wanglab/gogpt-training-data huggingface dataset:
Protein: FI06026p (A1ZBR1)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- GEO12048p1
- Uncharacterized protein
- Protein crossbronx-like
- FI17342p1
Sequence:
MLPNWLTEEYLQPKLRAYYKDDQLKVVKVWAKPATEKGQNYMSLMTRIHVEIQQGDGLLQNRTYIIKESLSEDCPQAKVFLEYDVYNREMDMYEFILPKMNELLQEVGLTGKFTADTIFVDREYRTIILEDLAQYNYVNADRVKQLDLAHTKLTLEVLAKFHAASIVVKQRHPELLTKSLFIHCFSRDNKGYTEVYEGVLSAFIRFINEQPVLKKKYGNKLQKIHENIMDYGARTFEVGEQELLTLSHGDCWTTNFLYQYDDASNPQSAVAIDFQFSNFTSPVNDLHQFFTVSLRDEVQDMESVLVEKYYSDLKTNVDTLSYKGIFPSLQGFQKQFESRRFMCLLAHLFKPVIIYDGTEVSSDFSSVYKDTEEGIRFQKAIYANERVLKSATKLLAMLDAKGVLNLQ
Protein: Photoreceptor dehydrogenase, isoform C (EC 1.1.1.-, EC 1.1.1.105) (Pigment cell dehydrogenase reductase) (Q7KNR7)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MSFRGKNAVVTGGAGGIGLQVSKQLLAAGAAKVAIIDLQDNLEEFVKLRAAHPTQSVMIIKMDVANKKGVEATYEEIAKTFGNIDIVVNVAGIFNDKDVQRTLLVNLGGIINSTLSALPYMGKDNGGKGGIVVNMSSVVGLDPMFIIPVYGATKAGIINFTRCLANEKYYQRSGIKFVTVCPGATMTDMFTNFTEKIIFPETSDETYRILDRLNKQSAADVSRCILNVLEKDKNGAVYVIEGKRVYPLEIKPQWTGKEQAL
Protein: Tripeptidyl aminopeptidase (Tap) (EC 3.4.14.-) (Q54410)
Organism: Streptomyces lividans
Function: Cleaves tripeptides from the N-termini of proteins. Does not cleave mono- or dipeptides, or N-terminally blocked peptides.
Subcellular location: Secreted {ECO:0000269|PubMed:7487044}.
Interaction partners:
Sequence:
MRKSSIRRRATAFGTAGALVTATLIAGAVSAPAASAAPADGHGHGRSWDREARGAAIAAARAARAGIDWEDCAADWNLPKPIQCGYVTVPMDYAKPYGKQIRLAVDRIGNTGTRSERQGALIYNPGGPGGSGLRFPARVTNKSAVWANTAKAYDFVGFDPRGVGHSAPISCVDPQEFVKAPKADPVPGSEADKRAQRKLAREYAEGCFERSGEMLPHMTTPNTARDLDVIRAALGEKKLNYLGVSYGTYLGAVYGTLFPDHVRRMVVDSVVNPSRDKIWYQANLDQDVAFEGRWKDWQDWVAANDAAYHLGDTRAEVQDQWLKLRAAAAKKPLGGVVGPAELISFFQSAPYYDSAWAPTAEIFSKYVAGDTQALVDAAAPDLSDTAGNASAENGNAVYTAVECTDAKWPANWRTWDRDNTRLHRDHPFMTWANAWMNLPCATWPVKQQTPLNVKTGKGLPPVLIVQSERDAATPYEGAVELHQRFRGSRLITERDAGSHGVTGLVNPCINDRVDTYLLTGRTDARDVTCAPHATPRP
Protein: Receptor activity-modifying protein 1 (Q9WTJ5)
Organism: Mus musculus (Mouse)
Function: Transports the calcitonin gene-related peptide type 1 receptor (CALCRL) to the plasma membrane. Acts as a receptor for calcitonin-gene-related peptide (CGRP) together with CALCRL.
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:O60894}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:O60894}.
Interaction partners:
- Calcitonin receptor
- Calcitonin gene-related peptide type 1 receptor
- Calcitonin gene-related peptide 2
- Pro-adrenomedullin
- Islet amyloid polypeptide
- Receptor activity-modifying protein 3
- Receptor activity-modifying protein 2
- DNA-directed RNA polymerase III subunit RPC9
- Calcitonin
- Protein ADM2
Sequence:
MAPGLRGLPRCGLWLLLAHHLFMVTACRDPDYGTLIQELCLSRFKENMETIGKTLWCDWGKTIQSYGELTYCTKHVAHTIGCFWPNPEVDRFFIAVHHRYFSKCPISGRALRDPPNSILCPFIALPITVTLLMTALVVWRSKRTEGIV
Protein: Ferredoxin-1 (Ferredoxin I) (FdI) (P00194)
Organism: Rhodospirillum rubrum
Function: Ferredoxins are iron-sulfur proteins that transfer electrons in a wide variety of metabolic reactions.
