wanglab/gogpt-training-data huggingface dataset:
Protein: GH02866p (Q9W281)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MDASRYKVDGENDNCGATLAAVNLNVLPDEILEFIFTYLPPYGDLEHCSLVCKRWHAIVKNLVRRSRHNLEKGLIDFRLRWEVFSQQTVNGGAGALLSFIAGRFAHSAVRQDNSMYVFGGGSSSDTTFNDLWRFDLTHMRWARPVATGTYPSPKGSASMVAWRNQLILFGGWRYPSLHPPYQPWCLFDELHYYDLGKNRWLLRSSLSSPPPMAGHSATVHGDRMVVFGGYQIKDDFNVNSNDTWVLDLPEQRWWQPLFVGNTRPSPRYGQIQVELGRNHLLIVGGCGGANRVYTDAWLLDMTRDVWSWKSIAVRNKRFGAVHMWCNPGCKVNNYLVVVGPSPNMPQDFQMMKQSRVPVVGGRGPPPPNPLQNVPPRGYRIPVPDRRLGGGGLGGPGQNRGGNIRPGVGGAAAALGPQEQYLANRRAILNQHMQQAQQFLHNSNVNNNNNNYQPRSGRLSDLHAPPAAAAAASPPSPPVRPNAPPSPADGDVDAAQRLQRNLALRCRDNEPRLPKRFDELYEDPFRMAAFNVPTRSRSASRDHNERIRRMEEKMNAIRNSRRSAPAAAQVEPQPLRAPSPKRLRCNVQSLFVCDISGILDSSEPALEWVEYKNFGVLKGAPDRLILSSLIAGNGELILFGGVHKETLTDITHHVSNSIHFLSVPRDII
Protein: Muscarinic acetylcholine receptor (B3DKN8)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Cell membrane {ECO:0000256|RuleBase:RU361191}; Multi-pass membrane protein {ECO:0000256|RuleBase:RU361191}. Postsynaptic cell membrane {ECO:0000256|RuleBase:RU361191}; Multi-pass membrane protein {ECO:0000256|RuleBase:RU361191}.
Interaction partners:
- Kininogen 1.
- Guanine nucleotide-binding protein subunit alpha
- Guanine nucleotide-binding protein
- Guanine nucleotide-binding protein subunit alpha
- Coiled-coil domain-containing 141.
- Guanine nucleotide-binding protein
- Guanine nucleotide-binding protein subunit alpha
- Guanine nucleotide-binding protein
Sequence:
MDTINFTFWNASDGNETMETADESPYKTVEVVFIVLVAGSLSLVTVIGNILVMLSIKVNRSLQTVNNYFLFSLACADLIIGLCSMNLYTVYIVIGYWPLGPVVCDLWLALDYVVSNASVMNLLIISFDRYFCVTKPLSYPVKRTTKMAGMMIAAAWVLSFILWAPAILFWQFIVGGRTVPEKECYIQFFSNAAVTFGTAIAAFYLPVIIMMVLYWQVSRASKSRVKKDNRKPSGGNLDVASSNQIRENSANKPTNNNLTAEETDRGQTQLTDDTINQHDAKLQNGKAPSTASGEAEEAGQANCIPAEEKESSNDSTSGSGAVTNQKEEAAPPSSAAANDSQTSTRHRAKAGGSKLTCIKIITKSPKGDCYAPSNATVEIVPAVERQNHVARKIVKMTKQPPKKKKAPSSREKKVTRTIMAILVAFVATWTPYNVMVLINTFCSSCIPNTVWTIGYWLCYINSTINPACYALCNITFKKTFKQLLLCQYKNIRSTR
Protein: Angiopoietin-related protein 3 (Angiopoietin-5) (ANG-5) (Angiopoietin-like protein 3) [Cleaved into: ANGPTL3(17-221); ANGPTL3(17-224)] (Q9Y5C1)
Organism: Homo sapiens (Human)
Function: Acts in part as a hepatokine that is involved in regulation of lipid and glucose metabolism. Proposed to play a role in the trafficking of energy substrates to either storage or oxidative tissues in response to food intake (By similarity). Has a stimulatory effect on plasma triglycerides (TG), which is achieved by suppressing plasma TG clearance via inhibition of LPL activity. The inhibition of LPL activity appears to be an indirect mechanism involving recruitment of proprotein convertases PCSK6 and FURIN to LPL leading to cleavage and dissociation of LPL from the cell surface; the function does not require ANGPTL3 proteolytic cleavage but seems to be mediated by the N-terminal domain, and is not inhibited by GPIHBP1. Can inhibit endothelial lipase, causing increased plasma levels of high density lipoprotein (HDL) cholesterol and phospholipids. Can bind to adipocytes to activate lipolysis, releasing free fatty acids and glycerol. Suppresses LPL specifically in oxidative tissues which is required to route very low density lipoprotein (VLDL)-TG to white adipose tissue (WAT) for storage in response to food; the function may involve cooperation with circulating, liver-derived ANGPTL8 and ANGPTL4 expression in WAT (By similarity). Contributes to lower plasma levels of low density lipoprotein (LDL)-cholesterol by a mechanism that is independent of the canonical pathway implicating APOE and LDLR. May stimulate hypothalamic LPL activity (By similarity).
