wanglab/gogpt-training-data huggingface dataset:
Protein: G protein-coupled receptor kinase 5 (EC 2.7.11.16) (G protein-coupled receptor kinase GRK5) (Q62833)
Organism: Rattus norvegicus (Rat)
Function: Serine/threonine kinase that phosphorylates preferentially the activated forms of a variety of G-protein-coupled receptors (GPCRs). Such receptor phosphorylation initiates beta-arrestin-mediated receptor desensitization, internalization, and signaling events leading to their down-regulation. Phosphorylates a variety of GPCRs, including adrenergic receptors, muscarinic acetylcholine receptors (more specifically Gi-coupled M2/M4 subtypes), dopamine receptors and opioid receptors. In addition to GPCRs, also phosphorylates various substrates: Hsc70-interacting protein/ST13, TP53/p53, HDAC5, and arrestin-1/ARRB1. Phosphorylation of ARRB1 by GRK5 inhibits G-protein independent MAPK1/MAPK3 signaling downstream of 5HT4-receptors. Phosphorylation of HDAC5, a repressor of myocyte enhancer factor 2 (MEF2) leading to nuclear export of HDAC5 and allowing MEF2-mediated transcription. Phosphorylation of TP53/p53, a crucial tumor suppressor, inhibits TP53/p53-mediated apoptosis. Phosphorylation of ST13 regulates internalization of the chemokine receptor (By similarity). Phosphorylates rhodopsin (RHO) (in vitro) and a non G-protein-coupled receptor, LRP6 during Wnt signaling (in vitro) (By similarity).
Subcellular location: Cytoplasm {ECO:0000269|PubMed:12052842}. Nucleus {ECO:0000269|PubMed:12052842}. Cell membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Note=Predominantly localized at the plasma membrane, targeted to the cell surface through the interaction with phospholipids. Nucleus localization is regulated in a GPCR and Ca(2+)/calmodulin-dependent fashion (By similarity). {ECO:0000250}.
Interaction partners:
- ARF GTPase-activating protein GIT1
- Beta-arrestin-2
- Beta-arrestin-1
- Mu-type opioid receptor
- ARF GTPase-activating protein GIT2
- NADH-ubiquinone oxidoreductase chain 1
- Beta-2 adrenergic receptor
- C-X-C chemokine receptor type 4
Sequence:
MELENIVANTVLLKAREGGGGKRKGKSKKWKEILKFPHINQCEDLRRTIDRDYYSLCDKQPIGRLLFRQFCETRPGLECYIQFLDLVAEYEITPDENLGAKGKEIMTKYLSPKSPVFIAQVGQDLVSQTEKKLLQSPCKELFSACAQSVHDYLKGDPFHEYLDSMYFDRFLQWKWLERQPVTKNTFRQYRVLGKGGFGEVCACQVRATGKMYACKRLEKKRIKKRKGESMALNEKQILEKVNSQFVVNLAYAYETKDALCLVLTIMNGGDLKFHIYNMGNPGFEEERALFYAAEILCGLEDLHRENTVYRDLKPENILLDDYGHIRISDLGLAVKIPEGDLIRGRVGTVGYMAPEVLNNQRYGLSPDYWGLGCLIYEMIEGQSPFRGRKEKVKREEVDRRVLETEEVYSPKFSEEAKSICNMLLTKDSKQRLGCQEEGAAEVKRHPFFRNMNFKRLEAGMLDPPFVPDPRAVYCKDVLDIEQFSTVKGVNLDHTDDDFYSKFSTGSVPIPWQNEMIETECFKELNVFGPNGTLSPDLNRSQPPEPPKKGLFHRLFRRQHQNNSKSSPTPKTSCNHRINSNHINSNSTGSS
Protein: Rifin (Q8IJ08)
Organism: Plasmodium falciparum (isolate 3D7)
Interaction partners:
Sequence:
MKMRYSEILFFSLSLNILITSSYAHNKNKIYIKSHTPTNTSRVLSECDMQTSNYDNDPDMKSVKENFERQTSQRFEEYEERMQEKRRKCKEQCDKDIQQIIVKDKIKKSLDEKVEKVCLKCGCGLGGVGASIGIFGAIAVSEVTKAATAAAVQNSIETGIATVVSELHDMTQSFLKVGIDIVGMINKETYRCPQALTTSIYAAKQEVCVGKIGETELVCNQLGQGGTPIWFGPKVLQATTEGIKIAKTTEDSKIALINAESSHLYSAIGYSVLAIFIIVLVMVIIYLFLRYRRKKKMNKKLQYTKLLNK
Protein: Neurotrophin 1 (Neurotrophic factor 1) (Protein spaetzle 2) (Protein spatzle 2) (B7TB45)
Organism: Drosophila melanogaster (Fruit fly)
Function: Neurotrophin which may function as a ligand for the Toll-related receptors Toll-7 and Tollo. Binds to Toll-7 and probably acts as its ligand in promoting motor axon targeting and neuronal survival in the central nervous system (CNS). Involved in synaptic targeting of ISNb/d motorneurons and also some SNa motorneurons. In larvae, involved in the negative regulation of the tracheal immune response to bacterial infection perhaps by acting as a ligand for the Toll-related receptor Tollo. May be involved in the normal development of specific neurons at the neuromuscular junction.
