wanglab/gogpt-training-data huggingface dataset:
Protein: Protein VAC14 homolog (Tax1-binding protein 2) (Q08AM6)
Organism: Homo sapiens (Human)
Function: Scaffold protein component of the PI(3,5)P2 regulatory complex which regulates both the synthesis and turnover of phosphatidylinositol 3,5-bisphosphate (PtdIns(3,5)P2). Pentamerizes into a star-shaped structure and nucleates the assembly of the complex. The pentamer binds a single copy each of PIKFYVE and FIG4 and coordinates both PIKfyve kinase activity and FIG4 phosphatase activity, being required to maintain normal levels of phosphatidylinositol 3-phosphate (PtdIns(3)P) and phosphatidylinositol 5-phosphate (PtdIns(5)P). Plays a role in the biogenesis of endosome carrier vesicles (ECV) / multivesicular bodies (MVB) transport intermediates from early endosomes.
Subcellular location: Endosome membrane {ECO:0000269|PubMed:15542851, ECO:0000269|PubMed:17556371}. Microsome membrane {ECO:0000250|UniProtKB:Q80W92}. Note=Mainly associated with membranes of the late endocytic pathway.
Interaction partners:
- Polyphosphoinositide phosphatase
- 1-phosphatidylinositol 3-phosphate 5-kinase
- WD repeat domain phosphoinositide-interacting protein 1
- DNA repair and recombination protein RAD54-like
- Lysosome-associated membrane glycoprotein 2
- DNA repair and recombination protein RAD54B
- Protein MTSS 2
- Amyloid-beta precursor protein
- Phosphatidylinositol 3-kinase catalytic subunit type 3
- N-acylethanolamine-hydrolyzing acid amidase
Sequence:
MNPEKDFAPLTPNIVRALNDKLYEKRKVAALEIEKLVREFVAQNNTVQIKHVIQTLSQEFALSQHPHSRKGGLIGLAACSIALGKDSGLYLKELIEPVLTCFNDADSRLRYYACEALYNIVKVARGAVLPHFNVLFDGLSKLAADPDPNVKSGSELLDRLLKDIVTESNKFDLVSFIPLLRERIYSNNQYARQFIISWILVLESVPDINLLDYLPEILDGLFQILGDNGKEIRKMCEVVLGEFLKEIKKNPSSVKFAEMANILVIHCQTTDDLIQLTAMCWMREFIQLAGRVMLPYSSGILTAVLPCLAYDDRKKSIKEVANVCNQSLMKLVTPEDDELDELRPGQRQAEPTPDDALPKQEGTASGGPDGSCDSSFSSGISVFTAASTERAPVTLHLDGIVQVLNCHLSDTAIGMMTRIAVLKWLYHLYIKTPRKMFRHTDSLFPILLQTLSDESDEVILKDLEVLAEIASSPAGQTDDPGPLDGPDLQASHSELQVPTPGRAGLLNTSGTKGLECSPSTPTMNSYFYKFMINLLKRFSSERKLLEVRGPFIIRQLCLLLNAENIFHSMADILLREEDLKFASTMVHALNTILLTSTELFQLRNQLKDLKTLESQNLFCCLYRSWCHNPVTTVSLCFLTQNYRHAYDLIQKFGDLEVTVDFLAEVDKLVQLIECPIFTYLRLQLLDVKNNPYLIKALYGLLMLLPQSSAFQLLSHRLQCVPNPELLQTEDSLKAAPKSQKADSPSIDYAELLQHFEKVQNKHLEVRHQRSGRGDHLDRRVVL
Protein: Temporin-1Te (TE) (Temporin-E) (P56920)
Organism: Rana temporaria (European common frog)
Function: Has no antibacterial activity. Has hemolytic activity.
Subcellular location: Secreted {ECO:0000269|PubMed:34235566, ECO:0000269|PubMed:9022710}.
Interaction partners:
Sequence:
VLPIIGNLLNSLL
Protein: Lin-52, isoform A (Lin-52, isoform B) (Myb-MuvB complex subunit Lin-52) (Q9W482)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Protein lin-54 homolog
- LD06557p
- LD07342p
- Retinoblastoma family protein
- RE32990p
- Transcription factor E2F2
- Myb protein
- LD05287p
- Chromatin assembly factor 1 p55 subunit
- Histone deacetylase HDAC1
Sequence:
MSNAETTTDLLSTETILKAADEEVEKASASSSSTLLAEKDVPEVKERPITPEDELISMETLRPSPVQWPERFPGMDEFLSMSDTPMYTRSTNYTSNLTDDDMVKINELAQLPPEDLIDKIKSMHDEIYQLGLREAMEMTRGKLLGIFDRDRAPKRQP
Protein: Protein SYG1 (P40528)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: May function in G-protein coupled signal transduction.
Subcellular location: Cell membrane {ECO:0000269|PubMed:7592711}; Multi-pass membrane protein {ECO:0000269|PubMed:7592711}.
