wanglab/gogpt-training-data huggingface dataset:
Protein: Dapper homolog 2 (Frodo 2) (Q673G8)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: Involved in regulation of intracellular signaling pathways during development. Specifically thought to play a role in canonical and/or non-canonical Wnt signaling pathways through interaction with DSH (Dishevelled) family proteins. Positive regulator of the Wnt signaling pathway which acts downstream of wnt1 indicative for non-canonical Wnt signaling. Also negatively regulates the Nodal signaling pathway, possibly by promoting the lysosomal degradation of Nodal receptors. Required for convergent extension movements in gastrulation.
Subcellular location: Cytoplasm. Late endosome. Nucleus. Cell membrane. Note=Predominantly cytoplasmic. Also found in late endosomes, the nucleus and at the cell membrane.
Interaction partners:
- Dapper homolog 3
Sequence:
MLGRKIPGSGVLGAGAGMDRGRTGERLHAALAGLQELHFLRDKQSAMVHWALTLNRDQPDPSKQENVSKEELRLEATLSLLKQQLTRLRRQDVGLKTHLQQLDQQITELKLDVCKASTEHLESDSRPSSGFYELSDGGSGSLSNSCTSVYSESLSSSSQTSLLPLLSTSYASHGRSSCGQTGVSRRCSADESTAQSDAPRSGVKLGSSLIRTATARADRARQRPVSTGDLDRMIGPGFGAFKSTDVKSSTPCSSPQNPSVDPKYQSNLVSSNGTEVYRYPSPLHAVALQSPIFSCTSDQGSSVALDEMPEEETQNLNEESTISSSVGYINKLLQRSSSRVNLLSSIKRIETVSGTHEQIPRSQEMIYGSLNGPQLLGSLQQLSMPLENALETGKTSALNNNQKQMDPPCLGSNFKEVEVQMLHHGKHPESSLDLQKNNFPINNTAGKVGAESDNGASEKRSGHFPKDLSVVQKPVERKSSFTSGREGSRASCHDKSSIPQSEFVHAQFVPAGSQRVKVRQADKKTKSVKLRKKSSEKPSAKKQHQKPLSREFCTKNRTDLKQSGSCRGKVTYLEESQAQSCSDCSCNGLINSHCIQNNHQQIPSSKSTKSRKAPEPVYHPLDHAKKKPSSRKWPSSSEIPLPPTLHTQRSKEMLNSRKVAMVRSVSARPRSGHWGCPPPRALPHSLSTSSYFSYLESRYPAAPVSSRHPPRCESEFSEYSAECASLFHSTIAASSDGEMSDYTTNRFGDSESSQGSQTASESDSSLSLDEEDLLEEEEEDEGGLVWAQAAMGTTAAGFSLQQHHRSESAACRIKASRALKKKIRRFQPASLKVMTLV
Protein: Cruzioseptin-14 (CZS-14) (C0HK10)
Organism: Cruziohyla calcarifer (Splendid leaf frog) (Agalychnis calcarifer)
Function: Has antimicrobial activity.
Subcellular location: Secreted {ECO:0000269|PubMed:27321580}.
Interaction partners:
Sequence:
GFLDIVLHVGLAAGKAALNAVNEAVNQ
Protein: Solute carrier family 37 member 4 (F7EWB7)
Organism: Rattus norvegicus (Rat)
Subcellular location: Endomembrane system {ECO:0000256|ARBA:ARBA00004127}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004127}.
Interaction partners:
Sequence:
MAITALSYSQPCSEATAFTTSTAKPSLLSCPPWWMRSLWTRTIWVSCSLLPFAAGLITSSQSAAYAISKFVSGVLSDQMSARWLFSSGLLLVGLVNVVFSWSSTVTAFAALWFLNGLAQGLGWPPCGKILRKWFEPSQFGTWWAVLSTSMNLAGSLGPILATILAQSYSWRSTLALSGSLCVVVSFFCLLLIHNEPADVGLRNLDPAPSKGKKGSSKEESTLQDLLLSPYLWVLSTGYLVVFGVKTCCTDWGQFFLIQERGQSALVGSSYISALEVGGLVGSIAAGYLSDRAMAKAGLSVYGNPRHSLLLLMMAGMAASMFLFRVTVTSDSPKIWILVLGAVFGFSSYGPIALFGVIANESAPPNLCGTSHAIVGLMANVGGFLAGLPFSTIAKHYSWSTAFWVAEVICIASTVVFFLLRNIRTKMGRVSKKAE
Protein: Myo-inositol transporter 1 (P30605)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Major transporter for myo-inositol.
Subcellular location: Cell membrane {ECO:0000269|PubMed:16233524}; Multi-pass membrane protein {ECO:0000255}. Note=Localizes to the cell membrane in conditions of low inositol. {ECO:0000269|PubMed:16233524}.