Interaction partners:
- Toll-like receptor 7
- RE45222p
- Protein spaetzle 4
- Toll-9, isoform A
- Toll-like receptor 6
- Toll-like receptor Tollo
Sequence:
MKAGRAFGCLFWALLYCVLYLDLVSGNSADDELMDFDFADSNDAAMEDWQLDDLEEAKKAEQAEKKLESNMLDFSVDLDEPEPEKQLPPFDWRERVLRNALAKALADEGLRQKFAEVLPILRMLSSQQRLALSALISAQMNAKKGHELKFEQVRMMFGNEKKLLLPIVFDIANLIKSSTRKYINLGSDLASSALYHTPINRREDDLTPEESQQDDQLGTIAVEVEPKKVSTEEVQLESLEDFFDEMGSEVLDPQMINEALTGDLHDNKTKTFKPENHGQRVRRSANEFVHKLTRSVPASVTEQQLLGGIAGRTIKLNTTAFQQPSSQEEEKMASSNGGQSYSEVEDLAFAGLNGTEIPLSADERLDLQRNSAEETEEPLPSPEELIAGPRYRLGKRPLPGQKSGSPIKRKRVTSSLRGRPKTAASSHKPVVTPPNKKCERFTSNMCIRTDDYPLEQIMGSIRRHKNAMSALLAEFYDKPNNNLEFSDDFDDFSLSKKRREDEGSAGGMCQSVVRYARPQKAKSASGEWKYIVNTGQHTQTLRLEKCSNPVESCSYLAQTYRSHCSQVYNYHRLLSWDKVRGLHVDIFKVPTCCSCQVDGYRQQFPPLSSIQAKDYSPQSPVINHSHNGYSTINEEDLDYAEESEEDELGLRYPSFNNRETNELYSSSNKVRVKLPGISSSVGPYLSPPDDDEDRYGGYKSSSSSSKKYYSQVSRRRPQHSEARLDLDLAPSETHSDQEPPPPQHHQHHHLQYHRPQEELPSAYDFHRPQVYQPEREQLPLVRDPALSPVSAPVLASPAPPLPMPPMPIKQVPSHHQAHHQQPHHHLHQSTGKVAANRDPASMHHQPPRRPTQQWLPGQRRPFRPSAPLSGSGISRRHYHNRRQSIQ
Protein: Meiotically up-regulated gene 24 protein (O13674)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Has a role in meiosis.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16823372}.
Interaction partners:
- RNA-binding protein mde7
- Serine/threonine-protein kinase oca2
- Meiotically up-regulated gene 28 protein
- Meiotically up-regulated gene 60 protein
- Meiotically up-regulated gene 133 protein
- Meiotically up-regulated gene 112 protein
Sequence:
MAIMHKIGCAGSEVETDRVLEKDQANNGHFVDSDCCFQETGSTGTANSICTLNDSEDDNSSLNSVDNNECTNLDCGGKKHKNLSPNPSFHVNINAAEFIPKSHNGYAPKSMNPPPEQLDSPCYPHFDQDSSSVIYPSPPSTYYPNMYVSANTFIPMPYAHYTDNMYHAKPVNRPNFLPREGTPPPFAQQPAEQFSPFNSEYESLLDFRALILGNLPVDYKISELLSLIHSGPLEKIQSNPGKRRIIITFLDSADAFFFYERYHPRGFIFHGRPLKLTFARPSPLPESIQNFCSNTAASRNVFIGNLPSSYHEKEIEEAFGKFGKIEHIKILSKKNIAFVHFLNIRDAIKVVRTLSCDPDYHSWRIFFGSDRCANHPPSFDERSCFTSKQNPDTTSDRCRQQESKDNGNRTVFLGNLHTKTKGHEICDLIRHGGLQDFHYIPEKHICFVTFITYSAANAFHDYLAEEEVLLHGRRIKVGWGKESGPLPRVLEDSILMGASRNVYFSHISDSLTTEELELILRQYGEIESIKYLKNRSSGFVAYTNISNAMKAVNGLPIHPLFKKSKIRYAPDRCEQELQKSKSNSPIQQNVPLQQFITPPFSYPVAYCPAIPPGSDPILNFGIQYQPFIPFTAVPSFPFNCNVPNYPQTSDHEND
Protein: Outer membrane channel protein CpnT (Channel protein with necrosis-inducing toxin) [Cleaved into: N-terminal channel domain; Tuberculosis necrotizing toxin (TNT) (NAD(+) glycohydrolase) (EC 3.2.2.5)] (O05442)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: Has a dual function in uptake of nutrients and induction of host cell death. The N-terminal domain (NTD) forms an outer membrane channel and is used for uptake of nutrients across the outer membrane. The secreted C-terminal toxic domain (TNT) acts as a glycohydrolase, which hydrolyzes the essential cellular coenzyme NAD(+) in the cytosol of infected macrophages, leading to necrotic host cell death. Both functions are required for survival, replication and cytotoxicity of M.tuberculosis in macrophages.
