wanglab/gogpt-training-data huggingface dataset:
Protein: 5-hydroxytryptamine receptor 2C (5-HT-2C) (5-HT2C) (5-HTR2C) (5-hydroxytryptamine receptor 1C) (5-HT-1C) (5-HT1C) (Serotonin receptor 2C) (P08909)
Organism: Rattus norvegicus (Rat)
Function: G-protein coupled receptor for 5-hydroxytryptamine (serotonin). Also functions as a receptor for various drugs and psychoactive substances, including ergot alkaloid derivatives, 1-2,5,-dimethoxy-4-iodophenyl-2-aminopropane (DOI) and lysergic acid diethylamide (LSD). Ligand binding causes a conformation change that triggers signaling via guanine nucleotide-binding proteins (G proteins) and modulates the activity of down-stream effectors. Beta-arrestin family members inhibit signaling via G proteins and mediate activation of alternative signaling pathways. Signaling activates a phosphatidylinositol-calcium second messenger system that modulates the activity of phosphatidylinositol 3-kinase and down-stream signaling cascades and promotes the release of Ca(2+) ions from intracellular stores. Regulates neuronal activity via the activation of short transient receptor potential calcium channels in the brain, and thereby modulates the activation of pro-opiomelacortin neurons and the release of CRH that then regulates the release of corticosterone. Plays a role in the regulation of appetite and feeding behavior, responses to anxiogenic stimuli and stress. Plays a role in insulin sensitivity and glucose homeostasis.
Subcellular location: Cell membrane {ECO:0000269|PubMed:3399891}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Guanine nucleotide-binding protein G
- 5-hydroxytryptamine receptor 2A
- 5-hydroxytryptamine receptor 2B
- Voltage-dependent L-type calcium channel subunit alpha-1D
- Guanine nucleotide-binding protein subunit alpha-11
- Voltage-dependent L-type calcium channel subunit alpha-1C
- Voltage-dependent L-type calcium channel subunit alpha
- 5-hydroxytryptamine receptor 1B
- Voltage-dependent L-type calcium channel subunit alpha-1S
- Basigin
Sequence:
MVNLGNAVRSLLMHLIGLLVWQFDISISPVAAIVTDTFNSSDGGRLFQFPDGVQNWPALSIVVIIIMTIGGNILVIMAVSMEKKLHNATNYFLMSLAIADMLVGLLVMPLSLLAILYDYVWPLPRYLCPVWISLDVLFSTASIMHLCAISLDRYVAIRNPIEHSRFNSRTKAIMKIAIVWAISIGVSVPIPVIGLRDESKVFVNNTTCVLNDPNFVLIGSFVAFFIPLTIMVITYFLTIYVLRRQTLMLLRGHTEEELANMSLNFLNCCCKKNGGEEENAPNPNPDQKPRRKKKEKRPRGTMQAINNEKKASKVLGIVFFVFLIMWCPFFITNILSVLCGKACNQKLMEKLLNVFVWIGYVCSGINPLVYTLFNKIYRRAFSKYLRCDYKPDKKPPVRQIPRVAATALSGRELNVNIYRHTNERVARKANDPEPGIEMQVENLELPVNPSNVVSERISSV
Protein: Dimethylnonatriene synthase (EC 1.14.14.59) (Cytochrome P-450 19) (Cytochrome P450 92C5) (Trimethyltridecatetraene synthase) (EC 1.14.14.58) (A0A1D6HSP4)
Organism: Zea mays (Maize)
Function: Involved in the biosynthesis of homoterpenes, attractants of herbivores parasitoids and predators (e.g. predatory mites and parasitoid wasps) (By similarity). Component of the volatile terpenes biosynthesis pathways. Converts mainly nerolidol to dimethylnonatriene (DMNT) and, to a lower extent, geranyllinalool to trimethyltridecatetraene (TMTT).
Subcellular location: Membrane {ECO:0000255}; Single-pass membrane protein {ECO:0000255}.
