wanglab/gogpt-training-data huggingface dataset:
Protein: Shal K[+] channel interacting protein, isoform I (A0A0B4KHV7)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Frizzled
Sequence:
MAVSNIVCEWLRALGLAQYAESFLDNGYDDLEICKQVGDPDLDAIGVENPAHRHKLLKSIRSLREKGAASVYFMLNDPNSLSGSMEILCETPPNNELELVLREQLETDGVRLTAHPYSTPPSSCLSDKEEDEIYGFGYGVFAPRVARGGLTQQQQLLQQQTLQTQQSIQQQQQQMQQQQQQLPIVPGQQQQGPHQHQTLPPNVAHLNFVQQNCLSPRSAYFYEFPPTAEGRETKKRTTLARLLKGLKTVNRRDRNNQQNGAQARAANDRLRHFQMINGGAGGQQHSFEETIHRLKVQEAMRKKEKFQREHEEILRDIRQGLLQMSRGEGRMDDTYMYDEALRTGGGMGIAGLGMPLGVGGNGGGGGAAHYAVSALHHQGHWYDEPPYESDPDDFLMAGLNCGPAATIQGGRVRFSNNRESTGVISLRSAGDISLPQRGPPRRGLIVPQQPPNPPTIIPLTHARSHDRESGDYAGSISDLQSVTSRFSTVSIGTNNCTARYRTLSGGIGESPSLSPSPSSDYEDIGVTRGHGCLPPSLLAAKAKKNGLPHGKANTICQKATVHHSGEMRSSAKEIGAFNENGRNFVATKDTSRDFSNSQDNTDRGSMSDQAFACSASSVESLPSASGSSTQALVRPGSPHSSISAEDRTSMASCICKAKALVDSLPNPYDKEALKFKKGDLIDVLSMNASGIWKGRCHGRVGHFKFINVEVLPEQRMKNSSSKTLAAGSRLANSGNGSHNGGPCSVEDLLIRIGLKEYTSVFVLNGYEDLELFKELEPADLDYLGILNQEHRAKLLTAVQLLHDIECSDVDIPGSSSENDEARLNNINMKHGASPFGRRHFPRDSGCYEGSPLPSSQTPTQAVNSTDESNSLDDVVTKCSSEIMKRVESARRCKDNPFKTTLPGGGRLGKKSFLGGNGLMADDTLTRGGLSEKSSDSGVSSSSLSSGPLKSSTXHLPTILAHELLLGVGSGMGMGLGLGTMSHGTTGTLTPHGVATATSPTAHSAPLGNICNTLPHAPSSSGGGGVSSSMASNLPLNRNLVMLRNHLRKNTGGSITGNGGVGASGVGAQLLQDQDDRLEDQ
Protein: Dimethyladenosine transferase (EC 2.1.1.183) (18S rRNA (adenine(1779)-N(6)/adenine(1780)-N(6))-dimethyltransferase) (18S rRNA dimethylase) (S-adenosylmethionine-6-N', N'-adenosyl(rRNA) dimethyltransferase) (P41819)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Specifically dimethylates two adjacent adenosines in the loop of a conserved hairpin near the 3'-end of 18S rRNA in the 40S particle.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:12628929}. Nucleus, nucleolus {ECO:0000269|PubMed:12628929}.
Interaction partners:
- Serine/threonine-protein kinase RIO2
- Ribosome biogenesis protein TSR1
- Essential nuclear protein 1
- Protein LTV1
- Periodic tryptophan protein 2
- U3 small nucleolar ribonucleoprotein protein IMP4
- U3 small nucleolar RNA-associated protein 12
- Nucleolar complex protein 4
- U3 small nucleolar RNA-associated protein 22
- Ribosomal RNA-processing protein 9
Sequence:
MGKAAKKKYSGATSSKQVSAEKHLSSVFKFNTDLGQHILKNPLVAQGIVDKAQIRPSDVVLEVGPGTGNLTVRILEQAKNVVAVEMDPRMAAELTKRVRGTPVEKKLEIMLGDFMKTELPYFDICISNTPYQISSPLVFKLINQPRPPRVSILMFQREFALRLLARPGDSLYCRLSANVQMWANVTHIMKVGKNNFRPPPQVESSVVRLEIKNPRPQVDYNEWDGLLRIVFVRKNRTISAGFKSTTVMDILEKNYKTFLAMNNEMVDDTKGSMHDVVKEKIDTVLKETDLGDKRAGKCDQNDFLRLLYAFHQVGIHFS
Protein: Large ribosomal subunit assembly factor BipA (EC 3.6.5.-) (GTP-binding protein BipA) (Q9HU67)
Organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Subcellular location: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00849}. Note=Binds to ribosomes. {ECO:0000256|HAMAP-Rule:MF_00849}.