Interaction partners:
Sequence:
AYKIEETCISCGACAAECPVNAIEQGDTIFVVNADTCIDCGNCANVCPVGAPVAE
Protein: Peptidoglycan-recognition protein SC2 (EC 3.5.1.28) (Q9V4X2)
Organism: Drosophila melanogaster (Fruit fly)
Function: N-acetylmuramyl-L-alanine amidase involved in innate immunity by degrading bacterial peptidoglycans (PGN). Probably plays a scavenger role by digesting biologically active PGN into biologically inactive fragments. Has no direct bacteriolytic activity (By similarity).
Subcellular location: Secreted {ECO:0000305}.
Interaction partners:
- Gram-negative bacteria-binding protein 1
- Peptidoglycan-recognition protein SA
- Modular serine protease
- Peptidoglycan-recognition protein SC1a
- LP12095p
- Serine protease 3
- Venom allergen-1
- trypsin
- Uncharacterized protein, isoform A
- Jonah 25Biii
Sequence:
MANKALILLAVLFCAQAVLGVTIISKSEWGGRSATSKTSLANYLSYAVIHHTAGNYCSTKAACITQLQNIQAYHMDSLGWADIGYNFLIGGDGNVYEGRGWNVMGAHATNWNSKSIGISFLGNYNTNTLTSAQITAAKGLLSDAVSRGQIVSGYILYGHRQVGSTECPGTNIWNEIRTWSNWKA
Protein: Inner membrane protein YqaA (P0ADR0)
Organism: Escherichia coli (strain K12)
Subcellular location: Cell inner membrane; Multi-pass membrane protein.
Interaction partners:
- Fructose-1-phosphate phosphatase YqaB
- Inner membrane protein YohD
- TVP38/TMEM64 family inner membrane protein YdjZ
- TVP38/TMEM64 family membrane protein YdjX
- Inner membrane protein YghB
- Inner membrane protein YabI
- Glutamate--cysteine ligase
- Inner membrane protein YqjA
Sequence:
MSEALSLFSLFASSFLSATLLPGNSEVVLVAMLLSGISHPWVLVLTATMGNSLGGLTNVILGRFFPLRKTSRWQEKATGWLKRYGAVTLLLSWMPVVGDLLCLLAGWMRISWGPVIFFLCLGKALRYVAVAAATVQGMMWWH
Protein: Tyrosine-protein phosphatase non-receptor type 6 (EC 3.1.3.48) (70Z-SHP) (Hematopoietic cell protein-tyrosine phosphatase) (PTPTY-42) (Protein-tyrosine phosphatase 1C) (PTP-1C) (SH-PTP1) (SHP-1) (P29351)
Organism: Mus musculus (Mouse)
Function: Modulates signaling by tyrosine phosphorylated cell surface receptors such as KIT and the EGF receptor/EGFR. Enhances the inhibition of mast cell activation mediated by the Lilrb4a receptor. The SH2 regions may interact with other cellular components to modulate its own phosphatase activity against interacting substrates. Together with MTUS1, induces UBE2V2 expression upon angiotensin II stimulation. Plays a key role in hematopoiesis.
Subcellular location: Cytoplasm. Nucleus {ECO:0000250}. Note=In neurons, translocates into the nucleus after treatment with angiotensin II. Shuttles between the cytoplasm and nucleus via its association with PDPK1 (By similarity). {ECO:0000250}.
Interaction partners:
- B-cell receptor CD22
- Tyrosine-protein kinase SYK
- Tyrosine-protein kinase JAK2
- Proto-oncogene vav
- B-cell differentiation antigen CD72
- Tyrosine-protein kinase ZAP-70
- Platelet endothelial cell adhesion molecule
- Lymphocyte cytosolic protein 2
- Tyrosine-protein kinase BTK
- Leukocyte immunoglobulin-like receptor subfamily B member 4A
Sequence:
MVRWFHRDLSGPDAETLLKGRGVPGSFLARPSRKNQGDFSLSVRVDDQVTHIRIQNSGDFYDLYGGEKFATLTELVEYYTQQQGILQDRDGTIIHLKYPLNCSDPTSERWYHGHISGGQAESLLQAKGEPWTFLVRESLSQPGDFVLSVLNDQPKAGPGSPLRVTHIKVMCEGGRYTVGGSETFDSLTDLVEHFKKTGIEEASGAFVYLRQPYYATRVNAADIENRVLELNKKQESEDTAKAGFWEEFESLQKQEVKNLHQRLEGQRPENKSKNRYKNILPFDHSRVILQGRDSNIPGSDYINANYVKNQLLGPDENSKTYIASQGCLDATVNDFWQMAWQENTRVIVMTTREVEKGRNKCVPYWPEVGTQRVYGLYSVTNSREHDTAEYKLRTLQISPLDNGDLVREIWHYQYLSWPDHGVPSEPGGVLSFLDQINQRQESLPHAGPIIVHCSAGIGRTGTIIVIDMLMESISTKGLDCDIDIQKTIQMVRAQRSGMVQTEAQYKFIYVAIAQFIETTKKKLEIIQSQKGQESEYGNITYPPAVRSAHAKASRTSSKHKEEVYENVHSKSKKEEKVKKQRSADKEKNKGSLKRK
Protein: Moesin/ezrin/radixin homolog 1 (O17905)
Organism: Caenorhabditis elegans
Subcellular location: Cell junction, adherens junction {ECO:0000256|ARBA:ARBA00004536}. Cell projection, rhabdomere {ECO:0000256|ARBA:ARBA00043944}.