Interaction partners:
- Dol-P-Glc:Glc
- Choline transporter
- Inositol-3-phosphate synthase
- Myo-inositol transporter 2
- Phosphatidylserine decarboxylase proenzyme 1, mitochondrial
- Protein INO2
- Transcriptional repressor OPI1
- CDP-diacylglycerol--serine O-phosphatidyltransferase
- Protein INO4
- Phosphatidyl-N-methylethanolamine N-methyltransferase
Sequence:
MGIHIPYLTSKTSQSNVGDAVGNADSVEFNSEHDSPSKRGKITLESHEIQRAPASDDEDRIQIKPVNDEDDTSVMITFNQSLSPFIITLTFVASISGFMFGYDTGYISSALISIGTDLDHKVLTYGEKEIVTAATSLGALITSIFAGTAADIFGRKRCLMGSNLMFVIGAILQVSAHTFWQMAVGRLIMGFGVGIGSLIAPLFISEIAPKMIRGRLTVINSLWLTGGQLVAYGCGAGLNYVNNGWRILVGLSLIPTAVQFTCLCFLPDTPRYYVMKGDLARATEVLKRSYTDTSEEIIERKVEELVTLNQSIPGKNVPEKVWNTIKELHTVPSNLRALIIGCGLQAIQQFTGWNSLMYFSGTIFETVGFKNSSAVSIIVSGTNFIFTLVAFFSIDKIGRRTILLIGLPGMTMALVVCSIAFHFLGIKFDGAVAVVVSSGFSSWGIVIIVFIIVFAAFYALGIGTVPWQQSELFPQNVRGIGTSYATATNWAGSLVIASTFLTMLQNITPAGTFAFFAGLSCLSTIFCYFCYPELSGLELEEVQTILKDGFNIKASKALAKKRKQQVARVHELKYEPTQEIIEDI
Protein: Transcription factor MYB46 (Myb-related protein 46) (AtMYB46) (Q9LXV2)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Transcription activator. Involved in the regulation of secondary wall biosynthesis in fibers and vessels. Transcription activator of the mannan synthase CSLA9 that recognizes and binds to the DNA consensus sequence 5'-[AG][GT]T[AT]GGT[GA]-3' cis-regulatory element of CSLA9 promoter. Transcription factor that acts as molecular switch in the NAC012/SND1-mediated transcriptional network regulating secondary wall biosynthesis. Is directly activated by NAC012/SND1. Functions redundantly with MYB83 in the transcriptional regulatory cascade leading to secondary wall formation in fibers and vessels. Transcription activator that binds to the DNA consensus sequence 5'-ACC[AT]A[AC][TC]-3', designated as the secondary wall MYB-responsive element (SMRE). Regulates directly numerous transcription factors and a number of genes involved in secondary wall biosynthesis that contain SMRE elements in their promoters. Is an obligate component of the transcriptional regulatory complex toward the commitment of secondary wall cellulose synthesis. Is required for functional expression of the three secondary wall CESA genes, CESA4, CESA7 and CESA8.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00625, ECO:0000269|PubMed:16581911, ECO:0000269|PubMed:17890373}.
Interaction partners:
- NAC domain-containing protein 30
- NAC domain-containing protein 43
- Cellulose synthase A catalytic subunit 4
- NAC domain-containing protein 12
- Cellulose synthase A catalytic subunit 8
- Cellulose synthase A catalytic subunit 7
- NAC domain-containing protein 73
- NAC domain-containing protein 66
- Homeobox protein knotted-1-like 7
- NAC domain-containing protein 10
Sequence:
MRKPEVAIAASTHQVKKMKKGLWSPEEDSKLMQYMLSNGQGCWSDVAKNAGLQRCGKSCRLRWINYLRPDLKRGAFSPQEEDLIIRFHSILGNRWSQIAARLPGRTDNEIKNFWNSTIKKRLKKMSDTSNLINNSSSSPNTASDSSSNSASSLDIKDIIGSFMSLQEQGFVNPSLTHIQTNNPFPTGNMISHPCNDDFTPYVDGIYGVNAGVQGELYFPPLECEEGDWYNANINNHLDELNTNGSGNAPEGMRPVEEFWDLDQLMNTEVPSFYFNFKQSI
Protein: Galactose-proton symporter (Galactose transporter) (P0AEP1)
Organism: Escherichia coli (strain K12)
Function: Uptake of galactose across the boundary membrane with the concomitant transport of protons into the cell (symport system).
Subcellular location: Cell inner membrane {ECO:0000269|PubMed:15919996}; Multi-pass membrane protein {ECO:0000269|PubMed:15919996}.
