHEATKVMQDTINEFGGTPEENRITIANVDLVLSKGNVDVALNMLRNILPKQSCYMEAREKMANIYLQTLRDRRLYIRCYRELCEHLPGPHTSLLLGDALMSILEPEKALEVYDEAYRQNPHDASLASRIGHAYVKAHQYTEAIEYYEAAQKINGQDFLCCDLGKLLLKLKKVNKAEKVLKQALEHDIVQDIPSMMNDVKCLLLLAKVYKSHKKEAVIETLNKALDLQSRILKRVPLEQPEMIPSQKQLAASICIQFAEHYLAEKEYDKAVQSYKDVFSYLPTDNKVMLELAQLYLLQGHLDLCEQHCAILLQTEQNHETASVLMADLMFRKQKHEAAINLYHQVLEKAPDNFLVLHKLIDLLRRSGKLEDIPAFFELAKKVSSRVPLEPGFNYCRGIYCWHIGQPNEALKFLNKARKDSTWGQSAIYHMVQICLNPDNEVVGGEAFENQGAESNYMEKKELEQQGVSTAEKLLQGQRPCPAGLGTSLRVPEADPQGAYAVEAPGQDPLGAE
Protein: ATP-dependent (S)-NAD(P)H-hydrate dehydratase (EC 4.2.1.93) (ATP-dependent NAD(P)HX dehydratase) (Nicotinamide nucleotide repair protein 2) (P36059)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Catalyzes the dehydration of the S-form of NAD(P)HX at the expense of ATP, which is converted to ADP. Together with NAD(P)HX epimerase, which catalyzes the epimerization of the S- and R-forms, the enzyme allows the repair of both epimers of NAD(P)HX, a damaged form of NAD(P)H that is a result of enzymatic or heat-dependent hydration.
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03157, ECO:0000269|PubMed:14562095}.
Interaction partners:
- NAD
- Enhancer of mRNA-decapping protein 3
- Glutamate decarboxylase
Sequence:
MLAELSHRELIKLAQKRCIPPLLPKFHKGQSGGRVCIIGGCEDYTGAPYFSANATALMGCDLTHVICEYNAGTVIKSYTPNLMVHPYLRMSNTKLDVDMDEQRKKINSLLDRIHVVVIGPGLGRDPLMLKSIKDIIRYILEKHEGKIPLVIDADGLFLVTQDSEVKEMLKSYPKGRVILTPNVVEFKRLCDAIGKKGDSHSEMGSLIAQELNCIVVEKGQSDKIFSPDSEKDMLTNSEEGSNKRVGGQGDTLTGAISCMLAFSRAMYDFKICEQEEKGESSNDKPLKNWVDYAMLSCYAGCTITRECSRLGFKAKGRAMQTTDLNDRVGEVFAKLFG
Protein: RNA-binding protein (RNA-binding protein 9, isoform C) (RNA-binding protein 9, isoform I) (RNA-binding protein 9, isoform K) (Q9VQJ0)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MVEGQTAVQQQQQQPSGAGGASGVGSTTGSAGGPATANNVTNSQAQTNGGTTATTTAAAGAGSTTNAAVGQATANNAASNNNNNNNNTNNNNNNNATANNNNNNEPDPKTNLIVNYLPQTMSQDEIRSLFVSFGEVESCKLIRDKVTGQSLGYGFVNYVKQEDAEKAINALNGLRLQNKTIKVSIARPSSESIKGANLYVSGLPKNMTQSDLESLFSPYGKIITSRILCDNITDEHAAGLSKGVGFIRFDQRFEADRAIKELNGTTPKNSTEPITVKFANNPSSNKNSMQPLAAYIAPQNTRGGRAFPANAAAGAAAAAAAAAIHPNAGRYSSVISRYSPLTSDLITNGMIQGNTIASSGWCIFVYNLAPDTEENVLWQLFGPFGAVQSVKVIRDLQSNKCKGFGFVTMTNYEEAVLAIQSLNGYTLGNRVLQVSFKTNKNKQT
Protein: Dual specificity tyrosine-phosphorylation-regulated kinase 2 (EC 2.7.12.1) (Protein smell impaired at 35A) (dDyrk2) (Q9V3D5)
Organism: Drosophila melanogaster (Fruit fly)
Function: In vitro; can phosphorylate exogenous substrates on Ser and Thr residues. May have a physiological role in development being involved in cellular growth and differentiation.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:12786602}.
