wanglab/gogpt-training-data huggingface dataset:
Protein: Filamin A (Q60FE5)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MPATEKDLAEDAPWKKIQQNTFTRWCNEHLKCVSKRIANLQTDLSDGLRLIALLEVLSQKKMHRKHNQRPTFRQMQLENVSVALEFLDRESIKLVSIDSKAIVDGNLKLILGLIWTLILHYSISMPMWDEEEDEEAKKQTPKQRLLGWIQNKLPQLPITNFSRDWQSGRALGALVDSCAPGLCPDWDSWDASKPVTNAREAMQQADDWLGIPQVITPEEIVDPNVDEHSVMTYLSQFPKAKLKPGAPLRPKLNPKKARAYGPGIEPTGNMVKKRAEFTVETRSAGQGEVLVYVEDPAGHQEEAKVTANNDKNRTFSVWYVPEVTGTHKVTVLFAGQHIAKSPFEVYVDKSQGDASKVTAQGPGLEPSGNIANKTTYFEIFTAGAGTGEVEVVIQDPMGQKGTVEPQLEARGDSTYRCSYQPTMEGVHTVHVTFAGVPIPRSPYTVTVGQACNPSACRAVGRGLQPKGVRVKETADFKVYTKGAGSGELKVTVKGPKGEERVKQKDLGDGVYGFEYYPMVPGTYIVTITWGGQNIGRSPFEVKVGTECGNQKVRAWGPGLEGGVVGKSADFVVEAIGDDVGTLGFSVEGPSQAKIECDDKGDGSCDVRYWPQEAGEYAVHVLCNSEDIRLSPFMADIRDAPQDFHPDRVKARGPGLEKTGVAVNKPAEFTVDAKHGGKAPLRVQVQDNEGCPVEALVKDNGNGTYSCSYVPRKPVKHTAMVSWGGVSIPNSPFRVNVGAGSHPNKVKVYGPGVAKTGLKAHEPTYFTVDCAEAGQGDVSIGIKCAPGVVGPAEADIDFDIIRNDNDTFTVKYTPRGAGSYTIMVLFADQATPTSPIRVKVEPSHDASKVKAEGPGLSRTGVELGKPTHFTVNAKAAGKGKLDVQFSGLTKGDAVRDVDIIDHHDNTYTVKYTPVQQGPVGVNVTYGGDPIPKSPFSVAVSPSLDLSKIKVSGLGEKVDVGKDQEFTVKSKGAGGQGKVASKIVGPSGAAVPCKVEPGLGADNSVVRFLPREEGPYEVEVTYDGVPVPGSPFPLEAVAPTKPSKVKAFGPGLQGGSAGSPARFTIDTKGAGTGGLGLTVEGPCEAQLECLDNGDGTCSVSYVPTEPGDYNINILFADTHIPGSPFKAHVVPCFDASKVKCSGPGLERATAGEVGQFQVDCSSAGSAELTIEICSEAGLPAEVYIQDHGDGTHTITYIPLCPGAYTVTIKYGGQPVPNFPSKLQVEPAVDTSGVQCYGPGIEGQGVFREATTEFSVDARALTQTGGPHVKARVANPSGNLTETYVQDRGDGMYKVEYTPYEEGLHSVDVTYDGSPVPSSPFQVPVTEGCDPSRVRVHGPGIQSGTTNKPNKFTVETRGAGTGGLGLAVEGPSEAKMSCMDNKDGSCSVEYIPYEAGTYSLNVTYGGHQVPGSPFKVPVHDVTDASKVKCSGPGLSPGMVRANLPQSFQVDTSKAGVAPLQVKVQGPKGLVEPVDVVDNADGTQTVNYVPSREGPYSISVLYGDEEVPRSPFKVKVLPTHDASKVKASGPGLNTTGVPASLPVEFTIDAKDAGEGLLAVQITDPEGKPKKTHIQDNHDGTYTVAYVPDVTGRYTILIKYGGDEIPFSPYRVRAVPTGDASKCTVTVSIGGHGLGAGIGPTIQIGEETVITVDTKAAGKGKVTCTVCTPDGSEVDVDVVENEDGTFDIFYTAPQPGKYVICVRFGGEHVPNSPFQVTALAGDQPSVQPPLRSQQLAPQYTYAQGGQQTWAPERPLVGVNGLDVTSLRPFDLVIPFTIKKGEITGEVRMPSGKVAQPTITDNKDGTVTVRYAPSEAGLHEMDIRYDNMHIPGSPLQFYVDYVNCGHVTAYGPGLTHGVVNKPATFTVNTKDAGEGGLSLAIEGPSKAEISCTDNQDGTCSVSYLPVLPGDYSILVKYNEQHVPGSPFTARVTGDDSMRMSHLKVGSAADIPINISETDLSLLTATVVPPSGREEPCLLKRLRNGHVGISFVPKETGEHLVHVKKNGQHVASSPIPVVISQSEIGDASRVRVSGQGLHEGHTFEPAEFIIDTRDAGYGGLSLSIEGPSKVDINTEDLEDGTCRVTYCPTEPGNYIINIKFADQHVPGSPFSVKVTGEGRVKESITRRRRAPSVANVGSHCDLSLKIPEISIQDMTAQVTSPSGKTHEAEIVEGENHTYCIRFVPAEMGTHTVSVKYKGQHVPGSPFQFTVGPLGEGGAHKVRAGGPGLERAEAGVPAEFSIWTREAGAGGLAIAVEGPSKAEISFEDRKDGSCGVAYVVQEPGDYEVSVKFNEEHIPDSPFVVPVASPSGDARRLTVSSLQESGLKVNQPASFAVSLNGAKGAIDAKVHSPSGALEECYVTEIDQDKYAVRFIPRENGVYLIDVKFNGTHIPGSPFKIRVGEPGHGGDPGLVSAYGAGLEGGVTGNPAEFVVNTSNAGAGALSVTIDGPSKVKMDCQECPEGYRVTYTPMAPGSYLISIKYGGPYHIGGSPFKAKVTGPRLVSNHSLHETSSVFVDSLTKATCAPQHGAPGPGPADASKVVAKGLGLSKAYVGQKSSFTVDCSKAGNNMLLVGVHGPRTPCEEILVKHVGSRLYSVSYLLKDKGEYTLVVKWGDEHIPGSPYRVVVP