Subcellular location: Secreted {ECO:0000250, ECO:0000305|PubMed:11877390}. Cell projection, lamellipodium {ECO:0000250|UniProtKB:Q9R182}. Note=Colocalized with HSPG2 and activated ITGB3 on podocytes. {ECO:0000250|UniProtKB:Q9R182}.
Interaction partners:
- Angiopoietin-like protein 8
- Lipoprotein lipase
- Angiopoietin-related protein 4
- Glycosylphosphatidylinositol-anchored high density lipoprotein-binding protein 1
- Apolipoprotein A-V
- Angiopoietin-1 receptor
- Apolipoprotein B-100
- Apolipoprotein C-III
- Tyrosine-protein kinase receptor Tie-1
- Endothelial lipase
Sequence:
MFTIKLLLFIVPLVISSRIDQDNSSFDSLSPEPKSRFAMLDDVKILANGLLQLGHGLKDFVHKTKGQINDIFQKLNIFDQSFYDLSLQTSEIKEEEKELRRTTYKLQVKNEEVKNMSLELNSKLESLLEEKILLQQKVKYLEEQLTNLIQNQPETPEHPEVTSLKTFVEKQDNSIKDLLQTVEDQYKQLNQQHSQIKEIENQLRRTSIQEPTEISLSSKPRAPRTTPFLQLNEIRNVKHDGIPAECTTIYNRGEHTSGMYAIRPSNSQVFHVYCDVISGSPWTLIQHRIDGSQNFNETWENYKYGFGRLDGEFWLGLEKIYSIVKQSNYVLRIELEDWKDNKHYIEYSFYLGNHETNYTLHLVAITGNVPNAIPENKDLVFSTWDHKAKGHFNCPEGYSGGWWWHDECGENNLNGKYNKPRAKSKPERRRGLSWKSQNGRLYSIKSTKMLIHPTDSESFE
Protein: Aminomethyltransferase (EC 2.1.2.10) (Glycine cleavage system T protein) (A0A1B0GTV8)
Organism: Homo sapiens (Human)
Subcellular location: Mitochondrion {ECO:0000256|ARBA:ARBA00004173, ECO:0000256|RuleBase:RU003981}.
Interaction partners:
Sequence:
MQRAVSVVARLGFRLQAFPPALCRPLSCAQEVLRRTPLYDFHLAHGGKMVAFAGWSLPVQYRDSHTDSHLHTRQHCSLFDVSHMLQTKILGSDRVKLMESLVVGDIAELRPNQGTLSLFTNEAGGILDDLIVTNTSEGHLYVVSNAGCWEKDLALMQDKVRELQNQGRDVGLEVLDNALLALQGPTAAQVLQAGVADDLRKLPFMTSAVMEVFGVSGCRVTRCGYTGEDGVEISVPVAGAVHLATAILKNPEVKLAGLAARDSLRLEAGLCLYGNDIDEHTTPVEGSLSWTLGTVTSGCPSPSLKKNVAMGYVPCEYSRPGTMLLVEVRRKQQMAVVSKMPFVPTNYYTLK
Protein: Cofilin-1 (Muscle cofilin 2) (Q6TH32)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
- Actin alpha 1, skeletal muscle b.
- LIM domain kinase 1a.
- LIM domain kinase 2
- LIM domain kinase 1
- Actin, cytoplasmic 1
- Slingshot protein phosphatase 1a.
- protein-serine/threonine phosphatase
- Actin, cytoplasmic 2
- Slingshot protein phosphatase 2b.
- Si:ch211-203d1.3.
