wanglab/gogpt-training-data huggingface dataset:
Protein: ATP-binding cassette sub-family C member 8 (Sulfonylurea receptor 1) (Q09428)
Organism: Homo sapiens (Human)
Function: Subunit of the beta-cell ATP-sensitive potassium channel (KATP). Regulator of ATP-sensitive K(+) channels and insulin release.
Subcellular location: Cell membrane {ECO:0000269|PubMed:24814349}; Multi-pass membrane protein {ECO:0000269|PubMed:29286281, ECO:0000269|PubMed:34815345}.
Interaction partners:
- ATP-sensitive inward rectifier potassium channel 8
- ATP-sensitive inward rectifier potassium channel 11
- Transient receptor potential cation channel subfamily M member 4
- Rap guanine nucleotide exchange factor 4
- Hexokinase-4
- cAMP-dependent protein kinase catalytic subunit beta
- cAMP-dependent protein kinase catalytic subunit alpha
- cAMP-dependent protein kinase catalytic subunit gamma
- Insulin
- ATP-binding cassette sub-family C member 9
Sequence:
MPLAFCGSENHSAAYRVDQGVLNNGCFVDALNVVPHVFLLFITFPILFIGWGSQSSKVHIHHSTWLHFPGHNLRWILTFMLLFVLVCEIAEGILSDGVTESHHLHLYMPAGMAFMAAVTSVVYYHNIETSNFPKLLIALLVYWTLAFITKTIKFVKFLDHAIGFSQLRFCLTGLLVILYGMLLLVEVNVIRVRRYIFFKTPREVKPPEDLQDLGVRFLQPFVNLLSKGTYWWMNAFIKTAHKKPIDLRAIGKLPIAMRALTNYQRLCEAFDAQVRKDIQGTQGARAIWQALSHAFGRRLVLSSTFRILADLLGFAGPLCIFGIVDHLGKENDVFQPKTQFLGVYFVSSQEFLANAYVLAVLLFLALLLQRTFLQASYYVAIETGINLRGAIQTKIYNKIMHLSTSNLSMGEMTAGQICNLVAIDTNQLMWFFFLCPNLWAMPVQIIVGVILLYYILGVSALIGAAVIILLAPVQYFVATKLSQAQRSTLEYSNERLKQTNEMLRGIKLLKLYAWENIFRTRVETTRRKEMTSLRAFAIYTSISIFMNTAIPIAAVLITFVGHVSFFKEADFSPSVAFASLSLFHILVTPLFLLSSVVRSTVKALVSVQKLSEFLSSAEIREEQCAPHEPTPQGPASKYQAVPLRVVNRKRPAREDCRGLTGPLQSLVPSADGDADNCCVQIMGGYFTWTPDGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLAALGEMQKVSGAVFWSSLPDSEIGEDPSPERETATDLDIRKRGPVAYASQKPWLLNATVEENIIFESPFNKQRYKMVIEACSLQPDIDILPHGDQTQIGERGINLSGGQRQRISVARALYQHANVVFLDDPFSALDIHLSDHLMQAGILELLRDDKRTVVLVTHKLQYLPHADWIIAMKDGTIQREGTLKDFQRSECQLFEHWKTLMNRQDQELEKETVTERKATEPPQGLSRAMSSRDGLLQDEEEEEEEAAESEEDDNLSSMLHQRAEIPWRACAKYLSSAGILLLSLLVFSQLLKHMVLVAIDYWLAKWTDSALTLTPAARNCSLSQECTLDQTVYAMVFTVLCSLGIVLCLVTSVTVEWTGLKVAKRLHRSLLNRIILAPMRFFETTPLGSILNRFSSDCNTIDQHIPSTLECLSRSTLLCVSALAVISYVTPVFLVALLPLAIVCYFIQKYFRVASRDLQQLDDTTQLPLLSHFAETVEGLTTIRAFRYEARFQQKLLEYTDSNNIASLFLTAANRWLEVRMEYIGACVVLIAAVTSISNSLHRELSAGLVGLGLTYALMVSNYLNWMVRNLADMELQLGAVKRIHGLLKTEAESYEGLLAPSLIPKNWPDQGKIQIQNLSVRYDSSLKPVLKHVNALIAPGQKIGICGRTGSGKSSFSLAFFRMVDTFEGHIIIDGIDIAKLPLHTLRSRLSIILQDPVLFSGTIRFNLDPERKCSDSTLWEALEIAQLKLVVKALPGGLDAIITEGGENFSQGQRQLFCLARAFVRKTSIFIMDEATASIDMATENILQKVVMTAFADRTVVTIAHRVHTILSADLVIVLKRGAILEFDKPEKLLSRKDSVFASFVRADK
Protein: Liprin-gamma, isoform E (A0A0B4LG34)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MQINGLAAGPTMAASEPPEPPPRNPDRINASLHKLGESKIAKSLDTSVSTGLKEKAASVNNNKPIRPLLSLDSSVTASTSSGATGSGGGGAPAKPSPLVLASKRDLTPSNESSSSPSSSNGSNQTLTPPMTADNQPLQQQLQHHQHRSPAYPGKPAEAAGGVPQQQQQQQQLPNGIGSSHCNSNSNGISSTCNSGTAMIHANNSNLIAAGHLAQAAGPAHNAPSSGSALNAEATMKLREENDRLNAELLRLRRLLELSTDGAVGGVDTAPEMEAVASGEGSAAKERIERLESELRSVKNQLLTMRLERKKLRTDKSDLLGQVKQLCASLQEKEQELRDFIRNYQERVRETETTNAKISGDRDRERFQLLKQARDEAERSLALAQQLSARDLQLQRLQEQLQEARRQLTGCLSDQESLHSFAPLTPPSAASGMLSQMAAASGMGGGLAGMRGTTEDSGRGNSLSAFSGSLSGGSGATAGDRNSCSNDSGLRNSSDRESTGGELNFSDGTCDNGPCITVDPDSISLVSSQNMYQFGTPKERSPTLSPLNSAAYSRSVEQLGSPVDPEGPGNGAISRKFANASKSGPLGARNGRGGTWGSISRVFARSRNKNKALSADGVTEYADYSWNPLTEEGYAEKLRLLREASQLPIDRWRATQVLAWLEVALGMPQYSARCAENVKSGKVLLELNDVELEAGLGLAHPMHRKKLRLAIEEQRRPEMVRYPLITQLGHTWVATEWLPDIGLPQYAEPFVQSLVDARMLDTLSKKELEKFLGVTRKFHQASIVHGIHVLRIVKYDRQTLAMRRVQSETVDTDPIVWTNQRFIRWVRSIDLGEYADNLKDSGVHGGLVVLEPSFSGDTMATALGIPPSKNIIRRHLNTEFDALILPARATLGQGIRSGCGVVPLTGPGGLQHYATTDRRSSGNLRISAWKGSQSSLSKAFRFNSKPHRTGDRSSFGNSTSPTPSYSSSEGGGGIYATIGHQYPNPHTNLQQQHYHHFLPPPTTAPPPIPSAGGIYSHGPPPGHRVSAPPVGGALDAVSTDPQMLYEQSRRRVKSISDIGASTSAGSVGACSLGGISASSESPE
Protein: At1g75290 (NAD(P)-binding Rossmann-fold superfamily protein) (B3LFB7)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
Sequence:
MASEKSKILVIGGTGHIGKLIIEASVKAGHSTLALVREASLSDPNKGKTVQNFKDFGVTLLHGDLNDHESLVKAIKQADVVISTVGSMQILDQTKIISAIKEAGNVKRFLPSEFGMDVDKSSAVEPAKSAFGRKLQTRRDIEAEGIPYTYLVTNYFAGYYLPTLVQLEPGLTSPPRDKVKIFGDGNVKAVINKEEDIAAYTIKAVDDPRTLNKTLYINPPNNTLSMNEIVTLWEKKIGKSVEKIYMSEEQIFKSIQESPVPFNVLLSINHAVFVKGDQTNFTIEPSFGFEASELYPDIKYTSIDEYLSYFALGTSLNT
Protein: Double-stranded RNA-binding protein 8 (dsRNA-binding protein 1) (OsDRB1) (dsRNA-binding protein 8) (Q0IQN6)
Organism: Oryza sativa subsp. japonica (Rice)
Function: Binds double-stranded RNA.