Interaction partners:
- Elongation factor Ts
- GMP synthase
- Large ribosomal subunit protein uL1
- Ribosome-binding ATPase YchF
- GTPase Der
- Trigger factor
Sequence:
MIENLRNIAIIAHVDHGKTTLVDKLLKLSGTLDRKEAESERVMDSNDQEKERGITILAKNTAIKWNGYNINIVDTPGHADFGGEVERVMSMVDSVLLVVDAQDGPMPQTRFVTQKAFKAGLRPIVVVNKIDRPGARPDWVIDQIFDLFDNLGATDEQLDFPIVYASALNGIAGLDHEKMDDNMDALFQAIIDHVPAPVVDTEGPFQMQISQLDYNSFLGVIGIGRITRGKVKSNTPVVAISDDGSKRNGRILKIMGHHGLQRVEVAEAEAGDIVCVSGMEELFISDTLCDPQNVEALPPLTVDQPTVSMTFQVNDSPFAGREGKFVTSRNIKERLEKELLHNVALRVEPGDSPEKFKVSGRGELHLSVLIETMRREGFELAVGRPEVVIIEKDGEKQEPYENVTIDIEEQHQGSVMEQMGLRKGDLSNMIPDGKGRVRLEYTIPARGLIGFRNNFLTLTSGTGILTSTFSHYGPIKAGEVSNRQNGVLVSMATGTALTYSLETLQSRGKLFLGPGDEIYEGQLAGINSRDNDLVINPTKGKKLDNMRASGKDEVIALVPPIRFTLEQALEFIADDELVEVTPKSIRLRKKMLNENDRKRYERSKV
Protein: G protein-coupled receptor class C group 5 member A (F5GWG3)
Organism: Homo sapiens (Human)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004651}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}.
Interaction partners:
Sequence:
MATTVPDGCRNGLKSKYYRLCDKAEAWGIVLETVATAGVVTSVAFMLTLPILVCKVQDSNRRKMLPTQFLFLLGVLGIFGLTFAFIIGLDGSTGPTRFFLFGILFSICFSCLLAHAVSLTKLVRGRKPLSLLVILGLAVGFSLVQDVIAIEYIVLTMNRTNVNVFSELSAPRRNEDFVLLLTYVLFLMALTFLMSSFTFCGSFTGWKRHGAHIYLTMLLSIAIWVAWITLLMLPDFDRRWDDTILSSALAANGWVFLLAYVSPEFWLLTKQRN
Protein: Probable proteasome subunit beta type-3 (Q9Y7T8)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Non-catalytic component of the proteasome, a multicatalytic proteinase complex which is characterized by its ability to cleave peptides with Arg, Phe, Tyr, Leu, and Glu adjacent to the leaving group at neutral or slightly basic pH. The proteasome has an ATP-dependent proteolytic activity (By similarity).
Subcellular location: Cytoplasm {ECO:0000255|PROSITE-ProRule:PRU00809, ECO:0000269|PubMed:16823372}. Nucleus {ECO:0000269|PubMed:16823372}.
Interaction partners:
- Probable proteasome subunit alpha type-5
- Probable proteasome subunit alpha type-3
- Probable proteasome subunit beta type-7
- Probable proteasome subunit beta type-2
- Probable proteasome subunit beta type-1
- Probable proteasome subunit beta type-4
- Probable proteasome subunit alpha type-7
- Probable proteasome subunit alpha type-6
- Probable proteasome subunit alpha type-1
- Probable proteasome subunit beta type-6
Sequence:
MSIMEYNGGSCVAMAGKNCVAIASDLRLGVQSISLTNNFPKVFAMGDKTYLGLTGLATDVQTLYELFRYKVNLYKFREERQIQPKTFANLVSSTLYEKRFGPYFSFPVVAGVSNDNTPFICGFDSIGCIDFAEDFIVSGTATEQLYGMCESVYEPNLEPDDLFETISQALLNAQDRDCISGWGCVVYVITADKCIKRLVKGRQD
Protein: Beta-crystallin B2 (Beta-B2 crystallin) (Beta-crystallin Bp) (P43320)
Organism: Homo sapiens (Human)
Function: Crystallins are the dominant structural components of the vertebrate eye lens.