Sequence:
MASGVTVEETVLTVFNEMKVRKAHCNEEEKSKRKKAVMFCLSDDKKHIIMEQGQEILQGDEGDPYLKFVKMLPPNDCRYALYDATYETKETKKEDLVFIFWAPESAPLKSKMIYASSKDAIKKKFTGIKHEWQVNGMDDIKDRKTLAEKLGGASVVSLEGKPLTD
Protein: Gibberellin 3-beta-dioxygenase 1 (EC 1.14.11.15) (GA 3-oxidase 1) (OsGA3ox1) (Gibberellin 3 beta-hydroxylase 1) (Q6AT12)
Organism: Oryza sativa subsp. japonica (Rice)
Function: Catalyzes the 3-beta-hydroxylation of the inactive gibberellin precursors, leading to the formation of bioactive gibberellins. In vitro, converts the precursors GA20, GA5, GA44 and GA9 to the corresponding 3-beta-hydroxylated bioactive products GA1, GA3, GA38 and GA4, respectively. Involved in the production of bioactive GA for vegetative growth and development. May possess 2,3-desaturase activity, catalyzing the conversion of GA9 to 2,3-dehydro-GA9, and GA20 to GA5 (2,3-dehydro GA20). May possess 2-beta-hydroxylase activity, catalyzing the conversion of GA1 and GA4 to the corresponding 2-beta-hydroxylated products GA8 and GA34, respectively.
Interaction partners:
- Gibberellin 20 oxidase 1
- Gibberellin 20 oxidase 3
- Gibberellin 2-beta-dioxygenase 5
- Gibberellin 2-beta-dioxygenase 1
- Gibberellin 2-beta-dioxygenase 2
- Gibberellin 3-beta-dioxygenase 2
- Gibberellin 2-beta-dioxygenase 3
- Os05g0208550 protein
- Os01g0209700 protein
- Gibberellin 2-beta-dioxygenase 6
Sequence:
MQIMTSSSTSPTSPTSPLAAAADNGVAAAYFNFRGAERVPESHVWKGMHEKDTAPVAAADADGGDAVPVVDMSGGDDAAVAAVARAAEEWGGFLLVGHGVTAEALARVEAQAARLFALPADDKARGARRPGGGNTGYGVPPYLLRYPKQMWAEGYTFPPPAIRDEFRRVWPDAGDDYHRFCSAMEEYDSSMRALGERLLAMFFKALGLAGNDAPGGETERKIRETLTSTIHLNMFPRCPDPDRVVGLAAHTDSGFFTFILQSPVPGLQLLRHRPDRWVTVPGTPGALIVVVGDLFHVLTNGRFHSVFHRAVVNRERDRISMPYFLGPPADMKVTPLVAAGSPESKAVYQAVTWPEYMAVRDKLFGTNISALSMIRVAKEEDKES
Protein: Potassium voltage-gated channel subfamily E regulatory subunit 4 (Q71FD8)
Organism: Rattus norvegicus (Rat)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004167}; Single-pass membrane protein {ECO:0000256|ARBA:ARBA00004167}.
Interaction partners:
- Potassium voltage-gated channel subfamily E member 3
- Potassium voltage-gated channel subfamily E member 2
- Potassium voltage-gated channel subfamily KQT member 1
- Potassium voltage-gated channel subfamily KQT member 4
- Potassium voltage-gated channel subfamily E regulatory subunit 5
- Potassium voltage-gated channel subfamily E member 1
- Potassium voltage-gated channel subfamily Q member 5
- Potassium voltage-gated channel subfamily A member 5
- Voltage-gated inwardly rectifying potassium channel KCNH2
Sequence:
MLRMEPLNSTHPSAAASSSPLESHVSSNSGGNGNEYFYILVVMSFYGIFLIGIMLGYMKSKRREKKSSLLLLYKDEERLWGEAMKPLPMMSGLRSGQVPMMLNMLQESVAPALSCTLCSMEGDSVSSESSSPDVHLTIQEEGADEELEETSETPLNESSEGSTENIHQNS
Protein: Stress response protein nst1 (Q09863)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: May act as a negative regulator of salt tolerance.
Subcellular location: Cytoplasm {ECO:0000250}.
