wanglab/gogpt-training-data huggingface dataset:
Protein: PTS system beta-glucoside-specific EIIBCA component (EIIBCA-Bgl) (EII-Bgl) [Includes: Beta-glucoside-specific phosphotransferase enzyme IIB component (EC 2.7.1.-) (PTS system beta-glucoside-specific EIIB component); Beta-glucoside permease IIC component (PTS system beta-glucoside-specific EIIC component); Beta-glucoside-specific phosphotransferase enzyme IIA component (PTS system beta-glucoside-specific EIIA component)] (P08722)
Organism: Escherichia coli (strain K12)
Function: The phosphoenolpyruvate-dependent sugar phosphotransferase system (sugar PTS), a major carbohydrate active -transport system, catalyzes the phosphorylation of incoming sugar substrates concomitantly with their translocation across the cell membrane. This system is involved in beta-glucoside transport.
Subcellular location: Cell inner membrane; Multi-pass membrane protein.
Interaction partners:
- Cryptic beta-glucoside bgl operon antiterminator
- 6-phospho-beta-glucosidase BglB
- PTS system glucose-specific EIICB component
- Phosphocarrier protein HPr
- 6-phospho-beta-glucosidase BglA
- 6-phospho-beta-glucosidase AscB
- Multiphosphoryl transfer protein 2
- Multiphosphoryl transfer protein 1
- PTS system fructose-specific EIIB'BC component
- PTS system 2-O-alpha-mannosyl-D-glycerate-specific EIIABC component
Sequence:
MTELARKIVAGVGGADNIVSLMHCATRLRFKLKDESKAQAEVLKKTPGIIMVVESGGQFQVVIGNHVADVFLAVNSVAGLDEKAQQAPENDDKGNLLNRFVYVISGIFTPLIGLMAATGILKGMLALALTFQWTTEQSGTYLILFSASDALFWFFPIILGYTAGKRFGGNPFTAMVIGGALVHPLILTAFENGQKADALGLDFLGIPVTLLNYSSSVIPIIFSAWLCSILERRLNAWLPSAIKNFFTPLLCLMVITPVTFLLVGPLSTWISELIAAGYLWLYQAVPAFAGAVMGGFWQIFVMFGLHWGLVPLCINNFTVLGYDTMIPLLMPAIMAQVGAALGVFLCERDAQKKVVAGSAALTSLFGITEPAVYGVNLPRKYPFVIACISGALGATIIGYAQTKVYSFGLPSIFTFMQTIPSTGIDFTVWASVIGGVIAIGCAFVGTVMLHFITAKRQPAQGAPQEKTPEVITPPEQGGICSPMTGEIVPLIHVADTTFASGLLGKGIAILPSVGEVRSPVAGRIASLFATLHAIGIESDDGVEILIHVGIDTVKLDGKFFSAHVNVGDKVNTGDRLISFDIPAIREAGFDLTTPVLISNSDDFTDVLPHGTAQISAGEPLLSIIR
Protein: Calpain 7 (Q7Z479)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MDATALERDAVQFARLAVQRDHEGRYSEAVFYYKEAAQALIYAEMAGSSLENIQEKITEYLERVQALHSAVQSKSADPLKSKHQLDLERAHFLVTQAFDEDEKENVEDAIELYTEAVDLCLKTSYETADKVLQNKLKQLARQALDRAEALGEPLTKPVGKISSTSVKPKPPPERAHFPLGANPFLERPQSFISPQSCDAQGQRYTAEEIEVLRTTSKINGIEYVPFMNVDLRERFAYPMPFCDRWGKLPLSPKQKTTFSKWVRPEDLTNNPTMIYTVSSFSIKQTIVSDCSFVASLAISAAYERRFNKKLITGIIYPQNKDGEPEYNPCGKYMVKLHLNGVPRKVIIDDQLPVDHKGELLCSYSNNKSELWVSLIEKAYMKVMGGYDFPGSNSNIDLHALTGWIPERIAMHSDSQTFSKDNSFRMLYQRFHKGDVLITASTGMMTEAEGEKWGLVPTHAYAVLDIREFKGLRFIQLKNPWSHLRWKGRYSENDVENWTPELQKYLNFDPRTAQKIDNGIFWISWDDLCQYYDVIYLSWNPGLFKESTCIHSTWDAKQGPVKDAYSLANNPQYKLEVQCPQGGAAVWVLLSRHITDKDDFANNREFITMVVYKTDGKKVYYPADPPPYIDGIRINSPHYLTKIKLTTPGTHTFTLVVSQYEKQNTIHYTVRVYSACSFTFSKIPSPYTLSKRINGKWSGQSAGGCGNFQETHKNNPIYQFHIEKTGPLLIELRGPRQYSVGFEVVTVSTLGDPGPHGFLRKSSGDYRCGFCYLELENIPSGIFNIIPSTFLPKQEGPFFLDFNSIIPIKITQLQ
Protein: Elongation factor 1-delta (EF-1-delta) (Antigen NY-CO-4) (P29692)
Organism: Homo sapiens (Human)
Function: EF-1-beta and EF-1-delta stimulate the exchange of GDP bound to EF-1-alpha to GTP, regenerating EF-1-alpha for another round of transfer of aminoacyl-tRNAs to the ribosome.