Interaction partners:
- DDB1- and CUL4-associated factor 7
- Serine/threonine-protein kinase polo
Sequence:
MLDRCEMPIQLDNEKLRRDVRLSGSRLDLPQLCNGSRRLDGHNNHVAANENTVTTTSLNGNGNGNGNSNSNNNNNIGSPVSSSTTNSSNGGNERGSSTKSNSSSGSGSSGNSASSTGSGELKCNTPMTPSELVKKFRNYLTDLEFEELKVYKEVWYFGQHASKNYNKPAPTANTTNLGYDDDNGNYKIIEHDHIAFRYEILEVIGKGSFGQVIRALDHKTNTHVAIKIIRNKKRFLNQAVVELNILDELREKDADGSHNVIHMLDYTYFRKHLCITFELMSLNLYELIKKNNYNGFSMSLIRRFCNSIVKCLRLLYKENIIHCDLKPENILLKQRGSSSIKVIDFGSSCYVDRKIYTYIQSRFYRSPEVILGLQYGTAIDMWSLGCILAELYTGFPLFPGENEVEQLACIMEVLGLPPKVLISVARRRRLFFDSRDAPRCITNTKGRKRSPGSKSLAHILHCQDRYFIDFLQRCLEWDPAERMTPDEAAHHEFLQPSASSRHRSCRMSSSSSSSGLNSVSQKSSCYSFSEISPGTNGPVVASITSTTAVHNAAIATTTKSRQQPPSQSHGHAQSNGHLPDIKLSASDKYNSMQKVAVRSKITSSVSDLESVQQYSLHRIYGGVGSGSTHHVSSAATRKHLPGTGSGIVGAMSSKYGSSTLAHNHHNVTHHNASTATIATTTHHHHHHGGQQQQQSSSGASTMAMSHSQSTGDVSDRAIFGRA
Protein: Vacuolar protein sorting-associated protein 9 (Vacuolar protein-targeting protein 9) (P54787)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Required for vacuolar protein sorting; may be required for the consumption of transport vesicles containing vacuolar protein precursors. May bind a Rab GTPase such as VPS21.
Subcellular location: Cytoplasm.
Interaction partners:
- Vacuolar protein sorting-associated protein 21
- Protein MUK1
- Vacuolar protein sorting-associated protein 8
- GTP-binding protein YPT53
- Vacuolar protein sorting-associated protein 29
- Ypt/Rab-type GTPase YPT7
- GTP-binding protein YPT52
- Vacuolar fusion protein CCZ1
- Polyubiquitin
- Vacuolar fusion protein MON1
Sequence:
MTDDEKREILKEFDPFSQLEQANGNPDKDVKFKKDDPNRAAAEETNRDISAQDKGDEEPFYDFQIFIKQLQTPGADPLVKYTKSFLRNFLAQRLLWTVSEEIKLISDFKTFIYDKFTLYEPFRSLDNSKMRNAKEGMEKLIMGKLYSRCFSPSLYEILQKPLDDEHMKDLTNDDTLLEKIRHYRFISPIMLDIPDTMPNARLNKFVHLASKELGKINRFKSPRDKMVCVLNASKVIFGLLKHTKLEQNGADSFIPVLIYCILKGQVRYLVSNVNYIERFRSPDFIRGEEEYYLSSLQAALNFIMNLTERSLTIEDHEDFEEAYQRNFKQLAEEKEEEEKKKQLEIPDELQPNGTLLKPLDEVTNIVISKFNELFSPIGEPTQEEALKSEQSNKEEDVSSLIKKIEENERKDTLNTLQNMFPDMDPSLIEDVCIAKKSRIGPCVDALLSLSE
Protein: E2 ubiquitin-conjugating protein (A0A1D8PQD4)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Interaction partners:
- Polyubiquitin
- Ubiquitin-ribosomal protein eS31 fusion protein
- Ubiquitin-activating enzyme E1 1
- Nucleoporin NSP1