Interaction partners:
- Uncharacterized protein C29E6.09
- Small ribosomal subunit protein uS9B
- Curved DNA-binding protein
- Probable thiamine biosynthetic bifunctional enzyme
- RNA polymerase II-associated protein 1 homolog
- Small ribosomal subunit protein uS9A
- SWR1-complex protein 5
Sequence:
MNDKALRTEALSVGLEPPSFKDLLIPIPNSGTKKKNKKKKKPKAKKNVETQANVDLLGSAGTDSAVTDVGANNGVIDHQASLELSNLNSRISHPQLVSANGDDSSLINVEGISSTDWQFTLESDDTIEHSPQCILSTSSFVDEAEFPVHIPGLEDATSSNMSPNSVQNNMNLNTVALGSSTSSKRKKKKKKKSKANSASLNVDDQRDFEQVYSTDVAITYRNGQALSYYNGSVRQASMNNNVNNNKSKDIWSSSNTEEREQIREFWLSLSESERRSLVKVEKEAVLQKMKEQQKYSCSCSVCGRKRLAIEEELEVLYDAYYEELEQYANIQRNLANTESVNASDEGSDKSQKGIISDSPKLLSIPLNNVPSKSLNDDITQDELNSSNADVDEEVIETTSLEEKNVDNQEFVTSISNGNQTLEDTSHSPQTQPPFQPPYPSKADEKNSYHSDLYNFGSSLTVKGGILTVADDLLKNDGKKFIEMMEQLAERRMQREDNSNFHEPELYESGLEYDEDEEEDEEDVDEDELDLMTDEQRMEEGRRMFQIFAARLFEQRVLQAYREKVAQQRQAKLLEEIEEENKRKQERELKKIREKEKKRDKKKQLKLAKEEERQRREAERLAEQAAQKALEAKRQEEARKKREEQRLKREQEKKQQELERQKREEKQKQKEREKKLKKQQQEADREKMAREQRLREEEEKRILEERKRREKLDKEEEERRRRELLEKESEEKERRLREAKIAAFFAPNQTKEGSDGCTTSSQLGLFEKKGDLVNDEDKLSSHLLDSVPNALRQAPIGLKNTNNLSERNASSNLLNSSLFSSFNSVNPLISLEPNPLNRTLNNSVNLTDFGRKPNGLHSPSSLLSNSNNFGLNPNARHSLSRANSPVHHYPFATPPSQRANKYPLNNGANVPALLNSFSSPQLSPLVNRVLNEPSSSPLSSSSLKSPLSKEGVLNQQGHEQYNFSLSPSIRNKLSPICRPSQGSSPKLKNNLSNTEERMGSRALLDDKTDSVITASNSTTSGLSRDESSNPNNYELLNAFNQNTWKISRSTSNKSLIPESPWGVALGAFTPNASTQSIPWGNRTWTD
Protein: Transcription elongation factor spt6 (Chromatin elongation factor spt6) (Q09915)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Plays a role in maintenance of chromatin structure during RNA polymerase II transcription elongation thereby repressing transcription initiation from cryptic promoters. Mediates the reassembly of nucleosomes onto the promoters of at least a selected set of genes during repression; the nucleosome reassembly is essential for transcriptional repression (By similarity).
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- DNA-directed RNA polymerase II subunit rpb1
- Transcription elongation factor spt4
- Transcription factor iws1
- Transcription elongation factor spt5
- FACT complex subunit spt16
- FACT complex subunit pob3
- DNA-directed RNA polymerase II subunit RPB3
- DNA-directed RNA polymerase II subunit rpb7
- Uncharacterized protein C13E7.08c
- Cell division control protein 73
Sequence:
MSENEVVGSPTTNGDKNEDGYPAENGEGTNVDDNNNEEEKDGIPLDNDNDENDSSEESATDEEAERQVREGFIVEDEEDEVPQEIRRKKKRKKHAESTADQDMLDEEDLELVMENTGQGSRFSKLRRLKRGRDQEETLENIFSEEEEEEENEVDDEAPNRTQGHRAGVIDEFADFIEQDEFEDEERQEEKYETGPPIESVRPEALGISDDDYIQIYEVFGDGTDYAFALEDEDAEDELEESVSLKTIFEPSELKDKMLTEEDEIIRITDEPERMQLYMKRNIDCSEDEFREQVAWIIDYLLKNRRDIDAELYEPFQTAVRYVVHFFIRDSLEVPFIWQHRRDYIVHNNRERNTITPLLSQNDLWNIFFLCTKFWSLHSKKQDILKLYSDLGINDDLVVPFCEAASSLDAIDDLNDYIHFTYSEQIRDRALLMGTGLRRPQGSKYSFFEKFRKSSLYNLVKEFGMSAKDFSFNVAQGARLRFVEDNTLSPEELSRTYVTNELSSPEQVLQKARRVLAEEIIHDPQFRKSFRDKLYNAGVVTVLATQKGVRKIGSEHPYYEFKYLKRKPLGSFELEPILFLKMLKAEEEGLIQLSIEFEDPDDVFKGLLELFVSDNFSENAMQWNAQRELVLKEVFKRFSALAPDAIRETLRSRYLDELGMRCRNQLFSRLDQAPYEPSTKNFDRGTIPSVLAVSNGKGESSDAIICVFVDDVGEPTDSLKLADLRDLANQAMFAEFVEKVKPDVIGVSGMSVSAHKIRQHVQDSLTSHEPVDLIMVNDEVARLYQNSTRAVDEFPTLPTISCYCVALARYVQNPLFEYAAMGRDLMSLSFDPWQHLLPPDVLWKYLETALVDISSLVGIDINEAVTNKYEANILPYIAGLGPRKADYVLKKIAATGGRIDNRSDLISKQIMSRKVFINCSSFFIIPNDEYPNMDILDSTRIHNEDYELARKMASDALELDEEDIEELETNRGVVYHLLEENETGKLDELVLEEYADQLEREFHQKKRNTLEKIRLELKDPYGEQRNVFHKLTPSEIFLMLTGENPEELQADAIVPVNVRRVTNRFVAVKLDCGIDGNIKADEVSDDFIPPPQLLQVGQTVEGVIISLDEANFMVDLSLRNSVLQSANSKRQTSSHRTSYWDTEAEKRDTERMQAETQAEQRVARVIKHPLFKDLNASQAEAYLSKMQVGDLVIRPSSKGSDHIVVTWKVAEGSYQHIDVLELEKENEFTIGQKLLVKGRFEKMTYQYSDLDELIVLHIKAIAKKIDEMCIHDKFRKGTQAETEKWLESYSEANPKRSCYAFCFDHQHPGYFILCFKASVNSPVTAWPVKVIPNAFFLQGNVYGDMTALCNGFKLLYAARTKNFRRM