Interaction partners:
- PIPK domain-containing protein
- Gamma-aminobutyric acid receptor subunit beta
- Protein kinase domain-containing protein
- FERM domain-containing protein 8
- FERM and PDZ domain-containing protein 4
- Protein madd-4
- Protein lin-2
- Neuroligin-1
Sequence:
MSNIPRGVGAPPPPGMNSSKRGRLVCIKVRMLDDTVAVFHLGHKAIGQTLLDEVCRHLNLLECDYFGLSFIDINGNHCWLDREKTILRQITNGSTDAKFYFVVKFYTPNPIDLEEEYTRYLFTMQIKRDLALGELHCSDNTASLLSAYLVQSECGDFSSEDYPDATYLSHTRFVPNQTLEFQKKVMDNHRNFIGMTPGESDLAMLEVARRCDFYGVKLHAAKDIDGNDAALSVMHLGIKVFRQLQLDTTFSWARIRKLSFKRKKLLVKLHPDSYQYLKETVEFSFETRDECKNFWKKCVEHHAFFRCVQAEEPKKETRFFISKGSSFRYHGRTQKQLIDYVREHHKRREPFTRPLRSAASTRKGTYSSTYGLVTDRPTKHRNGSVYEPNQTDPYNKHQNTHSSMPHIAHISSQPADHSFSGTLDARVGKSVTRDPSTSVTQHRLRQLKRSERCISDVDTVERPQRSSCRPVSHAINISSTSSKEQPDLSVSLPNVLSDDLQMVCKEIEIEQNDPPKSVSGDNFQQRRSSRDYDNVSEDSYRLSDHERSTRSEVGVGSKFAAATIFNSTFVARKPGSNVVKRVVAHTKSTPNSTDDEEGALKSASEYQTFRHIKEYPFARNANIVPIEIDGPNVDLSARRSPAATTTTTRTYANTTTTVTTTSKVLTSSGAVLMKPKVISNDHEPSSGTHSSRVSPESGTYGALGPLPGRVITKENMMITPEGFKEKKAKPNPPPKPSFPVQAVHSETEVVREIKTERASSHPLVHMQEEIPFSRAPLKFEDKKERKSSLSRPALISVQSEDNPDVQKCHLFNSDIPYTLTMRNVENTQSLPYSSFKDVSTAKKQGYESNSLKRVSKSPEFKRRKSLDLVPRKRLPSPGNFSAQDHTISPTTPDSDVLEYLLRRRSLLGDKSVIKTKSKRTDPRRQTQPVRFDLPPSPCSPTAGGSTPFISILNDDLFDECVSESRSLHEDMDRLDKTTPHNQSISSFMSQKSRRDSEDSDVMPPPPEEILNKAMISSSRPAPPPPPPKSLAAAVKVAEMKAAAAGKIYYSGSSRTGKITDSPPFIDDSPKNSSASDAPSVPSPQKNCFSDF
Protein: Hexose transporter HXT8 (P40886)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Probable glucose transporter.
Subcellular location: Membrane; Multi-pass membrane protein.