Interaction partners:
- Alpha-crystallin A2
- Alpha-crystallin B chain
- Gap junction alpha-8 protein
- Gap junction alpha-3 protein
- Phakinin
- Pituitary homeobox 3
- CCA tRNA nucleotidyltransferase 1, mitochondrial
- Lens fiber major intrinsic protein
- Heat shock protein beta-1
- Transmembrane protein 114
Sequence:
MASDHQTQAGKPQSLNPKIIIFEQENFQGHSHELNGPCPNLKETGVEKAGSVLVQAGPWVGYEQANCKGEQFVFEKGEYPRWDSWTSSRRTDSLSSLRPIKVDSQEHKIILYENPNFTGKKMEIIDDDVPSFHAHGYQEKVSSVRVQSGTWVGYQYPGYRGLQYLLEKGDYKDSSDFGAPHPQVQSVRRIRDMQWHQRGAFHPSN
Protein: AB hydrolase-1 domain-containing protein (E2QCS7)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MTIVLNLPVCVLFLLGTLVPSNSQKWIPYANPLDEQSQLQEIGLSDQNPDNFEQSQSQSQDQIVAQILPSDASLSGGQPPNNIIQLVDEGMDRPLLLQPQNRPIETVDQSQNLIQRKLQSQSQAQALAESQAQSQAQSQAQSQAQSQAQLQAQLQAQSQAQSQAQSQAQLQSQLQSQIQSQLQSDLQSQSQLQAQLQSQLDALKQQSGLQKLAFGQLKPQVSDQPILILDSIPKPRPQFVLLPPQNGPVQQDPNLRYVIIPSPPKRKRRISPDSSTIPKVYILTPDKQIKSNTSINIDQLLKLYKYKTDKERKIAELKRQIKELKKQNLFNLVPALQLRPAIPAIELQLPVESQSEIQSQIASQQSGSLSQLQSQQNSKSSGSQSNAQSSGSQSQYQLQSDSQSSGSQSQLQSQSNPQSSGTQSQLQSQNRRLQSQLQSQNRGSQSQLQSQINPQSSGSQSQLQSQINPQSSGSQSQLQSQNRGSQSQLQSQNRGSQSQLQSEISPQSSGSQSQLQSQIDLHSDASQSQLQSQLGYDSTGSQSQLQSQLDSQLSGAQSQLQSQFNSQSSESQSQLQSQAKFRSLGAQSQSQSQLNSQSLGSQSQSQSQLNSQSSGSQSQSQSQLNSQSSGSQSQSQSQLNSQSLGSQSQSQLQIRSQLGTQTLESQSPSEVLLHIQGPSTYQDNLAESNIQTQKNRINVVTPEYKVFKTPNYLTQEDILDNTKLTTVDLIEKYGYPSETNYVTSEDGYRLCLHRIPRPGAEPVLLVHGLMASSASWVELGPKDGLAYILYRKGYDVWMLNTRGNIYSRENLNRRLKPNKYWDFSFHEIGKFDVPAAIDHILIHTHKPKIQYIGHSQGSTVFFVMCSERPNYAHKVNLMQALSPTVYLQENRSPVLKFLGMFKGKYSMLLNLLGGYEISAKTKLIQQFRQHICSGSELGSSICAIFDFVLCGFDWKSFNTTLTPIVAAHASQGASAKQIYHYAQLQGDLNFQRFDHGAVLNRVRYESSEPPAYNLSQTTSKVVLHHGEGDWLGSTSDVIRLQERLPNLVESRKVNFEGFSHFDFTLSKDVRPLLYSHVLRHLSTSLSG
Protein: GRIP and coiled-coil domain-containing protein C365.11 (Q9Y7X7)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16823372}.
Interaction partners:
- COPII coat assembly protein sec16
- Protein transport protein sec31
Sequence:
METTVSAKNSLENENFLKEKSETVFLDEAAITKPPASKKKRKNRKKKKNNGPSEQFVGNNDLEEQRSGSIDSKDKEKPLDEKVKELENANKTLSDLVRRIQIQRDEAEQKAEIYNRDALNTKQEHLDIKKRLEKSDETVCKLKEENENLQDMLRNVGNELVESRDEIKELIEKQKVQKESVKSHESELSSVMSSEILPKASSDSAGSFEPPVISNISKELINKEYARNVLLQFLENHEHRDKILPILSTALDLEEVHQHLILKNLN
Protein: Matrix metalloproteinase-27 (MMP-27) (EC 3.4.24.-) (Q9H306)
Organism: Homo sapiens (Human)
Function: Matrix metalloproteinases degrade protein components of the extracellular matrix such as fibronectin, laminin, gelatins and/or collagens.
Subcellular location: Endoplasmic reticulum {ECO:0000269|PubMed:24548619}. Note=Retained in the endoplasmic reticulum due to a C-terminal extension (CTE). {ECO:0000269|PubMed:24548619}.
Interaction partners:
Sequence:
MKRLLLLFLFFITFSSAFPLVRMTENEENMQLAQAYLNQFYSLEIEGNHLVQSKNRSLIDDKIREMQAFFGLTVTGKLDSNTLEIMKTPRCGVPDVGQYGYTLPGWRKYNLTYRIINYTPDMARAAVDEAIQEGLEVWSKVTPLKFTKISKGIADIMIAFRTRVHGRCPRYFDGPLGVLGHAFPPGPGLGGDTHFDEDENWTKDGAGFNLFLVAAHEFGHALGLSHSNDQTALMFPNYVSLDPRKYPLSQDDINGIQSIYGGLPKEPAKPKEPTIPHACDPDLTFDAITTFRREVMFFKGRHLWRIYYDITDVEFELIASFWPSLPADLQAAYENPRDKILVFKDENFWMIRGYAVLPDYPKSIHTLGFPGRVKKIDAAVCDKTTRKTYFFVGIWCWRFDEMTQTMDKGFPQRVVKHFPGISIRVDAAFQYKGFFFFSRGSKQFEYDIKTKNITRIMRTNTWFQCKEPKNSSFGFDINKEKAHSGGIKILYHKSLSLFIFGIVHLLKNTSIYQ
Protein: Putative ATP-dependent RNA helicase ECM32 (EC 3.6.4.13) (DNA helicase B) (Hcs B) (DNA helicase III) (Extracellular mutant protein 32) (Helicase 1) (scHelI) (Modulator of translation termination protein 1) (P32644)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Probable RNA helicase, which may be involved in modulation of the translation termination process. Probably unwinds double-stranded RNA. In vitro, unwinds covalently closed, circular DNA in the presence of a DNA topoisomerase TOP1 and replication factor-A protein RFA1.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:10836794, ECO:0000269|PubMed:14562095}. Note=Associated with polyribosomes.
