wanglab/gogpt-training-data huggingface dataset:
Protein: C-C motif chemokine 7 (Monocyte chemoattractant protein 3) (Monocyte chemotactic protein 3) (MCP-3) (NC28) (Small-inducible cytokine A7) (P80098)
Organism: Homo sapiens (Human)
Function: Chemotactic factor that attracts monocytes and eosinophils, but not neutrophils. Augments monocyte anti-tumor activity. Also induces the release of gelatinase B. This protein can bind heparin. Binds to CCR1, CCR2 and CCR3.
Subcellular location: Secreted.
Interaction partners:
- C-C chemokine receptor type 3
- C-C chemokine receptor type 2
- C-C chemokine receptor type 1
- C-C chemokine receptor type 5
- C-X-C motif chemokine 6
- Cytokine SCM-1 beta
- Atypical chemokine receptor 2
- C-X-C chemokine receptor type 2
- CX3C chemokine receptor 1
- Interleukin-8
Sequence:
MKASAALLCLLLTAAAFSPQGLAQPVGINTSTTCCYRFINKKIPKQRLESYRRTTSSHCPREAVIFKTKLDKEICADPTQKWVQDFMKHLDKKTQTPKL
Protein: Ras-related protein RABA5a (AtRABA5a) (Q9FGK5)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Intracellular vesicle trafficking and protein transport.
Subcellular location: Cell membrane {ECO:0000269|PubMed:15060130}; Lipid-anchor {ECO:0000305}; Cytoplasmic side {ECO:0000305}.
Interaction partners:
- Geranylgeranyl transferase type-2 subunit beta 1
- Rab escort protein 1
- Kinesin-like protein KIN-14E
- Geranylgeranyl transferase type-2 subunit beta 2
Sequence:
MAFYSEDDKSEDYLFKIVLIGDSAVGKSNLLARFARDEFYPNSKSTIGVEFQTQKMDINGKEIKAQIWDTAGQERFRAVTSAYYRGAVGALLVYDISRRQTFHSIGRWLNELHTHSDMNVVTILVGNKSDLKDLREVSTAEGKALAEAQGLFFMETSALDSSNVAAAFETVVKEIYNILSRKVMSSQELNKQDPASLSNGKKVVIPSDGQGEFKKGGCCSS
Protein: Probable glutathione S-transferase DHAR1, cytosolic (EC 2.5.1.18) (GSH-dependent dehydroascorbate reductase 1) (OsDHAR1) (EC 1.8.5.1) (Glutathione-dependent dehydroascorbate reductase 1) (Q65XA0)
Organism: Oryza sativa subsp. japonica (Rice)
Function: Involved in ascorbate homeostasis. Maintains redox pools of ascorbate by recycling dihydroascorbate (DHA) to ascorbate (Probable). Involved in scavenging reactive oxygen species (ROS) under oxidative stresses. Possesses dehydroascorbate reductase (DHAR) activity in vitro. May function via a ping-pong reaction mechanism with an electron transfer at the active site. Possesses chaperone-like activity in vitro.
Subcellular location: Cytoplasm, cytosol {ECO:0000305}.
Interaction partners:
- Monodehydroascorbate reductase 1, peroxisomal
- Monodehydroascorbate reductase 3, cytosolic
- Monodehydroascorbate reductase 5, chlorplastic
- L-ascorbate peroxidase 1, cytosolic
- Monodehydroascorbate reductase 4, cytosolic
- Probable L-ascorbate peroxidase 7, chloroplastic
- Thylakoid lumenal 29 kDa protein, chloroplastic
- Probable L-ascorbate peroxidase 8, chloroplastic
- Glutathione peroxidase
- Glutathione synthetase
Sequence:
MGVEVCVKAAVGHPDTLGDCPFSQRVLLTLEEKKVPYEMKLIDVQNKPDWFLKISPEGKVPVFNGGDGKWIPDSDVITQVIEEKYPTPSLVTPPEYASVGSKIFSCFTTFLKSKDPNDGSEKALLTELQALEEHLKAHGPFINGQNISAADLSLAPKLYHLQVALEHFKGWKIPEDLTNVHAYTEALFSRESFIKTKAAKEHLIAGWAPKVNA
Protein: 15-cis-phytoene synthase (PSase) (EC 2.5.1.32) (P54975)
Organism: Paracoccus sp. (strain N81106 / MBIC 01143) (Agrobacterium aurantiacum)
Function: Involved in the biosynthesis of carotenoids for the production of astaxanthin. Catalyzes the condensation of two molecules of geranylgeranyl diphosphate (GGPP) to give prephytoene diphosphate (PPPP) and the subsequent rearrangement of the cyclopropylcarbinyl intermediate to yield 15-cis phytoene.