Interaction partners:
- Trimethyltridecatetraene synthase
Sequence:
MELASTMSVAMALAAAIFVVLCSVVASARGRREKALKLPPGPRGWPVLGSLGALAGALPPHRALAALAARHGPLMHLRLGSYHTVVASSADAARLVLRTHDSALADRPDTAAGEITSYGYLGIVHTPRGAYWRMARRLCATELFSARRVESFQDVRAQEMRALARGLFGCAAGRRAVAVREHVAGATMRNILRMAVGEKWSGCYGSPEGEAFRRSLDEAFAATGAVSNVGEWVPWLGWLDVQGFKRKMKRLHDLHDHFYEKILVDHEERRRLAQASGGEFVATDLVDVLLQLSEESTKLESESEARLPRDGVKALIQDIIAGGTESSAVTIEWAMAELLRHPEAMAKATDELDRVVGSGRWVAERDLPELHYIDAVVKETLRLHPVGPLLVPHYARERTVVAGYDVPAGARVLVNAWAIARDPASWPDAPDAFQPERFLGAAAAVDVRGAHFELLPFGSGRRICPAYDLAMKLVAAGVANLVHGFAWRLPDGVAAEDVSMEEHVGLSTRRKVPLFAVAEPRLPVHLYSATE
Protein: Adenine phosphoribosyltransferase (APRT) (EC 2.4.2.7) (P08030)
Organism: Mus musculus (Mouse)
Function: Catalyzes a salvage reaction resulting in the formation of AMP, that is energically less costly than de novo synthesis.
Subcellular location: Cytoplasm.
Interaction partners:
- GMP synthase
- Adenylosuccinate lyase
- Adenosine kinase
- Hypoxanthine-guanine phosphoribosyltransferase
- Bifunctional purine biosynthesis protein ATIC
- Purine nucleoside phosphorylase
- Purine nucleoside phosphorylase
- AMP deaminase 3
- AMP deaminase 2
- AMP deaminase 1
Sequence:
MSEPELKLVARRIRSFPDFPIPGVLFRDISPLLKDPDSFRASIRLLASHLKSTHSGKIDYIAGLDSRGFLFGPSLAQELGVGCVLIRKQGKLPGPTVSASYSLEYGKAELEIQKDALEPGQRVVIVDDLLATGGTMFAACDLLHQLRAEVVECVSLVELTSLKGRERLGPIPFFSLLQYD
Protein: Glutamyl-tRNA reductase 2, chloroplastic (GluTR) (EC 1.2.1.70) (P49294)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Catalyzes the NADPH-dependent reduction of glutamyl-tRNA(Glu) to glutamate 1-semialdehyde (GSA). Probably involved in wound-induced supply of heme to defensive hemoproteins outside plastids.
Subcellular location: Plastid, chloroplast {ECO:0000250}.
Interaction partners:
- Glutamate--tRNA ligase, cytoplasmic
- Glutamate--tRNA ligase, chloroplastic/mitochondrial
- Glutamate-1-semialdehyde 2,1-aminomutase 2, chloroplastic
- Glutamate-1-semialdehyde 2,1-aminomutase 1, chloroplastic
- Porphobilinogen deaminase, chloroplastic
- Magnesium-chelatase subunit ChlH, chloroplastic
- Magnesium-chelatase subunit ChlD, chloroplastic
- Chlorophyllide a oxygenase, chloroplastic
- Magnesium protoporphyrin IX methyltransferase, chloroplastic
- Glutamyl-tRNA reductase-binding protein, chloroplastic
Sequence:
MAVSSAFVVTPKLEKLLANHHNPTYSSSPAPLDVIGIRALPMNNRNKRGLIQRARCEISPSNKAASISALEQLKTSAIDRYTKERSSIVVIGLSIHTAPVEMREKLAIPEAEWPRAIAELCGLNHIEEAAVLSTCNRMEIYVLALSQHRGVKEVTEWMSKTSGIPVSEICQHRFLLYNKDVTQHIFEVSAGLDSLVLGEGQILAQVKQVVKVGQGVNGFGRNISGLFKHAITVGKRVRTETNIAAGAVSVSSAAVELALMKLPESSHASSARMLVVGAGKMGKLVIKHLVAKGCTKMVVVNRSEEKVAAVRNEMPPGVEIIYKPLDEMLSCAAEADVVFTSTASETPLFLKEQVETLPPVRDARLFVDISVPRNVGSCVAEIDGTRVFNVDDLKEVVAANKEDRVRKAMDAQAIITDESKHFEAWRDSLETVPTIKKLRGYTERIIAAEIEKSLPKMGIDMNKKMRKTVDDLIRGIVNKLLHGPMQHLRCDGNDSRTLSETLDNMQALNRMYGLDAEILEEKIRAKVEKK
Protein: Actin (EC 3.6.4.-) (P60010)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Actins are highly conserved proteins that are involved in various types of cell motility and are ubiquitously expressed in all eukaryotic cells.