Interaction partners:
- Nonsense-mediated mRNA decay protein 2
- Eukaryotic peptide chain release factor GTP-binding subunit
- General alpha-glucoside permease
- Nonsense-mediated mRNA decay protein 3
- E3 ubiquitin-protein ligase ITT1
- Maltose permease MAL31
- RNA annealing protein YRA1
- RNA-binding protein SGN1
- Eukaryotic peptide chain release factor subunit 1
Sequence:
MDFQCRTCSQAYDAEQMMKHLSSTRHKTVFDTSNDEDICCEECQDKNIHQLQIIRFGGEDMVLLCNSCFRKEYSETERPSTSYSLQNGSILKFWEKYVKVRECCCDECGEESNLNANRNGEVLCDKCLPKSNRAKDFVSEKSGRFLYIYLGLNETQNSTRKPRKKGGRRVGRGKKGRKGAKIKKEKKETFEAKISRIAYEVKKENSTIQSSSSSNLRNFKGFKAVESDPVVAAKVSKSETSRSNPGPSNRNKGKGNKANHKKNSGNGIGKEKERKTNIRNNVRNSQPIPEDRKNTNSHVTTNSGGKGKNESVDKHQLPQPKALNGNGSGSTNTTGLKKGKKDHAGQKTKGNDKTGNKNPREAKLNSAGRKNALGKKSNNQPNKGTSRWTIGSDTESSREPSISPNENTTSITKSRNRNKKASKPTLNEKSKTTTMPKKLETKNQEKNNGKTKDGKLIYEEGEPLTRYNTFKSTLSYPDLNTYLNDYSFALFLEQKLENEFVQNFNILWPRNEKDTAFIINVEKNNNSELEKLLPANLLALGRPAFNERQPFFFCTQDEQKVWYIFIKELSIQRGKYVLLVELFSWNNLSLPTKNGSSQFKLLPTSAQTSRILFAMTRITNPKFIDLLLGQKPIKEIYFDNRLKFSSDKLNRSQKTAVEHVLNNSITILQGPPGTGKTSTIEEIIIQVIERFHAFPILCVAASNIAIDNIAEKIMENRPQIKILRILSKKKEQQYSDDHPLGEICLHNIVYKNLSPDMQVVANKTRRGEMISKSEDTKFYKEKNRVTNKVVSQSQIIFTTNIAAGGRELKVIKECPVVIMDEATQSSEASTLVPLSLPGIRNFVFVGDEKQLSSFSNIPQLETSLFERVLSNGTYKNPLMLDTQYRMHPKISEFPIKKIYNGELKDGVTDEQKAWPGVQHPLFFYQCDLGPESRVRSTQRDIVGFTYENKHECVEIVKIIQILMLDKKVPLEEIGVITPYSAQRDLLSDILTKNVVINPKQISMQQEYDEIELFNAAGSQGTAGSLQNNVINIINGLHVATVDSFQGHEKSFIIFSCVRNNTENKIGFLRDKRRLNVALTRAKHGLIVVGNKNVLRKGDPLWKDYITYLEEQEVIFTDLTAY
Protein: 1-phosphatidylinositol-3-phosphate 5-kinase (EC 2.7.1.150) (B2KTE4)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
- Protein VAC14 homolog
- FIG4 phosphoinositide 5-phosphatase.
- Phosphatidylinositol 3-kinase catalytic subunit type 3
- Phosphatidylinositol 4-kinase beta
- Uncharacterized protein.
- Phosphatidylinositol 4-kinase type 2-alpha
- CDP-diacylglycerol--inositol 3-phosphatidyltransferase.