- HECT-type E3 ubiquitin transferase
- Uncharacterized protein
- E2 ubiquitin-conjugating protein
- Uncharacterized protein
- Large ribosomal subunit protein eL40
- SUMO family protein
Sequence:
MSRVKRIAKELEECRQDTQSGVSLNLNNENDLTHLTGYFKGPPGTPYEGGLFQVAIDIPQEYPFKPPQMKFITKIYHPNISSVTGAICLDILKDAWTPILTLKSSLISLQSLLQSPEPSDPQDAEVAKHYLSNKSGFEETAAYWTKIYASDGVDGSGSGSGSSNNNGGGAKLSDSALYGIDDEIVGQYESMGFPRDKTIQVLRRMGIKSFKGVGNKSELENKILEELLRECQ
Protein: Erythrocyte membrane protein 1, PfEMP1 (O96296)
Organism: Plasmodium falciparum (isolate 3D7)
Interaction partners:
Sequence:
MGSGKGGDPQDESVKHMFDRIGEDVYEQVKSETVNYVSELEGKLSLAPILGVESGSTNETCNLVQDYYNKPVYGNSNRYPCKNLKGITNEERFSDTLGGQCTNKKIKGNEYSTKSGKDCGACAPYRRLHLCSHNLESIDTTSMTHKLLLEVCMAAKYEGNSIDTHYPQHQRTNEDSPSQICTMLARSFADIGDIVRGKDLFYGNSKEKEKRDELETNLKTIFGKIHEKLKDKEGAETRYGSDTTNYYQLREDWWYANRATVWEAITCDVHGSDYFRQTCGDKETTATRVKDKCRCKDENGKKPGSNADQVPTYFDYVPQYLRWFEEWAEDFCRKKKKKLEKLEQQCRDYKQNLYCSGNGYDCTKTIYKKGKLVIGEHCTNCSVWCRLYESWIDNQKLEFLKQKQKYETEISNSGSCGGSGGVKGRNRKKRGAGVETATNYDGYEKKFYKELKESEYGKVDDFLKLLNNEDVCKKIKDEKEKIDFTKPADKNSNNEGTFYHSEYCKPCPDCGVKRKDNQWKDKYDGKCTRGKLYEPASGAQGTPIKILKSGEKQKEIETKLKAFCDQTNGDTTNSVARGGGADGSGSKSNSKELYEEWKCYNEVQKVKDDKNGEEEDEDEEDVDKVKKAGGLCILENKKHESRNNSSNEPEQFQKTFHDFFYFWIGRFLNDSMYWRGKVNSCINNPKRKKCRNECKDDCGCFKEWIGKKKEEWENIKKHFKTQEAFKNKRENSGIDMFSGLMDSADVVLELALELEQLFQDIKDGYGDVKELKGIKELLDEEKKKKQAEEAVVVVVADNQKKTTIDKLLQHEGDDANNCLKTHKEKCEETQPKPPGAGGPGAPSETGETTTLEDEEEEEDEEEDAGDEVEEGETVDTTEGDETETVEQPVKDTDREGEEEEAKKATDTTTSLDVCDTVKNALTNNDNLTDACKLKYGPGGKERFPNWKCVSSGEKSVATAGSSGATGKSGDKGAICVPPRRRRLYVGGLTKLTSAGTSSESPQGGSESSRASDVSQGNGGDDITTTESLRKWFIETAAIETFFLWHRYKKEWEAQKKAELQRNGLLLGTGASLNLGGDDSNPQTQLQKSGTIPLDFLRLMFYTLGDYRDILVRGVADDKNGGNNIILNASGNKDEKQKMEKIQEKIEQILPTSGNKETRGPQNSVNDRQSLWDRIAEHVWHGMVCALTYKDDDNGLKGVVKKPQKIENPEKLWNETTKKPKDEKYQYQTAKLEDESGEKRPDSSASGTKLTDFIKRPPYFRYLEEWGENFCKKRTEMLGKIKEDCYKNGGRCSGDGLKCNEIVIDKEKIFGDLLCPTCARHCRFYKKWINTKRDEFNKQSNAYSEQKKKYEEENDSAQKNNGVCGTLKDDAAEFLNRLKNGPCKNESEENKKAEDEIDFKKPDDTFKDADNCKPCSEFKIKCENHNCSSGGNTQGKCDGKTTIAATEIENIKTNTKEVTMLVSDDSKSATEFKDGLSECKDKGIFKGIRKDEWECGKVCGVDICNLKKKDNIGKESDKKYIIMKELLKRWLEYFLEDYNKIKHKISHCTKNGKGSKCIKGCVDKWVQQKKEEWKQIKERFNEQYKSKTSDEYFNVKSFLETWIPKIAVVNDQDNVIKLSKFGNSCGCSASAISTNGNEEDAIDCMIKKLEKKIDECKRKPGENSGQTCNETLTHPLDVQDEDEPLEETEENPVGKQHPSFCPPVEDKKKEEEGETCTPASPAPAPAPAPASPSPTPAPADEPFDPTILQTTIPLGIALALGSIAFLFLKKKTKHPVDLFSVINIPKSDYDIPTKLSPNRYIPYTSGKYRGKRYIYLEGDSGTDSGYTDHYSDITSSSESEYEEMDINDIYVPGSPKYKTLIEVVLEPSGNNTTASDTQNDIQNDGIPSNKFSDNEWNTLKDDFISNMLQNQPKDVPNDYKSGDIPFNTQPNTLYFDKPEEKPFITSIHDRNLLNGEEYSYNVNMSTNSMDDPKYVSNNVYSGIDLINDSLSGNKHIDIYDEVLKRKENELFGTNHVKHTSIHSVAKNTNSDPILNQINLFHTWLDRHRDMCEKWENHHERLAKLKEEWENETHSGNTHPSDSNKTLNTDVSIQIHMDNPKPINQFTNMDTILEDLDKPFNEPYYYDMYDDDIYYDVNDHDTSTVDTNAMDVPSKVQIEMDVNTKLVKEKYPIADVWDI
Protein: Ly-6/neurotoxin-like protein 1 (Endogenous prototoxin LYNX1) (Testicular tissue protein Li 112) (P0DP58)
Organism: Homo sapiens (Human)
Function: Acts in different tissues through interaction to nicotinic acetylcholine receptors (nAChRs). The proposed role as modulator of nAChR activity seems to be dependent on the nAChR subtype and stoichiometry, and to involve an effect on nAChR trafficking and its cell surface expression, and on single channel properties of the nAChR inserted in the plasma membrane. Modulates functional properties of nicotinic acetylcholine receptors (nAChRs) to prevent excessive excitation, and hence neurodegeneration. Enhances desensitization by increasing both the rate and extent of desensitization of alpha-4:beta-2-containing nAChRs and slowing recovery from desensitization. Promotes large amplitude ACh-evoked currents through alpha-4:beta-2 nAChRs. Is involved in regulation of the nAChR pentameric assembly in the endoplasmic reticulum. Shifts stoichiometry from high sensitivity alpha-4(2):beta-2(3) to low sensitivity alpha-4(3):beta-2(2) nAChR (By similarity). In vitro modulates alpha-3:beta-4-containing nAChRs. Reduces cell surface expression of (alpha-3:beta-4)(2):beta-4 and (alpha-3:beta-4)(2):alpha-5 nAChRs suggesting an interaction with nAChR alpha-3(-):(+)beta-4 subunit interfaces and an allosteric mode. Corresponding single channel effects characterized by decreased unitary conductance, altered burst proportions and enhanced desensitization/inactivation seem to depend on nAChR alpha:alpha subunit interfaces and are greater in (alpha-3:beta-2)(2):alpha-3 when compared to (alpha-3:beta-2)(2):alpha-5 nAChRs. Prevents plasticity in the primary visual cortex late in life (By similarity).