Interaction partners:
- Phosphate system positive regulatory protein PHO81
- Vacuolar transporter chaperone complex subunit 4
- Low-affinity phosphate transporter PHO90
- Inorganic phosphate transporter PHO87
- Glycerophosphocholine phosphodiesterase GDE1
- Vacuolar transporter chaperone complex subunit 2
- Low-affinity phosphate transporter PHO91
Sequence:
MKFADHLTESAIPEWRDKYIDYKVGKKKLRRYKEKLDAEEEQSSSYRSWMPSVSVYQTAFQQREPGKSRSDGDYRSGPAFKKDYSALQREFVADFIEDWLISFQLSKCNEFYLWLLKECDKKFEVLQSQLHYYSLQKNYERDNLNRSSSNVDMSTSLYAAGLAGRSDSRVNSIDSDSRSVMYGSMPCTKEAKKPRLSLLAYCQKVLKDNRLLPSWPKRGFSLLQDLRQDASSRGRETFAFGASFLETMTTTQARNLLSNAIIEYYLYLQLVKSFRDINVTGFRKMVKKFDKTCHTRELTTFMSYARTHYTLFKHADANVQLVAQKMQQITSSQPTPTSELSSAQRDKEPITWLETQITEWFTTALTNSPKDRKHNTHKLKKLTIQYSISEQMVHRNNRSIVQMLVVGLGIGVSMTLITYTLYLGISSEETSFTHKILFPLWGGWYMVLLIAFLFLVNCFIWHRTGINYRFIMLGEIQSKNGTQFFNNDFATSKIPLKLYFLTFFIVPCAVCSMLSFALEKLTPLGFLYIGIVSFLFLCPSGLIPYWDKVVHTRKWLVVTLIRLMMSGFFPVEFGDFFLGDIICSLTYSIADIAMFFCVYSHTPNNLCGSSHSRAMGVLSCLPSYWRFMQCLRRFADSGDWFPHLLNAAKYTLGIAYNATLCAYRLSDRSEQRRTPFIVCATLNSILTSAWDLVMDWSFAHNTTSYNWLLRDDLYLAGKKNWENGSYSFSRKLVYYFAMIWDILIRFEWIVYAIAPQTIQQSAVTSFILALLEVLRRFVWIIFRVENEHVANVHLFRVTGDAPLPYPIAQVGDDSMDSSDLGSKAFSSLNDIPITPSHDNNPHSFAEPMPAYRGTFRRRSSVFENISRSIPWAHATDFQRPTVNTVDDRSPETDSESEVESIM
Protein: Dipeptidyl peptidase 1 (EC 3.4.14.1) (Cathepsin C) (Cathepsin J) (Dipeptidyl peptidase I) (DPP-I) (DPPI) (Dipeptidyl transferase) [Cleaved into: Dipeptidyl peptidase 1 exclusion domain chain (Dipeptidyl peptidase I exclusion domain chain); Dipeptidyl peptidase 1 heavy chain (Dipeptidyl peptidase I heavy chain); Dipeptidyl peptidase 1 light chain (Dipeptidyl peptidase I light chain)] (P53634)
Organism: Homo sapiens (Human)
Function: Thiol protease. Has dipeptidylpeptidase activity. Active against a broad range of dipeptide substrates composed of both polar and hydrophobic amino acids. Proline cannot occupy the P1 position and arginine cannot occupy the P2 position of the substrate. Can act as both an exopeptidase and endopeptidase. Activates serine proteases such as elastase, cathepsin G and granzymes A and B. Can also activate neuraminidase and factor XIII.
Subcellular location: Lysosome {ECO:0000305|PubMed:7665576}.