Interaction partners:
- Carbon catabolite-derepressing protein kinase
- Uncharacterized protein YKR075C
- Uncharacterized globin-like protein YNL234W
Sequence:
MTDRKTNLPEEPIFEEAEDDGCPSIENSSHLSVPTVEENKDFSEYNGEEAEEVVVPEKPASAYATVSIMCLCMAFGGFMSGWDTGTISGFVNQTDFLRRFGNYSHSKNTYYLSNVRTGLIVSIFNVGSAIGCLFLSKLGDIYGRCMGLIIVIVVYMVGIVIQIASIDKWYQYFIGRIIAGIGAGSISVLAPMLISETAPKHIRGTLLACWQLMVTFAIFLGYCTNYGTKTYSNSVQWRVPLGLCFAWAIIMIGGMTFVPESPRFLVQVGKIEQAKASFAKSNKLSVDDPAVVAEIDLLVAGVEAEEAMGTASWKELFSRKTKVFQRLTMTVMINSLQQLTGDNYFFYYGTTIFKSVGMNDSFETSIVLGIVNFASCFFSLYSVDKLGRRRCLLLGAATMTACMVIYASVGVTRLYPNGKSEPSSKGAGNCTIVFTCFYIFCFSCTWGPVCYVIISETFPLRVRSKCMSVATAANLLWGFLIGFFTPFITSAINFYYGYVFMGCLAFSYFYVFFFVPETKGLTLEEVDEMWMDGVLPWKSESWVPASRRDGDYDNEKLQHDEKPFYKRMF
Protein: Diguanylate cyclase DgcP (DGC) (EC 2.7.7.65) (P76245)
Organism: Escherichia coli (strain K12)
Function: Catalyzes the synthesis of cyclic-di-GMP (c-di-GMP) via the condensation of 2 GTP molecules. Cyclic-di-GMP is a second messenger which controls cell surface-associated traits in bacteria.
Interaction partners:
- Cyclic di-GMP phosphodiesterase PdeL
- Probable cyclic di-GMP phosphodiesterase PdeG
- Probable cyclic di-GMP phosphodiesterase PdeC
- Probable cyclic di-GMP phosphodiesterase PdeN
- Probable cyclic di-GMP phosphodiesterase PdeB
- Probable cyclic di-GMP phosphodiesterase PdeD
- Oxygen sensor protein DosP
- Cyclic di-GMP phosphodiesterase PdeF
- Cyclic di-GMP phosphodiesterase PdeH
- Probable diguanylate cyclase CdgI
Sequence:
MSDQIIARVSQSLAKEQSLESLVRQLLEMLEMVTDMESTYLTKVDVEARLQHIMFARNSQKMYIPENFTVSWDYSLCKRAIDENCFFSDEVPDRWGDCIAARNLGITTFLSTPIHLPDGSFYGTLCAASSEKRQWSERAEQVLQLFAGLIAQYIQKEALVEQLREANAALIAQSYTDSLTGLPNRRAIFENLTTLFSLARHLNHKIMIAFIDLDNFKLINDRFGHNSGDLFLIQVGERLNTLQQNGEVIGRLGGDEFLVVSLNNENADISSLRERIQQQIRGEYHLGDVDLYYPGASLGIVEVDPETTDADSALHAADIAMYQEKKHKQKTPFVAHPALHS
Protein: L-dopachrome tautomerase yellow-f (EC 5.3.3.12) (Q9VG09)
Organism: Drosophila melanogaster (Fruit fly)
Function: Tautomerization of L-dopachrome with decarboxylation to give 5,6-dihydroxyindole (DHI). Also catalyzes the tautomerization of the methyl ester of L-dopachrome and dopamine chrome. May play a role in melanization reactions during late pupal and adult stages. May play a role in melanization reactions during larval and early pupal stages.
Subcellular location: Secreted {ECO:0000269|PubMed:12164780}.
Interaction partners:
- L-dopachrome tautomerase yellow-f2
Sequence:
MLSLDVLLLCAISGFQLLISADGDPMIEVFKWKQLDFYNRGDGYKDLWNRICIPDSHFYNSRKCLGSSSSGSFIQYNNVPQGVTHFRGRLFVTVPRRQPGIPSTLNYIDLAKDGWSQSPHLRAYPNLAVNQYNASEQNLVSVYRTSVDVCGRLWFVDTGMLEFPNNRQQIRHPSIWVIDLANDRLLKRFEIPQSIVEIGRGLASITIDVGARRCNDAYAYIPDLVNRRLHVYHLRSDRIWSFEHSFFNFDPLSDNLNIGGQTFRWDDGIFSATLGSYKPDGSRDVFFHPMASTNEFVVSNRVLQQEFNAARSDHGDDFHLLGTRGPSTQSTMHKYDPRTGVIFFAEVQKSGVGCWKTSKPFSTENHGSVYSNSSEMIYPSDLTIDEEGYIWVMSNSMPIFVYSKLDVEKYNFRIWRQSTLLAKRGTVCE
Protein: Leucine-rich repeat (LRR) family protein (Putative leucine-rich repeat disease resistance protein) (Q9SHU4)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
Sequence:
MTCLLLLLLLLLFSSADSLTSPSDVSALKAFKATVKPNSIPPWSCLASWDFTVSDPCASPRRTHFTCGITCSSDSTRVTQLTLDPAGYTGRLTPLISGLTELLTLDLAENNFYGLIPSSISSLTSLKTLILRSNSFSGSLPDSVTRLNSLESIDISHNSLTGPLPKTMNSLSNLRQLDLSYNKLTGAIPKLPKNLIDLALKANTLSGPISKDSFTESTQLEIVEIAENSFTGTLGAWFFLLESIQQVDLANNTLTGIEVLPPNLAGENNLVAVELGFNQIRGNAPASFAAYPRLSSLSMRYNVLHGVIPSEYERSKTLRRLYLDGNFLTGKPPARFVRTDAEVMGSLGNNCLQGCPGKAKMCAPSQKPFYICKQAYGGKPKS
Protein: Hypoxia up-regulated protein 1 (O46067)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Endoplasmic reticulum lumen {ECO:0000256|ARBA:ARBA00004319}.
