wanglab/gogpt-training-data huggingface dataset:
Protein: Growth/differentiation factor 8 (GDF-8) (Myostatin) (O18836)
Organism: Bos taurus (Bovine)
Function: Acts specifically as a negative regulator of skeletal muscle growth.
Subcellular location: Secreted {ECO:0000250|UniProtKB:O08689}.
Interaction partners:
- Activin receptor type-2B
- Follistatin
- TGF-beta receptor type-1
- Activin receptor type-2A
- Follistatin-related protein 3
- receptor protein serine/threonine kinase
- Myogenin
- Myogenic factor 5
- Myoblast determination protein 1
- Mothers against decapentaplegic homolog 2
Sequence:
MQKLQISVYIYLFMLIVAGPVDLNENSEQKENVEKEGLCNACLWRENTTSSRLEAIKIQILSKLRLETAPNISKDAIRQLLPKAPPLLELIDQFDVQRDASSDGSLEDDDYHARTETVITMPTESDLLTQVEGKPKCCFFKFSSKIQYNKLVKAQLWIYLRPVKTPATVFVQILRLIKPMKDGTRYTGIRSLKLDMNPGTGIWQSIDVKTVLQNWLKQPESNLGIEIKALDENGHDLAVTFPEPGEDGLTPFLEVKVTDTPKRSRRDFGLDCDEHSTESRCCRYPLTVDFEAFGWDWIIAPKRYKANYCSGECEFVFLQKYPHTHLVHQANPRGSAGPCCTPTKMSPINMLYFNGEGQIIYGKIPAMVVDRCGCS
Protein: Complement factor I (EC 3.4.21.45) (C3B/C4B inactivator) [Cleaved into: Complement factor I heavy chain; Complement factor I light chain] (Q9WUW3)
Organism: Rattus norvegicus (Rat)
Function: Trypsin-like serine protease that plays an essential role in regulating the immune response by controlling all complement pathways. Inhibits these pathways by cleaving three peptide bonds in the alpha-chain of C3b and two bonds in the alpha-chain of C4b thereby inactivating these proteins. Essential cofactors for these reactions include factor H and C4BP in the fluid phase and membrane cofactor protein/CD46 and CR1 on cell surfaces. The presence of these cofactors on healthy cells allows degradation of deposited C3b by CFI in order to prevent undesired complement activation, while in apoptotic cells or microbes, the absence of such cofactors leads to C3b-mediated complement activation and subsequent opsonization.
Subcellular location: Secreted, extracellular space {ECO:0000250|UniProtKB:P05156}.
Interaction partners:
- Complement factor H
- Complement C3
- Complement C4
- Complement component receptor 1-like protein
- Mannose-binding protein C
- Membrane cofactor protein
- Prothrombin
- Thrombomodulin
- Complement factor H-related 4
- Ficolin-2
Sequence:
MKLALLILLLLNPHLSSSKNTPASGQPQEDLVEQKCLLKNYTHHSCDKVFCQPWQKCIEGTCACKLPYQCPKAGTPVCATNGRGYPTYCHLKSFECLHPEIKFSNNGTCTAEEKFNVSLIYGSTDTEGIVQVKLVDQDEKMFICKNSWSTVEANVACFDLGFPLGVRDIQGRFNIPVNHKINSTECLHVRCQGVETSLAECTFTKKSSKAPHGLAGVVCYTQDADFPTSQSFQCVNGKRIPQEKACDGVNDCGDQSDELCCKGCRGQAFLCKSGVCIPNQRKCNGEVDCITGEDESGCEEDKKNKIHKGLARSDQGGETEIETEETEMLTPDMDTERKRIKSLLPKLSCGVKRNTHIRRKRVVGGKPAEMGDYPWQVAIKDGDRITCGGIYIGGCWILTAAHCVRPSRYRNYQVWTSLLDWLKPNSQLAVQGVSRVVVHEKYNGATYQNDIALVEMKKHPGKKECELINSVPACVPWSPYLFQPNDRCIISGWGREKDNQKVYSLRWGEVDLIGNCSRFYPGRYYEKEMQCAGTSDGSIDACKGDSGGPLVCKDVNNVTYVWGIVSWGENCGKPEFPGVYTRVASYFDWISYYVGRPLVSQYNV
Protein: Dual specificity protein kinase shkA (EC 2.7.11.1) (SH2 domain-containing protein 1) (SH2 domain-containing protein A) (Q54RB7)
Organism: Dictyostelium discoideum (Social amoeba)
Function: Required for proper chemotaxis and phagocytosis; proper spatiotemporal control of F-actin levels in chemotaxing cells. Negative regulator of the PI3K (phosphatidylinositol 3 kinase) pathway. Predominantly phosphorylates serines and threonines and tyrosines at a lower level.