Interaction partners:
Sequence:
MSDLVLTSTEAITQGSQSFATAAKLMPPGIRDDTVMLYAWCRHADDVIDGQALGSRPEAVNDPQARLDGLRADTLAALQGDGPVTPPFAALRAVARRHDFPQAWPMDLIEGFAMDVEARDYRTLDDVLEYSYHVAGIVGVMMARVMGVRDDPVLDRACDLGLAFQLTNIARDVIDDARIGRCYLPGDWLDQAGARVDGPVPSPELYTVILRLLDAAELYYASARVGLADLPPRCAWSIAAALRIYRAIGLRIRKGGPEAYRQRISTSKAAKIGLLGIGGWDVARSRLPGAGVSRQGLWTRPHHA
Protein: Immunoglobulin lambda variable 2-23 (Ig lambda chain V-II region NEI) (P01705)
Organism: Homo sapiens (Human)
Function: V region of the variable domain of immunoglobulin light chains that participates in the antigen recognition. Immunoglobulins, also known as antibodies, are membrane-bound or secreted glycoproteins produced by B lymphocytes. In the recognition phase of humoral immunity, the membrane-bound immunoglobulins serve as receptors which, upon binding of a specific antigen, trigger the clonal expansion and differentiation of B lymphocytes into immunoglobulins-secreting plasma cells. Secreted immunoglobulins mediate the effector phase of humoral immunity, which results in the elimination of bound antigens. The antigen binding site is formed by the variable domain of one heavy chain, together with that of its associated light chain. Thus, each immunoglobulin has two antigen binding sites with remarkable affinity for a particular antigen. The variable domains are assembled by a process called V-(D)-J rearrangement and can then be subjected to somatic hypermutations which, after exposure to antigen and selection, allow affinity maturation for a particular antigen.
Subcellular location: Secreted {ECO:0000303|PubMed:20176268, ECO:0000303|PubMed:22158414}. Cell membrane {ECO:0000303|PubMed:20176268, ECO:0000303|PubMed:22158414}.
Interaction partners:
Sequence:
MAWALLLLTLLTQDTGSWAQSALTQPASVSGSPGQSITISCTGTSSDVGSYNLVSWYQQHPGKAPKLMIYEGSKRPSGVSNRFSGSKSGNTASLTISGLQAEDEADYYCCSYA
Protein: F-box/kelch-repeat protein At3g16740 (Q9LUQ9)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Component of SCF(ASK-cullin-F-box) E3 ubiquitin ligase complexes, which may mediate the ubiquitination and subsequent proteasomal degradation of target proteins.
Subcellular location: Nucleus {ECO:0000250}.
Interaction partners:
- F-box protein At3g57590
- F-box protein At5g39250
- Putative F-box protein At4g38870
- F-box/LRR-repeat protein At2g42720
- F-box protein At5g49610
- Putative FBD-associated F-box protein At1g78730
- F-box/kelch-repeat protein At5g43190
- FBD-associated F-box protein At5g56370
- Iron-sulfur cluster assembly protein 3
- Iron-sulfur cluster assembly protein 1
Sequence:
MVQISDLPRDLTEEVLSRIPVTSMRAVRFTCKKWNTLSKDRSFTKKHLRGARAAAKKKQTKEFQVIMMIQFRVYLYSVNLLNPSIERIGKLISLDVEDHVDISKIFHCGGLLLCITKDISRLVVWNPYSGQTRWIKPRNSYHRLDRYALGYEEKNKSCRCYKILRFMDDYEDDRALRLIREFEIYDLNSDSWKVVNVTPDWDVEFYHRGLSLKGNTYWFAQEKLPPLPRGRVITISDMADFLLCFDFTRERFGPRLPLPFHSFVEDTVTLSSVRDKKLAVLFQPCSASTVKIWISRKIEPNAVSWRKVFLAVDMKSLTGFQFDINAASFFVDEKKKVAMVLDKDRFSYKFTRNIAYIIGKKGYFEKVDLGESTVSSCASLVCSYVPSSVQI
Protein: Diphosphomevalonate decarboxylase (EC 4.1.1.33) (Q388J2)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Isopentenyl-diphosphate delta-isomerase, putative
- Farnesyl pyrophosphate synthase
- phosphomevalonate kinase
- Diphosphomevalonate decarboxylase
- Mevalonate kinase
- Hydroxymethylglutaryl-CoA synthase
- Lanosterol synthase
Sequence:
MSDQCATVEAPINIAFIKYWGKREGGETLILPTNDSFSITLSASPFRSKTSVELRDDIETDTLRLNGTEVDVGKTPRVQSMLLHLRSTCPEDLKNKKVNIVSENNFPTAAGMASSASGYCAMSAALIRAFKSTTNVSMLARLGSGSACRSAFGGFVIWNKGEKPDGSDCVATQFVDETHWPEIQVMCAVLKGAQKDVSSTKGMQQSLKTSPLMKKRISETVPERMKIASRAIKARDFATFAEIAMLESDDLQEICATTEPKITYATEDSYAMIRLVKAYNAKKGRTALAYTFDAGANCFLFVLKEDLPEAVAMLMEHFPTPFEKFFFGDRELLEKVKVVSLPDEYKKLIDHPKKPFEMLLQSPVGCGVKYLGPSESLIPPRV
Protein: BCL2 modifying factor 2 isoform X1 (BCL2-modifying factor 2) (Bmf2) (Q0GKC4)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
- BCL2 modifying factor 1.