Interaction partners:
- Endoplasmic reticulum chaperone BiP
- Nucleotide exchange factor Sil1
- Heat shock protein 83
- Calreticulin
- LD25575p
- RE14391p
- Heat shock protein 83
- GrpE protein homolog, mitochondrial
- Protein disulfide-isomerase A6 homolog
- DnaJ-like-2, isoform A
Sequence:
MKLVLLLSALLAGIALSQGAAVMSVDLGSEWMKVGVVSPGVPMEIALNRESKRKTPAILAFRDGTRTIGEDAQTIGIKDPNSAYGYLLDLLGKTIDNPIVDLYRKRFPYYNIVGDPERNTVVFRKSDTDEFSVEELVAQLLVKAKQFAQESVQQPITECVLTVPGYFGQAEREALLSAAQLANLKVLQLINDYAAVALNYGVFHRGEINETAQYFLFYDMGAYKTSAAVVSYQLVKDKQTREINPVVQVLGVGYDRTLGGLEIQLRLRDYLAQEFNALKKTKTDVTTSPRALAKLFKEAGRLKNVLSANTEFFAQIENLIEDIDFKLPVTREKLEQLCEDLWPRATKPLEEALASSHLSLDVINQVILFGGGTRVPRVQETIKAVIKQELGKNLNADESATMGAVYKAADLSAGFKVKKFVVKDATLFPLQVSFERDPGDGAAVKQVKRALFALMNPYPQKKVITFNKHTDDFEFYVNYADLDRYSKEEIAALGSLNVTKVQLKQVKELLEKSKKELVDNKGIKAYFYLDDSGIFRCTGVEYVYEKQKPEDDADEDSTLSKFGSTLSKLFTKEGEEKKDNSEQEEAANAGEEPSKSEDNEKAKEEDASKEQKSEESTKQDTEAKNETIKLVTVKSPVTYESQTQFVVPLVGSAYDQSVAKLAAINKAEEQRVRLESAFNALEAHIIEVQQKLDEESYAKCATAEEKEKLLAECSTLGEWLYEDLEDPKAEIYEEKLAQLKKLSNVFLARHWEHEERPEAIKALKGMIDGAEKFLVTGRNLTKDTNPEKDVFTQVEIDTLDKVITETNAWLKTETAAQKKLAKNADIRLTVKDITDKMSLLDREVKYLVNKIKIWKPKVKPAAEKEKKKEEEVVASGSGDDTKSEDAEQQQEQATKEEQQEQEPVDEITPTPAEEETKTPHSEL
Protein: Delta-aminolevulinic acid dehydratase 1, chloroplastic (ALADH1) (EC 4.2.1.24) (Porphobilinogen synthase) (Q9SFH9)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Catalyzes an early step in the biosynthesis of tetrapyrroles. Binds two molecules of 5-aminolevulinate per subunit, each at a distinct site, and catalyzes their condensation to form porphobilinogen (By similarity).
Subcellular location: Plastid, chloroplast {ECO:0000250}.
Interaction partners:
- Porphobilinogen deaminase, chloroplastic
- Glutamate-1-semialdehyde 2,1-aminomutase 1, chloroplastic
- Glutamate-1-semialdehyde 2,1-aminomutase 2, chloroplastic
- Glutamyl-tRNA reductase 1, chloroplastic
- Uroporphyrinogen decarboxylase 1, chloroplastic
- Uroporphyrinogen decarboxylase 2, chloroplastic
- Probable glutamyl-tRNA reductase 3, chloroplastic
- Glutamyl-tRNA reductase 2, chloroplastic
- Probable delta-aminolevulinic acid dehydratase 2, chloroplastic
- At1g07280/F22G5_32
Sequence:
MATTPIFNASCSFPSTRGIDCKSYIGLRSNVSKVSVASSRIATSQRRNLVVRASESGNGHAKKLGMSDAECEAAVAAGNVPEAPPVPPKPAAPVGTPIIKPLNLSRRPRRNRASPVTRAAFQETDISPANFVYPLFIHEGEEDTPIGAMPGCYRLGWRHGLVQEVAKARAVGVNSIVLFPKVPEALKNSTGDEAYNDNGLVPRTIRLLKDKYPDLIIYTDVALDPYSSDGHDGIVREDGVIMNDETVHQLCKQAVSQARAGADVVSPSDMMDGRVGAIRSALDAEGFQNVSIMSYTAKYASSFYGPFREALDSNPRFGDKKTYQMNPANYREALIEAREDEAEGADILLVKPGLPYLDIIRLLRDKSPLPIAAYQVSGEYSMIKAGGVLKMIDEEKVMMESLMCLRRAGADIILTYFALQAATCLCGEKR
Protein: Syntaxin-11 (O75558)
Organism: Homo sapiens (Human)
Function: SNARE that acts to regulate protein transport between late endosomes and the trans-Golgi network.