Protein: Erythrocyte membrane protein 1, PfEMP1 (Q8I495)
Organism: Plasmodium falciparum (isolate 3D7)
Interaction partners:
Sequence:
MGPPGITGTQGETAKHMFDRIGKQVYETVKNEAENYISELEGKLSQATLLGERVSSLKTCQLVEDYRSKANGDVKRYPCANRSPVRFSDESRSQCTYNRIKDNETDDNACGACAPYRRLHLCDYNLEKMGKTSTTKHDLLAEVCMAAKYEGDSIKTHYTIHKHTNNDSAAELCTELARSFADIGDIIRGKDLYLGDIKKKQNGKKTEREKLEENLKRIFGKIHEDVTNGKKEVLKTRYKDINDPEFFKLREDWWTANRATVWKAITCHAGESDKYFRNTCNDSEHSGTFSQPNKYCRCNGDKPGEDKANVDPPTYFDYVPQYLRWFEEWAEDFCRIRKHKLKNAKEQCREKYKSGTDRYCSRNGYDCTQTIRGRNILVSDSECTNCSVVCTPFVKWIENKKLEFEKQKGKYTKEIEKANGTSNGTTIRTQYGTINNMYRKDFYQQLQSGYGDVNAFLELLNKETTCKDHPKVEEKSDIDFNEGTEKTFSHTEYCETCPWCATKKKGIDGNWEEQKYEEGCENYLMKPIDESKSTDIDLLVKDTSGTTMVEKLGGLCNDSSKRTVQMENWQCHYEKKSQYEDGFDKDYCVLKDDKKKKPEHRTIKSYYTLFPNWINEMLKDSIDWSKELKTCINNEKPTNCIRECKSKCDCFKKWVVQKEQEWKQLEEHYEKENFSGDFGPRISPYVTLEGNLQYSYLEMIRKYYAQEKPVQEIEQIIEKNKNNFEVKEDDNSITKFLQQEKGIATKCIEKQEECKQQKKQQRQKQPADKVVSRSGASPDTASPDTKATEEKEEEEEEEEEEDLGEESEEPEDQAVVDQDGQGETTEKKVPATTEEGSPKETTTPEKSVDVCKTVAELFSNVDNLKEACTQKYGGNNSRLGWKCIPTSGGEKATGGSGESTGSDATTGGSICVPPRRRRLYVTPLTTWASGGTTQVETQASGGNTETSQVSGETTPQGQTPSESEAQTASQDPSEKLRTAFIESAAVETFFLWDRYKKENTKRQSVLPLLEPINGDTISDDNNPEKLLKVGKIPPDFLRLMFYTLGDYRDILFSSSNTSDTTGKETPSSSNDNLKNIVIEAGGTDEKDKQKMKEIQQKIDKILKQSGTTPPTPVTHSPSSGTTPSSWWENNAKHIWKGMVCALTYKDNTNGGPPTQDNDLKKALWDDKTNEPKKSEYKYDQVELKEENSGTGVTKGHAEAPGDNTPLSKFVLRPPYFRYLEEWGETFCRERTRRLGKIKGECKVDDSGSGRGGVIKRQYSGDGEDCDKVHEDPTTLPDLGSSCPKSCSSYRKWIKIKKDEYEKQQKAYEQQKKNCEKESEGVENKSDICDQKFLQNLKNYGSIDSFLDRLKKGPCSKTYNESGEDNNKIFEDTEKTFGHQNYCGPCSEFKINCEKGNCDKTKGQECNGKKTIDAQNFEQMGQTAKEFVMRVSDNDTTKFEGHGLEDCNGAGIFKGIKENKWKCDKVCGYVVCKPKNGNGKNEGTYIIQIRALVRRWVEYFLEDYNKIRKKLKPCINDGKEPKCIKTCDKKCNCAGKWIKLKQDEWENIKNRFNEQYKNGNEGDYPVKTILEELISRIAAATDKAERGSLDKLKTSLGCNCSDNSQKKNTDERDIVECLLEKLQVKATSCQSQHSDKTEQQCQEYTPEPDEEDLLLEEENENQVENQKVGNKAPAFCPPPEKPPKEEPDEKCGDKEEEKEQEEEKDKGNEEQSGAPSSPSPSEGTKELPPPPEPPEEAKPPEPVKPTPAPAPAAPPAAPAQPTLPADEPFNRDILATTIPFGIAFALGSIAFLFLKKKTKSTIDLLRVINIPKSDYDIPTKLSPNRYIPYTSGKYRGKRYIYLEGDSGTDSGYTDHYSDITSSSESEYEEMDINDIYVPGSPKYKTLIEVVLEPSGNNTTASGNNTTASDTQNDIQNDGIPSNKFSDNEWNTLKDDFISQYLQSEQPNDLPNDYKSGNVTLNTEPNILYFDKPEEKPFITSIHDRNLYTGEEYSYNINMSTNSMDDIPINRDNNVYSGIDLINDALNGDYDIYDEMLKRKENELFGTNHVKQTSIHSVAKNTNSDPIHNQLELFHKWLDRHRDMCEQWENHHERLAKLKEEWENETHSGNTHPSDSNKTLNTDVSIQIDMDDGKPKKEFTNMDTILEDLDKYNEPYYDVQDDIYYDVNDHDTSTVNPNNMEKPSKVKIELDVNKKTIKEKYPISDVWDI
Protein: D-dopachrome decarboxylase (EC 4.1.1.84) (D-dopachrome tautomerase) (Phenylpyruvate tautomerase II) (P30046)
Organism: Homo sapiens (Human)
Function: Tautomerization of D-dopachrome with decarboxylation to give 5,6-dihydroxyindole (DHI).