Subcellular location: Membrane {ECO:0000269|PubMed:11274054}.
Interaction partners:
Sequence:
MATQQQQQQQQQQQQQIKARKDIQIQQAQSASDILGPPEISETEITTESILGDGSFGTVYKGRCRLKDVAVKVMLKQVDQKTLTDFRKEVAIMSKIFHPNIVLFLGACTSTPGKLMICTELMKGNLESLLLDPMVKLPLITRMRMAKDAALGVLWLHSSNPVFIHRDLKTSNLLVDANLTVKVCDFGLSQIKQRGENLKDGQDGAKGTPLWMAPEVLQGRLFNEKADVYSFGLVLWQIFTRQELFPEFDNFFKFVAAICEKQLRPSIPDDCPKSLKELIQKCWDPNPEVRPSFEGIVSELEEIIIDCCIPDEYGAILWKNHFKHENEANWKDFINVFSNFVGLTNANTPSMSDLLQFSPNLNGSTIELNFKCLKSIIVSSPKGPHEEEVVLMEQFGKVLAWFGNLKEDGSQILDKIRQLMECAWFHGDISTSESENRLRQKPEGTFLVRFSTSEYGAYTISKVSKNGGISHQRIHRPQGKFQVNNSKYLSVKELITGEAQALGINTPCLGSRFLSLIYKAQLSGYIN
Protein: tRNA pseudouridine(38/39) synthase (EC 5.4.99.45) (tRNA pseudouridine synthase 3) (tRNA pseudouridylate synthase 3) (tRNA-uridine isomerase 3) (Q9BZE2)
Organism: Homo sapiens (Human)
Function: Formation of pseudouridine at position 39 in the anticodon stem and loop of transfer RNAs.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- Pseudouridylate synthase TRUB1
- Pseudouridylate synthase 7 homolog
- Pseudouridylate synthase PUS7L
- Pseudouridylate synthase TRUB2, mitochondrial
- Pseudouridylate synthase RPUSD4, mitochondrial
- Pseudouridylate synthase RPUSD2
- tRNA
- tRNA pseudouridine synthase Pus10
- RNA pseudouridylate synthase domain-containing protein 1
- Large ribosomal subunit protein bL17m
Sequence:
MAYNDTDRNQTEKLLKRVRELEQEVQRLKKEQAKNKEDSNIRENSAGAGKTKRAFDFSAHGRRHVALRIAYMGWGYQGFASQENTNNTIEEKLFEALTKTRLVESRQTSNYHRCGRTDKGVSAFGQVISLDLRSQFPRGRDSEDFNVKEEANAAAEEIRYTHILNRVLPPDIRILAWAPVEPSFSARFSCLERTYRYFFPRADLDIVTMDYAAQKYVGTHDFRNLCKMDVANGVINFQRTILSAQVQLVGQSPGEGRWQEPFQLCQFEVTGQAFLYHQVRCMMAILFLIGQGMEKPEIIDELLNIEKNPQKPQYSMAVEFPLVLYDCKFENVKWIYDQEAQEFNITHLQQLWANHAVKTHMLYSMLQGLDTVPVPCGIGPKMDGMTEWGNVKPSVIKQTSAFVEGVKMRTYKPLMDRPKCQGLESRIQHFVRRGRIEHPHLFHEEETKAKRDCNDTLEEENTNLETPTKRVCVDTEIKSII
Protein: Derailed 2, isoform B (Derailed 2, isoform C) (GH27039p) (Q7JQT0)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Protein Wnt-5
Sequence:
MELLPLKSPLPILLLCLTISTSVSGYLNIFISHHEVMKLMGLEADLFYVHEGAINTYAMHFTVPVPADVHELEFSWQSLIAYPLPYAISIEYNNDQEALGTPTLSIPHKGLVPQEIESFLVYLPCTGNASLQMPVNVNMVVRAPPRFNDTRLHFKRNKICAKGISPEPNQSPAPAHAPSQGPALLSAAACALGLVLAVGLVASMMYVRARKQLRQDSLHTSFTTAAYGSHQNVFIRLDPLGRPPSATGSYATIASLNKYPADSKKSCSIFDRFRSSPTPTPYATALLPMNLEQTAETIYSKPESICPSRISYYASSQLTQPCSLSTPKSIRSNGNGNCTSGSGSLSLFGGIPTGSTITMASHGEKGNQRLRRITSVQPGALSYEELVKEGTFGRIYAGKLGESCEALVKTVIDGASLTQVACLLQDASLLIGVSHQHILAPLLANTELPGPPEIAYPHPSKGNLKMYLQKSRESSTALSTRQLVEFGLHITKGLAYLHSLGIVHKDIATRNCYLDEESYVKICDSALSRDLFPDDYDCLGDNENRPLKWLSLESLQKRVYATQGDVWALGVTYWELVTLAQMPHEEVDIFELTNYLAAGFRLEQPVNCPDEFFTVMNCCWHCEAKQRPTPSQLLSYLQDFHADLGMYI