Interaction partners:
- Glucokinase
- L-fucose-proton symporter
- UDP-galactopyranose mutase
- PTS system glucose-specific EIICB component
- HTH-type transcriptional regulator GalS
- Phosphoenolpyruvate-protein phosphotransferase
- HTH-type transcriptional regulator GalR
- PTS system glucose-specific EIIA component
- Phospho-2-dehydro-3-deoxyheptonate aldolase, Phe-sensitive
Sequence:
MPDAKKQGRSNKAMTFFVCFLAALAGLLFGLDIGVIAGALPFIADEFQITSHTQEWVVSSMMFGAAVGAVGSGWLSFKLGRKKSLMIGAILFVAGSLFSAAAPNVEVLILSRVLLGLAVGVASYTAPLYLSEIAPEKIRGSMISMYQLMITIGILGAYLSDTAFSYTGAWRWMLGVIIIPAILLLIGVFFLPDSPRWFAAKRRFVDAERVLLRLRDTSAEAKRELDEIRESLQVKQSGWALFKENSNFRRAVFLGVLLQVMQQFTGMNVIMYYAPKIFELAGYTNTTEQMWGTVIVGLTNVLATFIAIGLVDRWGRKPTLTLGFLVMAAGMGVLGTMMHIGIHSPSAQYFAIAMLLMFIVGFAMSAGPLIWVLCSEIQPLKGRDFGITCSTATNWIANMIVGATFLTMLNTLGNANTFWVYAALNVLFILLTLWLVPETKHVSLEHIERNLMKGRKLREIGAHD
Protein: Cell division cycle protein 27 homolog (Q6GQ04)
Organism: Xenopus laevis (African clawed frog)
Interaction partners:
Sequence:
MTVLQEPVQAAIWQALNHYAYRDAVFLAERLYAEVHSEEALFLLATCYYRSGKAYKAYRLLKAHSCTTPQCKYLLAKCCVDLGKLAEGEQILSGGVLNKQKSQEEIVTEFGDSACFTLSLLGHVYCKTDRLAKGAECYQKSLSLNPFLWSPFESLCEIGEKPDAEQTFKLTSLQSFSNCVPNTCTMTVNTHSVVQHRQPDTVLMETPQDTIELNRLNLESSNIKYPLNSDSSISYIDPGVISPDSLPLGTGNAILSKQVQNKPKTGRSLLGGPAALSPLTPSFGILPLETPSPGDGSYLQSYNSSCVLDVPSSGAPTKKSVARISQAGTKSVFSQSGNSRDVTPVLLVQTQGSGPQTSTTPQVLSPTIAAPPNALPRRSSRLFTSDSSTTKENSKKLKMKFPPKMPNRKTKSKTSKGGGTQTNLNDSLEISKLDSSIISEGKISSVAPQIQALTIQKAAAEGLMSLLRDMGKGYVALCSYNCKEAINILSHLPSHHYNTGWVLCQIGRAYFELAEYLQAERVFSEVRRIESYRVEGMEIYSTTLWHLQKDVALSVLSKDLTDMDKNSPEAWCAAGNCFSLQREHDIAIKFFQRAIQVDPGYAYAFTLLGHEFVLTEELDKALACFRNSIRVNSRHYNAWYGLGMIYYKQEKFSLAEMHFQKALDINPQSSVLLCHIGVVQHALKKSDKALDTLNKAISIDPKNPLCKFHRASILFANEKYKLALQELEELKQIVPKESLVYFLIGKVYKKLGQTHLALMNFSWAMDLDPKGANNQIKEAIDKRYLPDDEEAVTQEEQISECYPYESVATDESQESSMTDADDTQLHAAESDEF
Protein: Glutamate 2,3-aminomutase (EC 5.4.3.9) (Q185C5)
Organism: Clostridioides difficile (strain 630) (Peptoclostridium difficile)
Function: Catalyzes the interconversion of L-glutamate and L-beta-glutamate. Does not have L-lysine 2,3-aminomutase activity.
Interaction partners:
- protein-glutamate O-methyltransferase
Sequence:
MNEQTRISLERAAELKSKIDDYIQARKTINRGLEKEEEINKRKQKILSILNGTEEDWNNYKWQLSNRITDVDTLSKIITLTKKEKEYIKEVGTQFRWAISPYYLSLIDPEDICDPIKLLSIPTHIELEDEQEDLDPMGEEYTNPAGCITRRYPDRLIINVTNECAMYCRHCQRRRNIGQQDSHKSKAIIQESIDYIRENEEIRDVLVTGGDALTLKDDYLEWILSQLKEIPHVDYVRLGTRTLVTMPQRITDEFCNMLKKYHPVYINTHFNHPMEITKESKEACEKLANAGVPLGNQAVLLNGINNDKFVMRCLNQELLKIRVKPYYIFQSKHVKGTKHFNTSVDDGLEIMEYLRGYTSGMAIPTYIVNAPKGGGKTPLLPQYLVSKGTDYVMLRTWEGKVIKMEDEPAVDIKKLIKEQAQD
Protein: Guanine nucleotide-binding protein G(I)/G(S)/G(T) subunit beta-1 (Transducin beta chain 1) (P62871)
Organism: Bos taurus (Bovine)
Function: Guanine nucleotide-binding proteins (G proteins) are involved as a modulator or transducer in various transmembrane signaling systems. The beta and gamma chains are required for the GTPase activity, for replacement of GDP by GTP, and for G protein-effector interaction.