Subcellular location: [Isoform 2]: Nucleus {ECO:0000269|PubMed:21597468}.
Interaction partners:
- Elongation factor 1-gamma
- Elongation factor 1-beta
- Elongation factor 1-alpha 1
- Valine--tRNA ligase
- Kinectin
- Elongation factor 1-alpha 2
- Small ribosomal subunit protein eS19
- Small ribosomal subunit protein uS17
- Translationally-controlled tumor protein
- Large ribosomal subunit protein uL14
Sequence:
MATNFLAHEKIWFDKFKYDDAERRFYEQMNGPVAGASRQENGASVILRDIARARENIQKSLAGSSGPGASSGTSGDHGELVVRIASLEVENQSLRGVVQELQQAISKLEARLNVLEKSSPGHRATAPQTQHVSPMRQVEPPAKKPATPAEDDEDDDIDLFGSDNEEEDKEAAQLREERLRQYAEKKAKKPALVAKSSILLDVKPWDDETDMAQLEACVRSIQLDGLVWGASKLVPVGYGIRKLQIQCVVEDDKVGTDLLEEEITKFEEHVQSVDIAAFNKI
Protein: Zinc finger protein FZF1 (Sulfite resistance protein 1) (P32805)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: May function as a transcription factor.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- Sulfite efflux pump SSU1
- Uroporphyrinogen-III C-methyltransferase
- L-aminoadipate-semialdehyde dehydrogenase-phosphopantetheinyl transferase
- Flavohemoprotein
- Transcription factor tau 131 kDa subunit
Sequence:
MTDIGRTKSRNYKCSFDGCEKVYNRPSLLQQHQNSHTNQKPYHCDEPGCGKKFIRPCHLRVHKWTHSQIKPKACTLCQKRFVTNQQLRRHLNSHERKSKLASRIDRKHEGVNANVKAELNGKEGGFDPKLPSGSPMCGEEFSQGHLPGYDDMQVLQCPYKSCQKVTSFNDDLINHMLQHHIASKLVVPSGDPSLKESLPTSEKSSSTDTTSIPQLSFSTTGTSSSESVDSTTAQTPTDPESYWSDNRCKHSDCQELSPFASVFDLIDHYDHTHAFIPETLVKYSYIHLYKPSVWDLFEY
Protein: Ras-related protein Rap-1A (EC 3.6.5.2) (Ras-related protein Krev-1) (P62836)
Organism: Rattus norvegicus (Rat)
Function: Induces morphological reversion of a cell line transformed by a Ras oncogene. Counteracts the mitogenic function of Ras, at least partly because it can interact with Ras GAPs and RAF in a competitive manner. Together with ITGB1BP1, regulates KRIT1 localization to microtubules and membranes (By similarity). Plays a role in nerve growth factor (NGF)-induced neurite outgrowth. Plays a role in the regulation of embryonic blood vessel formation. Involved in the establishment of basal endothelial barrier function. May be involved in the regulation of the vascular endothelial growth factor receptor KDR expression at endothelial cell-cell junctions.
Subcellular location: Cell membrane {ECO:0000250}; Lipid-anchor {ECO:0000250}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:17724123}. Early endosome {ECO:0000269|PubMed:17724123}. Late endosome {ECO:0000269|PubMed:17724123}. Cytoplasm {ECO:0000250}. Cell junction {ECO:0000250}. Note=Localized with RAPGEF2 at cell-cell junctions. Colocalized with RAPGEF2 in the perinuclear region (By similarity). Recruited from early endosome to late endosome compartment after nerve growth factor (NGF) stimulation. {ECO:0000250}.