Protein: Vacuolar protein sorting-associated protein 38 (O60149)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Involved in endosome-to-Golgi retrograde transport as part of the vps34 PI3-kinase complex II. Mediates the interaction between atg6 and the pik3-ppk19 core complex, leading to the recruitment of atg6 to the membrane (By similarity).
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16823372}. Golgi apparatus, trans-Golgi network membrane {ECO:0000250|UniProtKB:Q05919}; Peripheral membrane protein {ECO:0000305}. Endosome membrane {ECO:0000250|UniProtKB:Q05919}; Peripheral membrane protein {ECO:0000305}.
Interaction partners:
- Serine/threonine-protein kinase vps15
- Phosphatidylinositol 3-kinase pik3
- Vacuolar protein sorting-associated protein atg6
- Autophagy-related protein 14
- PtdIns3K complex I subunit atg38
- Polyphosphoinositide phosphatase
- 1-phosphatidylinositol 3-phosphate 5-kinase fab1
- Ubiquitin-like protein ATG12
- Autophagy-related protein 18
- Protein VAC14 homolog
Sequence:
MSLELPGNYRLSRLKSIQIRNVQEIQNHSKFAINTTENLWKRDVQLKRAISEGTIRIFISLHVQSKKLPVYITETSGNANHIFYVDEKVTEKLQKYRHEEYFIVRTWCSSSSHAFKLHKEWKILRYDSNFRYIGNDPVFAVCHIRNGLLCEFNDGVYIYTTSQSSDIMRQTSFPKSASTYSIDRRKDGYTIQKITRILKLAECIDEMHIAKHEIRAHFQEEEFQQIRLMHKRMLLRDEKIDELAKLEHLWQKQINSITQMRTKFDKTKSWLSSKRNTLNKSKESLQKDEAEYVELANSLKTKVETNIEIRILMAHAIRMHVSHLSKIYPIQPSPGNHDEFTIRNLRLSFEPDKINNVEMAASIGFLAHLLQTLSKYLEKELAYPILCASSRSSILDTLTPDIPTRIFPLYPATRPIELFEHAIYLLNQDVNDFLETFGLPIDQSMDILRNFKKLLQFILSGQHLSFVQVTSTAP
Protein: Augmin complex subunit dgt2 (Dim gamma-tubulin 2) (Q9VKD6)
Organism: Drosophila melanogaster (Fruit fly)
Function: As part of the augmin complex, plays a role in centrosome-independent generation of spindle microtubules. The complex is required for mitotic spindle assembly through its involvement in localizing gamma-tubulin to spindle microtubules. dgt2 binds to microtubules in vitro.
Subcellular location: Cytoplasm, cytoskeleton, spindle {ECO:0000269|PubMed:17412918, ECO:0000269|PubMed:19289792}. Cytoplasm, cytoskeleton, spindle pole {ECO:0000269|PubMed:19289792, ECO:0000269|PubMed:23785300}. Note=Stably associates with the polar regions of some acentrosomal meiotic spindles in contrast to the uniform staining observed over mitotic spindles in syncytial embryos (PubMed:19289792, PubMed:23785300). {ECO:0000269|PubMed:19289792, ECO:0000269|PubMed:23785300}.
