wanglab/gogpt-training-data huggingface dataset:
Protein: Tensin 3 (E9PCX8)
Organism: Homo sapiens (Human)
Subcellular location: Cell junction, focal adhesion {ECO:0000256|ARBA:ARBA00004246}. Cell projection {ECO:0000256|ARBA:ARBA00004316}.
Interaction partners:
Sequence:
MNWLCRNQDPNPPPQPEELTSSLHAFKNKAFKKSKVCGVCKQIIDGQGISCRACKYSCHKKCEAKVVIPCGVQVRLEQAPGSSTLSSSLCRDKPLRPVILSPTMEEGHGLDLTYITERIIAVSFPAGCSEESYLHNLQEVTRMLKSKHGDNYLVLNLSEKRYDLTKLNPKIMDVGWPELHAPPLDKMCTICKAQESWLNSNLQHVVVIHCRGGKGRIGVVISSYMHFTNVSASADQALDRFAMKKFYDDKVSALMQPSQKRYVQFLSGLLSGSVKMNASPLFLHFVILHGTPNFDTGGVCRPFLKLYQAMQPVYTSGIYNVGPENPSRICIVIEPAQLLKGDVMVKCYHKKYRSATRDVIFRLQFHTGAVQGYGLVFGKEDLDNASKDDRFPDYGKVELVFSATPEKIQGSEHLYNDHGVIVDYNTTDPLIRWDSYENLSADGEVLHTQGPVDGSLYAKVRKKSSSDPGIPGGPQAIPATNSPDHSDHTLSVSSDSGHSTASARTDKTEERLAPGTRRGLSAQEKAELDQLLSGFGLEDPGSSLKEMTDARSKYSGTRHVVPAQVHVNGDAALKDRETDILDDEMPHHDLHSVDSLGTLSSSEGPQSAHLGPFTCHKSSQNSLLSDGFGSNVGEDPQGTLVPDLGLGMDGPYERERTFGSREPKQPQPLLRKPSVSAQMQAYGQSSYSTQTWVRQQQMVVAHQYSFAPDGEARLVSRCPADNPGLVQAQPRVPLTPTRGTSSRVAVQRGVGSGPHPPDTQQPSPSKAFKPRFPGDQVVNGAGPELSTGPSPGSPTLDIDQSIEQLNRLILELDPTFEPIPTHMNALGSQANGSVSPDSVGGGLRASSRLPDTGEGPSRATGRQGSSAEQPLGGRLRKLSLGQYDNDAGGQLPFSKCAWGKAGVDYAPNLPPFPSPADVKETMTPGYPQDLDIIDGRILSSKESMCSTPAFPVSPETPYVKTALRHPPFSPPEPPLSSPASQHKGGREPRSCPETLTHAVGMSESPIGPKSTMLRADASSTPSFQQAFASSCTISSNGPGQRRESSSSAERQWVESSPKPMVSLLGSGRPTGSPLSAEFSGTRKDSPVLSCFPPSELQAPFHSHELSLAEPPDSLAPPSSQAFLGFGTAPVGSGLPPEEDLGALLANSHGASPTPSIPLTATGAADNGFLSHNFLTVAPGHSSHHSPGLQGQGVTLPGQPPLPEKKRASEGDRSLGSVSPSSSGFSSPHSGSTISIPFPNVLPDFSKASEAASPLPDSPGDKLVIVKFVQDTSKFWYKADISREQAIAMLKDKEPGSFIVRDSHSFRGAYGLAMKVATPPPSVLQLNKKAGDLANELVRHFLIECTPKGVRLKGCSNEPYFGSLTALVCQHSITPLALPCKLLIPERDPLEEIAESSPQTAANSAAELLKQGAACNVWYLNSVEMESLTGHQAIQKALSITLVQEPPPVSTVVHFKVSAQGITLTDNQRKLFFRRHYPVNSVIFCALDPQDRKWIKDGPSSKVFGFVARKQGSATDNVCHLFAEHDPEQPASAIVNFVSKVMIGSPKKV
Protein: G-protein coupled receptor 83 (G-protein coupled receptor 72) (Q9NYM4)
Organism: Homo sapiens (Human)
Function: G-protein coupled receptor for PEN, a neuropeptide produced from the precursor protein, proSAAS (encoded by PCSK1N). Acts through a G(i)- and G(q)-alpha-alpha-mediated pathway in response to PEN. Plays a role in food intake and body weight regulation. May contribute to the regulation of anxiety-related behaviors (By similarity).
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:P30731}; Multi-pass membrane protein {ECO:0000255}. Note=Colocalizes with GPR171 in the paraventricular nucleus. Colocalizes with the ghrelin receptor GHSR1A in the hypothalamus. {ECO:0000250|UniProtKB:P30731}.