Interaction partners:
- Krev interaction trapped protein 1
- RAS guanyl-releasing protein 2
- Amyloid beta A4 precursor protein-binding family B member 1-interacting protein
- Ral guanine nucleotide dissociation stimulator
- RAF proto-oncogene serine/threonine-protein kinase
- Rap guanine nucleotide exchange factor 2
- Serine/threonine-protein kinase A-Raf
- Rap guanine nucleotide exchange factor 4
- Rap1 GTPase-activating protein
- Rap guanine nucleotide exchange factor 3
Sequence:
MREYKLVVLGSGGVGKSALTVQFVQGIFVEKYDPTIEDSYRKQVEVDCQQCMLEILDTAGTEQFTAMRDLYMKNGQGFALVYSITAQSTFNDLQDLREQILRVKDTEDVPMILVGNKCDLEDERVVGKEQGQNLARQWCNCAFLESSAKSKINVNEIFYDLVRQINRKTPVEKKKPKKKSCLLL
Protein: Dual specificity protein phosphatase 13B (EC 3.1.3.16) (EC 3.1.3.48) (Dual specificity phosphatase SKRP4) (Testis- and skeletal-muscle-specific DSP) (Q9UII6)
Organism: Homo sapiens (Human)
Function: Dual specificity phosphatase that dephosphorylates MAPK8/JNK and MAPK14/p38, but not MAPK1/ERK2, in vitro. Exhibits intrinsic phosphatase activity towards both phospho-seryl/threonyl and -tyrosyl residues, with similar specific activities in vitro.
Interaction partners:
Sequence:
MDSLQKQDLRRPKIHGAVQASPYQPPTLASLQRLLWVRQAATLNHIDEVWPSLFLGDAYAARDKSKLIQLGITHVVNAAAGKFQVDTGAKFYRGMSLEYYGIEADDNPFFDLSVYFLPVARYIRAALSVPQGRVLVHCAMGVSRSATLVLAFLMICENMTLVEAIQTVQAHRNICPNSGFLRQLQVLDNRLGRETGRF
Protein: Serine/threonine-protein kinase SRK2I (EC 2.7.11.1) (OST1-kinase-like 2) (Protein ATHPROKIN B) (SNF1-related kinase 2.3) (SnRK2.3) (Q39193)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Together with SRK2D, key component and activator of the abscisic acid (ABA) signaling pathway that regulates numerous ABA responses, such as seed germination, Pro accumulation, root growth inhibition, dormancy and seedling growth, and, to a lesser extent, stomatal closure. In response to ABA, phosphorylates the ESCRT-I complex component FREE1, which is required for ABA-induced FREE1 nuclear import.
Interaction partners:
- Protein phosphatase 2C 56
- Protein phosphatase 2C 77
- Protein phosphatase 2C 16
- Protein phosphatase 2C 37
- Probable protein phosphatase 2C 75
- ABSCISIC ACID-INSENSITIVE 5-like protein 4
- Protein ABSCISIC ACID-INSENSITIVE 5
- Protein phosphatase 2C 7
- Probable protein phosphatase 2C 24
- Probable protein phosphatase 2C 78
Sequence:
MDRAPVTTGPLDMPIMHDSDRYDFVKDIGSGNFGVARLMRDKLTKELVAVKYIERGDKIDENVQREIINHRSLRHPNIVRFKEVILTPTHLAIIMEYASGGELYERICNAGRFSEDEARFFFQQLLSGVSYCHSMQICHRDLKLENTLLDGSPAPRLKICDFGYSKSSVLHSQPKSTVGTPAYIAPEVLLRQEYDGKIADVWSCGVTLYVMLVGAYPFEDPEEPRDYRKTIQRILSVKYSIPDDIRISPECCHLISRIFVADPATRISIPEIKTHSWFLKNLPADLMNESNTGSQFQEPEQPMQSLDTIMQIISEATIPAVRNRCLDDFMTDNLDLDDDMDDFDSESEIDIDSSGEIVYAL
Protein: Leucine-rich repeat LGI family member 3 (LGI1-like protein 4) (Leucine-rich glioma-inactivated protein 3) (Q8N145)
Organism: Homo sapiens (Human)
Function: May participate in the regulation of neuronal exocytosis.
Subcellular location: Secreted {ECO:0000269|PubMed:35948005}. Cytoplasmic vesicle, secretory vesicle, synaptic vesicle {ECO:0000250|UniProtKB:Q8K406}. Synapse, synaptosome {ECO:0000250|UniProtKB:Q8K406}. Cell projection, axon {ECO:0000250|UniProtKB:Q8K406}. Note=Found in the synaptosomal membrane fraction. Within peripheral myelinated axons, LGI3 is highly expressed at the juxtaparanodal membrane and colocalizes with the voltage-gated potassium channels Kv1.1 (KCNA1) and Kv1.2 (KCNA2), and with CNTNAP2, DLG4, ADAM22 and ADAM23 (By similarity). {ECO:0000250|UniProtKB:Q8K406}.