Subcellular location: [N-terminal channel domain]: Cell outer membrane {ECO:0000269|PubMed:24753609}.; SUBCELLULAR LOCATION: [Tuberculosis necrotizing toxin]: Secreted {ECO:0000269|PubMed:24753609}. Cell surface {ECO:0000269|PubMed:24753609}. Host cytoplasm, host cytosol {ECO:0000269|PubMed:26237511}. Note=Secreted into the cytosol of infected macrophages while the bacteria are still confined to the phagosome. Access to the macrophage cytosol depends on the ESX-1 / type VII secretion system (T7SS). {ECO:0000269|PubMed:26237511}.
Interaction partners:
- Immunity factor for TNT
- ESAT-6-like protein EsxE
- ESAT-6-like protein EsxF
- Pullulanase
- ESX-4 secretion system protein eccD4
- Uncharacterized glycosidase Rv0584
- Hypothetical alanine and valine rich protein
- Sphingomyelinase
- Probable transcriptional regulatory protein
- Uncharacterized protein Rv1359
Sequence:
MAPLAVDPAALDSAGGAVVAAGAGLGAVISSLTAALAGCAGMAGDDPAGAVFGRSYDGSAAALVQAMSVARNGLCNLGDGVRMSAHNYSLAEAMSDVAGRAAPLPAPPPSGCVGVGAPPSAVGGGGGAPKGWGWVAPYIGMIWPNGDSTKLRAAAVAWRSAGTQFALTEIQSTAGPMGVIRAQQLPEAGLIESAFADAYASTTAVVGQCHQLAAQLDAYAARIDAVHAAVLDLLARICDPLTGIKEVWEFLTDQDEDEIQRIAHDIAVVVDQFSGEVDALAAEITAVVSHAEAVITAMADHAGKQWDRFLHSNPVGVVIDGTGQQLKGFGEEAFGMAKDSWDLGPLRASIDPFGWYRSWEEMLTGMAPLAGLGGENAPGVVESWKQFGKSLIHWDEWTTNPNEALGKTVFDAATLALPGGPLSKLGSKGRDILAGVRGLKERLEPTTPHLEPPATPPRPGPQPPRIEPPESGHPAPAPAAKPAPVPANGPLPHSPTESKPPPVDRPAEPVAPSSASAGQPRVSAATTPGTHVPHGLPQPGEHVPAQAPPATTLLGGPPVESAPATAHQPQWATTPAAPAAAPHSTPGGVHSTESGPHGRSLSAHGSEPTHDGASHGSGHGSGSEPPGLHAPHREQQLAMHSNEPAGEGWHRLSDEAVDPQYGEPLSRHWDFTDNPADRSRINPVVAQLMEDPNAPFGRDPQGQPYTQERYQERFNSVGPWGQQYSNFPPNNGAVPGTRIAYTNLEKFLSDYGPQLDRIGGDQGKYLAIMEHGRPASWEQRALHVTSLRDPYHAYTIDWLPEGWFIEVSEVAPGCGQPGGSIQVRIFDHQNEMRKVEELIRRGVLRQ
Protein: Transferrin 2 (Melanotransferrin) (Q9VTZ5)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Apicolateral cell membrane {ECO:0000269|PubMed:20935638}; Lipid-anchor, GPI-anchor {ECO:0000269|PubMed:20935638}. Cell junction, septate junction {ECO:0000269|PubMed:20935638}. Note=At embryonic stage 13, before septate junction formation, localizes evenly along the lateral and basal epithelial cell membranes (PubMed:20935638). Between stages 13 and 16, during septate junction maturation, enters and traffics through early and recycling endosomes; binding to Fe(3+) is required for Tsf2 endocytosis (PubMed:20935638). At embryonic stage 16, when the septate junctions are matured, specifically localizes to the apicolateral epithelial cell membranes (PubMed:20935638). {ECO:0000269|PubMed:20935638}.