Interaction partners:
- Pro-neuropeptide Y
- Peptide YY
- Pancreatic polypeptide prohormone
- Insulin receptor substrate 4
- Insulin receptor substrate 2
- Inhibitor of nuclear factor kappa-B kinase subunit alpha
- Insulin receptor substrate 1
- Inhibitor of nuclear factor kappa-B kinase subunit beta
- G-protein coupled receptor 171
- Adenylate cyclase type 3
Sequence:
MVPHLLLLCLLPLVRATEPHEGRADEQSAEAALAVPNASHFFSWNNYTFSDWQNFVGRRRYGAESQNPTVKALLIVAYSFIIVFSLFGNVLVCHVIFKNQRMHSATSLFIVNLAVADIMITLLNTPFTLVRFVNSTWIFGKGMCHVSRFAQYCSLHVSALTLTAIAVDRHQVIMHPLKPRISITKGVIYIAVIWTMATFFSLPHAICQKLFTFKYSEDIVRSLCLPDFPEPADLFWKYLDLATFILLYILPLLIISVAYARVAKKLWLCNMIGDVTTEQYFALRRKKKKTIKMLMLVVVLFALCWFPLNCYVLLLSSKVIRTNNALYFAFHWFAMSSTCYNPFIYCWLNENFRIELKALLSMCQRPPKPQEDRPPSPVPSFRVAWTEKNDGQRAPLANNLLPTSQLQSGKTDLSSVEPIVTMS
Protein: Proline--tRNA ligase (EC 6.1.1.15) (Prolyl-tRNA synthetase) (ProRS) (P9WFT9)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: Catalyzes the attachment of proline to tRNA(Pro) in a two-step reaction: proline is first activated by ATP to form Pro-AMP and then transferred to the acceptor end of tRNA(Pro). As ProRS can inadvertently accommodate and process non-cognate amino acids such as alanine and cysteine, to avoid such errors it has two additional distinct editing activities against alanine. One activity is designated as 'pretransfer' editing and involves the tRNA(Pro)-independent hydrolysis of activated Ala-AMP. The other activity is designated 'posttransfer' editing and involves deacylation of mischarged Ala-tRNA(Pro). The misacylated Cys-tRNA(Pro) is not edited by ProRS.
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01569}.
Interaction partners:
- Isoleucine--tRNA ligase
- Methionine--tRNA ligase
- Glutamate--tRNA ligase
- Arginine--tRNA ligase
- Leucine--tRNA ligase
- Lysine--tRNA ligase 1
- Lysylphosphatidylglycerol biosynthesis bifunctional protein LysX
- Phenylalanine--tRNA ligase beta subunit
- Aspartate--tRNA
- GMP synthase
Sequence:
MITRMSELFLRTLRDDPADAEVASHKLLIRAGYIRPVAPGLYSWLPLGLRVLRNIERVIRDEMNAIGGQEILFPALLPRAPYETTNRWTQYGDSVFRLKDRRGNDYLLGPTHEELFTLTVKGEYSSYKDFPLTLYQIQTKYRDEARPRAGILRAREFVMKDSYSFDIDAAGLKAAYHAHREAYQRIFDRLQVRYVIVSAVSGAMGGSASEEFLAESPSGEDAFVRCLESGYAANVEAVVTARPDTLPIDGLPEAVVHDTGDTPTIASLVAWANEADLGRTVTAADTLKNVLIKVRQPGGDTELLAIGVPGDREVDDKRLGAALEPADYALLDDDDFAKHPFLVKGYIGPKALRENNVRYLVDPRIVDGTSWITGADQPGRHVVGLVAGRDFTADGTIEAAEVREGDPSPDGAGPLVMARGIEIGHIFQLGSKYTDAFTADVLGEDGKPVRLTMGSYGIGVSRLVAVVAEQHHDELGLRWPSTVAPFDVHLVIANKDAQARAGATALAADLDRLGVEVLLDDRQASPGVKFKDAELLGMPWIVVVGRGWADGVVELRDRFSGQTRELVAGASLATDIAAAVTG
Protein: Proteasome subunit alpha type-5 (Macropain zeta chain) (Multicatalytic endopeptidase complex zeta chain) (Proteasome subunit alpha-5) (alpha-5) (Proteasome zeta chain) (P28066)
Organism: Homo sapiens (Human)
Function: Component of the 20S core proteasome complex involved in the proteolytic degradation of most intracellular proteins. This complex plays numerous essential roles within the cell by associating with different regulatory particles. Associated with two 19S regulatory particles, forms the 26S proteasome and thus participates in the ATP-dependent degradation of ubiquitinated proteins. The 26S proteasome plays a key role in the maintenance of protein homeostasis by removing misfolded or damaged proteins that could impair cellular functions, and by removing proteins whose functions are no longer required. Associated with the PA200 or PA28, the 20S proteasome mediates ubiquitin-independent protein degradation. This type of proteolysis is required in several pathways including spermatogenesis (20S-PA200 complex) or generation of a subset of MHC class I-presented antigenic peptides (20S-PA28 complex).