Interaction partners:
- Disintegrin and metalloproteinase domain-containing protein 23
- Disintegrin and metalloproteinase domain-containing protein 22
Sequence:
MAGLRARGGPGPGLLALSALGFCLMLQVSAKRPPKTPPCPPSCSCTRDTAFCVDSKAVPRNLPSEVISLTLVNAAFSEIQDGAFSHLPLLQFLLLNSNKFTLIGDNAFTGLSHLQYLFIENNDIWALSKFTFRGLKSLTHLSLANNNLQTLPRDIFRPLDILNDLDLRGNSLNCDCKVKWLVEWLAHTNTTVAPIYCASPPRFQEHKVQDLPLREFDCITTDFVLYQTLAFPAVSAEPFLYSSDLYLALAQPGVSACTILKWDYVERQLRDYDRIPAPSAVHCKPMVVDSQLYVVVAQLFGGSYIYHWDPNTTRFTRLQDIDPQRVRKPNDLEAFRIDGDWYFAVADSSKAGATSLYRWHQNGFYSHQALHPWHRDTDLEFVDGEGKPRLIVSSSSQAPVIYQWSRTQKQFVAQGEVTQVPDAQAVKHFRAGRDSYLCLSRYIGDSKILRWEGTRFSEVQALPSRGSLALQPFLVGGRRYLALGSDFSFTQIYQWDEGRQKFVRFQELAVQAPRAFCYMPAGDAQLLLAPSFKGQTLVYRHIVVDLSA
Protein: Follistatin-A (FS) (Activin-binding protein) (Follistatin-1) (zFst1) (Q9YHV4)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: Binds directly to activin and functions as an activin antagonist. Specific inhibitor of the biosynthesis and secretion of pituitary follicle stimulating hormone (fsh) (By similarity). Inhibits bmp-signaling during later stages of development including late phases of dorsoventral patterning, to refine the early pattern set up by the interaction of chordino and bmp2/4. Not involved in organizer function or early phases of dorsoventral pattern formation.
Interaction partners:
- Activin beta A subunit
- Inhibin beta B chain
- Inhibin subunit beta Ab.
- Growth/differentiation factor 8
- Chordin
- Inhibin beta B chain
- Inhibin subunit beta C.
- Growth/differentiation factor 8
- Bone morphogenetic protein 4.
- Follistatin 2
Sequence:
MLRMLKRQQLHPGMILLLFWLCYLIEDQKVQAGNCWLQQGKNGRCQVLYMPGMSREECCRSGRLGTSWTEEDVPNSTLFRWMIFNGGAPNCIPCKETCDNVDCGPGKRCKMNRRSKPRCVCAPDCSNVTWKGPVCGSDGKTYRDECALLKSKCKGHPDLEVQYQGKCKKTCRDVLCPGSSTCVVDQTNNAYCVTCNRICPEVMSPDQYLCGNDGIVYASACHLRRATCLLGRSIGVAYEGKCIKAKSCDDIHCSAGKKCLWDAKMSRGRCAVCAESCPESRSEEAVCASDNTTYPSECAMKQAACSLGVLLEVKHSGSCNCK
Protein: Synembryn (C8VNL0)
Organism: Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Interaction partners:
Sequence:
MDLRILQGSEKLQQVTKLLNSLEKDLKDNSLNSAQRTQILLQLRQYGTSPDNAGPIYSKKGIEILSKYGIDGETTDVRHAALRCVANALLLDSNMRQLFVDTGKGGRLAEMLKCDSSEHEMVISRILFLSTYDTNLNFDDLINNHSLGDNINYQILRHSKQFPKSGRKPLSQVDELAFTDTLKLVFNIAKLFQDLAPTFSPSIPYIFKIISRIDIPLKPLDGLLGTLLNCLSTLDLENKNKKPYDGNPIFPTFNQNCNVDKLINILDQAVSAYEPSELETKAIPLFHTLVTIHEVAPDGPRKYMQWLLLPDDNDRDRPIGQSDTLSSKLLKLSTMHYANLKVAISELMFVLSGKNAESLTKNIGYGFAAGLLASRGMDIPKSAGEAFATNSQDLNPEINPITGQRWAAEKEDTGPPMTKEEKEREAERLFVLFERAKANGILGVENPVTQALREGRLEELPDSDSE
Protein: Arabinan endo-1,5-alpha-L-arabinosidase B (EC 3.2.1.99) (Endo-1,5-alpha-L-arabinanase B) (ABN B) (Q5AZC8)
Organism: Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Function: Endo-1,5-alpha-L-arabinanase involved in degradation of pectin. Its preferred substrate is linear 1,5-alpha-L-arabinan.
Subcellular location: Secreted {ECO:0000250}.