Interaction partners:
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein G
- Rhodopsin
- Guanine nucleotide-binding protein G
- Beta-adrenergic receptor kinase 1
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein subunit alpha
Sequence:
MSELDQLRQEAEQLKNQIRDARKACADATLSQITNNIDPVGRIQMRTRRTLRGHLAKIYAMHWGTDSRLLVSASQDGKLIIWDSYTTNKVHAIPLRSSWVMTCAYAPSGNYVACGGLDNICSIYNLKTREGNVRVSRELAGHTGYLSCCRFLDDNQIVTSSGDTTCALWDIETGQQTTTFTGHTGDVMSLSLAPDTRLFVSGACDASAKLWDVREGMCRQTFTGHESDINAICFFPNGNAFATGSDDATCRLFDLRADQELMTYSHDNIICGITSVSFSKSGRLLLAGYDDFNCNVWDALKADRAGVLAGHDNRVSCLGVTDDGMAVATGSWDSFLKIWN
Protein: FlaA locus uncharacterized protein YlxG (ORF 8) (P23455)
Organism: Bacillus subtilis (strain 168)
Interaction partners:
- Flagellar biosynthetic protein FlhB
- Flagellar M-ring protein
- Flagellum-specific ATP synthase
- Flagellar motor switch phosphatase FliY
- Flagellar motor switch protein FliM
- Flagellar basal-body rod protein FlgC
- Probable flagellar hook-length control protein
- Flagellar hook-associated protein 1
- Flagellar hook-basal body complex protein FliE
- Flagellar basal body rod protein FlgB
Sequence:
MTSISSEYKLPEKTNTVSTNNSSLGKDEFLKILMTQVQNQDPLNPIDDKEFISQMATFSSLEQMMNLNTTMTQFVENQDPFTTYVDWMGKEVSWTDGKSATDKTGTVSSVKHFKGNYYLVLDDGTEISPANVMSVGQSSK
Protein: Interferon lambda-1 (IFN-lambda-1) (Cytokine Zcyto21) (Interleukin-29) (IL-29) (Q8IU54)
Organism: Homo sapiens (Human)
Function: Cytokine with antiviral, antitumour and immunomodulatory activities. Plays a critical role in the antiviral host defense, predominantly in the epithelial tissues. Acts as a ligand for the heterodimeric class II cytokine receptor composed of IL10RB and IFNLR1, and receptor engagement leads to the activation of the JAK/STAT signaling pathway resulting in the expression of IFN-stimulated genes (ISG), which mediate the antiviral state. Has a restricted receptor distribution and therefore restricted targets: is primarily active in epithelial cells and this cell type-selective action is because of the epithelial cell-specific expression of its receptor IFNLR1. Exerts an immunomodulatory effect by up-regulating MHC class I antigen expression.
Subcellular location: Secreted.
Interaction partners:
- Interferon lambda receptor 1
- Interleukin-10 receptor subunit beta
- Interferon lambda-3
- Interferon lambda-2
- Interferon beta
- Interferon alpha/beta receptor 1
- Interleukin-20 receptor subunit alpha
- Tyrosine-protein kinase JAK1
- Interferon alpha-2
- Interferon alpha/beta receptor 2
Sequence:
MAAAWTVVLVTLVLGLAVAGPVPTSKPTTTGKGCHIGRFKSLSPQELASFKKARDALEESLKLKNWSCSSPVFPGNWDLRLLQVRERPVALEAELALTLKVLEAAAGPALEDVLDQPLHTLHHILSQLQACIQPQPTAGPRPRGRLHHWLHRLQEAPKKESAGCLEASVTFNLFRLLTRDLKYVADGNLCLRTSTHPEST
Protein: Heparan sulfate 2-O-sulfotransferase 1 (2-O-sulfotransferase) (2OST) (EC 2.8.2.-) (Q7LGA3)
Organism: Homo sapiens (Human)
Function: Catalyzes the transfer of sulfate to the C2-position of selected hexuronic acid residues within the maturing heparan sulfate (HS). 2-O-sulfation within HS, particularly of iduronate residues, is essential for HS to participate in a variety of high-affinity ligand-binding interactions and signaling processes. Mediates 2-O-sulfation of both L-iduronyl and D-glucuronyl residues (By similarity).
Subcellular location: Golgi apparatus membrane {ECO:0000250|UniProtKB:Q8R3H7}; Single-pass type II membrane protein {ECO:0000250|UniProtKB:Q8R3H7}.