Protein: DNA damage-binding protein 2 (Damage-specific DNA-binding protein 2) (Q99J79)
Organism: Mus musculus (Mouse)
Function: Protein, which is both involved in DNA repair and protein ubiquitination, as part of the UV-DDB complex and DCX (DDB1-CUL4-X-box) complexes, respectively. Core component of the UV-DDB complex (UV-damaged DNA-binding protein complex), a complex that recognizes UV-induced DNA damage and recruit proteins of the nucleotide excision repair pathway (the NER pathway) to initiate DNA repair. The UV-DDB complex preferentially binds to cyclobutane pyrimidine dimers (CPD), 6-4 photoproducts (6-4 PP), apurinic sites and short mismatches (By similarity). Also functions as the substrate recognition module for the DCX (DDB2-CUL4-X-box) E3 ubiquitin-protein ligase complex DDB2-CUL4-ROC1 (also known as CUL4-DDB-ROC1 and CUL4-DDB-RBX1) (By similarity). The DDB2-CUL4-ROC1 complex may ubiquitinate histone H2A, histone H3 and histone H4 at sites of UV-induced DNA damage (By similarity). The ubiquitination of histones may facilitate their removal from the nucleosome and promote subsequent DNA repair (By similarity). The DDB2-CUL4-ROC1 complex also ubiquitinates XPC, which may enhance DNA-binding by XPC and promote NER (By similarity). The DDB2-CUL4-ROC1 complex also ubiquitinates KAT7/HBO1 in response to DNA damage, leading to its degradation: recognizes KAT7/HBO1 following phosphorylation by ATR (By similarity).
Subcellular location: Nucleus {ECO:0000269|PubMed:17635991}. Chromosome {ECO:0000250|UniProtKB:Q92466}. Note=Accumulates at sites of DNA damage following UV irradiation. {ECO:0000250|UniProtKB:Q92466}.
Interaction partners:
- Cullin-4A
- DNA damage-binding protein 1
- E3 ubiquitin-protein ligase RBX1
- Cellular tumor antigen p53
- Ubiquitin carboxyl-terminal hydrolase 24
- DNA repair protein complementing XP-A cells homolog
- Cullin-4B
- DET1 homolog
- E3 ubiquitin-protein ligase COP1
- DNA excision repair protein ERCC-8
Sequence:
MAPKKCPETQKSPDVAVLLRSKSRRGPQELEPEAKKLRVQGPVSSRTCESCCLLAELSSLQIPSRSSSIVRDLYQHKLGKATWSSLQQGLQKSFLHSLASYQVFRKAAPFDRRTTSLAWHPTHPSTLAVGSKGGDIMIWNFGIKDKPIFLKGIGAGGSITGLKFNHLNTNQFFASSMEGTTRLQDFKGNILRVYTSSNSCKVWFCSLDVSAKSRVVVTGDNMGHVILLSTDGKELWNLRMHKKKVAHVALNPCCDWLLATASIDQTVKIWDLRQIKGKDSFLYSLPHRHPVNAACFSPDGARLLTTDQNNEIRVYSASQWDSPLNLISHPHRHFQHLTPIKATWHSRHNLIVVGRYPDPNLKSCVPYELRTIDVFDGSSGKMMCQLYDPGYSGITSLNEFNPMGDTLASTMGYHILIWSQEEDGSQKDHERL
Protein: Type IV methyl-directed restriction enzyme EcoKMcrB subunit (EcoKMcrBC) (5-methylcytosine-specific restriction enzyme B) (EC 3.1.21.-) (P15005)
Organism: Escherichia coli (strain K12)
Function: Recognizes N4- and C5-methylcytosine (and 5-hydroxy-methylcytosines) produced by a broad range of DNA methylases and appears to act against 5-methylcytosine preceded by a purine residue. Binds to DNA containing methylated cytosines; also binds to GTP. Isoform 33 kDa is less active than isoform 51 kDa and may play a role in regulating the activity of isoform 51 kDa by competing with it in DNA and protein binding abilities.