Interaction partners:
- Elongation factor 1-gamma 1
- Elongation factor 1-gamma 3
- Elongation factor 1-gamma 2
- Elongation factor 1-beta
- Elongation factor 1-delta 2
- Elongation factor 1-delta 1
- 40S ribosomal protein S6
- 40S ribosomal protein S6
- Os08g0116500 protein
- Small ribosomal subunit protein eS1
Sequence:
MDMPPTPLPPETANTSPAPNGATAGIRVENCYVFKSRLQEYAQKTGLQTPEYHTFKEGPSHEPVFKSTVVINNTSYDSLPGFFNRKAAEQSAAEVALMEIVKSIPANANIPAVQETGLCKNLLQEYAQKMNYAIPSYICTKSASGLAPFICTVEIGGIQYIGAAARTKKDAEIKAARTALLAIQGQSEGSANGATKYIVVPGKRVGKEVEKRPIETPKPLKVKKGGFKKKWNKRKFMKKDGQAVDVEKDEARVAGDAHDSDVLMQPTVITQEASCGTLFLQPCEEAKRVEAEPPRDIEMVQPDKENQHSDAALVQPDDEARVEQEPSRDISVVQPNEEAISGKQEPSIDAAILQPKEEASSVKQEPFIDTAMLQACKEAGSVELGPARDTVISQLNEQDRAVKQEPAGDIVVPQPDVHARVVKE
Protein: SAMP-activating enzyme E1 (EC 2.7.7.-) (Ubiquitin-like activating enzyme of archaea) (Ubl-activating enzyme) (D4GSF3)
Organism: Haloferax volcanii (strain ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM B-1768 / DS2) (Halobacterium volcanii)
Function: Likely activates multiple ubiquitin-like SAMPs for protein conjugation as well as for sulfur transfer, via ATP-dependent adenylation at their C-terminus. In fact, it is required for the formation of all three SAMP1-, SAMP2- and SAMP3-protein conjugates, and for molybdenum cofactor (MoCo) biosynthesis and thiolation of tRNAs.
Interaction partners:
- Probable molybdopterin synthase
- Small archaeal modifier protein 2
- Large ribosomal subunit protein eL40
- Molybdopterin molybdenumtransferase
- Desampylase
- Small archaeal modifier protein 1
- Small archaeal modifier protein 3
- Phosphomethylpyrimidine kinase / phosphomethylpyrimidine phosphate kinase
- Phosphomethylpyrimidine synthase
- Thiamine-phosphate synthase
Sequence:
MTLSLDATQLDRYSRHIIMDEVGPEGQGRLLSSRVVVVGAGGLGAPAIQYLAAVGVGELVVVDDDVVERSNLQRQVVHCDDDVGTPKAESAAAFVRGLNPDVSVEPVEARVDKSNVHEVVAGSDVVVDASDNFPTRYLLNDVCRFEGIPLVHGAIYKFEGQATTLVPDGPCYRCLFPEAPEPGTVPDCATTGVLGVLPGTVGCIQATEAMKLLLDEGEALDGRLLFYDAMDMTFETVPYRTNPDCPVCGEGGVDSIEDIDYVESCAISLD
Protein: Tyrosine aminotransferase (TAT) (EC 2.6.1.5) (A1L4G7)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MDPYMIQMSSKGNLSSILDVHVNVGGRSSVPGKMKGRKARWSVRPSDMAKKTFNPIRAIVDNMKVKPNPNKTMISLSIGDPTVFGNLPTDPEVTQAMKDALDSGKYNGYAPSIGFLSSREEIASYYHCPEAPLEAKDVILTSGCSQAIDLCLAVLANPGQNILVPRPGFSLYKTLAESMGIEVKLYNLLPEKSWEIDLKQLEYLIDEKTACLIVNNPSNPCGSVFSKRHLQKILAVAARQCVPILADEIYGDMVFSDCKYEPLATLSTDVPILSCGGLAKRWLVPGWRLGWILIHDRRDIFGNEIRDGLVKLSQRILGPCTIVQGALKSILCRTPGEFYHNTLSFLKSNADLCYGALAAIPGLRPVRPSGAMYLMVGIEMEHFPEFENDVEFTERLVAEQSVHCLPATCFEYPNFIRVVITVPEVMMLEACSRIQEFCEQHYHCAEGSQEECDK
Protein: Mitochondrial coenzyme A transporter SLC25A42 (Solute carrier family 25 member 42) (Q8R0Y8)
Organism: Mus musculus (Mouse)
Function: Mitochondrial carrier mediating the transport of coenzyme A (CoA) in mitochondria in exchange for intramitochondrial (deoxy)adenine nucleotides and adenosine 3',5'-diphosphate.
Subcellular location: Mitochondrion inner membrane {ECO:0000250|UniProtKB:Q86VD7}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Large ribosomal subunit protein eL18
- Proliferating cell nuclear antigen
- Ribonucleoside-diphosphate reductase large subunit
- Replication factor C subunit 3
- Centromere protein T
- Trifunctional purine biosynthetic protein adenosine-3
Sequence:
MGNGVQEGSVRLREDAEAVLAGAVSSKRDHRQVLSSLLSGALAGALAKTAVAPLDRTKIIFQVSSKRFSAKEAFRLLYFTYLNEGFLSLWRGNSATMVRVIPYAAIQFSAHEEYKRILGHYYGFRGEALPPWPRLLAGALAGTTAASLTYPLDLVRARMAVTPKEMYSNIFHVFIRISREEGLKTLYFGFTPTVLGVIPYAGLSFFTYESLKSLHREYSGRPQPYPFERMVFGACAGLIGQSASYPLDVVRRRMQTAGVTGHQHGSILSTLRSIVREEGAVRGLYKGLSMNWLKGPIAVGISFTTFDLMQILLRRLQS
Protein: Protein ALEX (Alternative gene product encoded by XL-exon) (Q9Z213)
Organism: Rattus norvegicus (Rat)
Function: May inhibit the adenylyl cyclase-stimulating activity of guanine nucleotide-binding protein G(s) subunit alpha which is produced from the same locus in a different open reading frame.