Subcellular location: Cytoplasm {ECO:0000269|PubMed:12181345, ECO:0000269|PubMed:34711951}. Nucleus {ECO:0000269|PubMed:12181345, ECO:0000269|PubMed:34711951}. Note=Translocated from the cytoplasm into the nucleus following interaction with AKIRIN2, which bridges the proteasome with the nuclear import receptor IPO9. {ECO:0000269|PubMed:34711951}.
Interaction partners:
- Proteasome subunit alpha type-4
- 26S proteasome non-ATPase regulatory subunit 2
- 26S proteasome non-ATPase regulatory subunit 7
- Proteasome subunit beta type-1
- 26S proteasome non-ATPase regulatory subunit 12
- 26S proteasome non-ATPase regulatory subunit 13
- Proteasome subunit alpha type-6
- 26S proteasome regulatory subunit 10B
- Proteasome subunit beta type-3
- Proteasome subunit alpha type-3
Sequence:
MFLTRSEYDRGVNTFSPEGRLFQVEYAIEAIKLGSTAIGIQTSEGVCLAVEKRITSPLMEPSSIEKIVEIDAHIGCAMSGLIADAKTLIDKARVETQNHWFTYNETMTVESVTQAVSNLALQFGEEDADPGAMSRPFGVALLFGGVDEKGPQLFHMDPSGTFVQCDARAIGSASEGAQSSLQEVYHKSMTLKEAIKSSLIILKQVMEEKLNATNIELATVQPGQNFHMFTKEELEEVIKDI
Protein: G0/G1 switch protein 2 (G0/G1 switch regulatory protein 2) (Putative lymphocyte G0/G1 switch gene) (P27469)
Organism: Homo sapiens (Human)
Function: Promotes apoptosis by binding to BCL2, hence preventing the formation of protective BCL2-BAX heterodimers.
Subcellular location: Mitochondrion {ECO:0000269|PubMed:19706769}.
Interaction partners:
- Patatin-like phospholipase domain-containing protein 2
- 1-acylglycerol-3-phosphate O-acyltransferase ABHD5
- Apoptosis regulator Bcl-2
Sequence:
METVQELIPLAKEMMAQKRKGKMVKLYVLGSVLALFGVVLGLMETVCSPFTAARRLRDQEAAVAELQAALERQALQKQALQEKGKQQDTVLGGRALSNRQHAS
Protein: Arrestin domain-containing protein C584.15c (Q09889)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Interaction partners:
- E3 ubiquitin-protein ligase pub3
- E3 ubiquitin-protein ligase pub2
- Meiotically up-regulated gene 170 protein
- High-affinity glucose transporter ght5
- Uncharacterized protein C557.05
Sequence:
MNKIKGGRHKSPVKLFEVRLYNAEANVIVLYGNSMDTSARLSGIVVLSVSSPIRVKNIKLRLSGRSFVCWADESRHASPGNRIRRQVVQILDKSWSFLAPNESAKVIDQGNYEYPFYYELPPDIPDSIEGIPGCHIIYTLTASLERATQPPTNLETALQFRVIRTIPPNSLDLMHSVSVSDIWPLKVNYETSIPSKVYAIGSEIPVNITLYPLLKGLDVGKVTLVLKEYCTLFITSKAYSSTCRKEFKRALVKKTIPGLPMVDDYWQDQIMVKIPDSLGECTQDCDLNCIRVHHKLRLSISLLNPDGHVSELRNSLPLSLVISPVMFGARPTEGVFTGDHNSYVNENILPSYDKHVFDVLWDGIPSENPQLQSGFTTPNLSRRNSSDFGPNSPVNIHSNPVPISGQQPSSPASNSNANFFFGSSPQSMSSEQTDMMSPITSPLAPFSGVTRRAARTRANSASSVFNSQLQPLQTDLLSPLPSPTSSNSRLPRVRSACTLNVQELSKIPPYYEAHSAFTNVLPLDGLPRYEEATRPSSPTESVEIPSNTTTIAPSPVPTIIAPALPSTPAPPLPSHPMATRKSLSSTNLVRRGVR
Protein: Tropomyosin (Q9C8R6)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
Sequence:
MAYRRRQGITRASTFKEDIYHQPPDPDHGDLKGHSNGGSFRSSQSFSSHSSLAAQAIRASSQAQGFTAYEDKSESRGFWGILAQKAKSILEDEEEQQQQQQQQNDVIFEPSNPTIRKSIDKITTSLNHIGDSFEKAFEEGRTIVASQIRRKGSDLIDSDNNNYHQSSGSSSPWQPLTQPNPRESQLKASRDVAMATAAKAKLLLRELKTVKADLAFAKERCSQLEEENKRLRDNRDKGNNNPADDDLIRLQLETLLAEKARLAHENSIYARENRFLREIVEYHQLTMQDVVYIDEGIEEVAEVNPSITRTLSMASYSASELPSISPSPSSPASPSRLSVSTDIYPILVQQSSTNDITVESPKPVRPPSLGYTDDGKRPSSQLPSSQLSV
Protein: ADD domain-containing protein 1, isoform E (A0A0B4LEU5)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MSNSAPGSESGLAKVATPSPSPLAKLDADFTSSKFEMHPSLSDEERRFYLKMYPNVDLVNQRKVHCTVCKLHLGTAPAAESNIKMHPILRVTHCVKCHDFYNSGEFSKGEDGSELYCRWCGQGGEVYCCSTCPYVFCKSCIVKNLSKGVIVDIEQNENWNCFSCTSKILWPLRAQHWALVNYLQTQKRALQTLQLPEVEARRQMLKDNSNCCRLAKSKTSSLSDSMESLESNVSKRSQGSSAGSSKRGSMPKTIPPGPPSKRAKASNNEVVCTPDLLSMLEPDCQLSVTPKPTGRQTVTAANITTPRIVTVQQNYQPGQSSSNSGSNGSTNQQQRAPQVRVGNANPAPPPLQGLPPNANGGQTLMITPAPQPAPKVPTLVRLTFPNTPMGQARAQLQEQIFSAMDICTHLTGKVVSLTHSNAYNQVRSYLELKELYIHMSYLMTYAIGRFKNLQEKCLVDMREKGFKNDANSLENGQLAAAVDYVCYGQLDDVDLFNTGCNSFHNQVYEYRKSLHANLKDGEDCEPLPPLMPLGVRAEGDPIDEPEEPETVPEPQQDDTEKDHEDAAEFDYDEPEDLDDDLDDDDLDNEECGELGTEESMNRNEQAHAYDRKLTRLLREYPSLWCTRHPDYGKKEVTNKQWRVIASHFPRGDDIKLRWKNVRKRYVRIERRLKQGKRFKGYFDKATNYLENRDRPRSEWLAVDCGEDDGDGFERKHLDVIENKMEQKAHKQPAVKINLKGGSRIPTRPLEVRPIDQRIITFAKSHPVLWRKSADPEFNSIDEQTRKSLWQNFWKSAPNYACEYLVERWQQMYEMYKSFRLKSIKDKGIFANLELKYSKYLASLYFLYKIDEQDLRDEFEPLQDCVPSGTDSAGNLKDMPDDKQFCQQLVLAMRAYPTLWNPRHVDYSDVGARERLWPEVARRLPRFKRDAQACKLRWQMAKFAYECYLREMERHPRVNERKLQKLRSNFPLEEMRFLNI
Protein: Rho/Rac guanine nucleotide exchange factor 18 (A0A3B3IPE9)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
Sequence:
MGNAHSKSGDRHSALPGRPELSFYGSFPRKWSENVFLDNELLTSKILSVLRPQSERGFRAGDLRYPTHFLSTNSVLASVTASLKEHPRGTLLSDGSPALSRNVGMTVSQKGGPQPTPSPAGPGTQLGPITGEMDEADSAFLKFKQTADDSLSLTSPNTESIFVEDPYTASLRSEIESDGHEFEAESWSLAVDAAYAKKQKREVVKRQDVLYELMQTEVHHVRTLKIMLKVYSRALQEELQFSSKAIGRLFPCADDLLETHSHFLARLKERRQESLEEGSDRNYVIQKIGDLLVQQFSGENGERMKEKYGVFCSGHNEAVSHYKLLLQQNKKFQNLIKKIGNFSIVRRLGVQECILLVTQRITKYPVLVERIIQNTEAGTEDYEDLTQALNLIKDIISQVDAKVSECEKGQRLREIAGKMDLKSSSKLKNGLTFRKEDMLQRQLHLEGMLCWKTTSGRLKDILAILLTDVLLLLQEKDQKYVFASVDSKPPVISLQKLIVREVANEEKAMFLISASLQGPEMYEIYTSSKEDRNAWMAHIQRAVESCPDEEEGPFSLPEEERKVVEARATRLRDFQERLSMKDQLIAQSLLEKQQIYLEMAEMGGLEDLPQPRGLFRGGDPSETLQGELILKSAMSEIEGIQSLICRQLGSANGQAEDGGSSTGPPRRAETFAGYDCTNSPTKNGSFKKKVSSTDPRPRDWRGPPNSPDLKLSDSDIPGSSEESPQVVEAPGTESDPRLPTVLESELVQRIQTLSQLLLNLQAVIAHQDSYVETQRAAIQEREKQFRLQSTRGNLLLEQERQRNFEKQREERAALEKLQSQLRHEQQRWERERQWQHQELERAGARLQEREGEARQLRERLEQERAELERQRQAYQHDLERLREAQRAVERERERLELLRRLKKQNTAPGALPPDTLAEAQPPSHPPSFNGEGLEGPRVSMLPSGVGPEYAERPEVARRDSAPTENRLAKSDVPIQLLSATNQFQRQAAVQQQIPTKLAASTKGGKDKGGKSRGSQRWESSASFDLKQQLLLNKLMGKDESTSRNRRSLSPILPGRHSPAPPPDPGFPAPSPPPADSPSEGFSLKAGGTALLPGPPAPSPLPATPLSAKEDASKEDVIFF
Protein: Adiponectin receptor 1 (G3V6I6)
Organism: Rattus norvegicus (Rat)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
- 30 kDa adipocyte complement-related protein
- DCC-interacting protein 13-alpha
- Adiponectin receptor 2
- Leptin
- Cadherin-13
- Resistin