Subcellular location: Cytoplasm, cytoskeleton.
Interaction partners:
- RuvB-like protein 1
- Ino eighty subunit 4
- Enhancer of polycomb-like protein 1
- Protein BNI1
- RuvB-like protein 2
- Cofilin
- Profilin
- Myosin-1
- Fimbrin
- Actin-like protein ARP8
Sequence:
MDSEVAALVIDNGSGMCKAGFAGDDAPRAVFPSIVGRPRHQGIMVGMGQKDSYVGDEAQSKRGILTLRYPIEHGIVTNWDDMEKIWHHTFYNELRVAPEEHPVLLTEAPMNPKSNREKMTQIMFETFNVPAFYVSIQAVLSLYSSGRTTGIVLDSGDGVTHVVPIYAGFSLPHAILRIDLAGRDLTDYLMKILSERGYSFSTTAEREIVRDIKEKLCYVALDFEQEMQTAAQSSSIEKSYELPDGQVITIGNERFRAPEALFHPSVLGLESAGIDQTTYNSIMKCDVDVRKELYGNIVMSGGTTMFPGIAERMQKEITALAPSSMKVKIIAPPERKYSVWIGGSILASLTTFQQMWISKQEYDESGPSIVHHKCF
Protein: Caronte (Q9PUK2)
Organism: Gallus gallus (Chicken)
Subcellular location: Secreted {ECO:0000256|ARBA:ARBA00004613, ECO:0000256|PIRNR:PIRNR027807}.
Interaction partners:
Sequence:
MSLLLLQLLVLSCLGDTEPQPDSQQRKRRPLQHLFYLDRNLLESQSFHELVGENPVGVKETQEEPSFFIAFPQTAGESQKQGEKKMSRFILPNAELYAHQDLRTWAAPKEISPVENFSPSYYSNKRDVEPPYRKDAKKFWDHFMLRKNSASEEVVLPIKTNEMHQETCRTLPFSQSVAHESCEKVIVQNNLCFGKCSSFHVPGPDDRLYTFCSKCLPTKFSMKHFDLNCTSSVPVVKKVMIVEECNCETQKIEDPLLGSLQSDFLGNVPEHN
Protein: Elongation factor 1-alpha 3 (EF-1-alpha 3) (eEF-1A3) (Q0WL56)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: This protein promotes the GTP-dependent binding of aminoacyl-tRNA to the A-site of ribosomes during protein biosynthesis.
Subcellular location: Cytoplasm.
Interaction partners:
- Probable elongation factor 1-gamma 2
- Adenylyl-sulfate kinase 1, chloroplastic
- Adenylyl-sulfate kinase 3
- Adenylyl-sulfate kinase 2, chloroplastic
- Adenylyl-sulfate kinase 4, chloroplastic
- Large ribosomal subunit protein uL18y
- Small ribosomal subunit protein eS8z
- Large ribosomal subunit protein uL2x
- Small ribosomal subunit protein uS3y
- Large ribosomal subunit protein uL18z
Sequence:
MGKEKFHINIVVIGHVDSGKSTTTGHLIYKLGGIDKRVIERFEKEAAEMNKRSFKYAWVLDKLKAERERGITIDIALWKFETTKYYCTVIDAPGHRDFIKNMITGTSQADCAVLIIDSTTGGFEAGISKDGQTREHALLAFTLGVKQMICCCNKMDATTPKYSKARYDEIIKEVSSYLKKVGYNPDKIPFVPISGFEGDNMIERSTNLDWYKGPTLLEALDQINEPKRPSDKPLRLPLQDVYKIGGIGTVPVGRVETGMIKPGMVVTFAPTGLTTEVKSVEMHHESLLEALPGDNVGFNVKNVAVKDLKRGYVASNSKDDPAKGAANFTSQVIIMNHPGQIGNGYAPVLDCHTSHIAVKFSEILTKIDRRSGKEIEKEPKFLKNGDAGMVKMTPTKPMVVETFSEYPPLGRFAVRDMRQTVAVGVIKSVDKKDPTGAKVTKAAVKKGAK
Protein: LexA repressor (EC 3.4.21.88) (Q9A724)
Organism: Caulobacter vibrioides (strain ATCC 19089 / CIP 103742 / CB 15) (Caulobacter crescentus)
Function: Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Interaction partners:
- Protein RecA
- DNA polymerase IV
- Protein ImuB
- DNA methyltransferase CcrM
- UvrABC system protein B
- Protein ImuA
- UvrABC system protein A
- UvrABC system protein C
- Error-prone DNA polymerase
- DNA repair protein RecN
Sequence:
MLTRKQHELLMFIHERIKETGVSPSFDEMKEALDLASKSGIHRLITALEERGFIRRLAHRARALEVVKLPQQATAAAPPKGRGAFRPQVFEGGGAPPPAASPAAAANDSRELPILGRIAAGTPIDAIQHERERLPVPEAMLGAGEHYVLEVQGDSMIEAGILDGDYVIIKKGDTATSGEIVVALVGEEATLKRLRKKGGSIALEAANPKYETRIFGPDQVEVQGKLVGLIRRYH
Protein: Eyes absent homolog (EC 3.1.3.48) (A0A8I6AMN9)
Organism: Rattus norvegicus (Rat)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MEEEQDLPERPVKKAKMQEPGEQTLSQVNNPDTSDQKPETASLASNLSMSEEIMTCTDYIPRSSNDYTSQMYSAKPYAHILSVPVSETTYPGQTQYQTLQQSQPYAVYPQATQTYGLPPFGALWPGMKPESGLIQTPSPSQHSVLTCTTGLTTSQPSPAHYSYPIPASSTNASLISTSSAIANIPAAAVASISNQDYPTYTILGQNQYQACYPSSSFGVTGQTNSDTENTALAATTYQTEKPGAMGPAPATQRLPSDSSTSPPLSQTTPNKDADDQARKNMTVKNRGKRKADASSSQDSELERVFLWDLDETIIIFHSLLTGSYAQKYGKDPTVVIGSGLTMEEMIFEVADTHLFFNDLEECDQVHVEDVASDDNGQDLSNYSFSTDGFSGSGGSGSHGSSVGVQGGVDWMRKLAFRYRKVREIYDKHKSNVGGLLSPQRKEALQRLRAEIEVLTDSWLGTALKSLLLIQSRKNCVNVLITTTQLVPALAKVLLYGLGEIFPIENIYSATKIGKESCFERIVSRFGKKVTYVVIGDGRDEEIAAKQHNMPFWRITNHGDLVSLHQALELDFL
Protein: 6-pyruvoyl tetrahydrobiopterin synthase (PTP synthase) (PTPS) (EC 4.2.3.12) (Q1ZXI0)
Organism: Dictyostelium discoideum (Social amoeba)
Function: Involved in the biosynthesis of tetrahydrobiopterin, an essential cofactor of aromatic amino acid hydroxylases. Catalyzes the transformation of 7,8-dihydroneopterin triphosphate into 6-pyruvoyl tetrahydropterin (By similarity).
Interaction partners:
- GTP cyclohydrolase 1
- Sepiapterin reductase
- Aldose reductase C
- Aldose reductase B
- Aldose reductase A
- Alkaline phosphatase
- Tyrosine-protein phosphatase 1
- Ribose-phosphate pyrophosphokinase C
- Ribose-phosphate pyrophosphokinase B
- Ribose-phosphate pyrophosphokinase A
Sequence:
MSRTVILTRREVFSSSHRLYSDKLSLEENKKIYGKCINSHGHNYVLEVSIKGAVKEDIGMFMNITELKEILKEKVMDKLDHKNLENDVPELKGIVTTTENLSIFIWDQLFPSLKDFLYEVKILETENNFVVYRGE
Protein: 26S proteasome regulatory subunit 8 (26S proteasome AAA-ATPase subunit RPT6) (Proteasome 26S subunit ATPase 5) (Proteasome subunit p45) (Thyroid hormone receptor-interacting protein 1) (TRIP1) (p45/SUG) (P62195)
Organism: Homo sapiens (Human)
Function: Component of the 26S proteasome, a multiprotein complex involved in the ATP-dependent degradation of ubiquitinated proteins. This complex plays a key role in the maintenance of protein homeostasis by removing misfolded or damaged proteins, which could impair cellular functions, and by removing proteins whose functions are no longer required. Therefore, the proteasome participates in numerous cellular processes, including cell cycle progression, apoptosis, or DNA damage repair. PSMC5 belongs to the heterohexameric ring of AAA (ATPases associated with diverse cellular activities) proteins that unfolds ubiquitinated target proteins that are concurrently translocated into a proteolytic chamber and degraded into peptides.
Subcellular location: Cytoplasm {ECO:0000305}. Nucleus {ECO:0000305}.