Subcellular location: Cell membrane {ECO:0000255}; Lipid-anchor, GPI-anchor {ECO:0000255}. Cell projection, dendrite {ECO:0000250|UniProtKB:P0DP60}. Endoplasmic reticulum {ECO:0000250|UniProtKB:P0DP60}. Note=Detected in Purkinje cells soma and proximal dendrites. {ECO:0000250|UniProtKB:P0DP60}.
Interaction partners:
- Secreted Ly-6/uPAR-related protein 1
- Lymphocyte antigen 6H
- Ly6/PLAUR domain-containing protein 6
- Ly6/PLAUR domain-containing protein 2
- Neuronal acetylcholine receptor subunit beta-2
- Lymphocyte antigen 6K
- CD59 glycoprotein
Sequence:
MTPLLTLILVVLMGLPLAQALDCHVCAYNGDNCFNPMRCPAMVAYCMTTRTYYTPTRMKVSKSCVPRCFETVYDGYSKHASTTSCCQYDLCNGTGLATPATLALAPILLATLWGLL
Protein: Pepsin A-5 (EC 3.4.23.1) (Pepsin F) (Q9D106)
Organism: Mus musculus (Mouse)
Function: Shows particularly broad specificity; although bonds involving phenylalanine and leucine are preferred, many others are also cleaved to some extent (By similarity). May play a role as a specialized neonatal digestive enzyme (Probable).
Subcellular location: Secreted {ECO:0000305}.
Interaction partners:
Sequence:
MKWLWVLGLVALSECLVKIPLMKIKSMRENLRESQVLKDYLEKYPRSRAHVLLEQRRNPAVTYEPMRNYLDLVYIGIISIGTPPQEFRVVLDTGSSVLWVPSIYCSSPACAHHKAFNPLRSSTFLVSGRPVNVAYGSGEMSGFLAYDTVRIGDLTVVAQAFGLSLEEPGIFMEYAVFDGILGLGYPNLGLQGITPVFDNLWLQGLIPQNLFAFYLSSKDEKGSMLMLGGVDPSYYHGELHWVPVSKPSYWQLAVDSISMNGEVIACDGGCQGIMDTGTSLLTGPRSSIVNIQNLIGAKASGDGEYFLKCDTINTLPDIVFTIGSVTYPVPASAYIRKDRSHNCRSNFEEGMDDPSDPEMWVLGDVFLRLYFTVFDRANNRIGLAPAA
Protein: Anillin-like protein 1 (Q9XTT4)
Organism: Caenorhabditis elegans
Function: Required for contractile events in embryos that occur prior to mitosis, such as cortical ruffling and pseudocleavage. Promotes membrane ruffling by organizing cortical patches of septins and myosin II. Not generally required for cytokinesis in mitotic cells. Required for the asymmetric cleavage events that extrude the two polar bodies during oocyte meiosis. Not required for meiotic contractile ring assembly, initiation or closure but is required for the transformation of the contractile ring from a disk above the spindle to a tube around the spindle midzone. Promotes astral microtubule-directed cortical myosin polarization and cleavage furrow ingression. Regulates neuroblast cytokinesis during mid- to late-embryogenesis and is required for ventral enclosure.
Subcellular location: Cytoplasm, cell cortex. Cytoplasm, cytoskeleton. Cytoplasm, cytoskeleton, spindle. Midbody. Cleavage furrow.