Interaction partners:
- Contactin
- LD23292p
- LD32918p
- LD42595p
- Lachesin
Sequence:
MASSLVFVALVGALCFTLANAQHHYDEHKTTRMVWCTKSQAEQYKCQNLTVAIERDRALFDEVFLNLTCFMAYSADECIHHIDREKAHITTLDAGDVFTAGRYNSLIPIMQEKLEGGFADYQSVAVIKKGSLPDLNNLRDMRNKRVCFPWVGSLAGWIVPIHTLQREGGMEVVDCNNQVKTAASYFNNSCAVYSLSDKHNPIGDNSDKLCTLCTGKIPGGRCSSADPYFGYEGAFKCLLEKGDVAFLRHSTVNEMLQTTEFKNIAPDTFELLCRDGRRASINDYRQCNWGQVPADAIVTSSARSFSDRKQYQQFLKRIAELYSDGTRDDQSRQGGQSFNSRNNINDQNAYGQFDNNDPYRTQNQYDQYRSERLDSSFAEERNQQDGTNTSILYEKFRIFESKRYGKPNLLFQDSSRALTVIPEDDQSFTKYLGPAINFIYGIRECPVPAMTLCVTSENELDKCIKMRTALKAHLLKPELICKKMHSHINCMQFIEAGKADISVFDAGDVYTGGLNYDLVPFMSEVYNLGEPEYYVVAVAKEDDPDTELTYLKGKNTCHTGINTAAGWTYPMALFISNGWIRPYGCDSVRAAAEYFTKSCVPGAISNEYNTGVPYDSMCDLCHGTSYRYCRRDASEEYYGHTGAFRCLVEGGGHVAFMKHTTVMESTGGKRKEWWARNALNDDFELLCTDGTRAEIQDYKRCNLGKVKANAVVTRGGVNYNETQMNAYINLLTYAQQLYGRKEVDAFSFSMFSSPIGHYDLIFQDATRQLQVIPPNKRRYDAYLGSDFMRARRITDCYAGASQLALSVGLLLVGSLVAML
Protein: Urokinase plasminogen activator surface receptor (U-PAR) (uPAR) (CD antigen CD87) (Q05588)
Organism: Bos taurus (Bovine)
Function: Acts as a receptor for urokinase plasminogen activator. Plays a role in localizing and promoting plasmin formation. Mediates the proteolysis-independent signal transduction activation effects of U-PA.
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:P49616}; Lipid-anchor, GPI-anchor {ECO:0000250|UniProtKB:P49616}.
Interaction partners:
- Urokinase-type plasminogen activator
- Vitronectin
- Plasminogen activator inhibitor 1
- Plasminogen
- Tissue-type plasminogen activator
- GPI inositol-deacylase
- Serpin domain-containing protein
- Matrix metalloproteinase-9
- Receptor protein-tyrosine kinase
Sequence:
MGQPLLLLLLVYTYIPGSWGLRCLQCENTTSCSVEECTPGQDLCRTTVLSVWEGGNEMNVVRKGCTHPDKTNRSMSYRAADQIITLSETVCRSDLCNKPNPGRDATVSRNRYLECASCSSTDLSCERGWDQTMQCLKSRDQCVDVITHRSLKENPGDERHIRGCGILPGCPGPTGFHNNHTFHFLRCCNTTKCNAGSVLELQNLPPNGLQCYSCEGNGAHRCSSEETFLIDCRGPMNQCLEATGTKGLRNPSYTIRGCAAPSWCQSLHVAEAFDLTHVNVSCCTGSGCNHPARDDQPGKGGAPKTSPAHLSFFVSLLLTARLWGATLLCT
Protein: EPH receptor A6 (E7EU71)
Organism: Homo sapiens (Human)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004479}.
Interaction partners:
Sequence:
MQFPSPPAARSSPAPQAASSSEAAAPATGQPGPSCPVPGTSRRGRPGTPPAGRVEEEEEEEEEDVDKDPHPTQNTCLRCRHFSLRERKREPRRTMGGCEVREFLLQFGFFLPLLTAWPGDCSHVSNNQVVLLDTTTVLGELGWKTYPLNGWDAITEMDEHNRPIHTYQVCNVMEPNQNNWLRTNWISRDAAQKIYVEMKFTLRDCNSIPWVLGTCKETFNLFYMESDESHGIKFKPNQYTKIDTIAADESFTQMDLGDRILKLNTEIREVGPIERKGFYLAFQDIGACIALVSVRVFYKKCPFTVRNLAMFPDTIPRVDSSSLVEVRGSCVKSAEERDTPKLYCGADGDWLVPLGRCICSTGYEEIEGSCHACRPGFYKAFAGNTKCSKCPPHSLTYMEATSVCQCEKGYFRAEKDPPSMACTRPPSAPRNVVFNINETALILEWSPPSDTGGRKDLTYSVICKKCGLDTSQCEDCGGGLRFIPRHTGLINNSVIVLDFVSHVNYTFEIEAMNGVSELSFSPKPFTAITVTTDQDGKFHCCSLKTDP
Protein: Vacuolar protein sorting-associated protein 41 homolog (A0A8I6AV86)
Organism: Rattus norvegicus (Rat)
Subcellular location: Endosome membrane {ECO:0000256|PIRNR:PIRNR028921}; Peripheral membrane protein {ECO:0000256|PIRNR:PIRNR028921}. Late endosome membrane {ECO:0000256|PIRNR:PIRNR028921}; Peripheral membrane protein {ECO:0000256|PIRNR:PIRNR028921}. Early endosome membrane {ECO:0000256|PIRNR:PIRNR028921}; Peripheral membrane protein {ECO:0000256|PIRNR:PIRNR028921}. Lysosome membrane {ECO:0000256|PIRNR:PIRNR028921}; Peripheral membrane protein {ECO:0000256|PIRNR:PIRNR028921}. Golgi apparatus, trans-Golgi network {ECO:0000256|ARBA:ARBA00004601, ECO:0000256|PIRNR:PIRNR028921}. Cytoplasmic vesicle, clathrin-coated vesicle {ECO:0000256|PIRNR:PIRNR028921}. Late endosome {ECO:0000256|ARBA:ARBA00004603}.