Interaction partners:
- Apoptosis regulator Bcl-2
- Bcl-2-like protein 1
- BH3-interacting domain death agonist
- Granzyme A
- Protein ERGIC-53
- Chymase
- Putative glycosyltransferase 6 domain-containing protein 1
- Cystatin-F
- Granzyme B
- Cathepsin D
Sequence:
MGAGPSLLLAALLLLLSGDGAVRCDTPANCTYLDLLGTWVFQVGSSGSQRDVNCSVMGPQEKKVVVYLQKLDTAYDDLGNSGHFTIIYNQGFEIVLNDYKWFAFFKYKEEGSKVTTYCNETMTGWVHDVLGRNWACFTGKKVGTASENVYVNIAHLKNSQEKYSNRLYKYDHNFVKAINAIQKSWTATTYMEYETLTLGDMIRRSGGHSRKIPRPKPAPLTAEIQQKILHLPTSWDWRNVHGINFVSPVRNQASCGSCYSFASMGMLEARIRILTNNSQTPILSPQEVVSCSQYAQGCEGGFPYLIAGKYAQDFGLVEEACFPYTGTDSPCKMKEDCFRYYSSEYHYVGGFYGGCNEALMKLELVHHGPMAVAFEVYDDFLHYKKGIYHHTGLRDPFNPFELTNHAVLLVGYGTDSASGMDYWIVKNSWGTGWGENGYFRIRRGTDECAIESIAVAATPIPKL
Protein: Dolichyl-phosphate-mannose--protein mannosyltransferase 3 (EC 2.4.1.109) (P47190)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Protein O-mannosyltransferase involved in O-glycosylation which is essential for cell wall rigidity. Forms a heterodimeric complex with PMT5 and more rarely with PMT1 to transfer mannose from Dol-P-mannose to Ser or Thr residues on proteins. Seems to have redundant activity to PMT2.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P33775}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Dolichyl-phosphate-mannose--protein mannosyltransferase 2
- Dolichyl-phosphate-mannose--protein mannosyltransferase 5
- Dolichyl-phosphate-mannose--protein mannosyltransferase 1
- Probable alpha-1,6-mannosyltransferase MNN10
- Mannan polymerase complexes subunit MNN9
- Mannan polymerase I complex VAN1 subunit
- Putative glycosyltransferase HOC1
- Mannan polymerase II complex ANP1 subunit
- Dolichyl-phosphate-mannose--protein mannosyltransferase 4
- Probable alpha-1,6-mannosyltransferase MNN11
Sequence:
MPYRVATGYSEKSTDDDLIWRTPIVKEELEDADNFLKDDAELYDKVKNESAVSHLDTIVMPIIFTVLGMFTRMYKIGRNNHVVWDEAHFGKFGSYYLRHEFYHDVHPPLGKMLVGLSGYLAGYNGSWDFPSGEVYPDYIDYVKMRLFQAMFSSLCVPLAYFTGRAIGFSRLSVWLFTILVIFENSYATLGKFILLDSMLLFFTVSSYFCLAKFHTMRKSPFSARWWLWLCLTGLNLGCAISVKMVGLFIISVVGIYTISELWNLLSDRSVSWKVYVNHWLARIFGLIIIPVCVFLLCFKIHFDLLSNSGPGDSTMPSLFQASLNGTKVGKGPRDVALGSSIISIKNQALGGALLHSHVQPFPEGSEQQQVTVYGYSDANNEWFFQRIRGVEPWTDAENKTIEFVKGGEMYRLMHRLTGKNLHTHEVPAPISKSEYEVSAYGDVDLGDYKDNWIIEIVEQVGEEDPTLLHPLSTSFRIKNSILGCYLAQSGKHLPEWGFRQGEVVCLKHASKRDKRTWWNIETHENERLPQGEDFVYPKTSFFRNFMQLNSAMMATNNALVPNPEKFDGIASSAWQWPTLNVGVRLCEWSEKSIKYFLLGSPASVWPSSIAVCALIIHVIFLTLKWQRQCVILSDPVERDVFVMAAFYPLLAWLLHYMPFVVMSRVVYAHHYLPTLYFALMILSYYFDMITKRWATRNTGKFLRLGAYIVYGSIVIAGFFYFSPFSFGMDGPVDDYAYLAWLPTWQIVEDIRNT
Protein: TATA box binding protein (A0A8I6A9T0)
Organism: Rattus norvegicus (Rat)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MDQNNSLPPYAQGLASPQGAMTPGIPIFSPMMPYGTGLTPQPVQNTNSLSILEEQQRQQQQQQQQQQQQQQQAVATAAASVQQSTSQQPTQGASGQTPQLFHSQTLTTAPLPGTTPLYPSPMTPMTPITPATPASESSGIVPQLQNIVSTVNLGCKLDLKTIALRARNAEYNPKRFAAVIMRIREPRTTALIFSSGKMVCTGAKSEEQSRLAARKYARVVQKLGFPAKFLDFKIQNMVGSCDVKFPIRLEGLVLTHQQFSSYEPELFPGLIYRMIKPRIVLLIFVSGKVVLTGTSRPTSGVQPPWQPCPATAHLAGRRNTAALDSRRERGYGGRLRPDPEAVRTLAAGRRAGGRNARTPAPQVRAAPPGPTTQAARPLCLETARCAASRPVPPQRSPTPP
Protein: procollagen-proline 4-dioxygenase (EC 1.14.11.2) (Q8MSK0)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Endoplasmic reticulum lumen {ECO:0000256|ARBA:ARBA00004319}.