Subcellular location: Membrane {ECO:0000305}; Peripheral membrane protein {ECO:0000305}. Golgi apparatus, trans-Golgi network membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}.
Interaction partners:
- Syntaxin-binding protein 2
- Synaptosomal-associated protein 23
- Protein unc-13 homolog D
- Vesicle-associated membrane protein 8
- Vesicle-associated membrane protein 2
- Syntaxin-binding protein 5
- Ras-related protein Rab-27A
- Vesicle-associated membrane protein 4
- Syntaxin-binding protein 1
- Vesicle-associated membrane protein 3
Sequence:
MKDRLAELLDLSKQYDQQFPDGDDEFDSPHEDIVFETDHILESLYRDIRDIQDENQLLVADVKRLGKQNARFLTSMRRLSSIKRDTNSIAKAIKARGEVIHCKLRAMKELSEAAEAQHGPHSAVARISRAQYNALTLTFQRAMHDYNQAEMKQRDNCKIRIQRQLEIMGKEVSGDQIEDMFEQGKWDVFSENLLADVKGARAALNEIESRHRELLRLESRIRDVHELFLQMAVLVEKQADTLNVIELNVQKTVDYTGQAKAQVRKAVQYEEKNPCRTLCCFCCPCLK
Protein: Uncharacterized protein (Q38E27)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Uncharacterized protein
- Uncharacterized protein
- NADH-ubiquinone oxidoreductase complex I subunit
- Peptidyl-prolyl cis-trans isomerase
- NADH dehydrogenase 1 alpha subcomplex subunit 13
- NADH dehydrogenase subunit NI8M
- NADH-ubiquinone oxidoreductase complex I subunit
- Uncharacterized protein
- NADH dehydrogenase flavoprotein 1, mitochondrial
- Adrenodoxin reductase, putative
Sequence:
MRLRRIALGAFTPTVFTSVRSVSTRETLSVEEQRYLDQELPPRELLTSLRSRDRSPTDDNETDVTVPGDSFGIMRNRVAFYKPVPRDVYSGELGECFPEGCHPLRCVNPATLHHLSERFGVSIREAVKAMQNAQMDINIAIDELCRRKCIDPPAGSFGLVGLESYASETFCLVNFTLPSLEATRDDDVLDALHELTLSAAEIPLDTPTEDLVDKFVNNWTVEDGRSCKDVLDMYDLGVNKIVLLPHGDYSVEGFYVLHPVKEDTPNIGTGAAACCLDLRTGIHNRFRFHVERIADSVSEHVIRELVHYGQDVHVLRQAYWFKPEYSVEEYIRFKESLLQPSASVFEMRYAVLAVGSYALPGYRNLVEMEKLKVAQHKYEKHYEDFMSPGKWLTSDNSQLQTVAAGGGNAPGAALHMHTNGPDVALNAMETRAGPLRRTLETSIQAHGDRVFSRFYRNNHH
Protein: Anaerobic dimethyl sulfoxide reductase chain C (DMSO reductase anchor subunit) (P18777)
Organism: Escherichia coli (strain K12)
Function: Terminal reductase during anaerobic growth on various sulfoxide and N-oxide compounds. DmsC anchors the DmsAB dimer to the membrane and stabilizes it.
Subcellular location: Cell inner membrane; Multi-pass membrane protein.
Interaction partners:
- Anaerobic dimethyl sulfoxide reductase chain B
- Dimethyl sulfoxide reductase DmsA
- Tat proofreading chaperone DmsD
- Putative dimethyl sulfoxide reductase chain YnfE
- Probable dimethyl sulfoxide reductase chain YnfF
- Probable anaerobic dimethyl sulfoxide reductase chain YnfG
- Biotin sulfoxide reductase
- Hydrogenase-2 operon protein HybA
Sequence:
MGSGWHEWPLMIFTVFGQCVAGGFIVLALALLKGDLRAEAQQRVIACMFGLWVLMGIGFIASMLHLGSPMRAFNSLNRVGASALSNEIASGSIFFAVGGIGWLLAMLKKLSPALRTLWLIVTMVLGVIFVWMMVRVYNSIDTVPTWYSIWTPMGFFLTMFMGGPLLGYLLLSLAGVDGWAMRLLPAISVLALVVSGVVSVMQGAELATIHSSVQQAAALVPDYGALMSWRIVLLAVALCLWIAPQLKGYQPAVPLLSVSFILLLAGELIGRGVFYGLHMTVGMAVAS
Protein: Centractin (Actin-related protein A) (Q54I79)
Organism: Dictyostelium discoideum (Social amoeba)
Function: Component of a multi-subunit complex, PPK2 (poly P kinase complex 2) involved in microtubule based vesicle motility. It is associated with the centrosome. PPK2 complex can synthesize a poly chain of hundreds of phosphate residues linked by ATP-like bonds.