- Phosphatidylinositol-3,5-bisphosphate 3-phosphatase MTMR8
- Phosphatidylinositol-3,5-bisphosphate 3-phosphatase MTMR2
- Phosphatidylinositol 4-kinase, catalytic, alpha a
Sequence:
MAADDKASSSSSVMDWSSEPPPSPTSPSHLTHFKPLTPEQDEPPLRSAYSSFVSLFRFNKEEGRPPSVTEKSQSASSSPQGPRRNWSSPSHSIHGSETHRKHPELLRRTSAASEGRRKSEAPLGSHDPRTAVQLRTALKRLKEIMEGKSQDSDLKQYWMPDSQCKECYDCNEKFTTFRRRHHCRLCGQIFCSRCCNQEIPGKFMGYTGDLRACTYCRKIALSYAHSTDSSSIGEDLSALSDSPCSVCVLEPTEPRTPVGGRKASRNIFLEEDLAWQSHQESQNSGLNSRLTVVQEDIGKSPARKRSASVTNLSLDRSGSSMVPAYESSVSPQNSRALPKTDHSEEERKILLDSFQLKDIWKKICHNTTGMEFQDHRYWLRTYPNCIVGKELVNWLLRNGTISTRAQAIAIGQALVDGRWLDCVTHHDQIFRDEYALYRPLQSTEFSETPSPDSDSVNSLEGHSEPSWFKDIKFDDSDTEQLADENDYVTPSSSSPSKRTSVSSFHSAVDSDSAASISLNMEQDNVNFHIKKQAKYPHVPPYPAEQKMEVLLSEDGGQHISISDAFIKESLFNRRVEEKAKEMLFTPLGWHHSSLDQLREENGEKKAMERLLSANHSHMMALLQQLLYSESLSLSWRDIIVPVVRQVVQTVRPDVRSCDDDMDIRQFVHIKKIPGGKKFDSAVVNGFVCTKNIAHKKMNSYIKNPKILLLKCSIEYLYREETKFTCIDPIVLQEREFLKNYVQRIVDVRPNLVLVEKTVSRIAQDMLLEHGIAIVINVKPQVLDRVSRMTQGDLVISMDQLLTKPRLGTCHKFYLHSFQLPNSEVKTLMFFEGCPPQLGCTIKLRGASEYELARVKEIIIFMVCVAYHSQLEISFLMDEFAMPPSLAESSSFPCLLESTTLREEDETSGERESQDNDESTLGDDNLTLVPGDDFETGFTGTIKAHSREPSTSESSHKDGESPRINKNASITSFSGGEEENIKTSTPLSSFSSTFPQPVTPPFLISDVKEMSQEVVKGSGEGEKNKYLESTLVHQDSTSSETSLPPTRLFRDPLQDDTGLFVTEHVASSDDRLKSISALFKQELKDIILCISPFITFREPFLLTPAGLRCPSRDYFPEQVYLSPLLNKDSKELDGRRKRQLLKESSPGSGSLTNGSVSHQRAIQILPCHKLTSARIAEQVGSSQQLARMLADYRAQGGRIRQREGTQFREAPPPKAPIKADSEEDKGAGVIDMTWSTKLDCLNPINHQRLCVLFSSSSAQSNNAPNPCVSPWIVTMEFYGKNDLTLGVFLERYCFRPSYQCPSMYCETPMVHHIRRFVHGKGCVQIVLKELDSPVPGYQHTILNYSWCRICKQVTPVVPLSNDSWSMSFAKYLELRFYGHQYTRRANAEPCGHSIHKDYHQYFSYNQMVASFSYIPVRLLEICLPPPKIIIRNQGPSKSSLQQDLKDFSQKVAQVYLAIDDRLTSLKTDTFSKTREEKMEDMFAQKDMEESELRGWIEKLQVRLQTSVIDSSQQLQAVLESVVVKKQGLCETLQSWNNRLQELFQQEKGRKRLSVPPSPGRHRQPTTDESKTSALESSPRNPSPVVPNGDKEDRHLNTFPSSSGSSSLLQLPSPAEQPSDVITSGPSFPDQDSVSNPEDMFDGHLLGSNDSQVKEKSTMKTILANLLPGNSYNPIPFPFDPDKHYLMYEHERVPIAVCEREPSSIIAFALSCKEYKTALEELTKTTAKTGGDDTSQTISAGESRVKNSPAKPSDNSMSQLSRSSVDADPLKEPESADKQKKQTGNPHIELQFSDANAKFYCRIYYAEEFHKMREEIMESTEDDFVRSLSHCVNWQARGGKSGAVFYATEDDRFILKQMPRLEVQSFLDFAPHYFTYITGAVHLKRPTALAKILGVYRIGYKNSQNNTEKKLDLLVMENLFYGRKMAQVFDLKGSLRNRNVKTDQGKESCEVVLLDENLLKLVHDNPLYIRSHCKAILRAAIHSDALFLSSHLIIDYSLLVGRDDSTDELVVGIIDYIRTFTWDKKLEMVVKSTGILGGQGKMPTVVSPELYRTRFCEAMDKYFLMVPDHWSGLGLNC
Protein: 45 protein (Tegument protein) (P88983)
Organism: Murid herpesvirus 4 (MuHV-4) (Murine gammaherpesvirus 68)
Interaction partners:
Sequence:
MDPFKKPVRMLPIKGAPISRPISVFTFDVFNPPDDSDGSSTPDSVFEAETSPARTPPTPALILPYDYVSSEDSDDEAQEHADNRDTNDQVSESSTSEDSDSESESSCDDTQQTFVDDESTSSSGEEDRDDPFESNDQGAQGGSTSESEDDLPAILRAARETQSDSSSDSSGNSHKKRRVQEEESSRILKTPAPISGNGKYNWPWLD
Protein: Mevalonate kinase (MK) (EC 2.7.1.36) (Q9R008)
Organism: Mus musculus (Mouse)
Function: Catalyzes the phosphorylation of mevalonate to mevalonate 5-phosphate, a key step in isoprenoid and cholesterol biosynthesis.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:P17256}. Peroxisome {ECO:0000250|UniProtKB:P17256}.