Interaction partners:
- 26S proteasome regulatory subunit 6B
- 26S proteasome regulatory subunit 6A
- 26S proteasome non-ATPase regulatory subunit 11
- 26S proteasome non-ATPase regulatory subunit 3
- Proteasome subunit alpha type-2
- Ubiquitin carboxyl-terminal hydrolase 14
- 26S proteasome non-ATPase regulatory subunit 4
- 26S proteasome regulatory subunit 7
- Proteasome subunit beta type-5
- 26S proteasome non-ATPase regulatory subunit 6
Sequence:
MALDGPEQMELEEGKAGSGLRQYYLSKIEELQLIVNDKSQNLRRLQAQRNELNAKVRLLREELQLLQEQGSYVGEVVRAMDKKKVLVKVHPEGKFVVDVDKNIDINDVTPNCRVALRNDSYTLHKILPNKVDPLVSLMMVEKVPDSTYEMIGGLDKQIKEIKEVIELPVKHPELFEALGIAQPKGVLLYGPPGTGKTLLARAVAHHTDCTFIRVSGSELVQKFIGEGARMVRELFVMAREHAPSIIFMDEIDSIGSSRLEGGSGGDSEVQRTMLELLNQLDGFEATKNIKVIMATNRIDILDSALLRPGRIDRKIEFPPPNEEARLDILKIHSRKMNLTRGINLRKIAELMPGASGAEVKGVCTEAGMYALRERRVHVTQEDFEMAVAKVMQKDSEKNMSIKKLWK
Protein: Inner membrane transport protein YhjV (P37660)
Organism: Escherichia coli (strain K12)
Subcellular location: Cell inner membrane; Multi-pass membrane protein.
Interaction partners:
- Dipeptide transport ATP-binding protein DppF
Sequence:
MQHNTLSKHNQKLPFTRYDFGWVLLCIGMAIGAGTVLMPVQIGLKGIWVFITAAIIAYPATWVVQDIYLKTLSESDSCNDYTDIISHYLGKNWGIFLGVIYFLMIIHGIFIYSLSVVFDSASYLKTFGLTDADLSQSLLYKVAIFAVLVAIASGGERLLFKISGPMVVVKVGIIVVFGFAMIPHWNFANITAFPQASVFFRDVLLTIPFCFFSAVFIQVLNPMNIAYRKREADKVLATRLALRTHRISYITLIAVILFFAFSFTFSISHEEAVSAFEQNISALALAAQVIPGHIIHITSTVLNIFAVLTAFFGIYLGFHEAIKGIILNLLSRIIDTKKINSRVLTLAICAFIVITLTIWVSFRVSVLVFFQLGSPLYGIVSCLIPFFLIYKVAQLEKLRGFKAWLILLYGILLCLSPLLKLIE
Protein: Short transient receptor potential channel 5 (TrpC5) (Capacitative calcium entry channel 2) (CCE2) (Transient receptor protein 5) (TRP-5) (mTRP5) (Trp-related protein 5) (Q9QX29)
Organism: Mus musculus (Mouse)
Function: Thought to form a receptor-activated non-selective calcium permeant cation channel. Probably is operated by a phosphatidylinositol second messenger system activated by receptor tyrosine kinases or G-protein coupled receptors. Has also been shown to be calcium-selective. May also be activated by intracellular calcium store depletion (By similarity). Mediates calcium-dependent phosphatidylserine externalization and apoptosis in neurons via its association with PLSCR1.