Interaction partners:
- Augmin complex subunit msd1
- Augmin complex subunit dgt6
- Augmin complex subunit wac
- Augmin complex subunit dgt5
- Augmin complex subunit msd5
- Augmin complex subunit dgt3
- Augmin complex subunit dgt4
- GEO11018p1
Sequence:
MDDPSATLLPEHSEDLRLARDAELKKVLKLKLVLDELRRLDVGPNPSDEIKRALKLVSIGSYARLGEMEGAGQEQVLGLPSGSSFPPLNYTDRKTVRTKLSAQLRTTLQPIAELCDRIREEFPDAFGQEADLSCDQKEILRLEEEHRSGLEKLVALLTRKCTLLKETAELKLGPQLANELKLQQAQAQLVQTKAELLRGFFVHEAASRTEHSVKAHKEVEAHLDELLAAKK
Protein: Tryptophan-rich sensory protein (TSPO) (Translocator protein TspO) (TspO regulatory protein) (Q9RFC8)
Organism: Cereibacter sphaeroides (Rhodobacter sphaeroides)
Function: May play a role in the transmembrane transport of tetrapyrroles and similar compounds, and thereby contribute to the regulation of tetrapyrrole biosynthesis. Binds tetrapyrroles and promotes the photooxidative degradation of protoporphyrin IX. Binds protoporphyrin IX, hemin, and coproporphyrin III, but does not bind delta-aminolevulinic acid. Can bind bilirubin, curcumin, gossypol, retinoic acid, cholesterol and the benzodiazepine receptor agonist PK-11195 (in vitro). Plays a role in the response to low oxygen levels and in the regulation of the biosynthesis of photosynthetic pigments.
Subcellular location: Membrane {ECO:0000269|PubMed:10681549, ECO:0000269|PubMed:20541505, ECO:0000269|PubMed:23651039, ECO:0000269|PubMed:23952237, ECO:0000269|PubMed:25635101, ECO:0000269|PubMed:7673149}; Multi-pass membrane protein {ECO:0000269|PubMed:20541505, ECO:0000269|PubMed:25635101}. Cell inner membrane {ECO:0000305|PubMed:20541505}; Multi-pass membrane protein {ECO:0000269|PubMed:20541505, ECO:0000269|PubMed:25635101}. Note=Outer membrane proteins generally mediate transport processes by forming beta-barrel structures, and unlike TspO, their transmembrane domains do not contain any helices. Detected in the cell inner membrane when expressed in E.coli (PubMed:20541505). This suggest that TspO is in the inner membrane, even if experiments shown in PubMed:7673149 suggest location in the outer membrane. {ECO:0000269|PubMed:20541505, ECO:0000305}.
Interaction partners:
Sequence:
MNMDWALFLTFLAACGAPATTGALLKPDEWYDNLNKPWWNPPRWVFPLAWTSLYFLMSLAAMRVAQLEGSGQALAFYAAQLAFNTLWTPVFFGMKRMATALAVVMVMWLFVAATMWAFFQLDTWAGVLFVPYLIWATAATGLNFEAMRLNWNRPEARA
Protein: Prolyl 4-hydroxylase subunit alpha 2 (A8MXE0)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MKLWVSALLMAWFGVLSCVQAEFFTSIGHMTDLIYAEKELVQSLKEYILVEEAKLSKIKSWANKMEALTSKSAADAEGYLAHPVNAYKLVKRLNTDWPALEDLVLQDSAAGFIANLSVQRQFFPTDEDEIGAAKALMRLQDTYRLDPGTISRGELPGTKYQAMLSVD
Protein: Pheromone-regulated membrane protein 6 (Low affinity K(+) transporter 2) (Q04705)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Low affinity potassium transporter that, with KCH1, participates in high-affinity Ca(2+) influx system (HACS) activation during the response to mating pheromone. Directly promotes K(+) influx and HACS may electrochemically respond to this K(+) influx. KCH1 and PRM6/KCH2 act at the apex of the calcium signaling pathway that is used for survival during prolonged exposures to mating pheromones.
Subcellular location: Cell membrane {ECO:0000269|PubMed:23204190}; Multi-pass membrane protein {ECO:0000255}. Bud tip {ECO:0000269|PubMed:23204190}. Vacuole lumen {ECO:0000269|PubMed:23204190}. Note=Localizes to the distal tip of growing buds. {ECO:0000269|PubMed:23204190}.