Interaction partners:
- Diphosphomevalonate decarboxylase
- Phosphomevalonate kinase
- 3-hydroxy-3-methylglutaryl-coenzyme A reductase
- Hydroxymethylglutaryl-CoA synthase, cytoplasmic
- Squalene synthase
- Farnesyl pyrophosphate synthase
- Lanosterol synthase
- Squalene monooxygenase
- Cystathionine gamma-lyase
- Isopentenyl-diphosphate Delta-isomerase 1
Sequence:
MLSEALLVSAPGKVILHGEHAVVHGKVALAAALNLRTFLLLRPQSNGKVSVNLPNIGIKQVWDVGMLQRLDTSFLEQGDVSVPTLEQLEKLKKMGDLPRDRAGNEGMALLAFLYLYLAICRKQRTLPSLDMVVWSELPPGAGLGSSAAYSVCLAAALLTACEEVSNPLKDGVSVSRWPEEDLKSINKWAFEGERVIHGNPSGVDNAVSTWGGALRFQQGTMSSLKSLPSLQILLTNTKVPRSTKALVAAVRSRLTKFPEIVAPLLTSIDAISLECERVLGEMVAAPVPEQYLVLEELIDMNQHHLNALGVGHNSLDQLCQVTAAHGLHSKLTGAGGGGCGITLLKPGLEQATVEAAKQALTSCGFDCWETSIGAPGVSTHSAAAVGDPVRQALGL
Protein: 72 kDa type IV collagenase (EC 3.4.24.24) (72 kDa gelatinase) (Gelatinase A) (Matrix metalloproteinase-2) (MMP-2) [Cleaved into: PEX] (P33434)
Organism: Mus musculus (Mouse)
Function: Ubiquitinous metalloproteinase that is involved in diverse functions such as remodeling of the vasculature, angiogenesis, tissue repair, tumor invasion, inflammation, and atherosclerotic plaque rupture. As well as degrading extracellular matrix proteins, can also act on several nonmatrix proteins such as big endothelial 1 and beta-type CGRP promoting vasoconstriction. Also cleaves KISS at a Gly-|-Leu bond. Appears to have a role in myocardial cell death pathways. Contributes to myocardial oxidative stress by regulating the activity of GSK3beta. Cleaves GSK3beta in vitro. Involved in the formation of the fibrovascular tissues (By similarity).
Subcellular location: [Isoform 1]: Secreted, extracellular space, extracellular matrix {ECO:0000250}. Membrane {ECO:0000250}. Nucleus {ECO:0000250}. Note=Colocalizes with integrin alphaV/beta3 at the membrane surface in angiogenic blood vessels and melanomas. Found in mitochondria, along microfibrils, and in nuclei of cardiomyocytes (By similarity). {ECO:0000250}.; SUBCELLULAR LOCATION: [Isoform 2]: Cytoplasm. Mitochondrion.
Interaction partners:
- Metalloproteinase inhibitor 2
- Metalloproteinase inhibitor 3
- Matrix metalloproteinase-14
- Metalloproteinase inhibitor 1
- Thrombospondin-1
- Endothelin-1
- Vascular endothelial growth factor A, long form
- Proto-oncogene tyrosine-protein kinase Src
- NADPH oxidase 2
- Cytochrome b-245 light chain
Sequence:
MEARVAWGALAGPLRVLCVLCCLLGRAIAAPSPIIKFPGDVAPKTDKELAVQYLNTFYGCPKESCNLFVLKDTLKKMQKFFGLPQTGDLDQNTIETMRKPRCGNPDVANYNFFPRKPKWDKNQITYRIIGYTPDLDPETVDDAFARALKVWSDVTPLRFSRIHDGEADIMINFGRWEHGDGYPFDGKDGLLAHAFAPGTGVGGDSHFDDDELWTLGEGQVVRVKYGNADGEYCKFPFLFNGREYSSCTDTGRSDGFLWCSTTYNFEKDGKYGFCPHEALFTMGGNADGQPCKFPFRFQGTSYNSCTTEGRTDGYRWCGTTEDYDRDKKYGFCPETAMSTVGGNSEGAPCVFPFTFLGNKYESCTSAGRNDGKVWCATTTNYDDDRKWGFCPDQGYSLFLVAAHEFGHAMGLEHSQDPGALMAPIYTYTKNFRLSHDDIKGIQELYGPSPDADTDTGTGPTPTLGPVTPEICKQDIVFDGIAQIRGEIFFFKDRFIWRTVTPRDKPTGPLLVATFWPELPEKIDAVYEAPQEEKAVFFAGNEYWVYSASTLERGYPKPLTSLGLPPDVQQVDAAFNWSKNKKTYIFAGDKFWRYNEVKKKMDPGFPKLIADSWNAIPDNLDAVVDLQGGGHSYFFKGAYYLKLENQSLKSVKFGSIKSDWLGC
Protein: FK506-binding protein 59 (EC 5.2.1.8) (Peptidyl-prolyl cis-trans isomerase) (PPIase) (Rotamase) (dFKBP59) (Q9VL78)
Organism: Drosophila melanogaster (Fruit fly)
Function: May have a role in phototransduction; inhibits or prevents Ca(2+) induced stimulation of the trpl ion channel.
