wanglab/gogpt-training-data huggingface dataset:
Protein: Pyrin and HIN domain-containing protein 1 (Interferon-inducible protein X) (Q6K0P9)
Organism: Homo sapiens (Human)
Function: Major mediator of the tumor suppressor activity of IFN in breast cancer cells. Promotes ubiquitination and subsequent degradation of MDM2, which leads to p53/TP53 stabilization. Promotes ubiquitination and subsequent degradation of HDAC1, which in turn enhances maspin expression, and impairs invasive activity of cancer cells.
Subcellular location: [Isoform 1]: Nucleus, nucleoplasm.; SUBCELLULAR LOCATION: [Isoform 3]: Nucleus, nucleoplasm.; SUBCELLULAR LOCATION: [Isoform 5]: Nucleus. Nucleus speckle.
Interaction partners:
- Pyrin
Sequence:
MANNYKKIVLLKGLEVINDYHFRIVKSLLSNDLKLNPKMKEEYDKIQIADLMEEKFPGDAGLGKLIEFFKEIPTLGDLAETLKREKLKVANKIESIPVKGIIPSKKTKQKEVYPATPACTPSNRLTAKGAEETLGPQKRKKPSEEETGTKRSKMSKEQTRPSCSAGASTSTAMGRSPPPQTSSSAPPNTSSTESLKPLANRHATASKNIFREDPIIAMVLNATKVFKYESSENEQRRMFHATVATQTQFFHVKVLNINLKRKFIKKRIIIISNYSKRNSLLEVNEASSVSEAGPDQTFEVPKDIIRRAKKIPKINILHKQTSGYIVYGLFMLHTKIVNRKTTIYEIQDKTGSMAVVGKGECHNIPCEKGDKLRLFCFRLRKRENMSKLMSEMHSFIQIQKNTNQRSHDSRSMALPQEQSQHPKPSEASTTLPESHLKTPQMPPTTPSSSSFTKKDETHPGAQSSPANFRITSPTVAPPLSSDTSTNRHPAVP
Protein: Disrupted in schizophrenia 1 protein (Q9NRI5)
Organism: Homo sapiens (Human)
Function: Involved in the regulation of multiple aspects of embryonic and adult neurogenesis. Required for neural progenitor proliferation in the ventrical/subventrical zone during embryonic brain development and in the adult dentate gyrus of the hippocampus (By similarity). Participates in the Wnt-mediated neural progenitor proliferation as a positive regulator by modulating GSK3B activity and CTNNB1 abundance. Plays a role as a modulator of the AKT-mTOR signaling pathway controlling the tempo of the process of newborn neurons integration during adult neurogenesis, including neuron positioning, dendritic development and synapse formation (By similarity). Inhibits the activation of AKT-mTOR signaling upon interaction with CCDC88A (By similarity). Regulates the migration of early-born granule cell precursors toward the dentate gyrus during the hippocampal development. Inhibits ATF4 transcription factor activity in neurons by disrupting ATF4 dimerization and DNA-binding (By similarity). Plays a role, together with PCNT, in the microtubule network formation.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:12506198, ECO:0000269|PubMed:15797709}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:14962739, ECO:0000269|PubMed:15797709}. Mitochondrion {ECO:0000269|PubMed:12506198, ECO:0000269|PubMed:15797709}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000269|PubMed:12812986, ECO:0000269|PubMed:18955030}. Postsynaptic density {ECO:0000250|UniProtKB:Q811T9}. Note=Colocalizes with NDEL1 in the perinuclear region and the centrosome (By similarity). Localizes to punctate cytoplasmic foci which overlap in part with mitochondria (PubMed:12506198, PubMed:15797709). Colocalizes with PCNT at the centrosome (PubMed:18955030). {ECO:0000250|UniProtKB:Q811T9, ECO:0000269|PubMed:12506198, ECO:0000269|PubMed:15797709, ECO:0000269|PubMed:18955030}.