Interaction partners:
- Heparan-sulfate 6-O-sulfotransferase 1
- D-glucuronyl C5-epimerase
- Heparan sulfate glucosamine 3-O-sulfotransferase 1
- Bifunctional heparan sulfate N-deacetylase/N-sulfotransferase 1
- Bifunctional heparan sulfate N-deacetylase/N-sulfotransferase 2
- Exostosin-1
- Exostosin-2
- Heparan sulfate glucosamine 3-O-sulfotransferase 5
- Bifunctional heparan sulfate N-deacetylase/N-sulfotransferase 3
- Heparan-sulfate 6-O-sulfotransferase 2
Sequence:
MGLLRIMMPPKLQLLAVVAFAVAMLFLENQIQKLEESRSKLERAIARHEVREIEQRHTMDGPRQDATLDEEEDMVIIYNRVPKTASTSFTNIAYDLCAKNKYHVLHINTTKNNPVMSLQDQVRFVKNITSWKEMKPGFYHGHVSYLDFAKFGVKKKPIYINVIRDPIERLVSYYYFLRFGDDYRPGLRRRKQGDKKTFDECVAEGGSDCAPEKLWLQIPFFCGHSSECWNVGSRWAMDQAKYNLINEYFLVGVTEELEDFIMLLEAALPRFFRGATELYRTGKKSHLRKTTEKKLPTKQTIAKLQQSDIWKMENEFYEFALEQFQFIRAHAVREKDGDLYILAQNFFYEKIYPKSN
Protein: Misexpression suppressor of ras 4, isoform C (A0A0B4LFV9)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MMEALDQQQAKLTSNRDDGEAGRGSETGSEEGTGAGAAAGEEDDIEELHYVLDQAKEENESHQHGQNNNAKGNEDGKPKKNDDVIDVTMANGQGFKDTPEEETTGTEETAETEETAETEEAEQAEESLLNSRKSTDTPVDLGANCLTTGSPSKDLVKQELVEDKSEELKEPTSISLNEQFLDDIELKTEVEDKSDSLSETHMEFLTDSEEQPSESLGANHESEIDEKVDHFQPKESDSNEVEDKYFQSANEDSESEIEETVYTPPVINLETDSESGDKEFISIKDNESPVLEIEGGTEKSQTSGDLYQADVGEYASTAPPEVDETTSQTIGVPSLEGSDTLDSPSLTMDVDLPCSEDGAPPNVIKIESDMEDEAHSDSVKLKEHTVEVVPLIKLNGAHKALKEEKLEDGEVEEVEDPGEELEDPKEQSVITNHTGNNTKEEDTTASQVSALPLILPVGTTRSRSISSRSSTVSSASQPHLVIDHPESEHNAKPPALKLSLKRRRSKSSSVSQPEKQTKVEAGGFVSSLLLQRLQSNSNVIPPAISTESQQVLSCAKCNLQFDFERFQELNKHQAQCSGIQSANSSQLSQKQERFFRCSQCCSVHQCWHFFLHMREVHRRYICLYCNHVYPSVEKLSLHLENKHDIDQSHFAKDAWDQQQSKEDRARHLVCCTCQATFVQGSEFEDHDCSQLMQPCALCNQKGGHIIGCKNNKRKPTKRRRKVRRPPEPPLPVSQEAVEQPVPVEAIPEQLPQQLHLQSDIQNPFPAENTPEPVEDPPAPPIPKLVVPKIMLRVPKEFQKSVDAALSSTDTEDEELETAQPVEEAVSAPPEDLPFDAPPPPPPALSYDDSTSSKLNRVLAELERTKLDIERTKADIITKKQSKIIMANAHLENVVPQVVDPPQHLQPQQEEQRRWSLTPPASPHNNHVNLPEPPPALITEFQGQPDAVRRNSLGSDCMDMDDSLNAPEMEGSRDFTEAQKETLEPAPPSQDTQTADEPLAIQPLPPADGIMVAGPDTHTVDLQLDRPLDRFSMVDFVRLCLKSVYSLCLYCNHARRIAVNVKQLVIHLIGQHRFTATVDSITAEELYAETIVAKLKSFLPNLENEYMNAASCCSLENGKYVEPFNERIYECFTCRFVTSTHKELYTHNRRLHIKSNITCVMCQTNFYSYSEILCHICPGEVAGSVYDLQFRCCLCDMAPLPSAFRLMVHLRKQHQACDICLEDCQSQSKLSSHVWKHKLLHLCYRCGIAYRNKQDISKHLFWKHGTESAGCKQCLQKRWRHVYHFCVPPAEFPCEQCGFVFSKAIYLEVHQRMHTGDFRYACTEEGCEEKFVSRKLLLKHASSHVAKELPQAVSVEQTADAAPTEKLEDIKEELEEGEDEKEGAHNQEKLLSESLTNNETPKKEESDRIDNSIEPPLSKSENRKRRKKSKRNKESLEDLNLIAPNLSESDSSDDSDSDAPRSSHQEQPKLPMRSSVDDLDMPKVMLSPSSESDADELDGKSKLEDKEEKPLDGSTEEKALDADDELEPKKEEDQVDVSIWKNLLQNQAVAIPEEQAVKDEEREDSLVNLPPAKLHVAWSDHDYCKLYRTPAPSPVKQKSANKSSIKTPGENASSDSDSSSSSSSSDSDSSSCSCGSNCSCSSSNSSSSSGNSDDSDSSTARGSPQKRSRKKSLKVKKSSESLKIDQNGQNEQNQVEDTTAVNENNNPVAPPSPKPPMYNESDFDTAFSDTDEEFYDSHPQKLANELLTQKREALMAEHAPMRPSNNYDIVENSRPSTPSLPEEASAFADKREKVRNKKKKRERKSTCKSGKLQPVASTTPPPMDRIPGMPGMIAPLEPPTPILSHPESSLFPVTPLTHRQLQSSMTRMSEGSSCSDADGQLKRSKRQRRPNKFYGYTSDDENMSAVLAPPLQVGMQLIKPQPPPQLTWAKEDLPTPPKQRNRNNNNSSHHHHSHSNGGMAGSSRKRSKQRSLFGAGGSRPAKRHKPDPNDHLPPIPTLKIRPSLLPTTAPPSDSSESSSDDEEAEVNVTSVVPTPQPAPPPVLPTPLPVALPVPPPPPPAATAFNQPIPPALLPNPGFATLQYFKANNIRYPIRPPAGARLAREGESVYCYCRCPYDEVSEMIACDGDNCLIEWFHFECVGIMVAPQGKWFCAECRPKYSEGIYQGAKPQ
Protein: Thymus-specific serine protease (EC 3.4.-.-) (Serine protease 16) (Q9NQE7)
Organism: Homo sapiens (Human)
Function: Protease that may play a role in T-cell development.
Subcellular location: Cytoplasmic vesicle. Note=Vesicular, either lysosomal or endosomal.
Interaction partners:
- Proteasome subunit beta type-11
- Prolyl endopeptidase
Sequence:
MAVWLAQWLGPLLLVSLWGLLAPASLLRRLGEHIQQFQESSAQGLGLSLGPGAAALPKVGWLEQLLDPFNVSDRRSFLQRYWVNDQHWVGQDGPIFLHLGGEGSLGPGSVMRGHPAALAPAWGALVISLEHRFYGLSIPAGGLEMAQLRFLSSRLALADVVSARLALSRLFNISSSSPWICFGGSYAGSLAAWARLKFPHLIFASVASSAPVRAVLDFSEYNDVVSRSLMSTAIGGSLECRAAVSVAFAEVERRLRSGGAAQAALRTELSACGPLGRAENQAELLGALQALVGGVVQYDGQTGAPLSVRQLCGLLLGGGGNRSHSTPYCGLRRAVQIVLHSLGQKCLSFSRAETVAQLRSTEPQLSGVGDRQWLYQTCTEFGFYVTCENPRCPFSQLPALPSQLDLCEQVFGLSALSVAQAVAQTNSYYGGQTPGANKVLFVNGDTDPWHVLSVTQALGSSESTLLIRTGSHCLDMAPERPSDSPSLRLGRQNIFQQLQTWLKLAKESQIKGEV
Protein: Run domain Beclin-1-interacting and cysteine-rich domain-containing protein (Rubicon) (Q80U62)
Organism: Mus musculus (Mouse)
Function: Inhibits PIK3C3 activity; under basal conditions negatively regulates PI3K complex II (PI3KC3-C2) function in autophagy. Negatively regulates endosome maturation and degradative endocytic trafficking and impairs autophagosome maturation process. Can sequester UVRAG from association with a class C Vps complex (possibly the HOPS complex) and negatively regulates Rab7 activation (By similarity).
Subcellular location: Late endosome {ECO:0000269|PubMed:19270693}. Lysosome {ECO:0000269|PubMed:19270693}. Early endosome {ECO:0000269|PubMed:19270693}. Note=Predominantly located in late endosomes/lysosomes, only partially detected in early endosome and not at all in the Golgi apparatus.