- ATP synthase F
- Bcl-2-like protein 1
Sequence:
MDDEEDEQLPRCCETPLRNKRSEKRDAHGGDVGQTAHRHASTQTAGSVLNSARDADMAPFQGSQREASSLCRVVGARTAFRAPCGTGGLVSLTMGPGARGGPRALFHGNAGFRAHFPALFEPALDGLQNAEQREQDEGRPEEKEEDRDAGISVEVQIGRKLREMGDQFQQEHLQLVRVIHIRLILFFKAAGFQMCVVRNWWFQSRCKMTSLSAISVLNMQIPKRER
Protein: Ubiquitin-like protein (B5XFU9)
Organism: Salmo salar (Atlantic salmon)
Interaction partners:
Sequence:
MELTITLLNGNSLPLTVQPHTTVGSLKSLIEEHFKVATTKQRLLGVNGSNISLSDDSKTLSDYGLHSGSKVMVLITEPAPIQVFLKNEKGQTHTYDVVPGETVTQFKAKVQNKEGVPANQQRLIHEGRQLEDCQTLEYYNIRNQSTIHLTLRLRGG
Protein: CLIP domain-containing serine protease B15 (EC 3.4.21.-) [Cleaved into: CLIP domain-containing serine protease B15 light chain; CLIP domain-containing serine protease B15 heavy chain] (Q9NAS9)
Organism: Anopheles gambiae (African malaria mosquito)
Function: Serine protease (By similarity). Plays a role in innate immunity against infections by parasite P.berghei and by Gram-negative bacteria such as E.coli. In response to P.berghei infection, contributes to the clearing of parasite ookinetes independent of melanization, an innate immune response which consists in the deposition of melanin pigments on invading pathogens and parasites.
Subcellular location: Secreted {ECO:0000269|PubMed:16188883}. Note=Secreted in the hemolymph. {ECO:0000269|PubMed:16188883}.
Interaction partners:
Sequence:
MRWLVCLIVSWCSLVPLGATVGQSLNSGDPCQTPSGTAGTCEPVKNCSYVRKILKSPDFSHYDTTYLDTLKCGDLMVPMRKKPIPLLCCPKFSNSPTCGAQQLADRIYFGEETERGAHPWAALLFYNVGRNRTVPKCGGALISERYVITAAHCTVDKPNWKLLYVRFNEFNTSSADNCTTENDEVICREDYAVESIVPHPEYDMHNISRPNDICILRLASDVTFNDYVRPICLPFDPDVQQLPIVDEIFTVTGWGETEDRRPSDTQKHVELPGLEHEACNSVYAVANVTLSDKQLCIGGLNGSDSCRGDSGGPLMREVRGGWFLIGVVSFGARFCGTQNLPGVYTNVAKYLDWMETVMFVERYL
Protein: Collagen alpha-1(XXII) chain (Q8NFW1)
Organism: Homo sapiens (Human)
Function: Acts as a cell adhesion ligand for skin epithelial cells and fibroblasts.
Subcellular location: Secreted, extracellular space, extracellular matrix. Cytoplasm {ECO:0000250}.