Subcellular location: Cytoplasm {ECO:0000305|PubMed:8267597}.
Interaction partners:
- HLA class II histocompatibility antigen gamma chain
- D-dopachrome decarboxylase
Sequence:
MPFLELDTNLPANRVPAGLEKRLCAAAASILGKPADRVNVTVRPGLAMALSGSTEPCAQLSISSIGVVGTAEDNRSHSAHFFEFLTKELALGQDRILIRFFPLESWQIGKIGTVMTFL
Protein: Ras-related protein Rab-27A (Rab-27) (EC 3.6.5.2) (GTP-binding protein Ram) (Ram p25) (P23640)
Organism: Rattus norvegicus (Rat)
Function: Small GTPase which cycles between active GTP-bound and inactive GDP-bound states. In its active state, binds to a variety of effector proteins to regulate homeostasis of late endocytic pathway, including endosomal positioning, maturation and secretion. Plays a role in cytotoxic granule exocytosis in lymphocytes. Required for both granule maturation and granule docking and priming at the immunologic synapse.
Subcellular location: Membrane {ECO:0000250|UniProtKB:P51159}; Lipid-anchor {ECO:0000250|UniProtKB:P51159}. Melanosome {ECO:0000250|UniProtKB:P51159}. Late endosome {ECO:0000250|UniProtKB:P51159}. Lysosome {ECO:0000250|UniProtKB:P51159}. Note=Identified by mass spectrometry in melanosome fractions from stage I to stage IV. Localizes to endosomal exocytic vesicles. {ECO:0000250|UniProtKB:P51159}.
Interaction partners:
- Melanophilin
- Unconventional myosin-Va
- Synaptotagmin-like protein 2
- Rab effector MyRIP
- Synaptotagmin-like protein 4
- Synaptotagmin-like protein 1
- Protein unc-13 homolog D
- Rab effector Noc2
- Rabphilin-3A
- Synaptotagmin-like protein 5
Sequence:
MSDGDYDYLIKFLALGDSGVGKTSVLYQYTDGKFNSKFITTVGIDFREKRVVYRANGPDGTVGRGQRIHLQLWDTAGQERFRSLTTAFFRDAMGFLLLFDLTNEQSFLNVRNWISQLQMHAYCENPDIVLCGNKSDLEDQRAVKEEEARELAEKYGIPYFETSAANGTNISQAIEMLLDLIMKRMERCVDKSWIPEGVVRSNGHTSTDQLSEEKEKGLCGC
Protein: Protein SEY1 homolog (EC 3.6.5.-) (Q54W90)
Organism: Dictyostelium discoideum (Social amoeba)
Function: Probable GTP-binding protein that may be involved in cell development.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000255|HAMAP-Rule:MF_03109}; Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_03109}.
Interaction partners:
- Dynamin N-terminal domain-containing protein
- WD-40 repeat-containing protein
- Guanylate-binding protein
- Reticulon-like protein
- Dynamin-like protein C
- Dynamin-like protein B
Sequence:
MSEEITTNQTVEEEQQTNQPRLSNENIKQEDEEQQVQEQQEQQQQEQQEQIDDQDTQQQEDEFVVLEETKPVEPIRPTPTLQETPQQQKQQTQEQEHEYQDIVQFIDHKGDIVKEDNKNGRTTFLSTLSNRDDFLTKGFDYSVISILGPQSSGKSTLLNLLFNTRFAVMDASTGRKQTTQGVWMGVASTTNNKNETFLILDVEGTDGRERGEDEKAFERKTSLFSLALSSVLIINMWAHDIGRYNAANISLLKTVFELNLQLFQKKRNHKILIFFLIRDHDGVTPLERLKATLMEDITKLWTDLQKPEEFVGTRESDFFDFEFTTLPHKIYSPTAFLGQVEQLKQRFSDSGADSFIPKRKYRNDDIPADGFYQFSYQVWETIKSNRDLDLPSQKEMLALYRCDEFVEQSMTQFTRDIKPIKEHIERGRIQEQFGEKSKRILDQSLSVYDEPAQRYHLETVQKKRQVLTDRILTELKYLFDKQMERLNENTLVFYNSLIKEFTDSNTGSSSGSGNNNNKKRDGSSVLLTAASVGIIPQFSTWSNGIKKKSIEYFEIVANQSIVPGSDWSFENDLEQLKIKIDKELSILKENQLVRLSKLMRDKTFQQELTPLLTKITEQAPNNMWQKIKTYYDDALSSNEKEFRDRLVDFQLDEQKVNELINKFREQLADGLKNKITERAEFLQMRMRKRFEEKFNMDNRNLPRKWTKTDDIASIFQDARQNAEKLIDLFSYLRLDEEDSNVSFFKRLDNDEHEENTMVNSSKIIIPYKDCCLACENFRLTIKSDYMQALSEQNRLTSGGGVPGYMIILLCVLGFNEFISIISSPLLLLLTILLGGVGFVLFKLGLAGPFIDYSSQILVHFISKVKDIVLHVEQLQEQNHNNNNNNNNTPKQKRE
Protein: G-protein coupled receptor 61 (Biogenic amine receptor-like G-protein coupled receptor) (Q9BZJ8)
Organism: Homo sapiens (Human)
Function: Orphan G-protein coupled receptor. Constitutively activates the G(s)-alpha/cAMP signaling pathway. Shows a reciprocal regulatory interaction with the melatonin receptor MTNR1B most likely through receptor heteromerization. May be involved in the regulation of food intake and body weight (By similarity).