Interaction partners:
- Factor-induced gene 1 protein
- Low-affinity potassium transport protein
- High-affinity potassium transport protein
Sequence:
MESSLQKLKFQDIDINLIPTAKWTTKLQYILYTWCQSILHVAMFFSDIYTCIKLLAFNTWSNNIIQPFLEFRISKWLFSGCILCSSLILIWELVIGLRVYRKKEITSNYMNGISRLINCLFNFKKYQIFELIVLTDEKKFSKWLFFSYFEISGCLRLLFGDSPRQIINGLTLWSVLLTVSNETSSGTHSTQSLGNLDDLNGIINKIKHIAKTNYEESVILSFMLFSFIIWVILISKLILSIIIFIIFIRPRFLSSKRKVKGYELKLRKYVSKVIDENLSRTVYELGILIDDEEEGTICGDNKTQKKFDYDSPDYGDESTIPSYYCYSDVETYERVYTPIKAYFPQKYKHKYI
Protein: Syntabulin (Syntabulin isoform X2) (D3KVM2)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004167}; Single-pass membrane protein {ECO:0000256|ARBA:ARBA00004167}.
Interaction partners:
Sequence:
MVLSKGKRCFSGSETDFSSSSSAGSYKTRETQLSNSAGKNLSSRSRGPHIRSLPVFKPAGSPSAPRDAELYAPIRTPPKTPSFTNSSSCSNSSSSRRRTAPVRYHSCGDNHGIKPPNPEQYLTPLQQKEVAIRHLKTKLRDSENTVCDRESEIEELKSQLGRMREDWIEEECHRVEAQLALKEARKEIKQLRQVVETMKNSLMEKDKGIQKYFIDINIQNRKLESLLHSMELAQNGCNLQDEPTLDFICEAPESSTEAKMELELHCGEQAVEEMANSELLINDEMVNRVEILMSTAVDSSQDGSTKIISQPGLSCLEPSVSEKSTKEHVSSIPIGAEDKGIQTDDVIYSTDLQTLLYQLLKLQGGGFPGLLVPSPNQSHDISSAQAPKKSQKEELPEAHEQDVAISTAQIVPSDSGLGFSEPEVGPEFMEEMNSKNKAVVGKNHWSNNFFVDLVAVAAPVLPTVAWLYSQHGLVGGAPVYNIASLIRGCCVMGLHSLRHVSHGPDT
Protein: Cytoplasmic 60S subunit biogenesis factor REI1 (Required for isotropic bud growth protein 1) (pre-60S factor REI1) (P38344)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Pre-60S-associated factor involved in the cytoplasmic maturation of the 60S subunit. Involved in the dissociation and recycling of other late pre-60S factors like ARX1, TIF6 and ALB1 before newly synthesized large ribosomal subunits enter translation. Cooperates with the co-chaperone JJJ1 in the release of the nuclear-export factor ARX1. May act redundantly with REH1 to directly promote a stabilizing structural rearrangement in cytoplasmic 60S subunit maturation independent on ARX1 recycling.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:15107529}.
Interaction partners:
- 60S ribosomal export protein NMD3
- Ribosome biogenesis protein RLP24
- Large subunit GTPase 1
- Probable metalloprotease ARX1
- Eukaryotic translation initiation factor 6
- Nucleolar GTP-binding protein 1
- Large ribosomal subunit protein uL23
- Nucleolar GTP-binding protein 2
- Large ribosomal subunit protein uL22A
- Ribosome assembly factor MRT4
Sequence:
MSSSGVYTCNSCVLTFDSSDEQRAHMKSDWHRYNLKRRVAQLPPISFETFDSKVSAAAASTSKSAEKEKPVTKKELKRREKQALLEKKKKLLEIARANMLENMQKSQEGNTPDLSKLSLQENEENKEKEEPKKEEPEQLTEEEMAERVMQEKLRNRVDIPLEQCLFCEHNKHFKDVEENLEHMFRTHGFYIPEQKYLVDKIGLVKYMSEKIGLGNICIVCNYQGRTLTAVRQHMLAKRHCKIPYESEDERLEISEFYDFTSSYANFNSNTTPDNEDDWEDVGSDEAGSDDEDLPQEYLYNDGIELHLPTGIKVGHRSLQRYYKQDLKPEVILTEGQGTLVAAETRSFLPAFDKKGVQTQQRVWQTERFDKKRLDKRSAKFVNNQPHYRDQLLQ
Protein: CTD nuclear envelope phosphatase 1 (EC 3.1.3.16) (Serine/threonine-protein phosphatase dullard) (O95476)
Organism: Homo sapiens (Human)
Function: Serine/threonine protein phosphatase forming with CNEP1R1 an active phosphatase complex that dephosphorylates and may activate LPIN1 and LPIN2. LPIN1 and LPIN2 are phosphatidate phosphatases that catalyze the conversion of phosphatidic acid to diacylglycerol and control the metabolism of fatty acids at different levels. May indirectly modulate the lipid composition of nuclear and/or endoplasmic reticulum membranes and be required for proper nuclear membrane morphology and/or dynamics. May also indirectly regulate the production of lipid droplets and triacylglycerol. May antagonize BMP signaling.