Interaction partners:
- Collagen alpha-1
- Collagen alpha-1
- WD repeat-containing protein 90
Sequence:
MAGLRGNAVAGLLWMLLLWSGGGGCQAQRAGCKSVHYDLVFLLDTSSSVGKEDFEKVRQWVANLVDTFEVGPDRTRVGVVRYSDRPTTAFELGLFGSQEEVKAAARRLAYHGGNTNTGDALRYITARSFSPHAGGRPRDRAYKQVAILLTDGRSQDLVLDAAAAAHRAGIRIFAVGVGEALKEELEEIASEPKSAHVFHVSDFNAIDKIRGKLRRRLCENVLCPSVRVEGDRFKHTNGGTKEITGFDLMDLFSVKEILGKRENGAQSSYVRMGSFPVVQSTEDVFPQGLPDEYAFVTTFRFRKTSRKEDWYIWQVIDQYSIPQVSIRLDGENKAVEYNAVGAMKDAVRVVFRGSRVNDLFDRDWHKMALSIQAQNVSLHIDCALVQTLPIEERENIDIQGKTVIGKRLYDSVPIDFDLQRIVIYCDSRHAELETCCDIPSGPCQVTVVTEPPPPPPPQRPPTPGSEQIGFLKTINCSCPAGEKGEMGVAGPMGLPGPKGDIGAIGPVGAPGPKGEKGDVGIGPFGQGEKGEKGSLGLPGPPGRDGSKGMRGEPGELGEPGLPGEVGMRGPQGPPGLPGPPGRVGAPGLQGERGEKGTRGEKGERGLDGFPGKPGDTGQQGRPGPSGVAGPQGEKGDVGPAGPPGVPGSVVQQEGLKGEQGAPGPRGHQGAPGPPGARGPIGPEGRDGPPGLQGLRGKKGDMGPPGIPGLLGLQGPPGPPGVPGPPGPGGSPGLPGEIGFPGKPGPPGPTGPPGKDGPNGPPGPPGTKGEPGERGEDGLPGKPGLRGEIGEQGLAGRPGEKGEAGLPGAPGFPGVRGEKGDQGEKGELGLPGLKGDRGEKGEAGPAGPPGLPGTTSLFTPHPRMPGEQGPKGEKGDPGLPGEPGLQGRPGELGPQGPTGPPGAKGQEGAHGAPGAAGNPGAPGHVGAPGPSGPPGSVGAPGLRGTPGKDGERGEKGAAGEEGSPGPVGPRGDPGAPGLPGPPGKGKDGEPGLRGSPGLPGPLGTKAACGKVRGSENCALGGQCVKGDRGAPGIPGSPGSRGDPGIGVAGPPGPSGPPGDKGSPGSRGLPGFPGPQGPAGRDGAPGNPGERGPPGKPGLSSLLSPGDINLLAKDVCNDCPPGPPGLPGLPGFKGDKGVPGKPGREGTEGKKGEAGPPGLPGPPGIAGPQGSQGERGADGEVGQKGDQGHPGVPGFMGPPGNPGPPGADGIAGAAGPPGIQGSPGKEGPPGPQGPSGLPGIPGEEGKEGRDGKPGPPGEPGKAGEPGLPGPEGARGPPGFKGHTGDSGAPGPRGESGAMGLPGQEGLPGKDGDTGPTGPQGPQGPRGPPGKNGSPGSPGEPGPSGTPGQKGSKGENGSPGLPGFLGPRGPPGEPGEKGVPGKEGVPGKPGEPGFKGERGDPGIKGDKGPPGGKGQPGDPGIPGHKGHTGLMGPQGLPGENGPVGPPGPPGQPGFPGLRGESPSMETLRRLIQEELGKQLETRLAYLLAQMPPAYMKSSQGRPGPPGPPGKDGLPGRAGPMGEPGRPGQGGLEGPSGPIGPKGERGAKGDPGAPGVGLRGEMGPPGIPGQPGEPGYAKDGLPGIPGPQGETGPAGHPGLPGPPGPPGQCDPSQCAYFASLAARPGNVKGP
Protein: Seipin (Bernardinelli-Seip congenital lipodystrophy type 2 protein) (Q96G97)
Organism: Homo sapiens (Human)
Function: Plays a crucial role in the formation of lipid droplets (LDs) which are storage organelles at the center of lipid and energy homeostasis. In association with LDAF1, defines the sites of LD formation in the ER. Also required for growth and maturation of small nascent LDs into larger mature LDs. Mediates the formation and/or stabilization of endoplasmic reticulum-lipid droplets (ER-LD) contacts, facilitating protein and lipid delivery from the ER into growing LDs. Regulates the maturation of ZFYVE1-positive nascent LDs and the function of the RAB18-ZFYVE1 complex in mediating the formation of ER-LD contacts. Binds anionic phospholipids including phosphatidic acid. Plays an important role in the differentiation and development of adipocytes (By similarity).
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:14981520, ECO:0000269|PubMed:16574104, ECO:0000269|PubMed:18458148, ECO:0000269|PubMed:27879284, ECO:0000269|PubMed:30901948, ECO:0000269|PubMed:31708432}; Multi-pass membrane protein {ECO:0000255}. Lipid droplet {ECO:0000269|PubMed:27879284, ECO:0000269|PubMed:30970241}. Note=Localizes at endoplasmic reticulum-lipid droplets (ER-LD) contact sites. {ECO:0000269|PubMed:27879284}.