Subcellular location: Cell membrane {ECO:0000269|PubMed:28827538, ECO:0000269|PubMed:29226084}; Multi-pass membrane protein {ECO:0000255}. Endosome membrane {ECO:0000269|PubMed:28827538}; Multi-pass membrane protein {ECO:0000255}. Note=Colocalizes with ARRB2/beta-arrestin-2 in the endosome (PubMed:28827538). {ECO:0000269|PubMed:28827538}.
Interaction partners:
- G-protein coupled estrogen receptor 1
Sequence:
MESSPIPQSSGNSSTLGRVPQTPGPSTASGVPEVGLRDVASESVALFFMLLLDLTAVAGNAAVMAVIAKTPALRKFVFVFHLCLVDLLAALTLMPLAMLSSSALFDHALFGEVACRLYLFLSVCFVSLAILSVSAINVERYYYVVHPMRYEVRMTLGLVASVLVGVWVKALAMASVPVLGRVSWEEGAPSVPPGCSLQWSHSAYCQLFVVVFAVLYFLLPLLLILVVYCSMFRVARVAAMQHGPLPTWMETPRQRSESLSSRSTMVTSSGAPQTTPHRTFGGGKAAVVLLAVGGQFLLCWLPYFSFHLYVALSAQPISTGQVESVVTWIGYFCFTSNPFFYGCLNRQIRGELSKQFVCFFKPAPEEELRLPSREGSIEENFLQFLQGTGCPSESWVSRPLPSPKQEPPAVDFRIPGQIAEETSEFLEQQLTSDIIMSDSYLRPAASPRLES
Protein: Conserved oligomeric Golgi complex subunit 7 (COG complex subunit 7) (Component of oligomeric Golgi complex 7) (Q9VAD6)
Organism: Drosophila melanogaster (Fruit fly)
Function: Required for normal Golgi function.
Subcellular location: Golgi apparatus membrane {ECO:0000250|UniProtKB:P83436}; Peripheral membrane protein {ECO:0000250|UniProtKB:P83436}.
Interaction partners:
- Conserved oligomeric Golgi complex subunit 8
- Conserved oligomeric Golgi complex subunit 1
- Conserved oligomeric Golgi complex subunit 3
- Conserved oligomeric Golgi complex subunit 4
- Conserved oligomeric Golgi complex subunit 2
- Conserved oligomeric Golgi complex subunit 6
- Conserved oligomeric Golgi complex subunit 5
- Syntaxin-5
- Golgin-84
- Vacuolar protein sorting-associated protein 53 homolog
Sequence:
MDVSALSETTFSPAEWINANYKKFVEENGRDDSEAASAFIRSYVAKLQLYIFNVNNAVEESSRQVVASMPRIAKESAALQADVHRLQEKMSAMRLEVAAVQSETGECMATLERLNTKSQKLQVAKESLQESDGWGNLLAELEDGFERNDLKGVCDKLIALQKSLHAQEQLPGHAERQTQVEDFKNRLEALASPSVVQCFAEGNTEQAQHFVQIFTSIQRLPQLQQYYRAVQKNFWQQQWKQTLELQGTESQPQQQQFLTLYYDQLLEHCQRQVKWCSNLFGENSPQPFLVIAELLPALQPTRDAHILQLLKTSNERLEMLALFAKVNHSFVLHLNSLLEQSHITLSEELHRLLGEAIFEYFHKFIQQYPRLEETQLSTQVDRLSSNQATPSDGVRHLEESTRKLYEWLKEACERCASITSDLALCKLITLLNGIFKRQLESFGRIQRQIGLSLGSSSYAAQSENWSLLQYTMSQLQCLADFQVQLHQFEQDLHTRMVMLSNRLTKPSNRGPITIFQTCDHAARTQLLNSIADYQQKKSEATDSLGIFPQIYATLKSHFADTHDITLNILLQPIETHLAHIRPPVQDHAASGIEMPSFSFAPQESITQIGQYLLTLPQHLEPLLLSPSSLLKQALEVCNIKYTQAIPCADVLLSLVVEQCCVLYVTQILQIKSLPSSAATQLSVDIEYLSNVLEELGLSINLQLSQILTLLKAAPDQYLTLSSGCEPRLVTAIRQMRNIISTQ
Protein: Zinc finger CCCH domain-containing protein 11A (O75152)
Organism: Homo sapiens (Human)
Function: RNA-binding protein that interacts with purine-rich sequences and is involved in nuclear mRNA export; probably mediated by association with the TREX complex.