Interaction partners:
- Nuclear distribution protein nudE-like 1
- Nuclear distribution protein nudE homolog 1
- 3',5'-cyclic-AMP phosphodiesterase 4B
- 3',5'-cyclic-AMP phosphodiesterase 4A
- Pericentrin
- Glycogen synthase kinase-3 beta
- Dixin
- D
- Platelet-activating factor acetylhydrolase IB subunit beta
- Dysbindin
Sequence:
MPGGGPQGAPAAAGGGGVSHRAGSRDCLPPAACFRRRRLARRPGYMRSSTGPGIGFLSPAVGTLFRFPGGVSGEESHHSESRARQCGLDSRGLLVRSPVSKSAAAPTVTSVRGTSAHFGIQLRGGTRLPDRLSWPCGPGSAGWQQEFAAMDSSETLDASWEAACSDGARRVRAAGSLPSAELSSNSCSPGCGPEVPPTPPGSHSAFTSSFSFIRLSLGSAGERGEAEGCPPSREAESHCQSPQEMGAKAASLDGPHEDPRCLSRPFSLLATRVSADLAQAARNSSRPERDMHSLPDMDPGSSSSLDPSLAGCGGDGSSGSGDAHSWDTLLRKWEPVLRDCLLRNRRQMEVISLRLKLQKLQEDAVENDDYDKAETLQQRLEDLEQEKISLHFQLPSRQPALSSFLGHLAAQVQAALRRGATQQASGDDTHTPLRMEPRLLEPTAQDSLHVSITRRDWLLQEKQQLQKEIEALQARMFVLEAKDQQLRREIEEQEQQLQWQGCDLTPLVGQLSLGQLQEVSKALQDTLASAGQIPFHAEPPETIRSLQERIKSLNLSLKEITTKVCMSEKFCSTLRKKVNDIETQLPALLEAKMHAISGNHFWTAKDLTEEIRSLTSEREGLEGLLSKLLVLSSRNVKKLGSVKEDYNRLRREVEHQETAYETSVKENTMKYMETLKNKLCSCKCPLLGKVWEADLEACRLLIQSLQLQEARGSLSVEDERQMDDLEGAAPPIPPRLHSEDKRKTPLKVLEEWKTHLIPSLHCAGGEQKEESYILSAELGEKCEDIGKKLLYLEDQLHTAIHSHDEDLIQSLRRELQMVKETLQAMILQLQPAKEAGEREAAASCMTAGVHEAQA
Protein: Interstitial collagenase (EC 3.4.24.7) (Fibroblast collagenase) (Matrix metalloproteinase-1) (MMP-1) [Cleaved into: 22 kDa interstitial collagenase; 27 kDa interstitial collagenase] (P03956)
Organism: Homo sapiens (Human)
Function: Cleaves collagens of types I, II, and III at one site in the helical domain. Also cleaves collagens of types VII and X. In case of HIV infection, interacts and cleaves the secreted viral Tat protein, leading to a decrease in neuronal Tat's mediated neurotoxicity.
Subcellular location: Secreted, extracellular space, extracellular matrix {ECO:0000305|PubMed:2167156}.
Interaction partners:
- Metalloproteinase inhibitor 1
- Stromelysin-1
- Basigin
- Matrix metalloproteinase-9
- Metalloproteinase inhibitor 2
- 72 kDa type IV collagenase
- Proteinase-activated receptor 1
- Matrilysin
- Interleukin-1 beta
- Signal transducer and activator of transcription 3
Sequence:
MHSFPPLLLLLFWGVVSHSFPATLETQEQDVDLVQKYLEKYYNLKNDGRQVEKRRNSGPVVEKLKQMQEFFGLKVTGKPDAETLKVMKQPRCGVPDVAQFVLTEGNPRWEQTHLTYRIENYTPDLPRADVDHAIEKAFQLWSNVTPLTFTKVSEGQADIMISFVRGDHRDNSPFDGPGGNLAHAFQPGPGIGGDAHFDEDERWTNNFREYNLHRVAAHELGHSLGLSHSTDIGALMYPSYTFSGDVQLAQDDIDGIQAIYGRSQNPVQPIGPQTPKACDSKLTFDAITTIRGEVMFFKDRFYMRTNPFYPEVELNFISVFWPQLPNGLEAAYEFADRDEVRFFKGNKYWAVQGQNVLHGYPKDIYSSFGFPRTVKHIDAALSEENTGKTYFFVANKYWRYDEYKRSMDPGYPKMIAHDFPGIGHKVDAVFMKDGFFYFFHGTRQYKFDPKTKRILTLQKANSWFNCRKN
Protein: Synemin (Desmuslin) (O15061)
Organism: Homo sapiens (Human)
Function: Type-VI intermediate filament (IF) which plays an important cytoskeletal role within the muscle cell cytoskeleton. It forms heteromeric IFs with desmin and/or vimentin, and via its interaction with cytoskeletal proteins alpha-dystrobrevin, dystrophin, talin-1, utrophin and vinculin, is able to link these heteromeric IFs to adherens-type junctions, such as to the costameres, neuromuscular junctions, and myotendinous junctions within striated muscle cells.