Interaction partners:
- Transaldolase
Sequence:
MAVIFVLFFLVSMALSARIRPSFNGTALSGTSNKHPFEPGPNTIFREEVPPSAAASGFPSAHGTELRTHDPSIIKVGSIYYSYSVGPSITIHQAFSLDGPWTEVGALLSGESVIKKGDRKAPWAANTIYINGRYYCYYSVSNSGCRDSAIGVASSAFPGPGEWTDHGLIIQSGTGEGSDVFPLNQSNTIDPNVFVDGDGTAYLNFGSFWTGLWQVPLEEELVTVKGLQDGTLDAVHLAAEPGKVWRSKLANSKAKTVSTSKTGSPICGDPTGGHPIEGGFMAYHAPYYYMWFSWGRCCEFKDPAMRSNGKEYRIRVGRSTSARGPFVDKQGIDLVDGGGETVYGSNGDVFAPGGQGILTDEFGDILYYHYLNSSVSYDFADARLGYNRLEYVDGWPVAVY
Protein: Putative clathrin assembly protein At2g25430 (Q8LF20)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Membrane, clathrin-coated pit {ECO:0000250}. Golgi apparatus {ECO:0000250}. Cytoplasmic vesicle, clathrin-coated vesicle {ECO:0000250}. Note=Colocalized with clathrin in the Golgi area. {ECO:0000250}.
Interaction partners:
- Plastocyanin-like domain-containing protein
- Clathrin interactor EPSIN 2
- Clathrin interactor EPSIN 1
- Clathrin interactor EPSIN 3
- Protein transport protein SEC23
- Putative clathrin assembly protein At5g65370
- ENTH/VHS family protein
- Calcium-transporting ATPase 2, endoplasmic reticulum-type
- Protein CER1-like 2
- DNA repair DEAD helicase RAD3/XP-D subfamily protein
Sequence:
MAPSIRKAIGAVKDQTSIGIAKVASNMAPDLEVAIVKATSHDDDPASEKYIREILNLTSLSRGYILACVTSVSRRLSKTRDWVVALKALMLVHRLLNEGDPIFQEEILYSTRRGTRMLNMSDFRDEAHSSSWDHSAFVRTYAGYLDQRLELALFERKSGVSVNSGGNSSHHSNNDDRYGRGRDDFRSPPPRSYDYENGGGGGSDFRGDNNGYGGVPKRSRSYGDMTEMGGGGGGGGRDEKKVVTPLREMTPERIFGKMGHLQRLLDRFLSLRPTGLAKNSRMILIALYPVVRESFKLYADICEVLAVLLDKFFDMEYSDCVKAFDAYASAAKQIDELIAFYNWCKETGVARSSEYPEVQRITSKLLETLEEFVRDRAKRGKSPERKEIEAPPPVVEEEEPEPDMNEIKALPPPENYTPPPPPEPEPQPEKPQFTEDLVNLREDEVTADDQGNKFALALFAGPPGNNGKWEAFSSNGVTSAWQNPAAEPGKADWELALVETTSNLEKQTAALGGGFDNLLLNGMYDQGMVRQHVSTSQLTGGSASSVALPLPGKTNNQVLALPAPDGTVEKVNQDPFAASLTIPPPSYVQMAEMEKKQYLLSQEQQLWQQYQRDGMRGQASLAKMNTGPVPAYGMPPVNGMGPPPTGYYYNNPY
Protein: Regulator of G-protein signaling 16 (RGS16) (Retinal-specific RGS) (RGS-r) (Retinally abundant regulator of G-protein signaling) (P56700)
Organism: Rattus norvegicus (Rat)
Function: Regulates G protein-coupled receptor signaling cascades. Inhibits signal transduction by increasing the GTPase activity of G protein alpha subunits, thereby driving them into their inactive GDP-bound form. Plays an important role in the phototransduction cascade by regulating the lifetime and effective concentration of activated transducin alpha. May regulate extra and intracellular mitogenic signals.
Subcellular location: Membrane {ECO:0000250|UniProtKB:P97428}; Lipid-anchor {ECO:0000250|UniProtKB:P97428}.