Interaction partners:
- 1-acyl-sn-glycerol-3-phosphate acyltransferase beta
- Lipid droplet assembly factor 1
- Caveolae-associated protein 1
- Caveolin-1
- Transmembrane protein 19
- Prelamin-A/C
- CAAX prenyl protease 1 homolog
- Carbonic anhydrase-related protein 10
- Glycerol-3-phosphate acyltransferase 4
- Glycine--tRNA ligase
Sequence:
MVNDPPVPALLWAQEVGQVLAGRARRLLLQFGVLFCTILLLLWVSVFLYGSFYYSYMPTVSHLSPVHFYYRTDCDSSTTSLCSFPVANVSLTKGGRDRVLMYGQPYRVTLELELPESPVNQDLGMFLVTISCYTRGGRIISTSSRSVMLHYRSDLLQMLDTLVFSSLLLFGFAEQKQLLEVELYADYRENSYVPTTGAIIEIHSKRIQLYGAYLRIHAHFTGLRYLLYNFPMTCAFIGVASNFTFLSVIVLFSYMQWVWGGIWPRHRFSLQVNIRKRDNSRKEVQRRISAHQPGPEGQEESTPQSDVTEDGESPEDPSGTEGQLSEEEKPDQQPLSGEEELEPEASDGSGSWEDAALLTEANLPAPAPASASAPVLETLGSSEPAGGALRQRPTCSSS
Protein: Verruculogen synthase (EC 1.14.11.38) (Fumitremorgin biosynthesis protein F) (Q4WAW9)
Organism: Aspergillus fumigatus (strain ATCC MYA-4609 / CBS 101355 / FGSC A1100 / Af293) (Neosartorya fumigata)
Function: Verruculogen synthase; part of the gene cluster that mediates the biosynthesis of fumitremorgins, indole alkaloids that carry not only intriguing chemical structures, but also interesting biological and pharmacological activities. The biosynthesis of fumitremorgin-type alkaloids begins by condensation of the two amino acids L-tryptophan and L-proline to brevianamide F, catalyzed by the non-ribosomal peptide synthetase ftmA. Brevianamide F is then prenylated by the prenyltransferase ftmPT1/ftmB in the presence of dimethylallyl diphosphate, resulting in the formation of tryprostatin B. The three cytochrome P450 monooxygenases, ftmP450-1/ftmC, ftmP450-2/ftmE and ftmP450-3/FtmG, are responsible for the conversion of tryprostatin B to 6-hydroxytryprostatin B, tryprostatin A to fumitremorgin C and fumitremorgin C to 12,13-dihydroxyfumitremorgin C, respectively. The putative methyltransferase ftmMT/ftmD is expected for the conversion of 6-hydroxytryprostatin B to tryprostatin A (Probable). FtmPT2/FtmH catalyzes the prenylation of 12,13-dihydroxyfumitre-morgin C in the presence of dimethylallyl diphosphate, resulting in the formation of fumitremorgin B. Fumitremorgin B is further converted to verruculogen by ftmOx1/ftmF via the insertion of an endoperoxide bond between the two prenyl moieties. In some fungal species, verruculogen is further converted to fumitremorgin A, but the enzymes involved in this step have not been identified yet (Probable).
Interaction partners:
- 12-alpha,13-alpha-dihydroxyfumitremorgin C prenyltransferase
Sequence:
MTVDSKPQLQRLAADADVDRMCRLLEEDGAFILKGLLPFDVVESFNRELDVQMAIPPPKGERLLADKYPPHFKYVPNVATTCPTFRNTVLINPVIHAICEAYFQRTGDYWLSAAFLREIESGMPAQPFHRDDATHPLMHYQPLEAPPVSLSVIFPLTEFTEENGATEVILGSHRWTEVGTPERDQAVLATMDPGDVLIVRQRVVHAGGGNRTTAGKPRRVVLAYFNSVQLTPFETYRTMPREMVESMTVLGQRMLGWRTMKPSDPNIVGINLIDDKRLENVLQLKAADSPA
Protein: E3 ubiquitin-protein ligase TRIM7 (EC 2.3.2.27) (Glycogenin-interacting protein) (Tripartite motif-containing protein 7) (Q923T7)
Organism: Mus musculus (Mouse)
Function: E3 ubiquitin-protein ligase that have both tumor-promoting and tumor-suppressing activities and functions in several biological processes including innate immunity, regulation of ferroptosis as well as cell proliferation and migration. Acts as an antiviral effector against multiple viruses by targeting specific viral proteins for ubiquitination and degradation including norovirus NTPase protein. Mechanistically, recognizes the C-terminal glutamine-containing motif generated by viral proteases that process the polyproteins and trigger their ubiquitination and subsequent degradation. Mediates 'Lys-63'-linked polyubiquitination and stabilization of the JUN coactivator RNF187 in response to growth factor signaling via the MEK/ERK pathway, thereby regulating JUN transactivation and cellular proliferation (By similarity). Promotes the TLR4-mediated signaling activation through its E3 ligase domain leading to production of pro-inflammatory cytokines and type I interferon. Also plays a negative role in the regulation of exogenous cytosolic DNA virus-triggered immune response. Mechanistically, enhances the 'Lys-48'-linked ubiquitination of STING1 leading to its proteasome-dependent degradation. Mediates the ubiquitination of the SIN3-HDAC chromatin remodeling complex component BRMS1. Modulates NCOA4-mediated ferritinophagy and ferroptosis in glioblastoma cells by ubiquitinating NCOA4, leading to its degradation.