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:Q9UL62}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Short transient receptor potential channel 1
- Short transient receptor potential channel 4
- Stromal interaction molecule 1
- Voltage-dependent T-type calcium channel subunit alpha-1H
- Voltage-dependent T-type calcium channel subunit alpha
- Voltage-dependent T-type calcium channel subunit alpha
- Bone morphogenetic protein receptor type-2
- Short transient receptor potential channel 3
- Na
- SEC14 domain and spectrin repeat-containing protein 1
Sequence:
MAQLYYKKVNYSPYRDRIPLQIVRAETELSAEEKAFLSAVEKGDYATVKQALQEAEIYYNVNINCMDPLGRSALLIAIENENLEIMELLLNHSVYVGDALLYAIRKEVVGAVELLLSYRKPSGEKQVPTLMMDTQFSEFTPDITPIMLAAHTNNYEIIKLLVQKRVTIPRPHQIRCNCVECVSSSEVDSLRHSRSRLNIYKALASPSLIALSSEDPILTAFRLGWELKELSKVENEFKAEYEELSQQCKLFAKDLLDQARSSRELEIILNHRDDHSEELDPQKYHDLAKLKVAIKYHQKEFVAQPNCQQLLATLWYDGFPGWRRKHWVVKLLTCMTIGFLFPMLSIAYLISPRSNLGLFIKKPFIKFICHTASYLTFLFMLLLASQHIVRTDLHVQGPPPTVVEWMILPWVLGFIWGEIKEMWDGGFTEYIHDWWNLMDFAMNSLYLATISLKIVAYVKYNGSRPREEWEMWHPTLIAEALFAISNILSSLRLISLFTANSHLGPLQISLGRMLLDILKFLFIYCLVLLAFANGLNQLYFYYETRAIDEPNNCKGIRCEKQNNAFSTLFETLQSLFWSVFGLLNLYVTNVKARHEFTEFVGATMFGTYNVISLVVLLNMLIAMMNNSYQLIADHADIEWKFARTKLWMSYFDEGGTLPPPFNIIPSPKSFLYLGNWFNNTFCPKRDPDGRRRRHNLRSFTERHADSLIQNQHYQEVIRNLVKRYVAAMIRNSKTNEGLTEENFKELKQDISSFRYEVLDLLGNRKHPRRSLSTSSADFSQRDDTNDGSGGARAKSKSVSFNVGCKKKACHGAPLIRTVPRASGAQGKPKSESSSKRSFMGPSFKKLGLFFSKFNGQTSEPTSEPMYTISDGIAQQHCMWQDIRYSQMEKGKAEACSQSQMNLGEVELGEIRGAAARSSECPLACSSSLHCASGICSSNSKLLDSSEDVFETWGEACDLLMHKWGDGQEEQVTTRL
Protein: At3g01890 (SWIB/MDM2 domain superfamily protein) (Q147F4)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Chromatin structure-remodeling complex protein BSH
- Actin-related protein 4
- SWI/SNF complex subunit SWI3C
- SWI/SNF complex subunit SWI3A
- SWI/SNF complex subunit SWI3D
- SWI/SNF complex subunit SWI3B
- High mobility group B protein 10
- Chaperone DnaJ-domain superfamily protein
- High mobility group B protein 9
- High mobility group B protein 15
Sequence:
MSGNNELNALKGPQSSLPWPFGMASASFAPSHMAPPNFQPQFQLSQDQGISAPGRRFPHKPPIGGPPAVPPSMELTPASRKKKHKLPDKSSLQERVAAVLPESALYTQLLEFESRVDAALFRKKVDIQDSLKNPPSIQKTLRIYVFNTFSNQIPGPDPPTWTLRIFGRVLDPDHTGGLVQNSNPLYPKFSSFFKTLKISLDQSLYPENHLIEWKRDRSPAPLEGFEIKRIGCQEFAATILLEMNYVPEKFKTSPALMQVLGIEVDTRPRIIAAIWHYVKVRKLQNPNDPSFFNCDAALHSVFGEEKMKFTMLSHKISQHLSPPPPIQLVHKIKLSGNNPAISACYDVLVDIPAPVQTELSNLLANPEKNKEIEACDEAICGAIRKIHEHRRRRAFFLGFSQSPVEFTNALMESQTKDLKLVAGEASRNAEKEGRSEFFNQPWVEDAAIRYLNRKPAGG
Protein: Toll-like receptor 2 type-1 (Q9DD78)
Organism: Gallus gallus (Chicken)
Function: Participates in the innate immune response to microbial agents. Acts via MYD88 and TRAF6, leading to NF-kappa-B activation, cytokine secretion and the inflammatory response (By similarity). Does not respond to LPS and responds with less ability than TLR2-2 to mycoplasmal macrophage-activating lipopeptide-2kD (MALP-2).
Subcellular location: Membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}.
Interaction partners:
- Myeloid differentiation primary response protein MyD88
- TIR domain-containing protein
- Toll like receptor 1 type2
- TIR domain-containing protein.