Interaction partners:
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein subunit beta-5
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein subunit alpha-13
- G protein subunit alpha transducin 1
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein subunit alpha-12
Sequence:
MCRTIATFPNTCLERAKEFKTRLGIFLHKSELSSDTGGNGKFEWASKLSKERSFSEDVLGWRESFQSLLNSKNGVAAFHAFLKTEFSEENLEFWLACEEFKKIRSATKLASRAHHIFDEYIRSEAPKEVNIDHETRELTKTNLQAATTSCFDVAQGKTRTLMEKDSYPRFLKSPAYRDLAAQASATSASGSSPAEPSHT
Protein: Small nuclear ribonucleoprotein polypeptide A (M0QZG7)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MRGQAFVIFKEVSSATNALRSMQGFPFYDKPMRIQYAKTDSDIIAKMKGTFVERDRKREKRKPKSQETPATKKAVQGGGATPVVGAVQGPVPGMPPMTQAPRIMHHMPGQPPYMPPPGMIPPPGLAPGQIPPGAMPPQQLMPGQMPPAQPLSENPPNHILFLTNLPEETNELMLSMLFNQFPGF
Protein: Bruno 1, isoform F (Q8IP89)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MFTSRASFLANRRMIFDFSEKNNDIYLDAFGMSDKSSSATNSLPNSPIHSNNNNPSLLNNNNNNSNGTSSNNSLNVGNNNSNPSLGGSNSNALVSVGSNGIMSAAGLVNNNNNPCSANRNVVAMVDDDACFRLDTDATVTYGEKEPDPDNIKMFVGQVPKSMDESQLREMFEEYGAVHSINVLRDKATGISKGCCFVTFYTRHAALKAQDALHNVKTLNGMYHPIQMKPADSENRNERKLFVGMLNKKLNENDVRKLFEVHGAIEECTVLRDQNGQSKGCAFVTFATKHAAISAIKVTLSQNKIMEGCTSPLVVKFADTQKEKEQKKIQQIQANLWNLASNINIPLGQTATSVTTPILPNPPQQPSPVLGADAITPASIQLLQQLQAVGLQHQLLQALTGLGAQQSSSATDTSAVAAAGLLTPMTVQNLAAIAAMTQPSLSNAAAAAAAATSPGSAQLTNTAALLCLLGKKAAAKKSAKKTGSDPNPMASAYMSTAAGLPQFGSASALSTSPLASVALSAAAAAAAGKQIEGPEGCNLFIYHLPQEFTDTDLASTFLPFGNVISAKVFIDKQTSLSKCFGFVSFDNPDSAQVAIKAMNGFQVGTKRLKVQLKKPKDSKPY
Protein: FMRFamide-like neuropeptides 9 [Cleaved into: KPSFVRF-amide 1; KPSFVRF-amide 2] (Q18502)
Organism: Caenorhabditis elegans
Function: FMRFamides and FMRFamide-like peptides are neuropeptides.
Subcellular location: Secreted {ECO:0000305}.
Interaction partners:
- FMRFamide-like neuropeptides 11
- FMRFamide-like neuropeptides 7
- FMRFamide-like neuropeptides 1
- FMRF-Like Peptide
- FMRFamide-like neuropeptides 5
- FMRFamide-like neuropeptide 18
- FMRFamide-like neuropeptides 6
- FMRFamide-like neuropeptides 16
- FMRFamide-like neuropeptides 24
- FMRFamide-like neuropeptides 13
Sequence:
MNQFYALFLVACIAAMANAYEEPDLDALAEFCGKESNRKYCDQIAQLATQHAIGINQEQVRMEKRKPSFVRFGKRSGYPLVIDDEEMRMDKRKPSFVRFGRK
Protein: Adenylate cyclase (EC 4.6.1.1) (ATP pyrophosphate-lyase) (Adenylyl cyclase) (P9WQ35)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Subcellular location: Cell membrane {ECO:0000269|PubMed:11431477, ECO:0000269|PubMed:11447108}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
- cAMP/cGMP dual specificity phosphodiesterase Rv0805
- Bifunctional
- Pyruvate kinase
- Nucleoside diphosphate kinase
- Probable conserved membrane protein
- Riboflavin biosynthesis protein RibBA
- GTP 3',8-cyclase 2
- GTP 3',8-cyclase 1
- 3,4-dihydroxy-2-butanone-4-phosphate synthase
- GTP cyclohydrolase 1
Sequence:
MAARKCGAPPIAADGSTRRPDCVTAVRTQARAPTQHYAESVARRQRVLTITAWLAVVVTGSFALMQLATGAGGWYIALINVFTAVTFAIVPLLHRFGGLVAPLTFIGTAYVAIFAIGWDVGTDAGAQFFFLVAAALVVLLVGIEHTALAVGLAAVAAGLVIALEFLVPPDTGLQPPWAMSVSFVLTTVSACGVAVATVWFALRDTARAEAVMEAEHDRSEALLANMLPASIAERLKEPERNIIADKYDEASVLFADIVGFTERASSTAPADLVRFLDRLYSAFDELVDQHGLEKIKVSGDSYMVVSGVPRPRPDHTQALADFALDMTNVAAQLKDPRGNPVPLRVGLATGPVVAGVVGSRRFFYDVWGDAVNVASRMESTDSVGQIQVPDEVYERLKDDFVLRERGHINVKGKGVMRTWYLIGRKVAADPGEVRGAEPRTAGV