Interaction partners:
Sequence:
MYILKKLTFIGFLSACFINCQGFVNSNPKKSYAASTMELMKLLEVEDELVDNLKGYVKTLKMKFNLMERSLIDMSRENMEMKSDYESYLGNPLNSFRLIHRLHTSWRKWYQYAIKVENNALGHIENARLMRKMLPTSSDLQQACRGIHDLMYFYDLKPEELAAGNLAGYSQPGTGLTAYDCLALGEFGVQNQKDDLAEAWYNLSLTRFDNIIEKYQVHKAWALLLAKNKQLTEAFQHFENKPEGIVASNEVIHFEGVLATTQNCTAVVQKPSKKLHCRYNTSTTPFTRIAPLKMEELGLDPYMVVFHDVIYDTEIDGMLNSSDFGLSESVSGLKSEVRTSKDSHIVDAKTLNERVTDMTGLSMEMSDPFSLINYGLGGHFILHHDFHEYTNTTRLKQGDRIATVLFYLREVDSGGATVFPMLNITVMPKKGSAVFWYNLHNSGAVNSKTLHTACPVISGSKYVLTKWINELPQMFVTPCMKDSNLRPPQKE
Protein: HTH cro/C1-type domain-containing protein (Q9A407)
Organism: Caulobacter vibrioides (strain ATCC 19089 / CIP 103742 / CB 15) (Caulobacter crescentus)
Interaction partners:
- Addiction module killer protein
Sequence:
MVTLSRFDPVEMIDNAEAVAVFLADAFDTGDADYIQHMLGLIARSKGMAEVAEKAGLGRESLYKALKDGASPRFDTILRVVHALNLKLALVSATEANSAEDADDEAAA
Protein: Mediator of RNA polymerase II transcription subunit 21 (Mediator complex subunit 21) (RNA polymerase II holoenzyme component SRB7) (RNAPII complex component SRB7) (hSrb7) (Q13503)
Organism: Homo sapiens (Human)
Function: Component of the Mediator complex, a coactivator involved in the regulated transcription of nearly all RNA polymerase II-dependent genes. Mediator functions as a bridge to convey information from gene-specific regulatory proteins to the basal RNA polymerase II transcription machinery. Mediator is recruited to promoters by direct interactions with regulatory proteins and serves as a scaffold for the assembly of a functional preinitiation complex with RNA polymerase II and the general transcription factors.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- Mediator of RNA polymerase II transcription subunit 6
- Mediator of RNA polymerase II transcription subunit 11
- Mediator of RNA polymerase II transcription subunit 14
- Mediator of RNA polymerase II transcription subunit 30
- Mediator of RNA polymerase II transcription subunit 12
- Mediator of RNA polymerase II transcription subunit 4
- Mediator of RNA polymerase II transcription subunit 9
- Mediator of RNA polymerase II transcription subunit 8
- Mediator of RNA polymerase II transcription subunit 31
- Mediator of RNA polymerase II transcription subunit 16
Sequence:
MADRLTQLQDAVNSLADQFCNAIGVLQQCGPPASFNNIQTAINKDQPANPTEEYAQLFAALIARTAKDIDVLIDSLPSEESTAALQAASLYKLEEENHEAATCLEDVVYRGDMLLEKIQSALADIAQSQLKTRSGTHSQSLPDS
Protein: Basonuclin zinc finger protein 2 (H0Y6W5)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
SEEAEVDVRERETQRDREPKRARDLTLRDSCTDNSMQFGTRTTTAEPGFMGTWQNADTNLLFRMSQQAIRCTLVNCTCECFQPGKINLRTCDQCKHGWVAHALDKLSTQHLYHPTQVEIVQSNVVFDISSLMLYGTQAVPVRLKILLDRLFSVLKQEEVLHILHGLGWTLRDYVRGYILQDAAGKVLDRWAIMSREEEIITLQQFLRFGETKSIVELMAIQEKEGQAVAVPSSKTDSDIRTFIESNNRTRSPSLLAHLENSNPSSIHHFENIPNSLAFLLPFQYINPVSAPLLGLPPNGLLLEQPGLRLREPSLSTQNEYNESSESEVSPTPYKNDQTPNRNALTSITNVEPKTEPACVSPIQNSAPVSDLTKTEHPKSSFRIHRMRRMGSASRKGRVFCNACGKTFYDKGTLKIHYNAVHLKIKHRCTIEGCNMVFSSLRSRNRHSANPNPRLHMPMLRNNRDKDLIRATSGAATPVIASTKSNLALTSPGRPPMGFTTPPLDPVLQNPLPSQLVFSGLKTVQPVPPFYRSLLTPGEMVSPPTSLPTSPIIPTSGTIEQHPPPPSEPVVPAVMMATHEPSADLAPKKKPRKSSMPVKIEKEIIDTADEFDDEDDDPNDGGAVVNDMSHDNHCHSQEEMSPGMSVKDFSKHNRTRCISRTEIRRADSMTSEDQEPERDYENESESSEPKLGEESMEGDEHIHSEVSEKVLMNSERPDENHSEPSHQDVIKVKEEFTDPTYDMFYMSQYGLYNGGGASMAALHESFTSSLNYGSPQKFSPEGDLCSSPDPKICYVCKKSFKSSYSVKLHYRNVHLKEMHVCTVAGCNAAFPSRRSRDRNRNLRMERTIGPGHRDSLHLLPT