Interaction partners:
- Type IV methyl-directed restriction enzyme EcoKMcrBC
- Type I restriction enzyme EcoKI specificity subunit
- Type I restriction enzyme EcoKI endonuclease subunit
- Type IV methyl-directed restriction enzyme EcoKMcrA
- Type IV methyl-directed restriction enzyme EcoKMrr
- Gamma-glutamyl phosphate reductase
- Type I restriction enzyme EcoKI methylase subunit
- Small ribosomal subunit protein uS12
- UTP--glucose-1-phosphate uridylyltransferase
- Galactokinase
Sequence:
MESIQPWIEKFIKQAQQQRSQSTKDYPTSYRNLRVKLSFGYGNFTSIPWFAFLGEGQEASNGIYPVILYYKDFDELVLAYGISDTNEPHAQWQFSSDIPKTIAEYFQATSGVYPKKYGQSYYACSQKVSQGIDYTRFASMLDNIINDYKLIFNSGKSVIPPMSKTESYCLEDALNDLFIPETTIETILKRLTIKKNIILQGPPGVGKTFVARRLAYLLTGEKAPQRVNMVQFHQSYSYEDFIQGYRPNGVGFRRKDGIFYNFCQQAKEQPEKKYIFIIDEINRANLSKVFGEVMMLMEHDKRGENWSVPLTYSENDEERFYVPENVYIIGLMNTADRSLAVVDYALRRRFSFIDIEPGFDTPQFRNFLLNKKAEPSFVESLCQKMNELNQEISKEATILGKGFRIGHSYFCCGLEDGTSPDTQWLNEIVMTDIAPLLEEYFFDDPYKQQKWTNKLLGDS
Protein: START (StAR-related lipid-transfer) lipid-binding domain-containing protein (Q84JD1)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- At4g14500
- Polyketide cyclase/dehydrase and lipid transport superfamily protein
- At3g13062
- Pleckstrin homology
- Protein ENHANCED DISEASE RESISTANCE 2-like
- ENHANCED DISEASE RESISTANCE protein
- Polyketide cyclase/dehydrase and lipid transport superfamily protein
- AT3G54800 protein
Sequence:
MYHHLQTRIFLHQQNDLLRAENRARIHAMTSPSICRSCEEPIISTEERELWLENARLRSEIDTLTCFIWRLNSFRNLYPAFATSLTEVGYGVAVMTSLSLKEVVFLARQRTPMWTSNGRLNLDEYYSKLFPWYARNAPGFVHEVSRASAFVPCDASSLVANLMNHVSWQKIFPSIIADVSVESQQRGLQKINVNFMPQISPLIQTRNVKLLRRSRHIEDDTWAIAEISMYFSSYAQHLRPEYMRFPSGYLIQHIANGISKVTILDHWVYKEEEGMNTFNSNSEFGAQRWLTALQKHYYNTCPVSIPSIGHNIQIFDQICRKNLLNLSSFMVNVFCSGVCGITGQRWNRLNTVGVSANNIRMFTQESRGMSGIPCVLVSATGLARMHTKPEVMFGLINGAEKQEIWSYLESAKDMKELIRIGRHPNSWNEVSVFSIEWKGSKEWYLIQETYYDESGAMIIHTCVEAPYFAAAINGGDLSGVELLPSGFTIIPCESQECFVTASCYVKADQTMVTSPNELGSYMENMVTNILGNVQNALPVHR
Protein: High mobility group nucleosome binding domain 5 (Q5JSK6)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MPKRKPKRRSARLSAMLVPVTPEVKPKRTSSSRKMKTKSDMMEENIDTSAQAVAETKQEAVVEEDYNENAKNGEAKITEAPASEKEIVEVKEENIEDATEKGGEKKEAVAAEVKNEEEDQKEDEEDQNEEKGEAGKEDKDEKGEEDGKEDKNGNEKGEDAK
Protein: GTPase-activating protein pac-1 (GTPase-activating protein GAP) (CeGAP) (Protein par-6-at-contacts) (P34288)
Organism: Caenorhabditis elegans
Function: GTPase-activating protein for members of the Rho subfamily including Rac1, RhoA and cdc42 and other Ras-related subfamilies including let-60. Mediates radial (inner-outer) polarity and gastrulation by excluding par-6 from contacted cell surfaces; acts by inactivating cdc42 at inner cell surfaces which limits active cdc42 to outer cell surfaces devoid of cell-cell contacts, where cdc42 can bind and recruit par-6. Required for blastomere polarization.