Subcellular location: Nucleus {ECO:0000269|PubMed:29610341}. Nucleus speckle {ECO:0000269|PubMed:37356722}. Note=Retained in nuclear speckles though interaction with PABPN1. {ECO:0000269|PubMed:37356722}.
Interaction partners:
- Zinc finger BED domain-containing protein 6
- SAP domain-containing ribonucleoprotein
- THO complex subunit 1
- Nuclear cap-binding protein subunit 3
- Chromatin target of PRMT1 protein
- THO complex subunit 2
- THO complex subunit 5
- Polymerase delta-interacting protein 3
- Spliceosome RNA helicase DDX39B
- UAP56-interacting factor
Sequence:
MPNQGEDCYFFFYSTCTKGDSCPFRHCEAAIGNETVCTLWQEGRCFRQVCRFRHMEIDKKRSEIPCYWENQPTGCQKLNCAFHHNRGRYVDGLFLPPSKTVLPTVPESPEEEVKASQLSVQQNKLSVQSNPSPQLRSVMKVESSENVPSPTHPPVVINAADDDEDDDDQFSEEGDETKTPTLQPTPEVHNGLRVTSVRKPAVNIKQGECLNFGIKTLEEIKSKKMKEKSKKQGEGSSGVSSLLLHPEPVPGPEKENVRTVVRTVTLSTKQGEEPLVRLSLTERLGKRKFSAGGDSDPPLKRSLAQRLGKKVEAPETNIDKTPKKAQVSKSLKERLGMSADPDNEDATDKVNKVGEIHVKTLEEILLERASQKRGELQTKLKTEGPSKTDDSTSGARSSSTIRIKTFSEVLAEKKHRQQEAERQKSKKDTTCIKLKIDSEIKKTVVLPPIVASRGQSEEPAGKTKSMQEVHIKTLEEIKLEKALRVQQSSESSTSSPSQHEATPGARRLLRITKRTGMKEEKNLQEGNEVDSQSSIRTEAKEASGETTGVDITKIQVKRCETMREKHMQKQQEREKSVLTPLRGDVASCNTQVAEKPVLTAVPGITRHLTKRLPTKSSQKVEVETSGIGDSLLNVKCAAQTLEKRGKAKPKVNVKPSVVKVVSSPKLAPKRKAVEMHAAVIAAVKPLSSSSVLQEPPAKKAAVAVVPLVSEDKSVTVPEAENPRDSLVLPPTQSSSDSSPPEVSGPSSSQMSMKTRRLSSASTGKPPLSVEDDFEKLIWEISGGKLEAEIDLDPGKDEDDLLLELSEMIDS
Protein: NAD-dependent deacetylase sir2E (EC 2.3.1.286) (Silent information regulator 2E) (Q55DB0)
Organism: Dictyostelium discoideum (Social amoeba)
Function: NAD-dependent deacetylase, which plays an important role in the regulation of transcriptional repression (By similarity). May play a role in cell cycle. When overexpressed, the cell cycle is accelerated.
Subcellular location: Nucleus {ECO:0000269|PubMed:18707607}.
Interaction partners:
- NAD-dependent deacetylase sir2A
- NAD-dependent deacetylase sir2C
Sequence:
MTDDIVFENMVIDDTIVEEEDVEMKYYLKNKKEFEFLAKEMLSGKKILFITGAGLSINSGISAYRNTKTSVWSNFITEWGTRKKFEQDPAQFWNHFWLRTHEKQEYLDALPNSGHLAISNFVEYLGSNVITQNVDALHLKAKVPIEKLVEVHGRISLYKCITKGCRFEYDDTIDNIEIGDYSINGTTMKQGNLEITPPLCPECKKPILPQSLLFDENYSSHQFYNIEKAMDWIQEADIFIFIGTSFSVGITEEVICHAQSERKKMFNFNIFKETKISGLKSIVGKSEITLPLLERQLLYEAQKRNNGKKQIWYGNTIKRIVSENSMLLKEAMLKNDTKSSVKV
Protein: Bombesin (P84214)
Organism: Bombina bombina (Fire-bellied toad)
Function: Stimulates smooth muscle contraction. Role in induction of hypothermia, stimulation of DNA replication and release of many gastrointestinal hormones (By similarity).
Subcellular location: Secreted {ECO:0000269|PubMed:4537042}.