- Insulin-2
- Insulin-1
- Nicotinamide phosphoribosyltransferase
- Peroxisome proliferator-activated receptor gamma
Sequence:
MSSHKGSAVAQGNGAPSSNRAADTVELAELGPLLEEKGKRAATSPAKAEEEQACPVPQEEEEEVRVLTLPLQAHHAMEKMEEFVYKVWEGRWRVIPYDVLPDWLKDNDYLLHGHRPPMPSFRACFKSIFRIHTETGNIWTHLLGFVLFLFLGILTMLRPNMYFMAPLQEKVVFGMFFLGAVLCLSFSWLFHTVYCHSEKVSRTFSKLDYSGIALLIMGSFVPWLYYSFYCSPQPRLIYLSIVCVLGISAIIVAQWDRFATPKHRQTRAGVFLGLGLSGVVPTMHFTIAEGFVKATTVGQMGWFFLMAVMYITGAGLYAARIPERFFPGKFDIWFQSHQIFHVLVVAAAFVHFYGVSNLQEFRYGLEGGCTDDSLL
Protein: Signal transducer CD24 (Heat-stable antigen) (HSA) (Nectadrin) (CD antigen CD24) (Q07490)
Organism: Rattus norvegicus (Rat)
Function: May have a pivotal role in cell differentiation of different cell types. Signaling could be triggered by the binding of a lectin-like ligand to the CD24 carbohydrates, and transduced by the release of second messengers derived from the GPI-anchor. Modulates B-cell activation responses. In association with SIGLEC10 may be involved in the selective suppression of the immune response to danger-associated molecular patterns (DAMPs) such as HMGB1, HSP70 and HSP90. Plays a role in the control of autoimmunity (By similarity).
Subcellular location: Cell membrane; Lipid-anchor, GPI-anchor.
Interaction partners:
- P-selectin
- Sialic acid binding Ig-like lectin 10
- High mobility group protein B1
- High mobility group protein B1
- Epithelial cell adhesion molecule
- CD44 antigen
- T-cell surface glycoprotein CD4
- Prominin 1
- Neural cell adhesion molecule L1
- E-selectin
Sequence:
MGRAMVVRLGLGLLLLALLLPTQIYCNQTSVAPFSGNQSISAAPNPTNATTRSGCSSLQSTAGLLALSLSLLHLYC
Protein: Ribosomal protein L7Ae/L30e/S12e/Gadd45 domain-containing protein (Q57Y14)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Endoplasmic reticulum oxidoreductin, putative
- Glucose-regulated protein 78, putative
- Heat shock protein, putative
- Calreticulin
- Calreticulin
- Uncharacterized protein
Sequence:
MSSEQGGDSYGVAKPRRKRVRWDCNGRRKRVTATAFVSDFLPAPQANKVSDDVPKSPRERKGHFGNQNPPASQKVPVRLKPTVTRQVGPGKTLHAGKKHFLAKGKLRNPDGPFNHRARYSKFKRSIVELRREVFESLINGDQQSSIQDALAAVAVGSSVTSSSENTALTSPSHTLQPLQALVGKLHSLYARLHSEMNRKSYVKAARCLTTIRRLRKRLNKTALGWKGGVITVNTGATREDAPTVEPDRSQTRGECNEGASAGKQGDSEGAAKADNVGSDGEPNFVNFYPSLSLMGIGTHPLTAVIDQRSGRHPRQLTASEVAQLHNTTPDLLVAAANSNKPRNPIPRYLVSSCANILTDRLDDIVFTILQRQYTLQKRMKKEKPLQFKARKFYSTGMRETLRALRAAATRIPVVLIASDIELNGTLSPNIDKEFCVEREGTAENVVATVSRSQHKTVGELGVSGTLEEIHSHCVKGNIPLVTCMSRRKLAYALFAKGCNISIVVLHSAEGVHEEVRALRHYAHQLCEQYRRITPSEQGT
Protein: Transcription antitermination protein NusB (Antitermination factor NusB) (P65582)
Organism: Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4)
Function: Involved in transcription antitermination. Required for transcription of ribosomal RNA (rRNA) genes. Binds specifically to the boxA antiterminator sequence of the ribosomal RNA (rrn) operons.