Protein: glutamate--tRNA ligase (EC 6.1.1.17) (Glutamyl-tRNA synthetase) (Q587C5)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
- Tyrosyl/methionyl-tRNA synthetase, putative
- GST N-terminal domain-containing protein
- isoleucine--tRNA ligase
- proline--tRNA ligase
- leucine--tRNA ligase
- arginine--tRNA ligase
- 60S ribosomal protein L29
- 60S ribosomal subunit protein L31, putative
- 60S ribosomal protein L5, putative
- Tyrosyl-tRNA synthetase, putative
Sequence:
MLRLANKFTVKISLISRLLKEIPFCVMSKHEEDCQKAPEHDKLTLTNAEEGKVVTRFPPEASGFLHIGHAKAALINSMLALKYKGKLVMRFDDTNPSKEKDHFEQAILDDLATLGVTWDVGPTYSSDYMELLYEKADELIEKGLAYCDKTTREEMQKCRFNGVPTSYRDISIEETKRMWSEMKEGSAEGQETCLRAKISVDNENKAMRDPVIYRVNLTPHARQGTKYKAYPTYDFCCPIIDSVEGITHALRTNEYHDRNDQYYWFCDALGLRKPIVEDFSRLNMEYAVMSKRKLTQLIDSKVVDGWDDPRFPTVRALVRRGLKMSALRQFVQEQGMSKTVNFMEWSKLWYFNTQILDPSVPRYTVVSNTLKVRCVVEGIGGLEKCEKLLHKKAPDMGSKVFYKSGVIFLDAEDVALLKEGDEVTLMDWGNAFIRNIRTSGESGTITDADIVLNLEGDVKKTKHKLTWVAENPEAEVMEINEYDHLLTKKKPDPEESLDSILAAVTKYTQEVYSEAATSALKKGDIIQLERRGYYIVDNVIPRKVLIAIPDGREKVNHLSAKAHHLKYVAKVSQPAAANDLAAKRAAKAAKKAAQKQDSKSQNKEQAV
Protein: Large ribosomal subunit protein bL17 (50S ribosomal protein L17) (P9WHD3)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Interaction partners:
- Large ribosomal subunit protein uL15
- Large ribosomal subunit protein uL22
- Small ribosomal subunit protein uS11
- Small ribosomal subunit protein uS10
- Large ribosomal subunit protein bL32
- Small ribosomal subunit protein uS9
- Small ribosomal subunit protein uS14B
- Small ribosomal subunit protein uS12
- Large ribosomal subunit protein bL20
- Large ribosomal subunit protein bL25
Sequence:
MPKPTKGPRLGGSSSHQKAILANLATSLFEHGRITTTEPKARALRPYAEKLITHAKKGALHNRREVLKKLRDKDVVHTLFAEIGPFFADRDGGYTRIIKIEARKGDNAPMAVIELVREKTVTSEANRARRVAAAQAKAKKAAAMPTEESEAKPAEEGDVVGASEPDAKAPEEPPAEAPEN
Protein: BTB domain-containing protein (Q57YR0)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MYVDSDEEAAAVSTVVEQVAPYAAAVTPTSNAWSERVVARLRSLQRELCNFNVALPDVVSFRVDGKDFCVRRELLLKDPQSVLFLMAVKHFQQHTADRGVENAIEVPCRNPMLFGMLLNLLRGYKNPIPEAYRDACYAEARFYGLLRSWSSRYAVVVEGPFCPLPCSGRLFSDVVCATAGSYCRRGKYRITFNVLRCDTMAVGVISRDKEKMWADSVDQWEGFALCWNDGRTVHNFGEAVMERTGVTYAANARIRVELDCDEGILSWCFLERQQMSVVRLPPMSFAFVVVLARSSEVQIVGSD
Protein: Ferric reduction oxidase 7, chloroplastic (AtFRO7) (EC 1.16.1.7) (Ferric-chelate reductase 7) (Q3KTM0)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Ferric chelate reductase involved in iron mobilization from the cytosol into the chloroplast. May participate in the transport of electrons to a Fe(3+) ion via FAD and heme intermediates. Might be involved iron homeostasis in trichomes.