- Toll-interacting protein
- Interleukin-1
- Interleukin-6
- Interleukin-10
- GTPase cRac1A
- High mobility group protein B1
Sequence:
MFNQSKQKPTMKLMWQAWLIYTALAAHLPEEQALRQACLSCDATQSCNCSFMGLDFIPPGLTGKITVLNLAHNRIKLIRTHDLQKAVNLRTLLLQSNQISSIDEDSFGSQGKLELLDLSNNSLAHLSPVWFGPLFSLQHLRIQGNSYSDLGESSPFSSLRNLSSLHLGNPQFSIIRQGNFEGIVFLNTLRIDGDNLSQYEPGSLKSIRKINHMIISIRRIDVFSAVIRDLLHSAIWLEVREIKLDIENEKLVQNSTLPLTIQKLTFTGASFTDKYISQIAVLLKEIRSLRELEAIDCVLEGKGAWDMTEIARSKQSSIETLSITNMTILDFYLFFDLEGIETQVGKLKRLSIASSKVFMVPCRLARYFSSLLYLDFHDNLLVNNRLGETICEDAWPSLQTLNLSKNSLKSLKQAARYISNLHKLINLDISENNFGEIPDMCEWPENLKYLNLSSTQIPKLTTCIPSTLEVLDVSANNLQDFGLQLPFLKELYLTKNHLKTLPEATDIPNLVAMSISRNKLNSFSKEEFESFKQMELLDASANNFICSCEFLSFIHHEAGIAQVLVGWPESYICDSPLTVRGAQVGSVQLSLMECHRSLLVSLICTLVFLFILILVVVGYKYHAVWYMRMTWAWLQAKRKPKRAPTKDICYDAFVSYSENDSNWVENIMVQQLEQACPPFRLCLHKRDFVPGKWIVDNIIDSIEKSHKTLFVLSEHFVQSEWCKYELDFSHFRLFDENNDVAILILLEPIQSQAIPKRFCKLRKIMNTKTYLEWPPDEEQQQMFWENLKAALKS
Protein: Mitochondrial import receptor subunit tom7 (Translocase of outer membrane 7 kDa subunit) (O42999)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Mitochondrion outer membrane {ECO:0000250}; Single-pass membrane protein {ECO:0000255}.
Interaction partners:
- Mitochondrial import receptor subunit tom22
- Probable mitochondrial import receptor subunit tom40
- Mitochondrial import receptor subunit tom20
- Probable mitochondrial import receptor subunit tom70
- Mitochondrial distribution and morphology protein 10
- SAM50-like protein SPAC17C9.06
- Mitochondrial Rho GTPase 1
- Mitochondrial import inner membrane translocase subunit tim10
- Mitochondrial distribution and morphology protein 12
- Metaxin-like protein C409.19c
Sequence:
MQISEESKERLVKVFNIGKTVTHYGWIPLILWLGYTQSNPKPQLMRVINPLA
Protein: DNA-binding protein inhibitor ID-2 (Inhibitor of DNA binding 2) (Inhibitor of differentiation 2) (P41137)
Organism: Rattus norvegicus (Rat)
Function: Transcriptional regulator (lacking a basic DNA binding domain) which negatively regulates the basic helix-loop-helix (bHLH) transcription factors by forming heterodimers and inhibiting their DNA binding and transcriptional activity. Implicated in regulating a variety of cellular processes, including cellular growth, senescence, differentiation, apoptosis, angiogenesis, and neoplastic transformation. Inhibits skeletal muscle and cardiac myocyte differentiation. Regulates the circadian clock by repressing the transcriptional activator activity of the CLOCK-BMAL1 heterodimer. Restricts the CLOCK and BMAL1 localization to the cytoplasm. Plays a role in both the input and output pathways of the circadian clock: in the input component, is involved in modulating the magnitude of photic entrainment and in the output component, contributes to the regulation of a variety of liver clock-controlled genes involved in lipid metabolism (By similarity).
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:P41136}. Nucleus {ECO:0000250|UniProtKB:P41136}.