Interaction partners:
Sequence:
MTSPLLESRRQLRKCAFQALMSLEFGTDVETACRFAYTHDREDTDVQLPAFLIDLVSGVQAKKEELDKQITQHLKAGWTIERLTLVERNLLRLGVFEITSFDTPQLVAVNEAIELAKDFSDQKSARFINGLLSQFVTEEQ
Protein: Zn(2)-C6 fungal-type domain-containing protein (G8BBM2)
Organism: Candida parapsilosis (strain CDC 317 / ATCC MYA-4646) (Yeast) (Monilia parapsilosis)
Interaction partners:
- Glutamyl-tRNA
- Aminoacyl-transfer RNA synthetases class-II family profile domain-containing protein
Sequence:
MVAQNLSNNGDSSSSESRKQDEEYTNPQNQSASHSHITSNLKEDKDNLNESYDDSNSYNENNQAQDNAVEPKYPHHYTPEATSDPPHLFNSSNQINGTYGNQQSRPPTTQPSSGYLDPQWGNMMFDPSAADYLYDIELPSHLSQSGNNTGSNDTNIMHHIQYQNNVHPEVNNSPAPESFSNQNQRVSLPYREDTLSQSQSPQTTLSQQPRDFTPSVAAPHGPNSSKPTKQRRPCDQCRRRKTKCVIVPNTNNCVQCEAKQLTCTYTTPAAKRKSSELESDTQKRGRPNVAAPVENNRIPDVPIREVAPVQDYSAMNNSLLKKTLSLQFPRSSFYVGPTNYLYDVNLLNQIIDNRNNNNNPSGAAKIEQASLSSSISLRKVSDKVHFVLKDDQSPQSYQTMSNDVDTIEKLISPHGQILIDLYFRIIHPSYPIVHKKVFLEKYARTHREFTAPLIAAVYVLAIQWWDYDPQLNRFPKPNVELILKIGLKNYLQEILKRPKLSAVQAGLLLLQCKHIISCKATNNQVQNSGDADYSEWVLCSQVVSLAEELGLGLDCNNWKLPKWERGLRKRLAWAVYMEDKWLSLKDSRPSHINENNWIVLPLYEVDFPDKHGDGDLKEGSSDLDTGKKVFTNLIELSKILSEILDQFYSMKAMREITNISEVLKLAKPLQLQLRNWFYSLPSELQMNLVQPRKLCSNGYLHLAYFATELTLHRKITTIIYQQTNAGDPPPPELINVCRSAAKTRLLASIEFVRDLKPEHIHSFWHSSSSSNFTLIGTFAAILFISSPTQEEANFYRDQIFNYRWILKISSKGFDQVAEALSQLDLVLGNIPGLLNDNVDMPMVLPNVQDQQIMPPTSQSNSPFAVPQSQQPQSQQSQSQVPSVASRPNVSFNGNPTNQQKMRMPSNLRESPYNSPQSFYTPPFVPSPQTRAVNSPHNSQGTTSRAVSPKAYANRGSNYTGQSPHSSVVTKSPESTTK
Protein: chitinase (EC 3.2.1.14) (D0EW64)
Organism: Bacillus thuringiensis subsp. kurstaki
Interaction partners:
Sequence:
DSPKQSQKIVGYFPSWGIYGRNYQVADIDASKLTHLNYAFADICWNGKHGNPSTHPDNPNKQTWNCKESGVPLQNKEVPNGTLVLGEPWADVTKSYPGSGTTWEDCDKYARCGNFGELKRLKAKYPHLKTIISVGGWTWSNRFSDMAADEKTRKVFAESTVDFLREYGFDGVDLDWEYPGVETIPGGSYRPEDKQNFTLLLQDVRNALNKAGAEDGKQYLLTIASGASQRYADHTELKKISQILDWINIMTYDFHGGWEATSNHNAALYKDPNDPAADTKFYVDGAIDIYTNEGVPADKLVLGVPFYGRGWKSCGKENNGQYQPCKPGSDGKLASKGTWDDYSTGDTGVYDYGDLAANYVNKNGFVRGWNDVAKVPYLYNATTGTFISYDDNESMKYKTDYIKTKGLSGAMFWELSGDCRTSPKYSCSGPKLLDTLVKELLGGPITQKDTEPPTNVKNIAVTNKNSNSVQLNWTASTDNVGVTEYEITAGEEKWSTTTNSITIKNLKSNTEYTFSIIAKDAAGNKSQPTSIIVKTDDANTTTPGGNSNATFSVTSNWGSGYNFSIVIKNSGTTPIKNWKLEFDYNGNLTQVWDSKISSKINNHYVITNAGWNGEIPPGGAITIGGAGTGTPAELVNAVISEN
Protein: Structural polyprotein (p130) (Q66579)
Organism: Eastern equine encephalitis virus (EEEV) (Eastern equine encephalomyelitis virus)
Subcellular location: Host cell membrane {ECO:0000256|ARBA:ARBA00004598}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004598}. Host cell membrane {ECO:0000256|ARBA:ARBA00004402}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004402}. Host cytoplasm {ECO:0000256|ARBA:ARBA00004192}. Virion membrane {ECO:0000256|ARBA:ARBA00004385}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004385}. Virion membrane {ECO:0000256|ARBA:ARBA00004563}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004563}.