Interaction partners:
Sequence:
QQRLGNQWAVGHLM
Protein: RE62451p (Q6AWP2)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MGVTGLWKLIEPCGKPVPVETLEGKILAVDISIWLHQVVKGFQDNKGSALSNAHLLGLFHRLCKLLYYRVRPVFIFDGCVPQLKRDTIARRQQQRNKLSNEADRIQALLLQSLAKEKVVQQALGKNAELLLKSPVKRPPPAKKNDEDDLFKLPELPAASVQDNQDESEQDTSASASDSSFDESTARHSYNSSLQAIDVKSQHFRNLPADVRHEILTDIKETRKQSSWGRLHELPARSDDFCSFQMKRLLKRRAVQESLEQAEQEMGGHTLTYAELCDFFNEEGILTPTAIEQCTRQISSDEHTRFLLVRDLKKKAMESTKQEVKMEMIEEVPAEEEDEKPSTSTKKEAVKSVDLGTEFDEDLAKALSMSMEETKVYDEKDYEYDSDQELRLNRAQTKQLRHAAKGPARAYMIEYGGMNDEEVGNIMEATQFNDTQSLEKLLEITTVSTDMADNSIEEAKLISQAIEESKQLPQAIEESKKNLNEDKVEIVDTDTDSDLEEVMEVQELDKGKKNLEICVDITGQADSNDLFADIFEDGEANKIEKTISVEEDDDFIEVKDSEELKLDTEDENKPITNKSIKESNEVKPFIDEIIEVKDSQEAVPAEPNLKPDLESILNDLKKQTAAVKDIQLNVNEEEKPKPKVEISSILDELKVKMADVKNITLDNVKLSNSVPIILSSDDESTLKSSKIVPKQELIELCDSDDNKNNRLSPNKTPSKNKSIKDFFETSYVVKRTPDKSQASNETSPGTPKTPKPFFRKRTPKSGRKRASDANEDSDEEVSPTKRSSKASKSLFEPKEPEEEKTVDPEEIIKDAAEALKSQKTSEELQELATNLAQERKELEIERNRQDRMGMSISQRMSIDCQELLRLFGIPYIVAPMEAEAQCAFLNATDLTHGTITDDSDIWLFGGRTVYKNFFAQNKHVMEFRAEQIE
Protein: Ephrin type-A receptor 6 (EC 2.7.10.1) (EPH homology kinase 2) (EHK-2) (EPH-like kinase 12) (EK12) (Q9UF33)
Organism: Homo sapiens (Human)
Function: Receptor tyrosine kinase which binds promiscuously GPI-anchored ephrin-A family ligands residing on adjacent cells, leading to contact-dependent bidirectional signaling into neighboring cells. The signaling pathway downstream of the receptor is referred to as forward signaling while the signaling pathway downstream of the ephrin ligand is referred to as reverse signaling (By similarity).
Subcellular location: Membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}.
Interaction partners:
- Tyrosine-protein kinase ABL1
- Ephrin-A5
- Ephexin-1
- Ras GTPase-activating protein 1
- Ephrin-A2
- Ephrin-A1
- Ephrin-A4
- Ephrin-B2
- Ephrin type-A receptor 2
- Ephrin-A3
Sequence:
MGGCEVREFLLQFGFFLPLLTAWPGDCSHVSNNQVVLLDTTTVLGELGWKTYPLNGWDAITEMDEHNRPIHTYQVCNVMEPNQNNWLRTNWISRDAAQKIYVEMKFTLRDCNSIPWVLGTCKETFNLFYMESDESHGIKFKPNQYTKIDTIAADESFTQMDLGDRILKLNTEIREVGPIERKGFYLAFQDIGACIALVSVRVFYKKCPFTVRNLAMFPDTIPRVDSSSLVEVRGSCVKSAEERDTPKLYCGADGDWLVPLGRCICSTGYEEIEGSCHACRPGFYKAFAGNTKCSKCPPHSLTYMEATSVCQCEKGYFRAEKDPPSMACTRPPSAPRNVVFNINETALILEWSPPSDTGGRKDLTYSVICKKCGLDTSQCEDCGGGLRFIPRHTGLINNSVIVLDFVSHVNYTFEIEAMNGVSELSFSPKPFTAITVTTDQDAPSLIGVVRKDWASQNSIALSWQAPAFSNGAILDYEIKYYEKEHEQLTYSSTRSKAPSVIITGLKPATKYVFHIRVRTATGYSGYSQKFEFETGDETSDMAAEQGQILVIATAAVGGFTLLVILTLFFLITGRCQWYIKAKMKSEEKRRNHLQNGHLRFPGIKTYIDPDTYEDPSLAVHEFAKEIDPSRIRIERVIGAGEFGEVCSGRLKTPGKREIPVAIKTLKGGHMDRQRRDFLREASIMGQFDHPNIIRLEGVVTKRSFPAIGVEAFCPSFLRAGFLNSIQAPHPVPGGGSLPPRIPAGRPVMIVVEYMENGSLDSFLRKHDGHFTVIQLVGMLRGIASGMKYLSDMGYVHRDLAARNILVNSNLVCKVSDFGLSRVLEDDPEAAYTTTGGKIPIRWTAPEAIAYRKFSSASDAWSYGIVMWEVMSYGERPYWEMSNQDVILSIEEGYRLPAPMGCPASLHQLMLHCWQKERNHRPKFTDIVSFLDKLIRNPSALHTLVEDILVMPESPGEVPEYPLFVTVGDWLDSIKMGQYKNNFVAAGFTTFDLISRMSIDDIRRIGVILIGHQRRIVSSIQTLRLHMMHIQEKGFHV
Protein: Degringolade, isoform B (RE22765p) (Q8I0J6)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MSDSTIFRFSADSNVSSSSSNSSVSDSSVDSHSSIESNSGHNTSVESQSSAESDSSADSHSSLERPSPVERDLSVESDSSSATNTSESSVGEASNQLQSPQSNNPLNMANLSVSTEDAHSQIRSLTQDVIQMEAELDRMNRYCEEVVAQIDTFATRTSTPTTRRIRRRTSPVEVIDLSHLDRAPPVRSARNRDPDAFIDLCTPEGPRSRTVNLHSNDSLTILPRRSAENDPVVDLDVASPPKRVNRDIDESQKEELYKCPICMDSVSKREPVSTKCGHVFCRECIETAIRATHKCPICNKKLTARQFFRIYL
Protein: D-glycerol 3-phosphate phosphatase (D,L-glycerol 3-phosphate phosphatase) (G3P phosphatase) (O33194)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: Dephosphorylates D-glycerol 3-phosphate (sn-glycerol 1-phosphate). Is the final enzyme involved in the recycling/catabolism of glycerophospholipid polar heads. To a lesser extent, is also able to act on glycerol 2-phosphate and D-ribulose 5-phosphate, but cannot use D-glyceraldehyde 3-phosphate, dihydroxyacetone-phosphate, UMP or GMP as substrates.