Interaction partners:
- Transcription factor E2-alpha
- Oligodendrocyte transcription factor 1
- Oligodendrocyte transcription factor 2
- Transcription factor 4
- Myogenin
- Interleukin-7 receptor subunit alpha
- Class A basic helix-loop-helix protein 15
Sequence:
MKAFSPVRSVRKNSLSDHSLGISRSKTPVDDPMSLLYNMNDCYSKLKELVPSIPQNKKVTKMEILQHVIDYILDLQIALDSHPTIVSLHHQRPGQNQTSRTPLTTLNTDISILSLQASEFPSELMSNDSKVLCG
Protein: F-box only protein 5 (Early mitotic inhibitor 1) (Q9UKT4)
Organism: Homo sapiens (Human)
Function: Regulator of APC activity during mitotic and meiotic cell cycle. During mitotic cell cycle plays a role as both substrate and inhibitor of APC-FZR1 complex. During G1 phase, plays a role as substrate of APC-FZR1 complex E3 ligase. Then switches as an inhibitor of APC-FZR1 complex during S and G2 leading to cell-cycle commitment. As APC inhibitor, prevents the degradation of APC substrates at multiple levels: by interacting with APC and blocking access of APC substrates to the D-box coreceptor, formed by FZR1 and ANAPC10; by suppressing ubiquitin ligation and chain elongation by APC by preventing the UBE2C and UBE2S activities. Plays a role in genome integrity preservation by coordinating DNA replication with mitosis through APC inhibition in interphase to stabilize CCNA2 and GMNN in order to promote mitosis and prevent rereplication and DNA damage-induced cellular senescence. During oocyte maturation, plays a role in meiosis through inactivation of APC-FZR1 complex. Inhibits APC through RPS6KA2 interaction that increases FBXO5 affiniy for CDC20 leading to the metaphase arrest of the second meiotic division before fertilization (By similarity). Controls entry into the first meiotic division through inactivation of APC-FZR1 complex (By similarity). Promotes migration and osteogenic differentiation of mesenchymal stem cells.
Subcellular location: Nucleus {ECO:0000269|PubMed:11988738}. Cytoplasm {ECO:0000269|PubMed:11988738}. Cytoplasm, cytoskeleton, spindle {ECO:0000269|PubMed:15469984}. Note=In interphase, localizes in a punctate manner in the nucleus and cytoplasm with some perinuclear concentration (PubMed:11988738). In mitotic cells, localizes throughout the cell, particularly at the spindle (PubMed:15469984). {ECO:0000269|PubMed:11988738, ECO:0000269|PubMed:15469984}.
Interaction partners:
- Cell division cycle protein 20 homolog
- Anaphase-promoting complex subunit 4
- Fizzy-related protein homolog
- S-phase kinase-associated protein 1
- F-box/WD repeat-containing protein 1A
- Anaphase-promoting complex subunit 2
- Anaphase-promoting complex subunit 10
- Cell division cycle protein 23 homolog
- Cullin-1
- Cell division cycle protein 27 homolog
Sequence:
MSRRPCSCALRPPRCSCSASPSAVTAAGRPRPSDSCKEESSTLSVKMKCDFNCNHVHSGLKLVKPDDIGRLVSYTPAYLEGSCKDCIKDYERLSCIGSPIVSPRIVQLETESKRLHNKENQHVQQTLNSTNEIEALETSRLYEDSGYSSFSLQSGLSEHEEGSLLEENFGDSLQSCLLQIQSPDQYPNKNLLPVLHFEKVVCSTLKKNAKRNPKVDREMLKEIIARGNFRLQNIIGRKMGLECVDILSELFRRGLRHVLATILAQLSDMDLINVSKVSTTWKKILEDDKGAFQLYSKAIQRVTENNNKFSPHASTREYVMFRTPLASVQKSAAQTSLKKDAQTKLSNQGDQKGSTYSRHNEFSEVAKTLKKNESLKACIRCNSPAKYDCYLQRATCKREGCGFDYCTKCLCNYHTTKDCSDGKLLKASCKIGPLPGTKKSKKNLRRL
Protein: D-alanine--D-alanine ligase (EC 6.3.2.4) (D-Ala-D-Ala ligase) (D-alanylalanine synthetase) (Q6WRY5)
Organism: Enterococcus faecalis (Streptococcus faecalis)
Subcellular location: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00047}.
Interaction partners:
Sequence:
MQNKKIAVIFGGNSTEYEVSLQSASAVFENINTNKFDIIPIGITRSGEWYHYTGEKEKILNNTWFEDSKNLCPVVVSQNRSVKGFLEIASDKYRIIKVDLVFPVLHGKNGEDGTLQGIFELAGIPVVGCDTLSSALCMDKDRAHKLVSLAGISVPKSVTFKRFNEEAAMKEIEANLTYPLFIKPVRAGSSFGITKVIEKQELDAAIELAFEHDTEVIVEETINGFEVGCAVLGIDELIVGRVDEIELSSGFFDYTEKYTLKSSKIYMPARIDAEAEKRIQEAAVTIYKALGCSGFSRVDMFYTPSGEIVFNEVNTIPGFTSHSRYPNMMKGIGLSFSQMLDKLIGLYVE