Subcellular location: Cell membrane {ECO:0000269|PubMed:11447126}; Peripheral membrane protein {ECO:0000269|PubMed:11447126}. Cell projection, ruffle {ECO:0000269|PubMed:11447126}. Note=Predominantly associated with cell membrane ruffles.
Interaction partners:
Sequence:
MSPSPTRLTVRSVDPLKTPNLTSRAPVRPSRKSKWAETTAHLQRKPCHSRSNSPAWEISGPPWSSLDHLDPIRHQSLQPSDFGARTPTGAHPGLGAYSPPPEEAMPFEFNEPAQEDRCQPPLQVPDLAPGGPEAWVSRALPAEPGNLGFENTGFREDYSPPPEESVPFQLDGEEFGGDSPPPDSASHATNRHWRFEFPTVAVPSTLCLRPARTRLPSGSRAPLADHARLSDLLTSHTTFPQWRSPDPCLRLAEPPLGSTTTPLSIWTAPQSQVMARPSKSREPQLRASTQRDPHLSDKQPRQETALSAAPLQRRQKSPPSSEEKDPPPNLKQCISSQLLLRSPERTLPKPIRTQLHTQFFRSVLRKSEESQPCPPIFRLLLKMRAQMSGQNQTEGQPQPPLPSPKTTENQPPPPPPSQPPSQPLSQPPSQPPSQPPSQLPRQSLTPKPSLPPGQSPTPKRSPQPRQPLPRRRSLPPGQPPSPLRSPLPGLSLLPEPIQPPGLSLEPQRCQPLLGQPPLEQPMQVLWSGEPGHSRLLQPLGHPSLPAQQLPPEQPLLPAQSLPAGQPLPPQAGPILDPPARRSRLLTRLLRGLLRGRVPGLTNTNVAEAAAGMRLRPASARSSPPAMSRKKGPLAASSGFCGETAALASPGATQSGATRSATSSPEPSEAASVYLSVPDHDPSAPGRPRILWKRGANRCAKKPWRCESRSAQIRNAASSSTSNWRRRRWTTCVHTACCF
Protein: Vacuolar proton pump subunit B (V-ATPase subunit B) (Vacuolar proton pump subunit B) (Q383B1)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- 
- V-type ATPase, C subunit, putative
- V-type proton ATPase subunit F
- V-type proton ATPase subunit
- Uncharacterized protein
- ATP synthase, putative
- Vacuolar ATP synthase subunit D, putative
- V-type proton ATPase subunit a
- H
- V-type proton ATPase subunit H
Sequence:
MGGHNEEVRMLSKQELLTEHIKELQKDYSIKPRLEYTTIRAVNGPLVILGNVRLPTFAEIVNIELADGTLRRGQVLEVDGDKAVVQVFEGTSGIDVMRSKCEFTGKVMELGVSEDMLGRVFNGSGIPIDDGPPVLAEQYRDIQGIPINPRARVYPEEMIQTGISSIDVMTSISRGQKIPLFSGAGLPHNEIAAQIVRQAGLVRREGKQEDFCIVFAAMGVNQETARFFRTEFEENGSMEKTVLFMNLANDPTIERIVTPRLALTTAEYLAYDCGKHVLVILTDMSSYADALREVSAAREEVPGRRGFPGYMYTDLACIYERAGRVLGRAGSITQIPILTMPNDDITHPIPDLTGYITEGQIYVDRQLHNRQLYPPINILPSLSRLMKNAIGEGMTRKDHSGVSNQMYAAYAVSRDILAMKAVVGEETLSSEDLLHLEFLEKFEKKFICQGFYESRDVFQSLDLCWQLLRIFPKVLLNKIDVKTRNEFYDRQPANR
Protein: Phospholipase A2 group XV (cDNA FLJ57757, highly similar to 1-O-acylceramide synthase) (B4DPU0)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MGLHLRPYRVGLLPDGLLFLLLLLMLLADPALPAGRHPPVVLGDNNRIPVIGPLKIREQQRSAVSTSWLLPYNYTWSPEKVFVQTPTINYTLRDYRKFFQDIGFEDGWLMRQDTEGLVEATMPPGVQLHCLYGTGVPTPDSFYYESFPDRDPKICFGDGDGTVNLKSALQCQAWQSRQEHQVLLQELPGSEHIEMLANATTLAYLKRVLLGP
Protein: TraF protein (Q46705)
Organism: Escherichia coli
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004162}; Single-pass membrane protein {ECO:0000256|ARBA:ARBA00004162}.