Interaction partners:
- Kinesin-like protein
- Rac GTPase-activating protein 1
- Protein ECT2
- Myosin-11
- Septin
- Ras-like GTP-binding protein rhoA
- WAPL domain-containing protein
- Pseudocleavage protein nop-1
- Septin-type G domain-containing protein
- Rho-GAP domain-containing protein
Sequence:
MGDQFDSLMERIRVRQAEMSGEGEVAKENGPVTSKITSVKQEVASPTKVFGSSSKCNDGPSTPVHFHPQEPKETTPNMKENAENSLNSFKDATVNESSSKKTSRFSMLAQEIDEYEYDYQSQYNKPKEAYMKGRSPRMSIGETRPAVLCTPAGAQAMKSPNVAVSSKSAPEIALGMSDFEARRIKFAQPIVNVNYLPNESSIFSGGSGSSVNDQSTVLGGSAEMMNVTTSSLSCGELSMNQHITHENTIINAQSCDNREAILRERQQVSNEEYGPHTFMRKKVPKEASSATSSSSSTTTLTTISGASGSTTSGISNAPQDSASTKTTTNTFTSSYLLTKTSNNNINALVSSSPKPFSKDIGRSMFSPVHFTPKSTSSPKTLSESIFSPSKSAAVEGSIATTRRLQFEEKLKKSSSANVTAPPAPTSAPVPTPRHVAPLAPTVAQQSHLTPNHRHAAQQKKHLFPVVGIVATAPIPVQTQWRGQSNTPVVQGARADEKTAGNEPPVGAGVGKLKNLKSRWEFSSATGTPIHPDATEDSLIATAIKMKESAIPKQLGHRSERKGPSASSLYSQGARSNTASPASKSTRYEQEEEDDVFEAPEFNDGGDVISEDGILQEEEEDTSKFIDNAFGFMEGSGAGTPSPYREPPLQRLEKNRPPAEVIEEETENEDESEPYEPEEEEDDDATTQFPVPERSRKSSSQLAYSVSFYRKIQRDRNEESSTVLAGPVISQISPSAPPMSSSLTSQQKLRQLTTGPANGARIVESAKDAHDRIKRAIQVEEQLVAQSKRAMILARDKPSFRGSREEFEAQWAMLRHVEKHRALLTEYDRLKRDGPRIIDGPRGTITVSQLSVNMARDYVSANIASSKKSDEVFYFAAILRYGEQVDVSKMVTSDGGLNRRGVLEFPVPLMLTGIPPDFRATVEIYGQRSMRESTSHEDKYKLKNSTFKAKTRNTFLGGGSTSSANQSLFVDPAASSSSTSSTTSNFNLLGTFSFDINCPGKHLYNMSHTVYPLEGITQMKVRKQAIDGADITYHGFLSMYQRTGEGLGSWTRYWCALENGEMKFWKQPEDEGTKGYTALMDLSTCCRSEGASVVEDICPFPNSFHIDVWAPKMDTSDPRGIERLRVMLAADTAQDLQTWLSLINSTSKQLCTWRNPIVNQ
Protein: Uncharacterized protein C4B3.18 (Q9USK7)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus {ECO:0000269|PubMed:16823372}.
Interaction partners:
- Pantothenate kinase
- Pantoate--beta-alanine ligase
- Probable thymidylate synthase
- Uncharacterized protein C1F12.08
- Cysteine synthase 1
- Cysteine synthase 2
- Homocysteine synthase
- Cystathionine beta-lyase
- Aspartate aminotransferase, cytoplasmic
- Aspartate aminotransferase, mitochondrial
Sequence:
MPEMDKSNDFFEENPCPNSLGDVSSLIEDFINLQSNSQNIAFVTSGGTLVPLEQNTVRFIDNFSAGNRGAASAEYFCKSGYSVIFLYRNYSLMPFTRRYEGPWTNLFERSNGSQEKPWIVKQEFQSTVFNALNELDTYTKHHRLIMIPYTTLTEYLWYLKAIAERLQIIASRALFYLAAAVSDFHIPPKELSEHKIQSGSGSNKLEVKMHPVPKFLRFLVDTWAPEASIISFKLETDPSILIDKARVALQRYNHQLVIANLLSTRKRSVAFVTSKTVEWLHLSDDDIVKKVEIEQYIVSRAISLHKERIQEFAKAP
Protein: Bifunctional coenzyme A synthase (CoA synthase) (NBP) (POV-2) [Includes: Phosphopantetheine adenylyltransferase (EC 2.7.7.3) (Dephospho-CoA pyrophosphorylase) (Pantetheine-phosphate adenylyltransferase) (PPAT); Dephospho-CoA kinase (DPCK) (EC 2.7.1.24) (Dephosphocoenzyme A kinase) (DPCOAK)] (Q13057)
Organism: Homo sapiens (Human)
Function: Bifunctional enzyme that catalyzes the fourth and fifth sequential steps of CoA biosynthetic pathway. The fourth reaction is catalyzed by the phosphopantetheine adenylyltransferase, coded by the coaD domain; the fifth reaction is catalyzed by the dephospho-CoA kinase, coded by the coaE domain. May act as a point of CoA biosynthesis regulation.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:24360804}. Mitochondrion matrix {ECO:0000269|PubMed:24360804}. Note=The protein is mainly present in the mitochondrial matrix, probably anchored to the inner mitochondrial membrane, but is also present in cell lysate. {ECO:0000269|PubMed:24360804}.