Subcellular location: Nucleus {ECO:0000250|UniProtKB:Q9C029}. Cytoplasm {ECO:0000250|UniProtKB:Q9C029}. Golgi apparatus {ECO:0000250|UniProtKB:Q9C029}.
Interaction partners:
- Glycogenin-1
Sequence:
MATVGPRTGPNAGAEALALAAELQGEATCSICLEFFREPVSVECGHSFCRACIMRCWERPGAGTGTATRTLPCPLPCPQCREPARPSQLRPNRQLAAVVSLLRRFSLPPTAPGERGTPAVPARAAAARCSQHGEQLKLYCQDDGRAICVVCDRAREHRSHAVLPLEEAVQEAKELLDSRLRALKKVLEDYEAFRSTEERESKELLKQMAAEKEKVGAEFQALRAFLVEQEGRLLSRLEVLSREVTQKQNENLAQLEGEITQLSKLSGQIQETAQKPDLDFLQEFKSTLSKCSSVPSSKPTTVSSEMKNKVWNVSLKSFVLKGLLKKFKEDLQGELEKEEKVELTLDPDTANPRLILSLDLKSVRLGQRAQDLPNHPRRFDTNTRVLASCGFSSGRHHWEVEVGSKDGWAFGVARESVRRKGLTPFTPEEGVWAMQLNNGQYWAVTSPERTQLNCGHLSRVRVALDLEVGAVSFYAVEDMRHLYTFRVNFQERVFPLFSVCSTGTYLRIWP
Protein: Myomesin 2 (Q14BI5)
Organism: Mus musculus (Mouse)
Interaction partners:
- Myozenin-1
- Titin
- Alpha-actinin-3
- Troponin T, fast skeletal muscle
- Creatine kinase S-type, mitochondrial
- Telethonin
- Nebulin-related-anchoring protein
- Small muscular protein
- Calsequestrin-1
- Phosphoglycerate mutase 2
Sequence:
MSLVAVPFYQKRHKHFDQSYRNIQTRYLLDQYALKKQATTQSSSQRSLTERSSSKRASSQSSAGAMTCRLCAKRVSASEEEEVENENRYRSQAASYGEAKRQRFLSELAQLEENVHLARSQARDKLDKYFMEQTVEDNLAWERHSFEDRMSRAPEILVRLRSHTIWERMSVRLCFTVQGFPTPVVQWYKDGSLICQAGEPGKYRIESRYGVHTLEINRANFEDTATYSAVATNSHGQVSTNAAVVVRRYRGEEEPFHSVGLPIGLPLSSVIPYTHFDVQFLEKFGVTFRREGETVTLKCTLLVTPDLKRVQPRAEWYRDDVLLKESKWTKMFFGEGQASLSFSHLNKDDEGLYTLRIVSRGGVSDHSAFMFVRDADPLVTGAPGAPMDLQCHDANRDYVIVTWKPPNTTTESPVIGYFIDKCEVGTNNWVQCNDAPVKICKYPVTGLFEGRSYVFRVRAVNNAGISRPSRISDAVAALDPVDLRRLQAIHLEGEKEIVIYQDDLEGDVQIPGPPTNVQASEVSRNYVVLSWDPPSPRGKDPLMYFIEKSAVGSGSWQRVNAQTAVRSPRYAVFDLAEGKSYVFRVLSANKHGLSDPSEITPPIQAQDMIVVPSAPGRVLASRNTKTSVVVQWDRPKHEEDLLGYYVDCCVAGTNMWEPCNHKPIGYNRFVVHGLTTGEQYIFRVKAVNAVGTSENSQESEVIKVQAALTVPSHPYGITLLNCDGHSMTLGWKVPKFSGGSAIIGYYLDKREVHHKNWHEVNSSPVKERILTVEGLTEGSLYEFKIAATNLAGIGQPSDPSEHFKCEAWTDPEPGPAYDLTFCEVRDTSLVILWKAPVYSGSSPVSGYFVDFKEEDSGEWKTTSEAATPNRYLKVCDLQQGKTYVFRIRAVNASGPGKPSDTSEPVLVEARPGTKEISAGVDEEGNIYLGFDCQEMTDASQFTWCKAYEEIADEERFEVHTEGDHSKLYFKNPDKEDLGTYSVSVSDTDGVSSSFVLDEEELERLMALSNEIKNPTIPLKSELAYEIFDKGQVRFWLQAEHLSPDASFRFIINDREVSDSDTHRIKCDRSTGMIEMVMDRFTIENEGTYTVQIQDGKAKNQSSLVLIGDAFKAVLEEAEFQRKEFLRKQGPHFAEYLHWDVTEECEVRLVCKVANTKRETVFKWLKDDVLYETETPPDLEKGVCELLIPKLSKKDHGEYKATLKDDRGQDVSVLEVGGKVYEDMILAMSRVCGASASPLKVLCTPEGIRLQCFMKYFTEEMKVSWYHKEAKISSSEHMRIGGSEEMAWLQICEPTEKDKGKYTFEIFDGKDSHQRSLDLSGQAFDEAYAEFQQLKAAAFAEKNRGKVIGGLPDVVTIMEGKTLNLTCTVFGNPDPEVVWFKNDKDIELSEHFLVKMEQSKYVSLTIQGVTAEDSGKYSINVKNKYGGEKIDVTVSVYKHGEKIPDISPPQQAKPKLIPASTSSD