Interaction partners:
Sequence:
MARKSVDVDQELDENTGDGEFESERGGFNGSNRRSAPRMKAFVILMALLALVFIGITVMGKIRAPAKAEADKDGGKAQQANTLPNYSFNSDPDVNKPATAQNSPTDARAVQAAAQADADAGSSNTGARTSNKRKEPSPEELAMQRRLGGELAQTNQAATSNSPGAQPQDNETSEGSSALAKNLTPARLKASRAGVMANPSLTVPKGKMIPCGTGTELDTTVPGQVSCRVSQDVYSADGLVRLIDKGSWVDGQITGGIKDGQARVFVLWERIRNDQDGTIVNIDSAGTNSLGSAGIPGQVDAHMWERLAGAIMISLFSDTLTALVNQTQSNNIQYNSTENSGGQLASEALRSYMSIPPTLYDQQGDAVSIFVARDLDFSGVYTLADN
Protein: Homogentisate phytyltransferase 1, chloroplastic (AtHPT1) (EC 2.5.1.115) (Tocopherol polyprenyltransferase 1) (Vitamin E pathway gene 2-1 protein) (AtVTE2-1) (Q8VWJ1)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Involved in the synthesis of tocopherol (vitamin E). Catalyzes the condensation of homogentisate and phytyl diphosphate to form dimethylphytylhydrquinone. Low activity with geranylgeranyl diphosphate as substrate, but no activity with farnesyl diphosphate or solanesyl diphosphate. Tocopherol functions to limit lipid oxidation during seed desiccation, quiescence and germination and early seedling development. Protects thylakoid membrane lipids from photooxidation and is required for low-temperature adaptation.
Subcellular location: Plastid, chloroplast membrane {ECO:0000269|PubMed:21223386}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Tocopherol cyclase, chloroplastic
- 2-methyl-6-phytyl-1,4-hydroquinone methyltransferase, chloroplastic
- Geranylgeranyl diphosphate reductase, chloroplastic
- 4-hydroxyphenylpyruvate dioxygenase
- Homogentisate solanesyltransferase, chloroplastic
- Solanesyl diphosphate synthase 1, chloroplastic
- Solanesyl diphosphate synthase 2, chloroplastic
- 2-carboxy-1,4-naphthoquinone phytyltransferase, chloroplastic
- Isopentenyl-diphosphate Delta-isomerase I, chloroplastic
- Tocopherol O-methyltransferase, chloroplastic
Sequence:
MESLLSSSSLVSAAGGFCWKKQNLKLHSLSEIRVLRCDSSKVVAKPKFRNNLVRPDGQGSSLLLYPKHKSRFRVNATAGQPEAFDSNSKQKSFRDSLDAFYRFSRPHTVIGTVLSILSVSFLAVEKVSDISPLLFTGILEAVVAALMMNIYIVGLNQLSDVEIDKVNKPYLPLASGEYSVNTGIAIVASFSIMSFWLGWIVGSWPLFWALFVSFMLGTAYSINLPLLRWKRFALVAAMCILAVRAIIVQIAFYLHIQTHVFGRPILFTRPLIFATAFMSFFSVVIALFKDIPDIEGDKIFGIRSFSVTLGQKRVFWTCVTLLQMAYAVAILVGATSPFIWSKVISVVGHVILATTLWARAKSVDLSSKTEITSCYMFIWKLFYAEYLLLPFLK
Protein: Bacterial colonization factor (Q94247)
Organism: Caenorhabditis elegans
Interaction partners:
- Galectin
- Galectin
- C-type LECtin
- C-type LECtin
- Probable galaptin lec-8
- CUB_2 domain-containing protein
- G domain-containing protein
- Protein irg-7
Sequence:
MRLGIFLLALAGCCSFASAKQNCLVGNLIVSENVITSKSVELRECEGLCRKQTVKSPSGGLVLLTCEENKLMAFINKGQDCSSSELETSCFCEDELCNKVDLEENIPKPIEVINAPNNILCYVGFYANNTTPGFGSGDTVTCSPGNVCTSVSGVYNGYDAAAYACMPQGLCDSIFPNIDPNNPIACTNLAGTNIQGCCCYKQDCTSLAPMNNPPTPSPWNKNNQTCYQGISVNGALLYGGSFSQCLGECGSARIRTTYNGANVWGEIFVCDPVNVFTALNLDNGCMNLDTQNINGVPTALITGCACNSMDKCIDPTVVPPVYPVKQLRCAVGLYNGTTWLGAEMNCQGRCGRVRFNANGQQVSYFTCMPYDVCAGFGLASTEGQTYNPPQDEELEVYCCSASNNCNVNNPYILGRVNNSAVSTAKYPVLCYGGIWVNGVSITNSAYGLCQGECASASFTTTFANQVHNATIYTCDPVTMCQQAGISNSCGSVLGGVNACCCDNDLCIDPNRGSQRPQLRCYSGVSIPQDKYNTGGDQFCDGWCGSLNSVVNGKNATVYYCAPVGMCRYFGLGFGGSYGNCGQIPGADPQVTGCCCSETDNCLAPAGVNVTAIPARRDPRIVCYEGIHLNGQNISQPYYRMCDGECVSVSLGGTVNNNSHYATLYTCDPSSACAAMGLRNNCSTIDNSLTACCCDSNECIDPTYNRVPGKALKCYVGISTQHKGNIAGAEVLCDGYCATVSAVVGSDYVTAFHCAPRSMCRSLGLDNSNNTFYLDRFVNAYCCDVFDNCNVATSGFNVTIPPLAPNEMPRACYSGIFIGGSQISDGGWTACKGDCVAVNLNTTYNGVATTASLYTCDPSYICRMMNSTNRCHQQEQGFETCCCDSDACLDPTSTPPRKPYGDGNLCYVGAYSYDLKGNTIFNAGGEQYCEGNCASVTSTLANANVTVYACVPAYVCNSLYVYDSCRTLWYDRDITGCCCTNGPNCNLNQVVPRPPINNPGRRRPRVEYPITCPAGLIVDGFNQTPMEFSVCFGECASVSINATINGTLHTASFYTCDPSSVCYQLKVHNNCTSPEAGVTACCCDSDACLDPNRGKTVPTPPLKCYVGLYSTSVPSLQTGAEQLCDGKCASVSARIANDNVTLFACVPHSLCRSLELYDSCARMEPYYPEFRACCCDNADNCNVQQTHLANVINTTIPLTPLNDAPISCYSGLFINGTAYSSAGWQVCQGECVSVSITSQFNGQAGTAALYTCDPSRVCRNLNILNKCSSLENGITGCCCNTNACIDPTVYPARNPGNQLMCYAGISSNYIVNGSAVNVGAQIPCNGQCSSLSGVVGGFQVNTYHCMPNSICNSLELYDNCKPVWNDNQVTGCCCNNANNCNIANTTITPPPPPTSVDYAIACYTGLYVNGVPSTPVILGACQGQCASISLNTTLNGVATTATLYGCDPSTVCQSLNMNNWCASPIPGVSGCCCNTDLCLDPPKNKTVPSGFRKCFAGIYAQGKATGSEIFCPGKCASIQATLNQDPVAIFGCVPTQFCRQLEMYDECKPLPYDTTVTGCCCDNYNNCNVDLAGYGGKINTSMPVTNFRDYPIACFSGLYVNNMPISIAGWQACKGECASATLSTMYNGALTNATIYTCDPVSTCYQLGMNNNCTTIENGLSGCCCSTDACLDPTVSPPRTPNPLKCYVGLQSTYNSLSLGAETYCSGQCASLTGIVGGFNVTTYHCVADTICKSLEIKDTCRPLWSDREVTACCCNNADNCNLKDPNVKPGPAVLPDFPTACYQGLLVNNQTYGAPLTLQGCYGDCASITISTTIQNQNHTATLLTCDPTTVCQQLNMSNSCQTVEPGVSGCCCDTDGCLNPLTNTYPGPAKCYVGVYTSDGNVNVGGTVSCDGYCGSLETTVNNVLYKSYHCVPKTICKSLGLNNERKTISTDKDITGYCCTTGTNCNVKEAAVNTTNTIPVPTGIPMILCRSSIYLNGGPVTADSYSACAGSCASISYTAPYNGGNQTLTLYTCDPVTVCTSLNLTNSCASIDGGLSGCCCSTNNCVGPNNGPGIVTTQSPATTTKGSSSITFSILALFAAVYIALTRH
Protein: Protein immune deficiency (Q7K4Z4)
Organism: Drosophila melanogaster (Fruit fly)
Function: Essential for the imd/NF-kappa-B (Imd) humoral and epithelial immune response to Gram-negative bacteria. Functions as an adapter protein that transduces immunity signals from the activation of pathogen recognition receptors (PRRs) by bacterial infection to the Imd signaling pathway. Binding of diaminopimelic acid-type (DAP-type) bacterial peptidoglycans (PGN) causes multimerization or clustering of PGRP receptors which activate the Imd cascade probably by recruiting imd, Fadd and Dredd to the receptor complex. Once in proximity, Dredd cleaves imd in a Fadd-dependent manner to enable its association and activation by the ubiquitin E3-ligase DIAP2. The activated form of imd recruits and activates the Tab2/Tak1 complex thus acting upstream of the IKK complex (ird5 and key) to activate Rel and induce the expression of antimicrobial peptides such as Def, Dpt and Cecropin. Also able to inhibit the viral replication of the Sindbis virus. Involved in promoting the polyubiquitination and stability of faf which in turn, regulates the Imd pathway by controlling imd polyubiquitination and/or stability; they may therefore form a regulatory feedback mechanism within the Imd pathway. Not required for the cuticle melanization immune response to bacterial challenge.