Interaction partners:
- Heat shock protein 83
- Cytosolic Prostaglandin E synthase
- Inactivation-no-after-potential D protein
- Stress-induced-phosphoprotein 1
- Transient-receptor-potential-like protein
- GEO10024p1
- Estrogen-related receptor splice variant
- RE73310p
- Peptidyl-prolyl cis-trans isomerase
- ARF GTPase-activating protein Git
Sequence:
MPEGNKIDLSGDGGVLKEILKEGTGTETPHSGCTVSLHYTGRLVDGTEFDSSLSRNEPFEFSLGKGNVIKAFDMGVATMKLGERCFLTCAPNYAYGAAGSPPAIPPDATLIFELEMLGWKGEDLSPNQDGSIDRTILEASDKKRTPSDGAFVKAHISGSFEGRVFEDRDVEFDYGEGKAIGIIDGVEIALEKMNVGETSRIKIQAKYAFGAKGNEEFKIPPNATVEYTVKLVDCGKGLEEWKLSDEERLAEAKVYKEKGTNYFKKENWALAIKMYTKCKNILPTTVHTNEEVKKIKVATHSNIALCHQKSNDHFEAKQECNEVLALDKNNVKALYRRGQCNLTINELEDALEDFQKVIQLEPGNKAAANQVIICKQKLKESKNKEKKLYANMFTKLAANDKETEPPRETDVLSKCGEWSEEDAKREAELTLERDNIIMI
Protein: cDNA FLJ77177, highly similar to Homo sapiens arginine-rich, mutated in early stage tumors (ARMET), mRNA (A8K878)
Organism: Homo sapiens (Human)
Subcellular location: Secreted {ECO:0000256|ARBA:ARBA00004613}.
Interaction partners:
Sequence:
MRRMRRMWATQGLAVALALSVLPGSRALRPGDCEVCISYLGRFYQDLKDRDVTFSPATIENELIKFCREARGKENRLCYYIGATDDAATKIINEVSKPLAHHIPVEKICEKLKKKDSQICELKYDKQIDLSTVDLKKLRVKELKKILDDWGETCKGCAEKSDYIRKINELMPKYAPKAASARTDL
Protein: Cytosolic non-specific dipeptidase (EC 3.4.13.18) (CNDP dipeptidase 2) (Glutamate carboxypeptidase-like protein 1) (Peptidase A) (Threonyl dipeptidase) (Q96KP4)
Organism: Homo sapiens (Human)
Function: Catalyzes the peptide bond hydrolysis in dipeptides, displaying a non-redundant activity toward threonyl dipeptides (By similarity). Mediates threonyl dipeptide catabolism in a tissue-specific way (By similarity). Has high dipeptidase activity toward cysteinylglycine, an intermediate metabolite in glutathione metabolism. Metabolizes N-lactoyl-amino acids, both through hydrolysis to form lactic acid and amino acids, as well as through their formation by reverse proteolysis. Plays a role in the regulation of cell cycle arrest and apoptosis.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:12473676, ECO:0000269|PubMed:17121880}.
Interaction partners:
- Beta-Ala-His dipeptidase
- Carnosine synthase 1
- Histidine decarboxylase
- Histidine ammonia-lyase
- Carnosine N-methyltransferase
- 4-aminobutyrate aminotransferase, mitochondrial
- Aldehyde dehydrogenase family 3 member A2
- Beta-ureidopropionase
- 4-trimethylaminobutyraldehyde dehydrogenase
- Acidic amino acid decarboxylase GADL1
Sequence:
MAALTTLFKYIDENQDRYIKKLAKWVAIQSVSAWPEKRGEIRRMMEVAAADVKQLGGSVELVDIGKQKLPDGSEIPLPPILLGRLGSDPQKKTVCIYGHLDVQPAALEDGWDSEPFTLVERDGKLYGRGSTDDKGPVAGWINALEAYQKTGQEIPVNVRFCLEGMEESGSEGLDELIFARKDTFFKDVDYVCISDNYWLGKKKPCITYGLRGICYFFIEVECSNKDLHSGVYGGSVHEAMTDLILLMGSLVDKRGNILIPGINEAVAAVTEEEHKLYDDIDFDIEEFAKDVGAQILLHSHKKDILMHRWRYPSLSLHGIEGAFSGSGAKTVIPRKVVGKFSIRLVPNMTPEVVGEQVTSYLTKKFAELRSPNEFKVYMGHGGKPWVSDFSHPHYLAGRRAMKTVFGVEPDLTREGGSIPVTLTFQEATGKNVMLLPVGSADDGAHSQNEKLNRYNYIEGTKMLAAYLYEVSQLKD
Protein: Protein ROT1 (Reversal of TOR2 lethality protein 1) (Q03691)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Required for normal levels of the cell wall 1,6-beta-glucan. Involved in a protein folding machinery chaperoning proteins acting in various physiological processes including cell wall synthesis and lysis of autophagic bodies. Controls actin cytoskeleton polarization to the mother-bud neck and CLB2 protein stability.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000305|PubMed:14562095, ECO:0000305|PubMed:16567426, ECO:0000305|PubMed:17914748}; Single-pass type I membrane protein {ECO:0000305|PubMed:14562095, ECO:0000305|PubMed:16567426, ECO:0000305|PubMed:17914748}.