Interaction partners:
Sequence:
MNIEEQASCGMVEHLLAMCPGAAYPGLESPVKINQISLDESGEHMGVCSEDGKLQVFGLYSGEEFHETFDCPIKIVAVHPQFVRSSCKQFVTGGKKLLLFERTWMNRWKSSVLHEGEGNIRSVKWRGHLIAWANNMGVKIFDITSKQRITNVPRDDISLRPDMYPCSLCWKDAVTLIIGWGTSIKICSVKERHASEMRDLPSRYVEIVSQFETEFYISGLAPLCDQLVVLSYVKEVSEKTEREYCARPRLDIIQPLPETCEEISSDALTVRGFQENECRDYHLEYSEGESLFYVVSPRDVVVAKERDQDDHIDWLLEKKKYEEALMAAEISHRNIKRHKILEIGLAYVNHLVERGEYDMAARKCQKILGKNASLWEYEVYKFKEIGQLKAISPYLPRGDPVLKPLIYEMILHEFLESDYEGFATLIREWPGDLYNNSVIVQAVRDHLKKDSQNKTLLKTLAELYTYDKNYGNALEIYLTLRHKDVFQLIHKHNLFSSIKDKIVLLMDFDSEKAVDMLLDNEDKISIKKVVEELEDRPELQHVYLHKLFKRDHHKGQRYHEKQISLYAEYDRPNLLPFLRDSTHCPLEKALEICQQRNFVEETVYLLSRMGNSRSALKMIMEELHDVDKAIEFAKEQDDGELWEDLILYSIDKPPFITGLLNNIGTHVDPILLIHRIKEGMEIPNLRDSLVKILQDYNLQILLREGCKKILVADSLSLLKKMHRTQMKGVLVDEENICESCLSPILPTDAAKPFSVVVFHCRHMFHKECLPMPSLNAPAQYCNICSAKNRGPGSAILEMKK
Protein: Gaegurin-LK1 (C3RT17)
Organism: Limnonectes kuhlii (Kuhl's Creek frog) (Rana kuhlii)
Function: Has antimicrobial activity against Gram-positive bacteria S.aureus ATCC 2592 (MIC=5.0 uM), S.aureus ATCC 43300 (MIC=10.0 uM) and B.subtilis (MIC=20.0 uM), against Gram-negative bacteria E.coli ML-35P (MIC=50.0 uM), P.aeruginosa PA01 (MIC=10.0 uM) and P.aeruginosa ATCC 27853 (MIC=5.0 uM) and against fungus C.albicans ATCC 2002 (MIC=10.0 uM).
Subcellular location: Secreted {ECO:0000255, ECO:0000269|PubMed:23054029}.
Interaction partners:
Sequence:
MFTMKKSLLFLFFLGTINLSLCEEERNAEEEKRDGDDEMDVEVQKRFIGPVLKMATSILPTAICKGFKKC
Protein: Poly [ADP-ribose] polymerase tankyrase-2 (EC 2.4.2.30) (ADP-ribosyltransferase diphtheria toxin-like 6) (ARTD6) (Poly [ADP-ribose] polymerase 5B) (Protein poly-ADP-ribosyltransferase tankyrase-2) (EC 2.4.2.-) (TNKS-2) (TRF1-interacting ankyrin-related ADP-ribose polymerase 2) (Tankyrase II) (Tankyrase-2) (TANK2) (Tankyrase-like protein) (Tankyrase-related protein) (Q9H2K2)
Organism: Homo sapiens (Human)
Function: Poly-ADP-ribosyltransferase involved in various processes such as Wnt signaling pathway, telomere length and vesicle trafficking. Acts as an activator of the Wnt signaling pathway by mediating poly-ADP-ribosylation of AXIN1 and AXIN2, 2 key components of the beta-catenin destruction complex: poly-ADP-ribosylated target proteins are recognized by RNF146, which mediates their ubiquitination and subsequent degradation. Also mediates poly-ADP-ribosylation of BLZF1 and CASC3, followed by recruitment of RNF146 and subsequent ubiquitination. Mediates poly-ADP-ribosylation of TERF1, thereby contributing to the regulation of telomere length. Stimulates 26S proteasome activity.