Interaction partners:
- Fas-associated death domain protein
- Peptidoglycan-recognition protein LC
- Peptidoglycan-recognition protein LE
- Poor Imd response upon knock-in, isoform A
- Mitogen-activated protein kinase kinase kinase 7
- Death-associated inhibitor of apoptosis 2
- Caspase-8
- Nuclear factor NF-kappa-B p110 subunit
- Diptericin B
- Diptericin A
Sequence:
MSKLRNLLPTIFGGKEAQNPTPVEGRLEKDAAPVDDNEPDNNNSGALALPSTAGTPTASSDLTESVLRELSDPNYNSMDVVHSANIPGTLSNVQTNNTMNVHSAQQQVVMNFSNANNLHFGSVYNFNQNLSACSSRKGSTSTAEESVASPDGKPRASATRKTVSIVAMMQSQEEPDVRLLDVVSTHLGEGWKQVMRDLGMSEGQIDQAIIDHQMHGNIREVIYQLLLQWIRSSADGVATVGRLTTLLWESQHRDCVQRMKLVWKALEKRKTNS
Protein: MADS-box protein AGL71 (Protein AGAMOUS-LIKE 71) (Q9LT93)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: MADS-box transcription factor that acts with AGL42 and AGL72 in the control of flowering time. Promotes flowering at the shoot apical and axillary meristems. Seems to act through a gibberellin-dependent pathway. Interacts genetically with SOC1 and its expression is directly regulated by SOC1.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00251}.
Interaction partners:
- AGAMOUS-like 77
Sequence:
MVRGKIEIKKIENVTSRQVTFSKRRSGLFKKAHELSVLCDAQVAAIVFSQSGRLHEYSSSQMEKIIDRYGKFSNAFYVAERPQVERYLQELKMEIDRMVKKIDLLEVHHRKLLGQGLDSCSVTELQEIDTQIEKSLRIVRSRKAELYADQLKKLKEKERELLNERKRLLEEVNMHHSSKGNTEGGHRTKHSSEVETDLFIGLPVTRL
Protein: Cytoplasmic phosphatidylinositol transfer protein 1 (Mammalian rdgB homolog beta) (M-rdgB beta) (MrdgBbeta) (mM-rdgBbeta) (Retinal degeneration B homolog beta) (RdgBbeta) (Q8K4R4)
Organism: Mus musculus (Mouse)
Function: Catalyzes the transfer of phosphatidylinositol (PI) and phosphatidic acid (PA) between membranes (By similarity). Binds PA derived from the phospholipase D signaling pathway and among the cellular PA species, preferably binds to the C16:0/16:1 and C16:1/18:1 PA species (By similarity).
Subcellular location: [Isoform 1]: Cytoplasm {ECO:0000269|PubMed:12562526}.; SUBCELLULAR LOCATION: [Isoform 2]: Cytoplasm {ECO:0000269|PubMed:12562526}. Nucleus {ECO:0000269|PubMed:12562526}.
Interaction partners:
- Membrane-associated phosphatidylinositol transfer protein 3
- Ras-related protein Rab-1B
Sequence:
MLLKEYRICMPLTVDEYKIGQLYMISKHSHEQSDRGEGVEVVQNEPFEDPHHGNGQFTEKRVYLNSKLPSWARAVVPKIFYVTEKAWNYYPYTITEYTCSFLPKFSIHIETKYEDNKGSNDSIFDSEAKDLEREVCFIDIACDEIPERYYKESEDPKHFKSEKTGRGQLREGWRDNHQPIMCSYKLVTVKFEVWGLQTRVEQFVHKVVRDILLIGHRQAFAWVDEWYDMTMDEVREFERATQEATNKKIGVFPPAISISSIALLPSSVRSAPSSAPSTPLSTDAPEFLSIPKDRPRKKSAPETLTLPDPEKKATLNLPGVYTSEKPCRPKSE
Protein: Ranalexin (P39084)
Organism: Aquarana catesbeiana (American bullfrog) (Rana catesbeiana)
Function: Potent microbicidal activity, active against S.aureus and E.coli. It acts as well as a membrane-disruptive agent at higher concentrations.