Subcellular location: Endoplasmic reticulum membrane; Single-pass membrane protein. Nucleus membrane; Single-pass membrane protein.
Interaction partners:
- Nuclear envelope phosphatase-regulatory subunit 1
- Phosphatidate phosphatase LPIN1
- Phosphatidate phosphatase LPIN3
- Phosphatidate phosphatase LPIN2
- Bone morphogenetic protein receptor type-2
Sequence:
MMRTQCLLGLRTFVAFAAKLWSFFIYLLRRQIRTVIQYQTVRYDILPLSPVSRNRLAQVKRKILVLDLDETLIHSHHDGVLRPTVRPGTPPDFILKVVIDKHPVRFFVHKRPHVDFFLEVVSQWYELVVFTASMEIYGSAVADKLDNSRSILKRRYYRQHCTLELGSYIKDLSVVHSDLSSIVILDNSPGAYRSHPDNAIPIKSWFSDPSDTALLNLLPMLDALRFTADVRSVLSRNLHQHRLW
Protein: Uncharacterized protein, isoform A (Q9W2W1)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MLIEIYDYAAKLLNNMTARGVRNSVGKSAESRTKESTGKLGSLLGRTLAKVAKVARSNPAQHVTNLPVSALLLQALDVADVARGQGIDYPITSTTGTTFNIITTTTTTTTTTTGSDPTDVLGSQPPAFSFPANVTGAPGSAGNANAYLPAGNLSGFIESSTTAVMSTLPIPTSTMATLQAQTVATFIAATGSKNRPTTIVVYPTVSPESIVIPIVSCIFGFPILALLVICCLRRRAKLARERDRRRNYDMQDHAVSLVRFSPIHRLNYRSSRAISLRPERSLSQGFTSLELDTVLEERCSDVEQTQTEMFNAESPMDTTSYKMSFSSS
Protein: Transmembrane protein 63B (H3BLW6)
Organism: Homo sapiens (Human)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
Sequence:
XSILRKVAWDYGRLALVTDADSVASAMHGDSHDRYERLTSVSSSVDFDQRDNGFCSWLTAIFRIKDDEIRDKCGGDAVHYLSFQRHIIGLLVVVGVLSVGIVLPVNFSGDLLENNAYSFGRTTIANLKSGNNLLWLHTSFAFLYLLLTVYSMRRHTSKMRYKEDDLVKRTLFINGISKYAESEKIKKHFEEAYPNCTVLEARPCYNVARLMFLDAERKKAERGKLYFTNLQSKENVPTMINPKPCGHLCCCVVRGCEQVEAIEYYTKLEQKLKEDYKREKEKVNEKPLGMAFVTFHNETITAIILKDFNVCKCQGCTCRGEPRPSSCSESLHISNWTVSYAPDPQNIYWEHLSIRGFIWWLRCLVINVVLFILLFFLTTPAIIITTMDKFNVTKPVEYLNNPIITQFFPTLLLWCFSALLPTIVYYSAFFEAHWTRSGENRTTMHKCYTFLIFMVLLLPSLGLSSLDLFFRWLFDKKFLAEAAIRFECVFLPDNGAFFVNYVIASAFIGNAMDLLRIPGLLMYMIRLCLARSAAERRNVKRHQAYEFQFGAAYAWMMCVFTVVMTYSITCPIIVPFGLMYMLLKHLVDRYNLYYAYLPAKLDKKIHSGAVNQVVAAPILCLFWLLFFSTMRTGFLAPTSMFTFVVLVITIVICLCHVCFGHFKYLSAHNYKIEHTETDTVDPRSNGRPPTAAAVPKSAKYIAQVLQDSEVDGDGDGAPGSSGDEPPSSSSQDEELLMPPDALTDTDFQSCEDSLIENEIHQ
Protein: Mitogen-activated protein kinase PMK11 (MAPK PMK1) (EC 2.7.11.24) (G4N0Z0)
Organism: Pyricularia oryzae (strain 70-15 / ATCC MYA-4617 / FGSC 8958) (Rice blast fungus) (Magnaporthe oryzae)