Subcellular location: Cytoplasm, cytoskeleton. Cell junction, adherens junction. Note=There are at least two distinct SYNM subpopulations, one in which SYMN interacts with DES within the Z-lines, and another in which it interacts with both DTNA and DES at the costamere.
Interaction partners:
- Nestin
- Vinculin
- Talin-2
- Dystrobrevin alpha
- Zyxin
- Syncoilin
- Plectin
- Talin-1
- Desmin
- LIM/homeobox protein Lhx4
Sequence:
MLSWRLQTGPEKAELQELNARLYDYVCRVRELERENLLLEEELRGRRGREGLWAEGQARCAEEARSLRQQLDELSWATALAEGERDALRRELRELQRLDAEERAARGRLDAELGAQQRELQEALGARAALEALLGRLQAERRGLDAAHERDVRELRARAASLTMHFRARATGPAAPPPRLREVHDSYALLVAESWRETVQLYEDEVRELEEALRRGQESRLQAEEETRLCAQEAEALRREALGLEQLRARLEDALLRMREEYGIQAEERQRVIDCLEDEKATLTLAMADWLRDYQDLLQVKTGLSLEVATYRALLEGESNPEIVIWAEHVENMPSEFRNKSYHYTDSLLQRENERNLFSRQKAPLASFNHSSALYSNLSGHRGSQTGTSIGGDARRGFLGSGYSSSATTQQENSYGKAVSSQTNVRTFSPTYGLLRNTEAQVKTFPDRPKAGDTREVPVYIGEDSTIARESYRDRRDKVAAGASESTRSNERTVILGKKTEVKATREQERNRPETIRTKPEEKMFDSKEKASEERNLRWEELTKLDKEARQRESQQMKEKAKEKDSPKEKSVREREVPISLEVSQDRRAEVSPKGLQTPVKDAGGGTGREAEARELRFRLGTSDATGSLQGDSMTETVAENIVTSILKQFTQSPETEASADSFPDTKVTYVDRKELPGERKTKTEIVVESKLTEDVDVSDEAGLDYLLSKDIKEVGLKGKSAEQMIGDIINLGLKGREGRAKVVNVEIVEEPVSYVSGEKPEEFSVPFKVEEVEDVSPGPWGLVKEEEGYGESDVTFSVNQHRRTKQPQENTTHVEEVTEAGDSEGEQSYFVSTPDEHPGGHDRDDGSVYGQIHIEEESTIRYSWQDEIVQGTRRRTQKDGAVGEKVVKPLDVPAPSLEGDLGSTHWKEQARSGEFHAEPTVIEKEIKIPHEFHTSMKGISSKEPRQQLVEVIGQLEETLPERMREELSALTREGQGGPGSVSVDVKKVQGAGGSSVTLVAEVNVSQTVDADRLDLEELSKDEASEMEKAVESVVRESLSRQRSPAPGSPDEEGGAEAPAAGIRFRRWATRELYIPSGESEVAGGASHSSGQRTPQGPVSATVEVSSPTGFAQSQVLEDVSQAARHIKLGPSEVWRTERMSYEGPTAEVVEVSAGGDLSQAASPTGASRSVRHVTLGPGQSPLSREVIFLGPAPACPEAWGSPEPGPAESSADMDGSGRHSTFGCRQFHAEKEIIFQGPISAAGKVGDYFATEESVGTQTSVRQLQLGPKEGFSGQIQFTAPLSDKVELGVIGDSVHMEGLPGSSTSIRHISIGPQRHQTTQQIVYHGLVPQLGESGDSESTVHGEGSADVHQATHSHTSGRQTVMTEKSTFQSVVSESPQEDSAEDTSGAEMTSGVSRSFRHIRLGPTETETSEHIAIRGPVSRTFVLAGSADSPELGKLADSSRTLRHIAPGPKETSFTFQMDVSNVEAIRSRTQEAGALGVSDRGSWRDADSRNDQAVGVSFKASAGEGDQAHREQGKEQAMFDKKVQLQRMVDQRSVISDEKKVALLYLDNEEEENDGHWF
Protein: Myosin light chain 1 (Q03399)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MAPKKPEPKKEAAKPMNVKMLDFETFLPILAPAPAPAPAPAPAPAQHISRNKEQGTYEDFPEAPKEPAFDPKSVKVEGLRVFDKESNGTVIDFTADQIEEFKEAFMGAELRHVLATLGEKSLFDRTPTGEMKITYMTEAEVEQLLAGQEDGQCGDVLRALGQNPTANGCINYEAFVKHIMNAEVLRVLGKPKPEESG
Protein: DDRGK domain-containing protein 1 (A0A0A0MRX2)