Interaction partners:
Sequence:
MFPYPTLNYPPMAPINPMAYRDPNPPRRRWRPFRPPLAAQIEDLRRSIANLTLKQRAPNPPAGPPAKRKKPAPSLSLRRKKKRPPPPAKKQKRKPKPGKRQRMCMKLESDKTFPIMLNGQVNGYACVVGGRVFKPLHVEGRIDNEQLAAIKLKKASIYDLEYGDVPQCMKSDTLQYTSDKPPGFYNWHHGAVQYENNRFTVPRGVGGKGDSGRPILDNKGRVVAIVLGGVNEGSRTALSVVTWNQKGVTVKDTPEGSEPWSLATVMCVLANITFPCDQPPCMPCCYEKNPHETLTMLEQNYDSRAYDQLLDAAVKCNARRTRRDLDTHFTQYKLARPYIADCPNCGHSRCDSPIAIEEVRGDAHAGVIRIQTSAMFGLKTDGVDLAYMSFMNGKTQKSIKIDNLHVRTSAPCSLVSHHGYYILAQCPPGDTVTVGFHDGPNRHTCTVAHKVEFRPVGREKYRHPPEHGVELPCNRYTHKRADQGHYVEMHQPGLVADHSLLSIHSAKVKITVPSGAQVKYYCKCPDVREGTTSSDYTTTCTDVKQCRAYLIDNKKWVYNSGRLPRGEGDTFKGKLHVPFVPVKAKCIATLAPEPLVEHKHRTLILHLYPDHPTLLTTRSLGSDANPTRQWIERPTTVNFTVTGEGLEYTWGNHPPKRVWAQESGEGNPHGWPHEVVVYYYNRYPLTTIIGLCTCVAIIMVSCVTSVWLLCRTRNLCITPYKLAPNAQVPILLALLCCIKPTRADDTLQVLNYLWNNNQNFFWMQTLIPLAALIVCMRMLRCLFCCGPAFLLVCGALGAAAYEHTAVMPNKVGIPYKALVERPGYAPVHLQIQLVNTRIIPSTNLEYITCKYKTKVPSPVVKCCGATQCTSKPHPDYQCQVFTGVYPFMWGGAYCFCDTENTQMSEAYVERSEECSIDHAKAYKVHTGTVQAMVNITYGSVSWRSADVYVNGETPAKIGDAKLIIGPLSSAWSPFDNKVVVHGHEVYNYDFPEYGTGKAGSFGDLQSRTSTSNDLYANTNLKLQRPQAGIVHTPFTQAPSGFERWKRDKGAPLNDVAPFGCSIALEPLRAENCAVGSIPISIDIPDAAFTRISETPTVSDLECKITECTYASDFGGIATVAYKSSKAGNCPIHSPSGVAVIKENDVTLAESGSFTFHFSTANIHPAFKLQVCTSAVTCKGDCKPPKDHIVDYPAQHTESFTSAISATAWSWLKVLVGGTSAFIVLGLIATAVVALVLFFHRH
Protein: Protein phosphatase Slingshot homolog 1 (EC 3.1.3.16) (EC 3.1.3.48) (SSH-like protein 1) (SSH-1L) (hSSH-1L) (Q8WYL5)
Organism: Homo sapiens (Human)
Function: Protein phosphatase which regulates actin filament dynamics. Dephosphorylates and activates the actin binding/depolymerizing factor cofilin, which subsequently binds to actin filaments and stimulates their disassembly. Inhibitory phosphorylation of cofilin is mediated by LIMK1, which may also be dephosphorylated and inactivated by this protein.
Subcellular location: Cytoplasm, cytoskeleton. Cell projection, lamellipodium. Cleavage furrow. Midbody. Note=Also recruited to actin rich membrane protrusions such as lamellipodia, which may allow local control of actin dynamics at sites of cell locomotion. Also localized to the cleavage furrow and the midbody during cytokinesis.