Subcellular location: Cytoplasm. Golgi apparatus membrane; Peripheral membrane protein. Nucleus. Chromosome, telomere {ECO:0000305}. Note=Associated with the Golgi and with juxtanuclear SLC2A4/GLUT4-vesicles. Also found around the pericentriolar matrix of mitotic centromeres. During interphase, a small fraction of TNKS2 is found in the nucleus, associated with TRF1.
Interaction partners:
- Telomeric repeat-binding factor 1
- Axin-1
- SH3 domain-binding protein 2
- Hypoxia-inducible factor 1-alpha inhibitor
- Arpin
- 182 kDa tankyrase-1-binding protein
- Axin-2
- Induced myeloid leukemia cell differentiation protein Mcl-1
- E3 ubiquitin-protein ligase RNF146
- Arpin
Sequence:
MSGRRCAGGGAACASAAAEAVEPAARELFEACRNGDVERVKRLVTPEKVNSRDTAGRKSTPLHFAAGFGRKDVVEYLLQNGANVQARDDGGLIPLHNACSFGHAEVVNLLLRHGADPNARDNWNYTPLHEAAIKGKIDVCIVLLQHGAEPTIRNTDGRTALDLADPSAKAVLTGEYKKDELLESARSGNEEKMMALLTPLNVNCHASDGRKSTPLHLAAGYNRVKIVQLLLQHGADVHAKDKGDLVPLHNACSYGHYEVTELLVKHGACVNAMDLWQFTPLHEAASKNRVEVCSLLLSYGADPTLLNCHNKSAIDLAPTPQLKERLAYEFKGHSLLQAAREADVTRIKKHLSLEMVNFKHPQTHETALHCAAASPYPKRKQICELLLRKGANINEKTKEFLTPLHVASEKAHNDVVEVVVKHEAKVNALDNLGQTSLHRAAYCGHLQTCRLLLSYGCDPNIISLQGFTALQMGNENVQQLLQEGISLGNSEADRQLLEAAKAGDVETVKKLCTVQSVNCRDIEGRQSTPLHFAAGYNRVSVVEYLLQHGADVHAKDKGGLVPLHNACSYGHYEVAELLVKHGAVVNVADLWKFTPLHEAAAKGKYEICKLLLQHGADPTKKNRDGNTPLDLVKDGDTDIQDLLRGDAALLDAAKKGCLARVKKLSSPDNVNCRDTQGRHSTPLHLAAGYNNLEVAEYLLQHGADVNAQDKGGLIPLHNAASYGHVDVAALLIKYNACVNATDKWAFTPLHEAAQKGRTQLCALLLAHGADPTLKNQEGQTPLDLVSADDVSALLTAAMPPSALPSCYKPQVLNGVRSPGATADALSSGPSSPSSLSAASSLDNLSGSFSELSSVVSSSGTEGASSLEKKEVPGVDFSITQFVRNLGLEHLMDIFEREQITLDVLVEMGHKELKEIGINAYGHRHKLIKGVERLISGQQGLNPYLTLNTSGSGTILIDLSPDDKEFQSVEEEMQSTVREHRDGGHAGGIFNRYNILKIQKVCNKKLWERYTHRRKEVSEENHNHANERMLFHGSPFVNAIIHKGFDERHAYIGGMFGAGIYFAENSSKSNQYVYGIGGGTGCPVHKDRSCYICHRQLLFCRVTLGKSFLQFSAMKMAHSPPGHHSVTGRPSVNGLALAEYVIYRGEQAYPEYLITYQIMRPEGMVDG
Protein: ALG-1 (H2KY60)
Organism: Caenorhabditis elegans
Interaction partners:
Sequence:
MNGDGWQGPGRGGPHHMNGGGGGRRGGGGGMHNQRIQQNPHHGGMNRMMPHGFRPQQGQFMPQYPPPPPMGGMPDVMDINMRMDGMSLGSTPSGIPGQYGDMGPPPVQQWNQPAPFVPPPQQDDLYDPSGYGGGAGGGGGHHPSHMPPYGQRGNNQNQYGNRMQGGQGGYRGNQQRQQQQQPQQGFNMPPMMVPPGQPPFYGGNQPNHHHQQPSFAPSPFSMGGGGGGSQGGPHEQHGPGGNQNGGFGVSSSSMDDYSMWTDENDEDAKKKKSLRDKGLSGWGDADVSNSKPIRRWIVPEGQEEDFETAMERCPSHLKKKALNEEALRRRLTSENPQIVAQAQQQAEEEANAMMRIGRRPIVPSGWGDIPSEISTDKSEFDQSSSRGWDEGSISGGGSGRHPSHHQSNDNSMWNSPSVGGGQSNSETRNPFFAQHMQQQQHQQQHQPHYGGYGDNGVLDGGSLWSAAVMDGSSMVPPHPTMGVGSSASSSSIPIGMLMMSGSGNVGGGPPSSSSLLDEDGSQKKLAENLKLAVQKGHLDISLLSLPHIPPNVLDLLTEILAVIPRLDDYEDELKKLGENRPSNYDEGASKEEKESWMSKDQKNDHDKAVIGVVTAKIEVTQLSKKITEALIEAGLLPPQPQTSTSANTSTNHLNHRGGPPPGSDGGAGPSTSRSGGGGAAGGDSFNSSGGGGPPDHYYDYSFLG