Interaction partners:
- UV radiation resistance-associated protein
- Beclin-1
- Phosphatidylinositol 3-kinase catalytic subunit type 3
- Phosphoinositide 3-kinase regulatory subunit 4
- Beclin 1-associated autophagy-related key regulator
- Ras-related protein Rab-7a
- Activating molecule in BECN1-regulated autophagy protein 1
Sequence:
MRPEGAGMDLGGGDGERLLEKSRREHWQLLGNLKTTVEGLVSANCPNVWSKYGGLERLCRDMQNILYHGLIHDQVCCRQADYWQFVKDIRWLSPHSALHVEKFISLHESDQSDTDSVSERAVAELWLQHSLQCHCLSAQLRPLLGDRQYIRKFYTETAFLLSDAHVTAMLQCLEAVEQNNPRLLAQIDASMFARKQESPLLVTKSQSLTALPGSTYTPPASYAQHSYFGSSSSLQSMPQSSHSSERRSTSFSLSGPSWQPQEDRECLSPAETQTTPAPLPSDSTLAQDSPLTAQEMSDSTLTSPLEASWVSSQNDSPSDVSEGPEYLAIGNPAPHGRTASCESHSSNGESSSSHLFSSSSSQKLESAASSLGDQEEGRQSQAGSVLRRSSFSEGQTAPVASGTKKSHIRSHSDTNIASRGAAGGPRNITIIVEDPIAEGGQYLCSGEGMFRRPSEGQSLISYLSEQDFGSCADLEKENAHFSISESLIAAIELMKCNMMSQCLEEEEVEEEDSDREIQELKQKIRLRRQQIRTKNLLPAYRETENGSFRVTSSSSQFSSRDSTQLSESGSAEDADDLEIQDADIRRSAVSNGKSSFSQNLSHCFLHSTSAEAVAMGLLKQFEGMQLPAASELEWLVPEHDAPQKLLPIPDSLPISPDDGQHADIYKLRIRVRGNLEWAPPRPQIIFNVHPAPTRKIAVAKQNYRCAGCGIRTDPDYIKRLRYCEYLGKYFCQCCHENAQMVVPSRILRKWDFSKYYVSNFSKDLLLKIWNDPLFNVQDINSALYRKVKLLNQVRLLRVQLYHMKNMFKTCRLAKELLDSFDVVPGHLTEDLHLYSLSDLTATKKGELGPRLAELTRAGAAHVERCMLCQAKGFICEFCQNEEDVIFPFELHKCRTCEECKACYHKTCFKSGRCPRCERLQARRELLAKQSLESYLSDYEEEPTEALALEATVLETT
Protein: FERM domain-containing protein 4B (GRP1-binding protein GRSP1) (Golgi-associated band 4.1-like protein) (GOBLIN) (Q920B0)
Organism: Mus musculus (Mouse)
Function: Member of GRP1 signaling complexes that are acutely recruited to plasma membrane ruffles in response to insulin receptor signaling. May function as a scaffolding protein that regulates epithelial cell polarity by connecting ARF6 activation with the PAR3 complex. Plays a redundant role with FRMD4A in epithelial polarization.
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000269|PubMed:11445584}. Cell junction, tight junction {ECO:0000269|PubMed:20080746}. Cell junction, adherens junction {ECO:0000269|PubMed:20080746}. Note=Colocalized with PARD3 at adherens junction and tight junction (PubMed:20080746). {ECO:0000269|PubMed:20080746}.
Interaction partners:
- Cytohesin-1
- Cytohesin-3
Sequence:
MASVFMCGVEDLLFSGSRFVWNLTVSTLRRWYTERLRACHQVLRTWCGLRDVYQMTEGRHCQVHLLDDRRLELLVQPKLLSRELLDLVASHFNLKEKEYFGITFIDDTGQENWLQLDHRVLEHDLPKKPGPTLLHFAVRFYIESISFLKDKNTVELFFLNAKACVHKGQIEVDSETIFKLAALVLQESKGDYTSDENARKDLKTLPVFPTKTLQEHPSLAYCEDRVIEHYLKIKGLTRGQAVVQYMKIVEALPTYGVHYYAVKDKQGLPWWLGISYKGIGQYDLQDKVKPRKLFQWKQLENLYFREKKFAVEVHDPRRISVSRRTFGQSGLFVQTWYANSSLIKSIWVMAISQHQFYLDRKQSKAKIPSARSLDDIAMDLTETGTQRGSKLVTLEAKSQFIMASNGSLISSGSQDSEGMEEQKREKILELKKKEKLLQEKLLQKVEELKKICLREAELTGRMPKEYPLNIGEKPPQVRRRVGTTFKLDDNLLPTEEDPALQELESNFLIQQKLVEAAKKLASEPDLCKTVKKKRKQDYTDAVKRLQEIENSINEYRIRCGKKPSQKAAVVPPEDIIPSESSSLSDTTTYDDPNDSFTLAGQRPSSVPHSPRILPPKSLGIERIHFRKSSINEQFMDTRHSREMLSTHSSPYKTLERRPQGGRSMPTTPVLTRNAYSSSHLEPDSSSQHCRQRSGSLESQSHLLSEMDSDKPFFTLSKSQRSSSTEILDDGSSYTSQSSSEYYCVTPAASPYYTTQTLDTRARGRRRSKKHSVSTSNSGSMPNLAQKDPLRNGVYSKGQDPPPSGYYIAGYPPYAECDLYYSGGYVYENDTEGQYSVNPSYRSSAHYGYDRQRDYSRSFHEDEVDRVPHNPYATLRLPRKAAVKSEHITKNIHKALVAEHLRGWYQRASGQKDQGHSPQTSFDSDRGSQRCLGFAGLQVPCSPSSRASSYSSVSSTNASGNWRTQLTIGLSEYENPVHSPYTSYYGSIYNPLSSPSRQYAETTPLDGTDGSQLEDNLEGSEQRLFWHEDSKPGTLV
Protein: Monalysin (beta-barrel pore-forming toxin) (beta-PFT) (Q1I8U1)
Organism: Pseudomonas entomophila (strain L48)
Function: Pore-forming toxin that contributes to the virulence of P.entomophila against Drosophila, playing an important role in host intestinal damage and lethality. Displays cytolytic and hemolytic activity.