Protein: non-specific serine/threonine protein kinase (EC 2.7.11.1) (Q7KMI3)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Nucleosomal histone kinase 1
- Ankyrin repeat and LEM domain-containing protein 2 homolog
- Barrier-to-autointegration factor
- Dual specificity protein phosphatase
Sequence:
MGKRLQLERPTTDRSARKRKRSAVKAAEKRQRLSGGSSSANGFEFHENDDEESCSSAGSAAGTEADPPTLLHTPQARSLLLTGASIASDHNNSSVMESPRPVYTLRPSVVNGTILRDVLSKAWRLGRPIGKGNFGEIFLASDDTVCPASSETAKYVVKIEPHSNGPLFVEIHCLINTSRNNDLSDAAEDAASLPAPQTHVLSRGPPSGIPSFIASGTHYFGDVRYRFLVLPRFDRDLHSLIKNSRVQQKSLLVLAVHIINVLENLHDKGYCHNDIKAQNLMVSKCKYLRRQVVPKGNGYEDHYEEKQQTTDSGNSSEQETNDDDYFLKSEKFALKKIVDIKQDEDEDDEDFDDGATSNSNNSNSLDVFHTPVNKKRSARNAIQFSGSNPVRACRREKRNSMYEEMVKSHYLRPTKRISYREEFNEDGYPKETAENSDESPESSDNESDEFIPPSSRRSVIKRGRSAQIATPKKTPVSTRASRQEKVKKEPNGDQKLRSRGSKHLDNNPTEYKFLPTEEEHVFLIDFGLASKFQDRGVHRPFIMDQRRAHDGTLEFTSRDAHLGAHSRRSDLECLGYNLLYWSEGYLPWKDVAQQQQQEKVHRAKELFMTDVPEMLRQFYGKQVPKYLGEFLLQIGQLAYQERPNYERYRKIFKREYQRLGYDPCQMRLSSEEILRTCVSTKDVVDGSKCDIFELNNKAAVNVMRNSTLSTPFQEHSLTNRVSPKNLRSKSNKKTTKKKFSWAEVLSQDPDQIARERAVKEFEREETICPLESRLPRRYEGKPTYAILDMEQRRREKGLVVQEHIEEEEEDADEDDEEENQEAMDIDQEEDGEAADSAEGEDESDRSMEGSDCSDHSQKRARGRPKGTSRKQTTSRQAQPHQNQPPVKVHRGVGRPGKNSGVVKLAAGAVSKNRTTPLSAVASNKRGCATRKENSTLASATGEGERKLKSGRTRRALYKTEPKHGEHDAENNSSLLVVQNLYGEYDDENNYGKGRSVHSSRHCRK
Protein: Acyl-CoA-binding domain-containing protein 3 (Acyl-CoA binding protein 3) (Q9STX1)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Binds medium- and long-chain acyl-CoA esters with very high affinity. Can interact in vitro with arachidonyl-CoA, barely with oleoyl-CoA, but not with palmitoyl-CoA.
Subcellular location: Secreted, extracellular space {ECO:0000269|PubMed:16231156}.
Interaction partners:
- Acyl-CoA-binding domain-containing protein 4
- Acyl-CoA-binding domain-containing protein 5
- Acyl-CoA-binding domain-containing protein 6
- Ankyrin repeat-containing protein BDA1
- AT3G13950 protein
- Ankyrin
- Uncharacterized CRM domain-containing protein At3g25440
Sequence:
MEVFLEMLLTAVVALLFSFLLAKLVSVATVENDLSSDQPLKPEIGVGVTEDVRFGMKMDARVLESQRNFQVVDENVELVDRFLSEEADRVYEVDEAVTGNAKICGDREAESSAAASSENYVIAEEVILVRGQDEQSDSAEAESISSVSPENVVAEEIKSQGQEEVTELGRSGCVENEESGGDVLVAESEEVRVEKSSNMVEESDAEAENEEKTELTIEEDDDWEGIERSELEKAFAAAVNLLEESGKAEEIGAEAKMELFGLHKIATEGSCREAQPMAVMISARAKWNAWQKLGNMSQEEAMEQYLALVSKEIPGLTKAGHTVGKMSEMETSVGLPPNSGSLEDPTNLVTTGVDESSKNGIP
Protein: GEO10158p1 (IP02458p) (Mitochondrial ribosomal protein S14, isoform A) (Mitochondrial ribosomal protein S14, isoform B) (Q9VWI3)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Small ribosomal subunit protein uS15m
- Small ribosomal subunit protein uS12m
- Small ribosomal subunit protein uS2m
- Small ribosomal subunit protein uS9m
- Small ribosomal subunit protein bS16m
- Small ribosomal subunit protein uS7m
- Small ribosomal subunit protein uS5m
- Mitochondrial ribosomal protein S11
- Small ribosomal subunit protein bS6m
- Small ribosomal subunit protein uS10m
Sequence:
MNSLARIGGFVCQSVQIAGCGLQQVRTKYADWKMIRDVKRRKCVKENAVERLRVNSLRKNDILPPELREVADAEIAAFPRDSSLVRVRERCALTSRPRGVVHKYRLSRIVWRHLADYNKLSGVQRAMW
Protein: Fc receptor-like protein 5 (FcR-like protein 5) (FcRL5) (BXMAS1-like protein 2) (mBXMH2) (Fc receptor homolog 3) (FcRH3) (moFcRH3) (CD antigen CD307e) (Q68SN8)
Organism: Mus musculus (Mouse)
Function: May play a role in fertilization.
Subcellular location: Cell membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}.
Interaction partners:
- Complement receptor type 2
Sequence:
MSGSFSPCVVFTQMWLTLLVVTPVNGQHEAAQQSVVSLQPPWTTFFRGEVVTLTCYRFGFSVPQKTKWYQKRKTVKQTPGALVIKAHTLKVHESGEYWCQADSLLPSMHVNVEFSEDFLVLQAPPAVFEGDSVVLRCYAKKGIEAETLTFYKDGKALTLHPQSSEFYIHRANLKDNGQYKCTSKKKWSFGSLYTSNTVVVQVQELFPRPVLRARPSHPIDGSPVTLTCQTQLSAQKSDARLQFCFFRNLQLLGSGCSRSSEFHIPAIWTEESKRYQCKAETVNSQVSKQSTAFIIPVQRASARFQTHIIPASKLVFEGQLLLLNCSVKGVPGPLKFSWYKKDMLNKETKILKSSNAEFKISQVNISDAGEYYCEANNSRRSFVSRAFPITIKVPVSQPVLTLSTGKTQALEGDLMTLHCQSQRGSPCILYEFFYENVSLGNSSILSGGGAYFNFSMSTERSGNYYCTADNGLGAQCSEAIRISIFDMTKNRSVPMAAGITVGLLIMAVGVFLFYCWFSRKAGGKPTSDDSRNPSDSEPQEPTYYNVPACIELQPVYSNEPEENVIYTEVRRTQPRQKHADQESESPRSRCQMAEKK
Protein: Auxin-responsive protein IAA10 (Indoleacetic acid-induced protein 10) (Q38828)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Aux/IAA proteins are short-lived transcriptional factors that function as repressors of early auxin response genes at low auxin concentrations. Repression is thought to result from the interaction with auxin response factors (ARFs), proteins that bind to the auxin-responsive promoter element (AuxRE). Formation of heterodimers with ARF proteins may alter their ability to modulate early auxin response genes expression.
Subcellular location: Nucleus {ECO:0000250}.
Interaction partners:
- Auxin response factor 7
- Auxin response factor 5
- Protein TRANSPORT INHIBITOR RESPONSE 1
- Auxin response factor 18
- Protein TOPLESS
- Auxin response factor 9
- Auxin-responsive protein IAA18
- Auxin response factor 19
- Auxin-responsive protein IAA33
- Auxin-responsive protein IAA2
Sequence:
MNGLQEVCSSSGSVMIGLPAEEDENAAHSSEDSSCPDESVSETELDLALGLSIGRRKVRSSLSSSSSSLTRESGTKRSADSSPAAASNATRQVAVGWPPLRTYRINSLVNQAKSLATEGGLSSGIQKETTKSVVVAAKNDDACFIKSSRTSMLVKVTMDGVIIGRKVDLNALDSYAALEKTLDLMFFQIPSPVTRSNTQGYKTIKETCTSKLLDGSSEYIITYQDKDGDWMLVGDVPWQMFLGSVTRLRIMKTSIGAGVGK
Protein: At2g27260/F12K2.16 (Expressed protein) (Late embryogenesis abundant (LEA) hydroxyproline-rich glycoprotein family) (Q9XIN3)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004167}; Single-pass membrane protein {ECO:0000256|ARBA:ARBA00004167}.
Interaction partners:
Sequence:
MQDPSRPATGYPYPYPYPNPQQQQPPTNGYPNPAAGTAYPYQNHNPYYAPQPNPRAVIIRRLFIVFTTFLLLLGLILFIFFLIVRPQLPDVNLNSLSVSNFNVSNNQVSGKWDLQLQFRNPNSKMSLHYETALCAMYYNRVSLSETRLQPFDQGKKDQTVVNATLSVSGTYVDGRLVDSIGKERSVKGNVEFDLRMISYVTFRYGAFRRRRYVTVYCDDVAVGVPVSSGEGKMVGSSKRCKTY