Subcellular location: Cytoplasm {ECO:0000250}. Cell junction {ECO:0000269|PubMed:18583611, ECO:0000269|PubMed:25938815}. Cell junction, adherens junction {ECO:0000269|PubMed:25938815}. Note=Locates to inner but not outer surfaces of early embryonic somatic (EES) cells (PubMed:18583611). Specifically localizes to cell contacts in hmr-1-dependent and -independent manner in embryos (PubMed:25938815). {ECO:0000269|PubMed:18583611, ECO:0000269|PubMed:25938815}.
Interaction partners:
- PAC-1 interacting and coiled-coil domain-containing protein 1
- Partitioning defective protein 6
- Alpha-catenin-like protein hmp-1
- Juxtamembrane domain-associated catenin
- Cell division control protein 42 homolog
Sequence:
MEEHHRRLHVKAERASVIGGDIVDGAFGSWALRAARSEHQLKQQSNEDLAQNARISALLGEMRPRMSAMPPNGHQQQYQPQLRRKANTTNIVDVSSQVPSARNAIYGSWQDRHRPTRLYGSQLVSSSSTLPKYDQLYCNTASPLTGNGSTNTIATTGIRREPPEYGNVGRSVSTWQVTNSEHRPSLQAGWLKSSRPLARGALSPAAYFRDLENRHGSGASSPIVGGLSVVAVPITQRHAPTAGLAPISDDISTSKVSLDTENQQLNNEDSDKISGSALSRNTPRQASFMAAMQRHPLKESSTSIESNGGGTNTEEDQTVSATSKEDPSEDTGHDDPEETQEISETPIRRSRNRNASLRNRQSSRSLGGLDFEKLRMGTARVGDSNEATAENGTSSSSSRKNSRDDGLTSSPTTVAGPVFTTSSTSSISTSGEASSTAVAAAAAGSVAATTSRQTSSNSSVDSNHNEAMKMIRRARPKSYVLATSASMNEDVLSSSIIANEQSSSISHDTTTSGRELPSSLMGSTISMEMRSGGASSATTTTTSNSGQQTSRSLNAPHPPATHRLQRFIALFNSSKTSDGSGEHKKSRMKRSRTSLPASRFALPGTILQRDGVARQTWVKHQEIALGKSGKRNNWEDRWAVLCRRSLYLCVESPAYTTEKTIELGSHTRVDVCNAIVDIAYDWLSSSFSKQRHVVRIVTQNRSEHLIELNTESEMLSWISVLQSSSEDGIATGSSVDENELSTTGRHNNNAVSNSSALLHNSQSIASLASSSCSTATTSEFLNSQHTLQQQQQQQTNQKHQQTVNELSAGIVSHLPTSKSFGGLSTTASSTTENAKNRLIMHRYIAKNSQLQSPTANKKMETDPSTVPSSSQTMATTSSSFHHHSSQAGPSRDIENGEAPTATATTPKSGRKWKKSKAAKQGSGGGSSGSSSGSQQQGAAGAPQPVLGVRIADCPTGSCEDHVPMIVQACVCVIETYGMDTVGIYRIPGNTAAVNALKESLSNRGFDSVDLSKVESLDPRWRDVNVVSSLLKMFLRKLPEPLLTDKLYPFFIDANRISTHHNRLHKLRNLLRKLPRPHYDTLRFLIVHLSEITKHSDVNKMECRNLALMFGPSIVRPSDDNMATMVTHMSDQCKIIETLIHYNLWMFDESSTTEDAVPEQHPADGQNPLEPGGYGVGVPTGVSAASFNDMHNLIRKANEDQAAAMMNEGKGQKIKNMLRRNSRRDKSKSKLKIESTAPAAVNPRGWTQPTPSNTSAASVESAFCGNYQERDIDAEIESRQTVSPQMTSGSADGASSTRLDQSPSLESSLGSLPDTSRTEPILGSSGYDDDEAKEAARRKRQEEMYSARRIFIAGAAGAAAAATTTADAEKAAIDALANHSQHLHLASSPAFEVLSEETREKIRRMQKKQSWHDTKELRSGELLKTYSPTKDLTDALSCTSDYSTTSSAPLSTNPPLAVACADQPNSSSDYASSDPSPCARNPSTSPASRPSNLAISPAQLHATSSSGQSHQPMSRSQKIRLRTKLGSRDPARRHTLSDVDTLKEGRLDKLARWFGIRKSSPDVSRDEVSDDEKNHQEAPPLPAAAPPVIVRTSPNELTPVSGDELL
Protein: Putative phagocytic receptor 1a (Q55FP0)
Organism: Dictyostelium discoideum (Social amoeba)
Function: Involved in adhesion, phagocytosis of hydrophilic particles and intracellular killing of bacteria. Associates with proteins harboring glycine-rich transmembrane domains and ensures their efficient localization to the cell surface.