Subcellular location: Secreted {ECO:0000269|PubMed:21980286}. Host cell membrane {ECO:0000305|PubMed:21980286}.
Interaction partners:
Sequence:
MTIKEELGQPQSHSIELDEVSKEAASTRAALTSNLSGRFDQYPTKKGDFAIDGYLLDYSSPKQGCWVDGITVYGDIYIGKQNWGTYTRPVFAYLQYVETISIPQNVTTTLSYQLTKGHTRSFETSVNAKYSVGANIDIVNVGSEISTGFTRSESWSTTQSFTDTTEMKGPGTFVIYQVVLVYAHNATSAGRQNANAFAYSKTQAVGSRVDLYYLSAITQRKRVIVPSSNAVTPLDWDTVQRNVLMENYNPGSNSGHFSFDWSAYNDPHRRY
Protein: Deoxyhypusine hydroxylase (DOHH) (EC 1.14.99.29) (Deoxyhypusine dioxygenase) (Deoxyhypusine monooxygenase) (Q17949)
Organism: Caenorhabditis elegans
Function: Catalyzes the hydroxylation of the N(6)-(4-aminobutyl)-L-lysine intermediate produced by deoxyhypusine synthase/DHPS on a critical lysine of the eukaryotic translation initiation factor 5A/eIF-5A. This is the second step of the post-translational modification of that lysine into an unusual amino acid residue named hypusine. Hypusination is unique to mature eIF-5A factor and is essential for its function.
Interaction partners:
- Deoxyhypusine synthase
- Eukaryotic translation initiation factor 5A-2
- Eukaryotic translation initiation factor 5A-1
- Small ribosomal subunit protein mS29
- Adenylosuccinate synthetase
- Bifunctional glyoxylate cycle protein
- Probable multifunctional protein ADE2
- Bifunctional purine biosynthesis protein ATIC
- Ornithine decarboxylase
- Probable succinyl-CoA:3-ketoacid coenzyme A transferase, mitochondrial
Sequence:
MVASQKFSDAEIDSFGEALNDTKKPLKARFRALFILRNIGCDRSVDWIGKCLNDESALLKHELAYCLGQMQNKHAIPTLVSVLEDEKQEPMVRHEAGEALGAIADPSVKDVLRKYAQDPCPEVSETCQIALGRVEWVEKSGKDTNSPYDSVDPTPSASTSDVEELAATLIDASLPLFDRYRAMFSLRNIKTDKSIKALAQGLYCEDSALFRHEVAYVLGQLQSPVATQELKDRLLLSTENCMVRHECAEALGAIANEECTEILKQYVNDEERVVRESCEVALDMAEYENSDDLQYAHV
Protein: Septin (Q7KLG8)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Protein peanut
- Septin-1
- Septin
- Septin-2
- AT21693p
- Anillin
Sequence:
MVHLVTEKKTQEVATKVPRLLQLGGHVGFDTLPDQLVNKSVQNGFSFNILCIGETALGKSTLMDTLFNTSFGSTPSPHNLPNVKLKANTYELQESNVRLKLTVCDTIGYGDQVNKADSYKALVEYVDSQFEAYLQEELKIQRAMASAHDGRVHACLYFICPTGHGLKAMDLVCMKQLDTRVNIIPVIAKADTISKSELSGFKERIMDELRRNNVSIYQFPMDDETVSETNAAMNGHLPFAVVGSTEFVKVAGKQVRARQYPWGAVHIENEAHCDFVKLREMLIRTNMEDLREQTHTRHYELFRQRRLQQMGFVDVDSNNQPVSFQQTFESKRSDHLACLQAKEEEVRQMFVQRVKQKENELKDNEKELHTKFDRLKREHLEEKAQLEEARRQLEEDCQELQRRRLQMANGSHTLTLGRGKKK