Protein: Ribonuclease 7 (RNase 7) (EC 3.1.27.-) (Skin-derived antimicrobial protein 2) (SAP-2) (Q9H1E1)
Organism: Homo sapiens (Human)
Function: Exhibits a potent RNase activity. Has broad-spectrum antimicrobial activity against many pathogenic microorganisms and remarkably potent activity (lethal dose of 90% < 30 nM) against a vancomycin resistant Enterococcus faecium. Causes loss of bacterial membrane integrity. Probably contributes to urinary tract sterility. Bactericidal activity is independent of RNase activity.
Subcellular location: Secreted {ECO:0000269|PubMed:12244054, ECO:0000269|PubMed:25075772}. Note=Detected in urine. {ECO:0000269|PubMed:25075772}.
Interaction partners:
- Protein S100-A7
- Beta-defensin 103
- Defensin beta 4A
- Cathelicidin antimicrobial peptide
Sequence:
MAPARAGFCPLLLLLLLGLWVAEIPVSAKPKGMTSSQWFKIQHMQPSPQACNSAMKNINKHTKRCKDLNTFLHEPFSSVAATCQTPKIACKNGDKNCHQSHGAVSLTMCKLTSGKHPNCRYKEKRQNKSYVVACKPPQKKDSQQFHLVPVHLDRVL
Protein: Glucose-insensitive transcription protein 7 (O59709)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Involved in cyclic AMP (cAMP) pathway, possibly by participating in the assembly or the conformational activation of specific multiprotein complexes.
Interaction partners:
- Heat shock protein 90 homolog
- Adenylate cyclase
- Suppressor of kinetochore protein 1
- Adenylate cyclase activation protein git1
- Glucose receptor protein git3
- Guanine nucleotide-binding protein subunit beta
- Protein ecdysoneless homolog
- Tuberous sclerosis 1 protein homolog
- NAD reductase coq12
- Guanine nucleotide-binding protein subunit gamma
Sequence:
MGVDLSDINDSLFKLSDKLSNDLAKQRNLCIVKEPSFSIEEHIKCFTTCINTYKPFSCLKHANWALLLAKKKSDTGLIGYCQSLRGLAYYLLEQYQSSAICFGFALKHLKKEDLTKWQVQLDSMLTIVHEQQNQDTSSLIPDECPNIPELEAAKIEGDEEFLNMSLKAPEGQIEKNEEKLSNRIRYDWSQTSFSLNIDIYAKKVKDEDVSLLMEKNTLKIEIKLEDGSIFSLVLDPLYEEIVPEKSSFKLFSSKVEITLIKKVSEIKWEALVKSPANNSVNVYAKDSNHSSASGNTKNKAKDWDSLAKLADLEEDEPTGEAALANLFQNLYKNADDDTRRAMMKSYTESNGTALSTNWKDVKSKTFETKPPQGMEPKKF
Protein: Solute carrier family 15 member 2 (Peptide transporter 2) (PEPT2) (B0S6T2)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: Proton-coupled amino-acid transporter that transports oligopeptides of 2 to 4 amino acids with a preference for dipeptides.
Subcellular location: Apical cell membrane {ECO:0000250|UniProtKB:Q63424}; Multi-pass membrane protein {ECO:0000255}. Cytoplasmic vesicle, phagosome membrane {ECO:0000250|UniProtKB:Q16348}; Multi-pass membrane protein {ECO:0000255}. Cell membrane {ECO:0000305|PubMed:16317081}; Multi-pass membrane protein {ECO:0000255}. Note=Associated with the cell membrane in resting macrophages and enriched in phagocytic cups and phagosomes after particle internalization. {ECO:0000250|UniProtKB:Q16348}.