Interaction partners:
- Cofilin-1
- Cofilin-2
- LIM domain kinase 1
- Protein phosphatase Slingshot homolog 3
- Protein phosphatase 3 catalytic subunit alpha
- Serine/threonine-protein phosphatase 2B catalytic subunit beta isoform
- Serine/threonine-protein phosphatase 2B catalytic subunit gamma isoform
- Protein phosphatase Slingshot homolog 2
- Calcineurin subunit B type 1
- Calcineurin subunit B type 2
Sequence:
MALVTLQRSPTPSAASSSASNSELEAGSEEDRKLNLSLSESFFMVKGAALFLQQGSSPQGQRSLQHPHKHAGDLPQHLQVMINLLRCEDRIKLAVRLESAWADRVRYMVVVYSSGRQDTEENILLGVDFSSKESKSCTIGMVLRLWSDTKIHLDGDGGFSVSTAGRMHIFKPVSVQAMWSALQVLHKACEVARRHNYFPGGVALIWATYYESCISSEQSCINEWNAMQDLESTRPDSPALFVDKPTEGERTERLIKAKLRSIMMSQDLENVTSKEIRNELEKQMNCNLKELKEFIDNEMLLILGQMDKPSLIFDHLYLGSEWNASNLEELQGSGVDYILNVTREIDNFFPGLFAYHNIRVYDEETTDLLAHWNEAYHFINKAKRNHSKCLVHCKMGVSRSASTVIAYAMKEFGWPLEKAYNYVKQKRSITRPNAGFMRQLSEYEGILDASKQRHNKLWRQQTDSSLQQPVDDPAGPGDFLPETPDGTPESQLPFLDDAAQPGLGPPLPCCFRRLSDPLLPSPEDETGSLVHLEDPEREALLEEAAPPAEVHRPARQPQQGSGLCEKDVKKKLEFGSPKGRSGSLLQVEETEREEGLGAGRWGQLPTQLDQNLLNSENLNNNSKRSCPNGMEDDAIFGILNKVKPSYKSCADCMYPTASGAPEASRERCEDPNAPAICTQPAFLPHITSSPVAHLASRSRVPEKPASGPTEPPPFLPPAGSRRADTSGPGAGAALEPPASLLEPSRETPKVLPKSLLLKNSHCDKNPPSTEVVIKEESSPKKDMKPAKDLRLLFSNESEKPTTNSYLMQHQESIIQLQKAGLVRKHTKELERLKSVPADPAPPSRDGPASRLEASIPEESQDPAALHELGPLVMPSQAGSDEKSEAAPASLEGGSLKSPPPFFYRLDHTSSFSKDFLKTICYTPTSSSMSSNLTRSSSSDSIHSVRGKPGLVKQRTQEIETRLRLAGLTVSSPLKRSHSLAKLGSLTFSTEDLSSEADPSTVADSQDTTLSESSFLHEPQGTPRDPAATSKPSGKPAPENLKSPSWMSKS
Protein: Acyl-homoserine-lactone synthase (EC 2.3.1.184) (Autoinducer synthesis protein RhlI) (P54291)
Organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Function: Required for the synthesis of BHL (N-butanoyl-L-homoserine lactone), and HHL (N-hexanoyl-L-homoserine lactone) autoinducer molecules which bind to RhlR and thus acts in elastase biosynthesis regulation.
Interaction partners:
- HTH-type quorum-sensing regulator RhlR
- Transcriptional activator protein LasR
- Quorum-sensing control repressor
- 3-
- Acyl-homoserine-lactone synthase
- Elastase
- Multiple virulence factor regulator MvfR
- 2-heptyl-3-hydroxy-4
- Protease LasA
- S-adenosylmethionine synthase
Sequence:
MIELLSESLEGLSAAMIAELGRYRHQVFIEKLGWDVVSTSRVRDQEFDQFDHPQTRYIVAMSRQGICGCARLLPTTDAYLLKDVFAYLCSETPPSDPSVWELSRYAASAADDPQLAMKIFWSSLQCAWYLGASSVVAVTTTAMERYFVRNGVILQRLGPPQKVKGETLVAISFPAYQERGLEMLLRYHPEWLQGVPLSMAV
Protein: Guanylyl cyclase-activating protein 1 (GCAP 1) (Guanylate cyclase activator 1A) (P46065)
Organism: Bos taurus (Bovine)
Function: Stimulates retinal guanylyl cyclase when free calcium ions concentration is low and inhibits guanylyl cyclase when free calcium ions concentration is elevated. This Ca(2+)-sensitive regulation of retinal guanylyl cyclase is a key event in recovery of the dark state of rod photoreceptors following light exposure. May be involved in cone photoreceptor light response and recovery of response in bright light (By similarity).
Subcellular location: Membrane; Lipid-anchor {ECO:0000269|PubMed:7520254}. Photoreceptor inner segment {ECO:0000269|PubMed:9620085}. Cell projection, cilium, photoreceptor outer segment {ECO:0000269|PubMed:9620085}. Note=Subcellular location is not affected by light or dark conditions. {ECO:0000250|UniProtKB:P43081}.
Interaction partners:
- Retinal guanylyl cyclase 1
- Retinal guanylyl cyclase 2
- Guanylyl cyclase-activating protein 2
- Translation factor GUF1, mitochondrial
- Cyclic nucleotide-gated channel alpha-1
- Rhodopsin kinase GRK1
- Rhodopsin
- Rhodopsin kinase GRK7
- Guanylate cyclase
- Cyclic nucleotide-gated channel beta-1
Sequence:
MGNIMDGKSVEELSSTECHQWYKKFMTECPSGQLTLYEFRQFFGLKNLSPWASQYVEQMFETFDFNKDGYIDFMEYVAALSLVLKGKVEQKLRWYFKLYDVDGNGCIDRDELLTIIRAIRAINPCSDSTMTAEEFTDTVFSKIDVNGDGELSLEEFMEGVQKDQMLLDTLTRSLDLTRIVRRLQNGEQDEEGASGRETEAAEADG