Subcellular location: Plastid, chloroplast membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
- Protein TIC 21, chloroplastic
- Metal transporter Nramp3
- ABC transporter I family member 11, chloroplastic
- Vacuolar iron transporter 1
- Probable metal-nicotianamine transporter YSL4
- Metal transporter Nramp4
- Fe
- Protein MITOFERRINLIKE 1, chloroplastic
- Solute carrier family 40 member 1
- Probable metal-nicotianamine transporter YSL6
Sequence:
MDDHETPLLSKDLSSSSSSSSSSSSVVVSSLKWILKVVMSVIFVTWVVFLMMYPGSLGDQILTNWRAISSNTLFGLTGSMFLIFSGPILVIAILASLYLIISGEETVFTKKKITKFPRFRLWTFPVLVDGPFGVVSAAEFLGIMVFSVFFLWAIYAYTLRNLNVLDYFHVLPNNRSIFLLELTGLRFGMIGLLCMVFLFLPISRGSILLRLIDIPFEHATRYHVWLGHITMTFFSLHGLCYVVGWTIQGQLLELLFEWKATGIAVLPGVISLVAGLLMWVTSLHTVRKNYFELFFYTHQLYIVFVVFLALHVGDYLFSIVAGGIFLFILDRFLRFYQSRRTVDVISAKSLPCGTLELVLSKPPNMRYNALSFIFLQVKELSWLQWHPFSVSSSPLDGNHHVAVLIKVLGGWTAKLRDQLSTLYEAENQDQLISPESYPKITTCVEGPYGHESPYHLAYENLVLVAGGIGITPFFAILSDILHRKRDGKDCLPGKVLVVWAIKNSDELSLLSAIDIPSICHFFSKKLNLEIHIYVTRQSEPCLEDGMVHKVVHPSVKTPWTNGCSMSVLVGTGDNIWSGLYLIISTIGFIAMITLVDIFYINKYNITTWWYKGLLFVVCMVASVLIFGGLVVVFWHRWEHKTGEVEANGNDKVDLNGEETHNPSAAELKGLAIEEDVQNYTTIRYGTRPAFREIFESLNGKWGSVDVGVIVCGPATLQTTVAKEIRSHSIWRSANHPLFHFNSHSFDL
Protein: Leucine-rich repeat receptor-like serine/threonine-protein kinase At2g14510 (EC 2.7.11.1) (Q9ZQR3)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Cell membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}.
Interaction partners:
Sequence:
METRNKFMLLACATFSIMSLVKSQNQQGFISLDCGLPSKESYIEPSSNLTFISDVNFIRGGKTGNIQNNSRTNFIFKPFKVLRYFPDGIRNCYSLSVKQGTKYLIRTLFYYGNYDGLNTSPRFDLFLGPNIWTSVDVLIADVGDGVVEEIVHVTRSNILDICLVKTGTSTPMISAIELRPLRYDTYTARTGSLKSMAHFYFTNSDEAIRYPEDVYDRVWMPYSQPEWTQINTTRNVSGFSDGYNPPQGVIQTASIPTNGSEPLTFTWNLESSDDETYAYLFFAEIQQLKVNETREFKILANGVDYIDYTPWKFEARTLSNPAPLKCEGGVCRVQLSKTPKSTLPPLMNAIEIFSVIQFPQSDTNTDEVIAIKKIQSTYQLSRISWQGDPCVPKQFSWMGVSCNVIDISTPPRIISLDLSLSGLTGVISPSIQNLTMLRELDLSNNNLTGEVPEFLATIKPLLVIHLRGNNLRGSVPQALQDREKNDGLKLFVDPNITRRGKHQPKSWLVAIVASISCVAVTIIVLVLIFIFRRRKSSTRKVIRPSLEMKNRRFKYSEVKEMTNNFEVVLGKGGFGVVYHGFLNNEQVAVKVLSQSSTQGYKEFKTEVELLLRVHHVNLVSLVGYCDEGIDLALIYEFMENGNLKEHLSGKRGGSVLNWSSRLKIAIESALGIEYLHIGCQPPMVHRDVKSTNILLGLRFEAKLADFGLSRSFLVGSQAHVSTNVAGTLGYLDPEYYLKNWLTEKSDVYSFGIVLLESITGQPVIEQSRDKSYIVEWAKSMLANGDIESIMDPNLHQDYDSSSSWKALELAMLCINPSSTQRPNMTRVAHELNECLEIYNLTKIRSQDQNSSKSLGHTVTFISDIPSAR
Protein: GPI transamidase component GAA1 (Q7YTW5)
Organism: Trypanosoma brucei brucei
Interaction partners:
Sequence:
MLQAGTKKFLREYGSTCAPLFLALGVCLICCLPAACPKENFIDENAISVSRVPVITGMLGELHMDTRISQYTRVVRGRRSVGSESIAVYVNAAFEPSVVLANHLIYVLREKENMACDTNFYFFNDTSKDWPIPDSFVRAAIVINVTSFHTNNLCFNVFGANGMQPNQDLFNLAVAIAEKWRFNIDVLCQNPYISFSTSRPIYEHYFLALQTALVAPLRYQPWYKMRSRGISLLAISTEKSERRTKSSYGYNMAAAHEQLIATLSYLHERFHHSTSVWIPLSVDQYVEYDVIQFATILFVASLLSTCYSIYEVEGFSFSPCAALVSATGLAALVSTLNFGTAGFFVSSGVLTVGLGAFAWDMSWGAINAVVLCLLIILQPVAGLVMGFGATLQLQFIHVRCRKWHVLLIGAILSWIVLVALTEVMKAKLFDTETTAGVYFSFFLYPNALWISSRQIRSTLGA