Interaction partners:
- Solute carrier family 25 member 47-A
- Putative glutathione-specific gamma-glutamylcyclotransferase 2
- Cytosolic non-specific dipeptidase
Sequence:
MGKMKDKDVDAEKYEKAQRSPKLCGTNYPVSIAFIVVNEFCERFSYYGMKAVLTLYFMNYLHWDKNLSTAIYHAFSGLCYFTPLLGALIADSWLGKFKTIIYLSIVYVIGHVVKSVGAIPDVGDSTVHIALSMVGLGLIALGTGGIKPCVAAFGGDQFDEDNIDERRKFFSIFYMSINAGSVLSTIITPILRGDVQCFGGDCYALAFGVPAALMVIALVVFISGSGLYKKSPPEGNVLVRVCKCIGFAISNRWTNSKKSPKRSHWLDWAEEKYSKRLIQEIKMVCRVLVLYIPLPMFWALFDQQGSRWTLQATRMNMDFGGGFIIKPDQMQMLNALLILVFIPIFDMGIYPLVGLCRIKLTPLKKMATGMILAALAFCAATAVEVYVIKTVVEPPPAKESLVQVYNLMDSDVTVQFPAHNVFSEPLKPYEEPSGYSSLPLTGESQLQNVVVSHNGMNYQCRLTFTERMAYSLLLHPTAQHNGSVCNLVKDHITKSETGAAYIRFINTHTENINVTVGTEEVHASANYGISRNISVPRGEYNKAVCVTDTKEYEINLGLLDFGAFYTVILSEAGNNLAVKKMEDIQANNIHIGWQIPQYVFLTAGEVMFSITGLEFSYSQAPASMKSVLQAGWLMTVAFGNVIVLIVAEGAGMEQWVEFLLFAALLVAVSIIFSIMAYFYTYVDPDQLDKLFKEDGDGGKVESSKKDELSLGDMPKQTKM
Protein: Trigger factor (TF) (EC 5.2.1.8) (PPIase) (P56420)
Organism: Helicobacter pylori (strain ATCC 700392 / 26695) (Campylobacter pylori)
Function: Involved in protein export. Acts as a chaperone by maintaining the newly synthesized protein in an open conformation. Functions as a peptidyl-prolyl cis-trans isomerase (By similarity).
Subcellular location: Cytoplasm. Note=About half TF is bound to the ribosome near the polypeptide exit tunnel while the other half is free in the cytoplasm. {ECO:0000250}.
Interaction partners:
- Large ribosomal subunit protein uL23
- Peptide deformylase
- Small ribosomal subunit protein uS7
- Large ribosomal subunit protein uL3
- Small ribosomal subunit protein uS3
- Small ribosomal subunit protein uS2
- Large ribosomal subunit protein uL2
- Small ribosomal subunit protein uS9
- Large ribosomal subunit protein uL22
- Small ribosomal subunit protein uS10
Sequence:
MNLEVKKIDTANARLSAKLSIENLEKRYDKIAQKIAQKVKIDGFRRGKVPLSLVKTRYQAQIEQDAQEEMIQEVLKNAFKELGIENKDLIGSPNLTKFEKKDTHFEIEADIGLKPTIVLDKIKECVPSVGVEVPNEEKIDERLKQLAKDYAKFVDTNTQRKAQNDDKLTIDFEGFIDNAPFEGGKAENFNLILGSKQMLEDFEKALLGMQAGEEKEFPLTFPSKYHAEHLAGKEAFFKVKLHQIQAREMLEINDELAKIVLANEENATLKLLKERVEGQLFLENKARLYNEELKEKLIENLDEKIVFDLPKTIIEQEMDLLFRNALYSMQAEEVKSLQESQEKAKEKRESFRNDATKSVKITFIIDALAKEEKIGVHDNEVFQTLYYEAMMTGQNPENLIEQYRKNNMLAAVKMAMIEDRVLAYLLDKNLPKEQQEILEKMRPNAQKIQAG
Protein: Protein unc-119 homolog A (Q1RM42)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000256|ARBA:ARBA00004300}. Cytoplasm, cytoskeleton, spindle pole {ECO:0000256|ARBA:ARBA00004647}.
Interaction partners:
- ADP-ribosylation factor-like protein 3
- ADP-ribosylation factor-like 2
- ADP-ribosylation factor-like protein 3
- Protein XRP2
- Thioredoxin reductase-like selenoprotein T1a
Sequence:
MSYSCTSTGNSQDPSSSKKSGGVNPGSCSSSNGDTGNGNNRHSIRGSKANSKPDSTEAMKVKKGCNTTDLGVPVTTEEELLANKTISPEDVLGLQKITENYLCSPEDNLYNIDFTRFKIRDMETGTVLFEITKPPSTDRGDKRDVDPNAGRFVRYQFTPAFLRLRQVGATVEFTVGDIPINNFRMIERHYFREQLLKSFDFEFGFCIPSSKNTCEHIYEFPPLSEDLIREMILHPYETQSDSFYFVDNKLVMHNKADYSYSGGP