Function: Mitogen-activated protein kinase; part of the MST11-MST7-PMK1 MAP kinase (MAPK) cascade that is essential for appressorium formation, penetration and invasive growth. Central regulator of appressorium development that acts downstream of the cAMP signal. The MST11-MST7-PMK1 MAP kinase cascade transduces signals from the cell surface sensors MDB2 and SHO1 that recognize various surface signals such as surface hydrophobicity, cutin monomers, and rice leaf waxes. Regulates expression of secreted fungal effector proteins implicated of host immune defenses, preventing reactive oxygen species generation and excessive callose deposition at plasmodesmata. Furthermore, controls the hyphal constriction required for fungal growth from one rice cell to the neighboring cell, enabling host tissue colonization and blast disease. Targets downstream of the PMK1-MAPK pathway include transcription factor MST12 and pathogenicity-related genes GAS1 and GAS2, both of which are expressed during appressorium formation, even if regulation of MST12 is not associated with expression of GAS1 or GAS2.
Interaction partners:
- Mitogen-activated protein kinase kinae MST7
- Transcription factor MST12
- protein-tyrosine-phosphatase
- protein-tyrosine-phosphatase
- Cytokinesis protein sepA
- von Willebrand RING finger domain-containing protein
- Mitogen-activated protein kinase kinae kinase MST11
- mitogen-activated protein kinase kinase
- Response regulatory domain-containing protein
- MADS-box MEF2 type transcription factor MIG1
Sequence:
MSRANPPSNSSGSRKISFNVSEQYDIQDVVGEGAYGVVCSAIHKPSGQKVAIKKITPFDHSMFCLRTLREMKLLRYFNHENIISILDIQKPRSYETFNEVYLIQELMETDMHRVIRTQDLSDDHCQYFIYQTLRALKAMHSANVLHRDLKPSNLLLNANCDLKVCDFGLARSAASQEDNSGFMTEYVATRWYRAPEIMLTFKEYTKAIDVWSVGCILAEMLSGKPLFPGKDYHHQLTLILDVLGTPTMEDYYGIKSRRAREYIRSLPFKKKVPFRTLFPKTSDLALDLLEKLLAFNPVKRITVEEALKHPYLEPYHDPDDEPTAPPIPEEFFDFDKHKDNLSKEQLKQFIYQEIMR
Protein: Long chain fatty acid elongation enzyme (Q5K4I1)
Organism: Gossypium hirsutum (Upland cotton) (Gossypium mexicanum)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
Sequence:
MEVPFFPTLFSCIKGLVVQQALFSTLEDWLVKHPKILQFSWENGQTPASSHRFLTLTVLSYISFTFVLSQLSRPSLSHPLLKSIAAVHNIFLLTLSFTMALGCLVSIFSQVPNFNTLVCFPRGTSPSGPLFFWAYIFYLSKIVEFMDTLLIILSGSMKRLSFLHVYHHSMVVIMCYICLDSAQSSVPMVLITNCVVHVVMYSYYLLCTLGMHPKWKKMVTDFQLVQFRLSFLIMAMLVFYHFTASGCSGILSWCFNGAFNVSLLYLFSDFHAKSYSTNAKVFKGN
Protein: Calcitonin gene-related peptide 2 (CGRP2) (Beta-type CGRP) (Beta-CGRP) (Calcitonin gene-related peptide II) (CGRP-II) (P10092)
Organism: Homo sapiens (Human)
Function: CGRP induces vasodilation. It dilates a variety of vessels including the coronary, cerebral and systemic vasculature. Its abundance in the CNS also points toward a neurotransmitter or neuromodulator role.
Subcellular location: Secreted {ECO:0000269|PubMed:1318039}.