Organism: Homo sapiens (Human)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004167}; Single-pass membrane protein {ECO:0000256|ARBA:ARBA00004167}.
Interaction partners:
Sequence:
MVAPVWYLVAAALLVGFILFLTRSRGRAASAGQEPLHNEELAGAGRVAQPGPLEPEEPRAGGRPRRRRDLGSRLQAQRRAQRVAWAEADENEEEAVILAQEEEGVEKPAETHLSGKIGAKKLRKLEEKQARKAQREAEEAEREERKRLESQREAEWKKEEERLRLEEEQKEEEERKAREEQAQREHEEYLKLKEAFVVEEEGVGETMTEEQSQSFLTEFINYIKQSKVVLLEDLASQVGLRTQVSPGTWPAVCSVARGLWLAERTCPKDRVLMHRLPCPQPRVSSAQKSPGTLGILHF
Protein: MORN repeat-containing protein 3 (Q6PF18)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasmic vesicle, secretory vesicle, acrosome {ECO:0000250|UniProtKB:Q8C5T4}. Note=Localized in the acrosome in germ cells throughout spermiogenesis, it is also present in the manchette of elongating spermatids. {ECO:0000250|UniProtKB:Q8C5T4}.
Interaction partners:
- MORN repeat-containing protein 5
- Radial spoke head 1 homolog
Sequence:
MPVSKCPKKSESLWKGWDRKAQRNGLRSQVYAVNGDYYVGEWKDNVKHGKGTQVWKKKGAIYEGDWKFGKRDGYGTLSLPDQQTGKCRRVYSGWWKGDKKSGYGIQFFGPKEYYEGDWCGSQRSGWGRMYYSNGDIYEGQWENDKPNGEGMLRLKNGNRYEGCWERGMKNGAGRFFHLDHGQLFEGFWVDNMAKCGTMIDFGRDEAPEPTQFPIPEVKILDPDGVLAEALAMFRKTEEGD
Protein: long-chain-fatty-acid--CoA ligase (EC 6.2.1.3) (Long-chain-fatty-acid--CoA ligase) (H7BZH4)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
XHPAGISDLLAEVSAEVDGPVPGYLSSPQSITDTCLYIFTSGTTGLPKAARISHLKILQCQGFYQLCGVHQEDVIYLALPLYHMSGSLLGIVGCMGIGATVVLKSKFSAGQFWEDCQQHRVTVFQYIGELCRYLVNQPPSKAERGHKVRLAVGSGLRPDTWERFVRRFGPLQVLETYGLTEGNVATINYTGQRGAVGRASWLYKHIFPFSLIRYDVTTGEPIRDPQGHCMATSPGEPGLLVAPVSQQSPFLGYAGGPELAQGKLLKDVFRPGDVFFNTGDLLVCDDQGFLRFHDRTGDTFRWKGENVATTEVAEVFEALDFLQEVNVYGVTVPGHEGRAGMAALVLRPPHALDLMQLYTHVSENLPPYARPRFLRLQAVGAYLPLTTARYSALLAGNLRI
Protein: Anti-FlhC(2)FlhD(4) factor YdiV (EAL-like protein YdiV) (c-di-GMP regulator CdgR) (Q8ZPS6)
Organism: Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Function: Acts as an anti-FlhC(2)FlhD(4) factor by binding to FlhD, decreasing its ability to bind DNA, and thus negatively regulates expression of flagellar class II operons, decreasing motility in nutrient-poor medium. Required for resistance to host phagocyte oxidase. Suppresses killing of macrophages, while promoting resistance to hydrogen peroxide. Data regarding c-di-GMP is controversial; suppresses bacterial c-di-GMP levels but neither synthesizes nor degrades c-di-GMP.