Subcellular location: Secreted.
Interaction partners:
Sequence:
MFTLKKSLLLLFFLGTINLSLCEEERNAEEERRDNPDERDVEVEKRFLGGLIKIVPAMICAVTKKC
Protein: VH1 protein (A2N884)
Organism: Gallus gallus (Chicken)
Interaction partners:
Sequence:
MSPLVSSLLLLAALPGLMAAVTLDESGGGLQTPGGALSLVCKASGFTFSSYNMGWVRQAPGKGLEFVAGIDNTGSSTGYGSAVKGRATISRDNGQSTVRLQLNNLRAEDTGTYYCAKAAG
Protein: Protein RCC2 (Q8BK67)
Organism: Mus musculus (Mouse)
Function: Multifunctional protein that may affect its functions by regulating the activity of small GTPases, such as RAC1 and RALA. Required for normal progress through the cell cycle, both during interphase and during mitosis. Required for the presence of normal levels of MAD2L1, AURKB and BIRC5 on inner centromeres during mitosis, and for normal attachment of kinetochores to mitotic spindles. Required for normal organization of the microtubule cytoskeleton in interphase cells. Functions as guanine nucleotide exchange factor (GEF) for RALA. Interferes with the activation of RAC1 by guanine nucleotide exchange factors (By similarity). Prevents accumulation of active, GTP-bound RAC1, and suppresses RAC1-mediated reorganization of the actin cytoskeleton and formation of membrane protrusions. Required for normal cellular responses to contacts with the extracellular matrix of adjacent cells, and for directional cell migration in response to a fibronectin gradient (in vitro) (By similarity).
Subcellular location: Nucleus, nucleolus {ECO:0000250|UniProtKB:Q9P258}. Nucleus {ECO:0000250|UniProtKB:Q9P258}. Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:Q9P258}. Chromosome, centromere {ECO:0000250|UniProtKB:Q9P258}. Cytoplasm, cytoskeleton, spindle {ECO:0000250|UniProtKB:Q9P258}. Chromosome {ECO:0000250|UniProtKB:Q9P258}. Midbody {ECO:0000250|UniProtKB:Q9P258}. Cell membrane {ECO:0000250|UniProtKB:Q9P258}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q9P258}; Cytoplasmic side {ECO:0000250|UniProtKB:Q9P258}. Note=Appears in the nucleus at G2, then concentrates at the inner centromere region of chromosomes during prophase. Redistributes to the midzone of the mitotic spindle during anaphase. Here, the protein covers the entire equatorial diameter from cortex to cortex. Colocalizes with cytoplasmic microtubules in interphase cells. Colocalizes with RAC1 at the cell membrane. {ECO:0000250|UniProtKB:Q9P258}.
Interaction partners:
- Cell division cycle protein 20 homolog
- Serine/threonine-protein kinase PLK1
- Inner centromere protein
- Aurora kinase B
- Nuclear migration protein nudC
- Borealin
Sequence:
MPRKKGAAWEEPSSGNGTARAGPRRRGGPAGRKRERPERCSSSSGGGSSGDEDGPELDGAPGGGKRTARPATAGKAAGAAAIITEPEHTKERVKLEGSKCKGQLLIFGATNWDLIGRKEVPKQQAAYRNLGQNLWGPHRYGCLSGVRVRTVVSGSCAAHSLLITTEGKLWSWGRNEKGQLGHGDTKRVEAPRLIEALSHEAIVLAACGRNHTLALTDTGSVFAFGENKMGQLGLGNQTDAVPSPAQIMYNGQPITKMACGAEFSMLMDCKGNLYSFGCPEYGQLGHNSDGKFIARAQRIEYDCELVPRRVAIFIEKTKDGQILPVPNVVVRDVACGANHTLVLDSQKRVFSWGFGGYGRLGHAEQKDEMVPRLVKLFDFPGRGATQIYAGYTCSFAVSEVGGLFFWGATNTSRESTMYPKAVQDLCGWRIRSLACGKSSIIVAADESTISWGPSPTFGELGYGDHKPKSSTAAQEVKTLDGIFSEQVAMGYSHSLVIARDESEAEKEKLQRLPEYTPRTL