Interaction partners:
- Calcitonin gene-related peptide type 1 receptor
- Receptor activity-modifying protein 1
- Islet amyloid polypeptide
- Receptor activity-modifying protein 3
- Pro-adrenomedullin
- Receptor activity-modifying protein 2
- Calcitonin receptor
- Calcitonin
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein G
Sequence:
MGFRKFSPFLALSILVLYQAGSLQAAPFRSALESSPDPATLSKEDARLLLAALVQDYVQMKASELKQEQETQGSSSAAQKRACNTATCVTHRLAGLLSRSGGMVKSNFVPTNVGSKAFGRRRRDLQA
Protein: Glycosyltransferase involved in cell wall biogenesis (O06406)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Interaction partners:
- Uncharacterized glycosyltransferase Rv0539
- Probable UDP-glucose 4-epimerase GalE3
- Probable conserved integral membrane protein
- S-methyl-5'-thioadenosine phosphorylase
- Probable conserved transmembrane protein
- Possible transferase
- 5'-methylthioadenosine/S-adenosylhomocysteine nucleosidase
- Possible conserved membrane protein
- Mycothione reductase
Sequence:
MSCLPVSVLVVAKAPEPGRVKTRLAAAIGDKVAADIAAAALLDTLDAVAAAPVTARAVALTGDLDSAADSAEIRRRLKSFTVFRQRGDAFADRLANAHVDAADGYPVLQIGMDTPQVTAELLADCARLLLQIPAVLGLAFDGGWWVLGIRTPTAAECLRAVPMSQPDTGELTLKALRDNGIDVTLVQRLGDFDIVDDIALVRDCCAPGSRFAQATRAAGL
Protein: TRIM29 protein (Q0P6H7)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MEPGETRRNSYPRADTGLFSRSKSGSEEVLCDSCIGNKQKAVKSCLVCQASFCELHLKPHLEGAAFRDHQLLEPIPTCSARKCPVHGKTMELFCQTDQTCICYLCMFQEHKNHSTVTVEEAKAEKETELSLQKEQLQLKIIEIEDEAEKWQKEKDRIKSFTTNEKAILEQNFRDLVRDLEKQKEEVRAALEQREQDAVDQVKVIMDALDERAKVLHEDKQTREQLHSISDSVLFLQEFGALMSNYSLPPPLPTYHVLLEGEGLGQSLGNFKDDLLNVCMRHVEKMCKADLSRNFIERNHMENGGDHRYVNNYTNSFGGEWSAPDTMKRYSMYLTPKGGVRTSYQPSSPGRFTKETTQKNFNNLYGTKGNYTSRVWEYSSSIQNSDNDLPVVQGSSSFSLKGYPSLMRSQSPKAQPQTWKSGKQTMLSHYRPFYVNKGNGIGSNEAP
Protein: Ribosomal proteins L36, putative (Q38C82)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- 60S acidic ribosomal protein P0
- 60S ribosomal protein L39, putative
- 60S ribosomal protein L13a, putative
- 60S ribosomal protein L27, putative
- 60S ribosomal protein L19, putative
- 60S ribosomal protein L17, putative
- 60S ribosomal protein L27a
- 60S ribosomal protein L10, putative
- 60S ribosomal protein L6, putative
- 60S ribosomal protein L29
Sequence:
MAATKKEAPAPRTGIIAGFNKGHKTTRRARRPSSNDRYALPHKKLRAVKAIISDLVGFSPMERRVQELLRVGKDKRALKFCKKRLGSIKAAKKRRAKVEEALRQQTKKK
Protein: Metabolism of cobalamin associated A (A0A3B3ITP4)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MPMLLPHPHQHFLKGLLRAPFRCYHFIFHSSTHLGSGIPCAQPFNSLGLHCTKWMLLSDGLKRKLCVQTTLKDHTEGLSDKEQRFVDKLYTGLIQGQRACLAEAITLVESTHSRKKELAQVLLQKVLLYHREQEQSNKGKPLAFRVGLSGPPGAGKSTFIEYFGKMLTERGHKLSVLAVDPSSCTSGGSLLGDKTRMTELSRDMNAYIRPSPTRGTLGGVTRTTNEAILLCEGAGYDIILIETVAGGDELQGIKRGIIEMADLVAVTKSDGDLIVPARRIQAEYVSALKLLRKRSQVWKPKVIRISARSGEGISEMWDKMKDFQDLMLASGELTAKRRKQQKVWMWNLIQESVLEHFRTHPTVREQIPLLEQKVLIGALSPGLAADFLLKAFKSRD