Protein: Probable disease resistance protein At5g66890 (Q9FKZ2)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Possible disease resistance protein.
Interaction partners:
- Powdery mildew resistance protein, RPW8 domain-containing protein
- Disease resistance protein
- Protein DA1-related 5
- ADP-ribosyl cyclase/cyclic ADP-ribose hydrolase
- Disease resistance protein ADR2
Sequence:
MNSNSIQSFDALPHNLRECFLDMASFLEDQRIIASTIIDLWSASYGKEGMNNLQDLASRNLLKLLPIGRNEYEDGFYNELLVKQDNVLREFAINQCLKESSSIFERKRLNLEIQDNKFPNWCLNPKQPIVINASLFSISTDDSFASSWFEMDCPNVEALVLNISSSNYALPNFIATMKELKVVIIINHGLEPAKLTNLSCLSSLPNLKRIRFEKVSISLLDIPKLGLKSLEKLSLWFCHVVDALNELEDVSETLQSLQEIEIDYCYNLDELPYWISQVVSLKKLSVTNCNKLCRVIEAIGDLRDLETLRLSSCASLLELPETIDRLDNLRFLDVSGGFQLKNLPLEIGKLKKLEKISMKDCYRCELPDSVKNLENLEVKCDEDTAFLWKILKPEMKNLTITEEKTEHNLNLLQLF
Protein: Transcriptional activator POG1 (Promoter of growth protein 1) (P40473)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Transcriptional activator which promotes cell cycle recovery with CLN2, after pheromone induced G1 arrest, probably inhibiting the ability of STE20 to activate the pheromone response pathway. Binds the promoters of genes that function in cell cycle regulation, cytoskeletal organization, and spindle assembly. May also be involved in stress-resistance.
Subcellular location: Nucleus {ECO:0000269|PubMed:14562095}.
Interaction partners:
- Protein GTS1
Sequence:
MKQEPHRQSEEKEKPKGPMAVEREQHTSLSSGTTVTASTGDESTNSRPVESSQTEKSLSLRIRILKQLGFDDIQELNACDTGLVEQFLNVRLINDTKELEKIRESNLAKLNQIIDKCMESDKISDSTLNKILDMSMNRDTNNDNNNHLTIPSPITTKKRKINASELASPRGHRRYRSDIPTVSEVETGVGYPQIHQQPGAYTLPMPANQWMSNPYMQPPQPQVQQIMPQYLYPPGMGPQAQLPTMSSNSESQTPVMSSQFLSLNQHGLYQQNIGAHPVMSMGPQANIYGQQHQLQPGQERDQSRKSFSHRRSQSANISMANFRSPMRNPQPASSQRPVNFLIHTPKHPPPT
Protein: V(D)J recombination-activating protein 1 (EC 2.3.2.27) (EC 3.1.-.-) (Q99NN7)
Organism: Rattus norvegicus (Rat)
Subcellular location: Nucleus {ECO:0000256|RuleBase:RU366024}.