Interaction partners:
- Tetratrico peptide repeat group 5 domain-containing protein
- NAD kinase
- Uncharacterized protein
- DNA repair protein RecN
- 16S/23S rRNA
- Glycerol kinase
- Putative acyltransferase plsB1
- Glycerol-3-phosphate acyltransferase
- NADP-dependent alcohol dehydrogenase C
- Putative lipoprotein LprJ
Sequence:
MKSIAQEHDCLLIDLDGTVFCGRQPTGGAVQSLSQVRSRKLFVTNNASRSADEVAAHLCELGFTATGEDVVTSAQSAAHLLAGQLAPGARVLIVGTEALANEVAAVGLRPVRRFEDRPDAVVQGLSMTTGWSDLAEAALAIRAGALWVAANVDPTLPTERGLLPGNGSMVAALRTATGMDPRVAGKPAPALMTEAVARGDFRAALVVGDRLDTDIEGANAAGLPSLMVLTGVNSAWDAVYAEPVRRPTYIGHDLRSLHQDSKLLAVAPQPGWQIDVGGGAVTVCANGDVDDLEFIDDGLSIVRAVASAVWEARAADLHQRPLRIEAGDERARAALQRWSLMRSDHPVTSVGTQ
Protein: Oxysterol-binding protein related protein (Q59TM0)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
- Phosphatidylinositol-binding protein
- 1-phosphatidylinositol 4-kinase
- Transcription elongation factor SPT6
- Protein EFR3
Sequence:
METLEVHSKDFLIKWINAPDNSIIDWEAKPLKKSINFSFYKKKEESLNQSETSLLDTNSTAALEPPTAIAPPPQRTRSRSASTASVNQFTKSNDVYRSKSRASTLLSINESDLILIKNYNKLVANELIHGKFEVEKGGMFAFVFDNSFSKTIAKSVQFSAKIVSKSKSEEHIAQQKVVAEVHDQHLFDENDVAPGETLQSIMLKKRRKKLQGFTKRYFVLNFGRETLSYFKVDDNKLRGQMPVKDCIVSANPSSREFIIDSGMEVWHLKAINKADFNAWVNAFNTVKKEETVVPTSTTEESDSKEPVIASTPLGASNSELQLIAQKLAQLKTENPSPLANEIHQDFLNLLTRAKGQSSSSPGSADVQSVFSSDFHDAVDHFDETGVYFLDDEGKIQEDEEVADDGESSSEEEEEEDEEFVQVAPSGVHADQGIVQDKELPQPTVEADDDNLYPLPHDPVSRSSDIPICTHTPPSILSFVRKNVGKDLSTIAMPVTYNEPTTVLQKFAEMLEYPEVATNALISDFQDESGEKLLRVAAFALSYLSTQRAKERNKRKPFTPLLGETYELVREDLGFRLISEKVSHRPPVFAYHIDTEHWTLDYALSPGQKFWGKQSEVTTKGTVYLKDKSTGEVFTWTQPTTMIKNIIAGETYAEPTGSVTIKSSNGYKAVAEFAKGGMWSGRSEGVIVKAFDNRKKELTYSVEGNWTESFTLKTKSTEKTIWQAGELLPQYQKKFGFTEFAGTLNKITEMEKGKLAPTDSRNRPDLQLYEKGDTDTAETLKNKLEQDQRDRRKQLETAGEEHIPKFFKLKRNGPVDEAEWEFIQGEKSYWNRRKKGDWDDLIKLW
Protein: Hyphally-regulated cell wall protein N-terminal domain-containing protein (G8BA82)
Organism: Candida parapsilosis (strain CDC 317 / ATCC MYA-4646) (Yeast) (Monilia parapsilosis)
Interaction partners:
Sequence:
MRFFETLLFAITWLTLQVAAAPVNKRFFSPSSPTFSLIAVHNGTTFNSNLVKFNGSAIKLGSDDKAFFGTIQANKGYILNLPFTNNSNETSTINVAVSNSTHLLTTTTKNGSASEHFGITNGWLSYLNSTQFLACPESASNATATTNSTSNSTIEYDLFSNPLNKTQCETGQGYNVKLLVQLSVPISFSPESNSFGFFKRDNVVKRFIDKLFK
Protein: Myosin 10A, isoform E (EC 5.6.1.8) (M9PGV5)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
Sequence:
MSQSVRASKSSSCQAVQLNSGGGSVPHKFSSIVNKVESLISKMHHDKVNNFKLLQQQGQQQDQDPNRERDRDRDRDRGAQDDGEQECKCASLDSLNNLTDEEHEMLYTDSDDAEIAHITGTTAAQVHHAQMQMQSLHQHHQQQQQQQHIRRSDLDQLTNESIRELNEQCCASMGMHEAGGDLCGSGSGGDLGMANDNAWSVEEDIVYKCCTTATLTSNSSAGSLCEQCCLEEQLNFKMQMSQRDDNNNNEEQDMPHMESHPTSSSSCSPAPASVPASAPAPGPAPASAPSPITTSNLIAFQGGNNPLASTAMLIPGGNKTRRVSNASSGSVSRMETILEEPTESKISVKEILARFETMNSNESQSKASTLSSGARAAAQTLNVPLERLESRQAHAQRNEHGVDGGSRQNEQLQQSELHHHLQQQQQQQQQQQHHQQQQQQQQLEDAMEEQHMATDHQQQQQQQLGQQQGQQQRFLKQQSYLHSARKSNAGQQPSSLTNGQVHHQEQMLQQQQQQSQSLPHHDLDANYLQDESNGGTPPSVTKYSLLQFAMQHFRNDQLRDADRHHERHQSAANRSYAELVKWQGHAIRLPLLRLPNDLAPLALECFDCILRYCGDIPLDPDLTEVKCVYTVLMHCHKYLALRDEVYCQLMKQTTANRSPCPDSSQRAWRLLSILAAYFGCSDALRPYLMEHLTSAASDRRRSCHGTAAVCLTNLRKTARCGGRKNVPSVEEVTAVSAGRSARRQIYRLPGGAERVVNTRCSTVVADVIAELCALLGVESEAEQQEFSLYCIVQGDAFTMPLAADEYILDVTTELLKSGQPFYLIFCRSVWHFALKREPAPMPLYVEVLFNQVAPDYLEGLLLELPGNGVPVPEMVRDMARIAALLHRAADLSHVPAMKEIKFLLPKPALGIREIRPAQWVGLVQSAWPQVANLSPGQVKAQFLNVLATWPLFGSSFFAVKRIWAEEGPHVEDNHSPMWRDLILALNRRGVLFLDPNTHETLQHWSFMEVISTRKVRSEDGALFLDMKVGNLMQQRVIRVQTEQAHEISRLVRQYITMAQISQRDKRELN
Protein: Phosphatidylinositol-3-phosphate phosphatase MTMR7 (EC 3.1.3.64) (Inositol 1,3-bisphosphate phosphatase) (Myotubularin-related protein 7) (Q9Z2C9)
Organism: Mus musculus (Mouse)
Function: Phosphatase that specifically dephosphorylates phosphatidylinositol 3-phosphate (PtdIns(3)P) and inositol 1,3-bisphosphate (Ins(1,3)P2).
Subcellular location: Cytoplasm {ECO:0000269|PubMed:12890864}. Endomembrane system {ECO:0000269|PubMed:12890864}; Peripheral membrane protein {ECO:0000269|PubMed:12890864}; Cytoplasmic side {ECO:0000269|PubMed:12890864}. Note=May partially localize to endosomes and/or the Golgi apparatus. {ECO:0000269|PubMed:12890864}.
Interaction partners:
- Myotubularin-related protein 9
- Polyphosphoinositide phosphatase
- Phosphatidylinositol-3-phosphatase SAC1
- 1-phosphatidylinositol 3-phosphate 5-kinase
- CDP-diacylglycerol--inositol 3-phosphatidyltransferase
- Type II inositol 3,4-bisphosphate 4-phosphatase
- Inositol polyphosphate-4-phosphatase type I A
- Phosphatidylinositide phosphatase SAC2
- Type 2 phosphatidylinositol 4,5-bisphosphate 4-phosphatase
- Type 1 phosphatidylinositol 4,5-bisphosphate 4-phosphatase
Sequence:
MEHIRTPKVENVRLVDRVSCKKAALGTLYLTATHVIFVENAPDTRKETWILHSQISTIEKQATTATGCPLLIRCKNFQIVQLVIPQERDCHDVYISLIRLARPVKYEELYCFSFNPKLDKEEREQGWLLVDLSEEYKRMGLPDNYWQLSDVNRDYRVCDSYPTELYVPRSATAHIIVGSSKFRSRRRFPALSYYCKDSHASICRSSQPLSGFSARCLEDEQMLQAIRKANPGSDFIYVVDTRPKLNAMANRAAGKGYENEDNYSNIKFQFIGIENIHVMRNSLQKMLEVCELKSPSMSDFLWGLENSGWLRHIKAIMDAGIFIAKAVSEEGASVLVHCSDGWDRTAQVCSVASLLLDPYYRTLKGFMVLIEKDWISFGHKFNHRYGNLDGDPKEISPVIDQFIECVWQLTEQFPCAFEFNERFLTHIQHHVYSCQFGNFLCNSQKERRELKIQERTYSLWSNLWKNRADYLNPLFRADHSQTQGSLHLPTAPCNFTYKFWNGMYNRFEKGLQPRQSVTDYLMAVKEESQQLEEELESLEERLEKIQKVHLHGTKVKSKQSEPSKHSGFSTSDHSTANTPQDYSGNSKSFPSRSPSQGDEDSALILTQDNLKSSDPDLSVNSDQESGVEDLSCRSPSGGEHAPSEDSGKDRDSDEAVFLTA