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000269|PubMed:15496465}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000269|PubMed:15496465}.
Interaction partners:
- Actin-related protein 10
Sequence:
MSSVEFSNQPVVIDNGSGVIKAGFAGQDPPSHIFQSLVGNPKYKKVMGLNIENESTYFVGDRINDWRGILKLKHPMDHGIVSNWSDMERVWTYTYDQLKIQPSEHPVLLTDVPNNPRLHRERAAQLFFETYNAPALYFSIPAVLSLYASGRTTGIVLDSGDGVTHVVPVFEGFALPHAISRIDIAGRDITEYLQHLLRRSGYNFKTSAEKEVVRIIKEKTCYVAHDPQKEEELLEPDSSSSKPVQPQYTLPDGNVIELGAERFRAPEILFHPDIIGDESLGIHQCLDMSIRKSDLDLRKTFYSNIILGGGSTLFQGFGDRLLNEVKKLAPKDIKIKITAPPERKYSAWMGGSILASLSTFKDLWVTRQEYEEDGCSVIHRKIF
Protein: Protein dbl-1 (Dpp and BMP-like protein 1) (G5EEL5)
Organism: Caenorhabditis elegans
Function: Ligand for the serine/threonine-protein kinase receptor type-1 sma-6 which activates a TGF-beta-like signaling pathway. Multifunctional protein that is involved in body size, male ectodermal patterning, innate immunity, lipid metabolism and neural plasticity. Dose-dependent regulator of body size, probably influencing the sizes of some or all cells rather than their number. Plays a role in patterning of male-specific genital sensilla (simple sense organs), known as rays, and mating-associated structures, spicules. Plays a protective role in response to infection by the Gram-negative bacterium S.marcescens, by activating expression of genes involved in innate immunity. Regulator of lipid homeostasis, acting non cell-autonomously in the hypodermis; partly dependent on the Insulin/IGF-1-like signaling (IIS) mediated pathway. Required for aversive olfactory learning of pathogenic bacteria in adults. Involved in gland cell morphology, possibly via activation of a Smad-independent TGF-beta signaling pathway. Required to oppose the autoregulation of expression of Runt-related transcription factor rnt-1.
Subcellular location: Secreted {ECO:0000305}.
Interaction partners:
- Serine/threonine-protein kinase receptor sma-6
- Cell surface receptor daf-4
- Cell surface receptor daf-1
- CTCK domain-containing protein
- SMAll.
- Smad protein daf-8
- Dwarfin sma.
- Smad-related protein daf-14
- Repulsive guidance molecule B homolog drag-1
- Insulin-like receptor
Sequence:
MNDSVRTTTTISSTKSLVHSFQLSAILHLFLLISFTPMSAAADQHASHATRRGLLRKLGLEHVPVQTGPSIDVPQHMWDIYDDDNDVDWVRHYYPKEIIEDNEGFLLSYNLSLAARNAHNEEVTKATLKLRLRRNNKARRSGNISIYFFEDDINNDRFQIESRSVDNLTEWIDFDVTAAFLRRTNRISFFIDLPEDVEIEETQSSSLSSLPYARAQSAPLIVFSDLSEPSSVRRKRSAQTGNSERKNRKKGRKHHNTEAESNLCRRTDFYVDFDDLNWQDWIMAPKGYDAYQCQGSCPNPMPAQLNATNHAIIQSLLHSLRPDEVPPPCCVPTETSPLSILYMDVDKVIVIREYADMRVESCGCR
Protein: Lysosome-associated membrane glycoprotein 5 (Brain and dendritic cell-associated LAMP) (Brain-associated LAMP-like protein) (BAD-LAMP) (Lysosome-associated membrane protein 5) (LAMP-5) (Q9D387)
Organism: Mus musculus (Mouse)
Function: Plays a role in short-term synaptic plasticity in a subset of GABAergic neurons in the brain.