Subcellular location: Membrane {ECO:0000255}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Integrin beta-like protein A
- Membrane-associated sulfotransferase kil1
- Integrin beta-like protein C
- Substrate-adhesion molecule
- Large ribosomal subunit protein eL15
Sequence:
MKINKKQIVFFILFSIFLNHVNGIFYLPGMIPHDFAQGEEGAIKVNKITSVHTQIPYKYYQLPGVCQPKEGIIDDTENLGEILLGDRIENSDYTFNFLTDGGKCKVINSESCSPIIKKEDLKVLEDRIQNQYRVHWLLDGLPVRQTGRLASDPGFDLGFMTLAEGQTVATAEKYLNNHLEITIFYHSNPTDNTSRIVGFEIFPTSRQYKKVENWKGDTGDDCPQYGENFEQLSVSVKEGEDQERFVLWTYEVKYTPSPVLWNKRWDIYFESNDNSVHWFSILNSLMIVFILTVMVAMIIIRTLKKDIRRYTSIDTSEDRDSQEETGWKMIHGDVFRPPSHPMLLSVCIGSGVQIFSMTLITMIFAVLGFLSPANIGGLATALIVLFVLSAMFAGYFSTRVFTIFKGRNWKKNTIYTALSMPGIIFGIFFFVNMFLRGAKSSAAVPFGTFASIIAMWFGISVPLVFLGSYFASKKPVPEDPVRTNQIPRQVPDQIWYMNPYLSILMGGILPFGAVFIELHFILTSLWDNQFYYIFGFLFIVLMILIVTSAEISIVMCYFQLCAEDHHWWWRSFLTAGSSSLYMFIYSVSFFRYLGITKFISSLLDFSYSFIMSLAFAALTGTIGFYSCYFLVRKIYSSIHIN
Protein: V-type proton ATPase subunit G (Q8R2H0)
Organism: Rattus norvegicus (Rat)
Subcellular location: Endomembrane system {ECO:0000256|ARBA:ARBA00004308}.
Interaction partners:
- V-type proton ATPase catalytic subunit A
- V-type proton ATPase subunit B, brain isoform
- V-type proton ATPase 21 kDa proteolipid subunit c''
- V-type proton ATPase 116 kDa subunit a 1
- V-type proton ATPase subunit C 1
- V-type proton ATPase subunit E 1
- V-type proton ATPase subunit F
- V-type proton ATPase subunit D
- V-type proton ATPase 16 kDa proteolipid subunit c
- V-type proton ATPase subunit e 2
Sequence:
MASQSQGIQQLLQAEKRAAEKVADARKRKARRLKQAKEEAQMEVEQYRREREQEFQSKQQAAMGSQGNLSAEVEQATRRQVQGMQSSQQRNRERVLTQLLGMVCDVRPQVHPNYRITV
Protein: SNARE protein, putative (Q8IET3)
Organism: Plasmodium falciparum (isolate 3D7)
Subcellular location: Endomembrane system {ECO:0000256|ARBA:ARBA00046280}; Single-pass type IV membrane protein {ECO:0000256|ARBA:ARBA00046280}.
Interaction partners:
- SNARE protein, putative
- Syntaxin, Qa-SNARE family
- Vacuolar protein sorting-associated protein 33, putative
- Syntaxin, Qa-SNARE family
- Syntaxin, Qa-SNARE family
- Vacuolar protein sorting-associated protein 16, putative
- Syntaxin, Qa-SNARE family
- SNARE protein, putative
Sequence:
MSIIYGLIAREKTVLAEYTEYGGNFSNISRLLLEIIPPHTSRKSYIYDDYVFHQLIKNGITFMAMTDKELGFLTPYAFLEQISKIFFKNFNNTSDLITLSLDEEFKPVLKENMRVFNEYETNDVHNIKNQISNIQNIIIENIEKILERREKIDILVNKTEKLYQENINFRRQAMNFNFHMWLENNRMTLYFISSIIIFIFFIWSLYNV