Interaction partners:
- Protein BIG1
- Beta-1,6-glucan synthesis-associated protein KEG1
- Beta-glucan synthesis-associated protein KRE6
- Glucosidase 2 subunit alpha
- Cell wall synthesis protein KRE9
- Mannosyl-oligosaccharide glucosidase
- Killer toxin-resistance protein 5
- Beta-glucan synthesis-associated protein SKN1
- Endoplasmic reticulum chaperone BiP
- Cell wall synthesis protein KNH1
Sequence:
MWSKKFTLKKLILGGYLFAQKVYCEDESNSIYGTWSSKSNQVFTGPGFYDPVDELLIEPSLPGLSYSFTEDGWYEEATYQVSGNPRNPTCPMASLIYQHGTYNISENGTLVLNPIEVDGRQLFSDPCNDDGVSTYSRYNQTETFKEYAVGIDPYHGIYTLQLYQYDGTPMQPLYLAYRPPMMLPTETLNPTSSATSTDDPSSNKKRSLRSLVRRSLENRHKTNAIKRQNTSFLTSNAIWYISAGMLGVGSLLFLAF
Protein: Vomeronasal 2, receptor 120 (A0A3Q4EHP3)
Organism: Mus musculus (Mouse)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004651}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}.
Interaction partners:
Sequence:
MLIFVSVLLFLNFPVASCEPINPGCSLGMADAIFQDGDVLVDCHFVLLTVSIALQKIFHFLRFHLSFPMFIYRIHPNKYQYVIALNFAIEEINKNIHLLPNISLGYDMYSIVQYQATILEHSIRFLTGLKEAIPNYTCRKESKLIAVVTGTSWEFPSRISTILGLYKYPQNPLGLFEIYGIVFFTSLHIFFSHQLTFGPFDPMLSDHVKFPFIYQMAPEDTSLALGMVSLMVHFSWTWVGLIITENEKGIKFLSDLKREMKKNSVCAAFVQMLSLKYRYNWNDLLSTDPAIMGEMTPLSVCSTSCAPGLMKSPQEGKASCCFDCHPCLENEISNETDSIQCIKCPDDQYANTEQTHCIPKAVTFLAYEDPLGMALACMALCFSALTALVLGVFVKHHETPIVKANNRTLSYILLISLILCFLCSLPFIGLPNMATCILQQMSFGVVFTIAVSTVLAKTVTVVLAFRSTVPGRRMRWILVSPNLIIPICTLIQMVLCAIWLGASAPFVDINAHNERGHITIMCNKGSATAFYCVLGYLGFLAMGTLTVAFWARNLPDIFNEAKFLTFSMLVFCSVWVTFLPVYHSTKGKVMVAVEVFSILASSAGLLGCIFVPKCYIILIRPKNGSFKGLRGTRVCK
Protein: Probable sigma-70 factor, ECF subfamily (Q9I646)
Organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Interaction partners:
- Probable transmembrane sensor
- Probable sigma-70 factor, ECF subfamily
- Anti-sigma factor FoxR
- Probable transmembrane sensor
- Probable transmembrane sensor
- Probable sigma-70 factor, ECF subfamily
- Sigma factor regulator, FemR
- Probable transmembrane sensor
- Metal-pseudopaline receptor CntO
- Probable transmembrane sensor
Sequence:
MSAGDVSNSEFVGSLYRDHRGWLLAWLNRNLGCRQRAEDLSQDTFVRLLGRPELPGLREPRAFLAKVARGLMIDHFRRAALEQAYLAELALVPEAEQPSAEEQYLILEDLREIDRLLGTLSLKARSAFLYSRLDGMPHAEIAERLGVSVPRVRQYLAQGLRQCYIALYGEPR
Protein: Prolactin (PRL) (P01238)
Organism: Sus scrofa (Pig)
Function: Prolactin acts primarily on the mammary gland by promoting lactation.
Subcellular location: Secreted.
Interaction partners:
- Prolactin receptor
- Leptin
- Somatotropin
- Erythropoietin
- Pro-opiomelanocortin
- Thrombopoietin
- Granulocyte colony-stimulating factor
- Growth hormone receptor
- Leptin receptor
- Tyrosine-protein kinase JAK2
Sequence:
MDNRGSSQKGSLLLLLLLVSNLFLCKSVASLPICPSGAVNCQVSLRDLFDRAVILSHYIHNLSSEMFNEFDKRYAQGRGFITKAINSCHTSSLSTPEDKEQAQQIHHEVLLNLILRVLRSWNDPLYHLVTEVRGMQEAPDAILSRAIEIEEQNKRLLEGMEKIVGQVHPGIKENEVYSVWSGLPSLQMADEDTRLFAFYNLLHCLRRDSHKIDNYLKLLKCRIIYDSNC