Subcellular location: Cytoplasmic vesicle membrane {ECO:0000269|PubMed:17215451}; Single-pass type I membrane protein {ECO:0000305}. Cell membrane {ECO:0000269|PubMed:17215451}; Single-pass type I membrane protein {ECO:0000269|PubMed:17215451}. Cell projection, dendrite {ECO:0000269|PubMed:17215451}. Cytoplasmic vesicle, secretory vesicle, synaptic vesicle membrane {ECO:0000269|PubMed:27272053}; Single-pass type I membrane protein {ECO:0000305}. Cell projection, growth cone membrane {ECO:0000269|PubMed:17215451}; Single-pass type I membrane protein {ECO:0000305}. Early endosome membrane {ECO:0000269|PubMed:17215451}; Single-pass type I membrane protein {ECO:0000269|PubMed:17215451}. Recycling endosome {ECO:0000269|PubMed:17215451}. Endoplasmic reticulum-Golgi intermediate compartment membrane {ECO:0000250|UniProtKB:Q9UJQ1}; Single-pass type I membrane protein {ECO:0000305}. Endosome membrane {ECO:0000250|UniProtKB:Q9UJQ1}; Single-pass type I membrane protein {ECO:0000305}. Note=Recycles from the vesicles of the endocytic recycling compartment (ERC) to the plasma membrane (PubMed:17215451). Colocalizes with UNC93B1 in large endosomal intracellular vesicles (By similarity). Accumulates in the endoplasmic reticulum-Golgi intermediate compartment (ERGIC) before its disappearance upon activation by CpG dinucleotides (By similarity). Associates with cortical membranes (By similarity). Localizes mostly in cytoplasmic vesicles of neuronal cell body (PubMed:17215451). Localizes to synaptic vesicles in a subset of GABAergic neurons (PubMed:27272053). {ECO:0000250|UniProtKB:Q9UJQ1, ECO:0000269|PubMed:27272053}.
Interaction partners:
Sequence:
MDLRVRTLLGGDRLRILLMFFHVMVQTVAEQEVENLSGLSTNPEKDIFVVRENGTTCLMAEFAAKFIVPYDVWASNYVDLITEQAEISLTRGAEVKGHCGHNESELEVFWVDHAYTLRMLFVKESHNTSKGPEATWNLNKVHFVYDSSEKTHFKAPVKVNKYIASSHHLSALVTPAGMSYECQAQQTISLASSDPQKTVTMILSAVHIQPFDIISDFVFSEEHKCPVDEQEQLEETLPLILGLILGLVIVITLVIYHIHHKMTANQVQIPRDRSQYKHMG
Protein: Glyceraldehyde-3-phosphate dehydrogenase 2 (EC 1.2.1.12) (Glyceraldehyde-3-phosphate dehydrogenase II) (GAPDH II) (P07487)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cytoplasm.
Interaction partners:
- Triosephosphate isomerase
- Glyceraldehyde-3-phosphate dehydrogenase 1
- Phosphoglycerate kinase
- Enolase
- Fructose-bisphosphate aldolase
- Glucose-6-phosphate isomerase
- Fructose-bisphosphate aldolase
- Pyruvate kinase
- Probable transaldolase
- transketolase
Sequence:
MSKIGINGFGRIGRLVLRAAIDKGANVVAVNDPFIDVNYMVYLFKFDSTHGRFKGTVAAEGGFLVVNGQKITVFSERDPANINWASAGAEYIVESTGVFTTIDKASTHLKGGAKKVIISAPSADAPMFVCGVNLDAYKPDMKVVSNASCTTNCLAPLAKVINDNFEIVEGLMTTVHATTATQKTVDGPSGKLWRDGRGAAQNIIPASTGAAKAVGKVIPALNGKLTGMAFRVPTPNVSVVDLTVRLGKGASYDEIKAKVQEAANGPLKGILGYTDEEVVSTDFLSDTHSSVFDAKAGISLNDKFVKLISWYDNEFGYSNRVIDLIKYMQSKD
Protein: At4g28210 (Embryo defective 1923) (Q9M0I6)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Glycine-rich protein family
- Protein PELOTA 1
- Protein RST1
- Small ribosomal subunit protein eS6y
- Oleosin 21.2 kDa
- 3-phosphoinositide-dependent protein kinase 1
- Metal-nicotianamine transporter YSL3
- Serine/threonine-protein kinase D6PK
Sequence:
MTLLALSSSLSSPSFFCRNSRIRFSPVSRISSLNGDNKLTNSPPQFLNAGASLRRFVAPGKFPSVRLRVLTRCEKENAPKGGIEDDAERFARRESTMPDRFRYLTKEAPDSPIIWPWFVALGFLVYAWRAVLFELSNWRKAAFAILAFVGDLSKFALALVFHFIGDPITSLISLVETAMYSVRAFYSGIVAYTPVRELTTVILLASSVLAIGEAVAPESISKQPYVVTIAGLVGYAAVQSYISEPFFWTVLLGLYGYSRLIKKRDDVTSALPSAAVLAGVGEPWVRVVAITGYLALAMYHNSTKTSSEEESQILRRAPPMPLLAAALAIGVRLAAKWAGYRHLTWMIV