Protein: non-specific serine/threonine protein kinase (EC 2.7.11.1) (A0A1D8PQT9)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Interaction partners:
- Eukaryotic translation initiation factor 2 subunit alpha
- Serine/threonine-protein kinase TOR
- Ubiquitin-binding TORC1 subunit
- Amino acid starvation-responsive transcription factor
- Target of rapamycin complex subunit LST8
- Gcn1p
- Elongation factor 3
- Aspartate--tRNA ligase
- Translation initiation factor eIF2B subunit alpha
- Eukaryotic translation initiation factor 2A
Sequence:
MPETSITSDLEHRQQDEISSISSIYGDIFKDITPTGLVWNKKPSPHFQVFLSSSNNPDRPTVSITLDIEFTPTYPLSPPKVKLLNARNLLKINIAKLEKKCKDLIKEYPEQEVSFTIISELIFMLDEIQTTTEKVLSLEEERELRLRNERRALEEKEAKQKKDEELARKKQNKELNEQIQKIQGEFDDDFTDDQDLDMSTTNDNNNSLIPLDKDQFFIFENAMEATIPNTRRKFKFRAISGFIRYNQKGVFNSIGSQYIVKPFIDNEIRNKIENKGSDLAFLLTVIDLTNEYWQTDKGKREIQDLESELQSIMSINHSNILKLIGFQIDKTNVWRVRLLTEFSPVSETLYDILPTAEFINWALARTWLIQLLPAMEYLHNAGFIHKLICPMTIVIFQEKDQLYYQNSTNELLSNSIGGGGGGGEDSLTISAKKVLKLCHPSYGYRLLEMISLHPNEGETLDRSPQVNPPAWLAPELKTSGYHYKSDIWDLGVLFLRVMLGFDILNTTYHTPSDFINKFSVKDFVGAEEYASLVYDVLSKMLQVKLSKRPSPLELNAVKFLRDGPIISKLQSETNLSRMKKNVETDLVSSTNTRHVQIQGHEQDSTATTKHLNIYHQNISRRRLSNQNTQHPYFGENSSLIMPSGSQRNMGRYARDFEEIGKLGRGGFGEVVKARSRMEGIFYAVKKIKHRADKLDSLLSEVLSLARLNHQYIVRYYGTWVEELEDTSAIPSNSTSAIASDDEEEEEEEDDTEGDFGDDDLESTFSSRVGRSSSVLPSYDNSFQVDYISTSFDPRIEFDESSEEDDQNEDDDPFVFANSTDDISNNETEDRSKSDSKEVSVKKPKDVVNSSKNASPKSILYIQMEFCENNTLLNLIEQGLPNNPDEYWRLFRQLLEAVSYIHREGFIHRDLKPMNIFIDRSNNIKVGDFGLAKNSQFSSVVSTNNQVEAKDNELSTVVGTLFYTANEVATGQYDEKVDMYSLGIIFFEMCYPLATGMQRAKTLNDLRLKSVEFPTNFIASKYKTEKKIIRLLLDHDPKIRPSAAQLLQSGWLPVEHQDQVIQEALKSLADPASPWQQQVREALFNQPYSLAKDLMFDKQNEHNSHNKHVELDTSNDYLLFDKIMKELTKIFTNHGAIENLNTNLVLPKAPSQSRELVYDFLDRSGAVLTLPYDLTLPTARFLSKTDMTIPKTFRHEFVYRPNVRGIGIPDRYSAVNFDIAGGSEVNKATLFAHDAECLKVIDEIVNTLPCFKNTIIVINHYDILDAVVSFSFGNIGIDDKKKLDIFGVLSQLGIDKSPDEIKRYLREDFQVPHTVTKDLVENFNFTCEVERARQKLQKLMVDSPQLLKVERAYTYLIEVVKILKQMNIKTSMIFNPLSNYNSKYYIHGIMFQAVFKPDRSKRYTRVVTGGRYDSLIESFSNVTTTTKQITPHGVGFSLTTSLLFILMKTLISRGKSKLDLVNKWKGNRCKVLISSTQQQFLSQVGYQLVSKFWNKNISADITSVAAKTQDEIFQNGNSEGAIWIVIIRSLPTTIGNSFSSLNGGSGGSSSSTTTTSTSIRRSKKSGSGFKPLKLRNIITGKDIDLDYDEVIDYLVTELLEDSEHEENDQDNGTMTNSTTLLTSSSLSSKTNQEEELLNGPIDSVEIDQKIIVVKNDAPRSRKNKRDKWESENDAKLAGQQCIKNLSGGPVVVIDARDEILDMISITSIHQQDEWIRKVVYTTNNFPKSFAMNIYNTLIKEFNKGSIWCILVSSRTQHTTIVDLRR
Protein: Adenosine receptor A2b (P29275)
Organism: Homo sapiens (Human)
Function: Receptor for adenosine. The activity of this receptor is mediated by G proteins which activate adenylyl cyclase.