Interaction partners:
- Phosphopantothenoylcysteine decarboxylase
- Phosphopantothenate--cysteine ligase
- Pantothenate kinase 2, mitochondrial
- Pantothenate kinase 1
- Pantothenate kinase 3
- L-aminoadipate-semialdehyde dehydrogenase-phosphopantetheinyl transferase
- Cytochrome c oxidase assembly protein COX19
- Coiled-coil domain-containing protein 30
- Ectonucleotide pyrophosphatase/phosphodiesterase family member 1
- Ectonucleotide pyrophosphatase/phosphodiesterase family member 3
Sequence:
MAVFRSGLLVLTTPLASLAPRLASILTSAARLVNHTLYVHLQPGMSLEGPAQPQSSPVQATFEVLDFITHLYAGADVHRHLDVRILLTNIRTKSTFLPPLPTSVQNLAHPPEVVLTDFQTLDGSQYNPVKQQLVRYATSCYSCCPRLASVLLYSDYGIGEVPVEPLDVPLPSTIRPASPVAGSPKQPVRGYYRGAVGGTFDRLHNAHKVLLSVACILAQEQLVVGVADKDLLKSKLLPELLQPYTERVEHLSEFLVDIKPSLTFDVIPLLDPYGPAGSDPSLEFLVVSEETYRGGMAINRFRLENDLEELALYQIQLLKDLRHTENEEDKVSSSSFRQRMLGNLLRPPYERPELPTCLYVIGLTGISGSGKSSIAQRLKGLGAFVIDSDHLGHRAYAPGGPAYQPVVEAFGTDILHKDGIINRKVLGSRVFGNKKQLKILTDIMWPIIAKLAREEMDRAVAEGKRVCVIDAAVLLEAGWQNLVHEVWTAVIPETEAVRRIVERDGLSEAAAQSRLQSQMSGQQLVEQSHVVLSTLWEPHITQRQVEKAWALLQKRIPKTHQALD
Protein: Inner membrane transport permease YhhJ (P0AGH1)
Organism: Escherichia coli (strain K12)
Subcellular location: Cell inner membrane; Multi-pass membrane protein.
Interaction partners:
- Probable multidrug ABC transporter ATP-binding protein YbhF
- Uncharacterized protein YhiI
- Ribosome-associated ATPase
- Inner membrane amino-acid ABC transporter permease protein YhdY
- Putative transport protein YdiK
- Probable diguanylate cyclase DgcI
Sequence:
MRHLRNIFNLGIKELRSLLGDKAMLTLIVFSFTVSVYSSATVTPGSLNLAPIAIADMDQSQLSNRIVNSFYRPWFLPPEMITADEMDAGLDAGRYTFAINIPPNFQRDVLAGRQPDIQVNVDATRMSQAFTGNGYIQNIINGEVNSFVARYRDNSEPLVSLETRMRFNPNLDPAWFGGVMAIINNITMLAIVLTGSALIREREHGTVEHLLVMPITPFEIMMAKIWSMGLVVLVVSGLSLVLMVKGVLGVPIEGSIPLFMLGVALSLFATTSIGIFMGTIARSMPQLGLLVILVLLPLQMLSGGSTPRESMPQMVQDIMLTMPTTHFVSLAQAILYRGAGFEIVWPQFLTLMAIGGAFFTIALLRFRKTIGTMA