Interaction partners:
Sequence:
DYVSGPFTVVVKESCDGMGDVSEKHGSGPAVPEKAVRFSFTVMRVTVEHGSQNVKIFEEPKPNSELCCKPLCLMLADESDHETLTAILSPLIAEREAMKSSELLLEMGGIPRTFKFIFRGTGYDEKLVREVEGLEASGSVYICTLCDATRLEASQNLVFHSITRSHAENLQRYEVWRSNPYHESVEELRDRVKGVSAKPFIETVPSIDALHCDIGNAAEFYKIFQLEIGEVYKNPNASKEERKRWQATLDKHLRKR
Protein: Cystathionine beta-lyase (A0A0H2UPA3)
Organism: Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4)
Interaction partners:
Sequence:
MTDIKTLALKYGGYTSLDKVYLDQLLAGKTDQEQLTLITPPPSVVNAYFAELYQKKSPQAATDYFAELSQELNLYNTEPSFTLENKPFIRLNLSGKSFGFCYESDGLGRIFFENEEKISDDLLFEIAQIFPHQLVFEESGKIYMKPVEDEEVISLESLTALTDLERLADGRKRLKGYSQEDLLQEAAAFSGKRYFRSENRTAMLYID
Protein: Visual system homeobox 1 (Transcription factor vsx1) (Xvsx1) (Q0P031)
Organism: Xenopus laevis (African clawed frog)
Function: Involved in the differentiation of bipolar cells, the last neurons of the retina to form. Together with other retinal homeobox proteins, acts as an effector of a cellular clock which, depending on cell cycle progression, establishes the generation of distinct retinal neuronal cell types.
Subcellular location: Nucleus {ECO:0000250|UniProtKB:O42250}.
Interaction partners:
Sequence:
MTGRDDISEAKSKGKILAPSVGNEKSGRLHGPAMRSKGFAITDLLGLEAELQPPSISLPNCEGPGVSLGGVSLTNGSLPLGLGFLCGFASQQPPGTTCLLPTHIPFLQPRPDHHYLHTSDKHKENISDDDSILGDKNDLKASSAQSKRKKRRHRTVFTAHQLDELEKSFNEAHYPDVYAREMLALKTELPEDRIQVWFQNRRAKWRKREKCWGRSSVMAEYGLYGAMVRHSIPLPESIINSAKNGLVGSCAPWLLGMHKKSVDITSKVDADDLVTERSRGESQVRDFTNPHSESHRSPRHHSHSMDISEERAIDLSSTAKQENQSSGRHNSIRDSQSDFTDSDH
Protein: PACE4A (Q62030)
Organism: Mus musculus (Mouse)
Interaction partners:
Sequence:
PRAADVARGAGAAGRHGLPPLALRPWRWLLLLALPAACSALPPPRPVYTNHWAVQVLGGPGAADRVAAAHGYLNLGQIGNLDDYYHFYHSKTFKRSTLSSRGPHTFLRMDPQVKWLQQQEVKRRVKRQARSDSLYFNDPIWSNMWYMHCTDKNSRCRSEMNVQAAWKRGYTGKNVVVTILDDGIERNHPDLAPNYDSYASYDVNGNDYDPSPRYDASNENKHGTRCAGEVAASANNSYCIVGIAYNAKIGGIRMLDGDVTDVVEAKSLGIRPNYIDIYSASWGPDDDGKTVDGPGRLAKQAFEYGIKKGRQGLGSIFVWASGNGGREGDHCSCDGYTNSIYTISVSSTTENGHKPWYLEECASTLATTYSSGAFYERKIVTTDLRQRCTDGHTGTSVSAPMVAGIIALALEANNQLTWRDVQHLLVKTSRPAHLKASDWKVNGAGHKVSHLYGFGLVDAEALVLEARKWTAVPSQHVCVATADKRPRSIPIVQVLRTTALTNACADHSDQRVVYLEHVVVRISISHPRRGDLQIHLISPSGTKSQLLAKRLLDFSNEGFTNWEFMTVHCWGEKAEGEWTLEVQDIPSQVRNPEKQGKLKEWSLILYGTAEHPYRTFSSHQSRSRMLELSVPEQEPPKAAGQPPQAETPEDEEEYTGVCHPECGDKGCDGPNADQCLNCVHFSLGNSKTNRKCVSECPLGYFGDAAARRCRRCHKGCETCTGRSPAQCLSCRRGFYHHQETNTCVTLCPAGLYADESQRLCLRCHPSCQKCVDEPEKCTVCKEGFSLARGSCIPDCEPGTYFDSELVKCGECHHTCRTCVGPSREECIHCAKSFHFQDWKCVPACGEGFYPEEMPGLPHKVCRRCEENCLSCEGSSRNCSRCKAGFTQLGTSCITNHTCSNADETFCEMVKSNRLCERKLFIQFCCRTCLLAG