Subcellular location: Cell membrane; Multi-pass membrane protein.
Interaction partners:
- Guanine nucleotide-binding protein G
- Adenosine receptor A2a
- Guanine nucleotide-binding protein G
- Netrin-1
- Guanine nucleotide-binding protein G
- Ectonucleoside triphosphate diphosphohydrolase 1
- 5'-nucleotidase
- Adenylate cyclase type 5
Sequence:
MLLETQDALYVALELVIAALSVAGNVLVCAAVGTANTLQTPTNYFLVSLAAADVAVGLFAIPFAITISLGFCTDFYGCLFLACFVLVLTQSSIFSLLAVAVDRYLAICVPLRYKSLVTGTRARGVIAVLWVLAFGIGLTPFLGWNSKDSATNNCTEPWDGTTNESCCLVKCLFENVVPMSYMVYFNFFGCVLPPLLIMLVIYIKIFLVACRQLQRTELMDHSRTTLQREIHAAKSLAMIVGIFALCWLPVHAVNCVTLFQPAQGKNKPKWAMNMAILLSHANSVVNPIVYAYRNRDFRYTFHKIISRYLLCQADVKSGNGQAGVQPALGVGL
Protein: Translocase of outer mitochondrial membrane 40 (K7EJ57)
Organism: Homo sapiens (Human)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}. Mitochondrion outer membrane {ECO:0000256|ARBA:ARBA00004294}.
Interaction partners:
Sequence:
MGNVLAASSPPAGPPPPPAPALVGLPPPPPSPPGFTLPPLGGSLGAGTSTSRSSERTPGAATASASGAAEDGACGCLPNPGTFEECHRKCKELFPIQMEGVKLTVNKGLSNHFQVNHTVALSTIGESNYHFGVTYVGTKQLSPTEAFPVLVGDMDNSGSLNAQVIHQLGPGLRSKMAIQTQQSKFVNWQVDGEYRGSDFTAAVTLGNPDVLVGS
Protein: Zinc finger protein 384 (CAG repeat protein 1) (CAS-interacting zinc finger protein) (Nuclear matrix transcription factor 4) (Nuclear matrix protein 4) (Trinucleotide repeat-containing gene 1 protein) (Q8TF68)
Organism: Homo sapiens (Human)
Function: Transcription factor that binds the consensus DNA sequence [GC]AAAAA. Seems to bind and regulate the promoters of MMP1, MMP3, MMP7 and COL1A1 (By similarity).
Subcellular location: Nucleus {ECO:0000250}.
Interaction partners:
- Cleavage and polyadenylation specificity factor subunit 7
- Breast cancer anti-estrogen resistance protein 1
- Double homeobox protein 4-like protein 2
- Myocyte-specific enhancer factor 2D
Sequence:
MEESHFNSNPYFWPSIPTVSGQIENTMFINKMKDQLLPEKGCGLAPPHYPTLLTVPASVSLPSGISMDTESKSDQLTPHSQASVTQNITVVPVPSTGLMTAGVSCSQRWRREGSQSRGPGLVITSPSGSLVTTASSAQTFPISAPMIVSALPPGSQALQVVPDLSKKVASTLTEEGGGGGGGGGSVAPKPPRGRKKKRMLESGLPEMNDPYVLSPEDDDDHQKDGKTYRCRMCSLTFYSKSEMQIHSKSHTETKPHKCPHCSKTFANSSYLAQHIRIHSGAKPYSCNFCEKSFRQLSHLQQHTRIHSKMHTETIKPHKCPHCSKTFANTSYLAQHLRIHSGAKPYNCSYCQKAFRQLSHLQQHTRIHTGDRPYKCAHPGCEKAFTQLSNLQSHRRQHNKDKPFKCHNCHRAYTDAASLEVHLSTHTVKHAKVYTCTICSRAYTSETYLMKHMRKHNPPDLQQQVQAAAAAAAVAQAQAQAQAQAQAQAQAQAQAQASQASQQQQQQQQQQQQQQQQPPPHFQSPGAAPQGGGGGDSNPNPPPQCSFDLTPYKTAEHHKDICLTVTTSTIQVEHLASS
Protein: Larval cuticle protein 65Ab2 (Larval cuticle protein 5) (C0HL63)
Organism: Drosophila melanogaster (Fruit fly)
Function: Component of the cuticle of the larva.
Interaction partners:
Sequence:
MKFLIVFVALFAMAVARPNLAEIVRQVSDVEPEKWSSDVETSDGTSIKQEGVLKNAGTDNEAAVVHGSFTWVDEKTGEKFTITYVADENGYQPQGAHLPVAPVA