Interaction partners:
- Flagellar transcriptional regulator FlhD
- Diguanylate cyclase/phosphodiesterase domain 2
- Flagellar transcriptional regulator FlhC
- Protein FliZ
- Probable HTH-type transcriptional regulator LrhA
- Anti-FlhC
- Anti-FlhC
- Anti-FlhC
- Flagellin
- Anti-FlhC
Sequence:
MIASLDELYHSELFFLPVMDENARLVGLEIIATFAAEDGAVRMPTELVAPRLSVEEQYCLFVEKLALLETCQHFFIQHKLIAWLNLPPAISDLLLLDSELFSRAARFPFLELAINENYPGLNQGKNNETLANLAMHFPLMLANFGAGEASTKAIFDGLFKRVMLDKNFIQQRAEMISFEPFMHAIVAQISSSCESLMIAGIDTEAMFARAAPLGFSAFQGGLWPPVPVSQLIKLVQR
Protein: Conserved protein (O06570)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Interaction partners:
- Uncharacterized protein
- Guanylate cyclase domain-containing protein
Sequence:
MQSGPHLVGRVGTSFPLIARHQGATRDDAGDTGQPDPLPHVAHPDRLYPPMVHGVDPSTLALDRALNETRTGDLWLFRGRSRPDRAIQTLTNAPVNHVGMTVAIDDLPPLIWHAELGDKLLDVWTGTNHRGVQLNDARQVVQQWAGRYRQRCWLRQLTPHANRDQEDKLLRVIARMNGTPFPTTARLTGRWLRGRLPTLNDWLRGIPVLDRKVREQTQRRKQQQRTMGLATAYCAETVAITYEEMGLLVTDKDAHWFDPGKFWSGDSLPLAPGYRLGHEIAVDVGG
Protein: Late embryogenesis abundant protein 18 (Late embryogenesis abundant protein 4-2) (AtLEA4-2) (Q96273)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Involved dehydration tolerance. Involved in the adaptive response of vascular plants to withstand water deficit. May possess chaperone-like activity under water deficit. Binds to negatively charged membranes of liposomes. This binding induces partial folding of the largely unstructured LEA18 protein, vesicle aggregation, and leakage of soluble content from liposomes.
Interaction partners:
- Late embryogenesis abundant protein 46
- Late embryogenesis abundant protein 29
- Late embryogenesis abundant protein 7
- Late embryogenesis abundant protein
- F-box/LRR-repeat protein At3g59200
- At2g23110
- Late embryogenesis abundant
- F6D8.10
- Late embryogenesis abundant domain-containing protein / LEA domain-containing protein
- Late embryogenesis abundant protein
Sequence:
MQSAKEKISDMASTAKEKLNIGGAKAQGHAEKTMARTKKEKKLAQEREKSKEAQAKADLHQSKAEHAADAQVHGHHLPGHSTYPTRATGANYPPGQI
Protein: Secreted aspartic protease 8 (ACP 8) (Aspartate protease 8) (EC 3.4.23.24) (Candidapepsin-8) (Q5AEM6)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Function: Secreted aspartic peptidases (SAPs) are a group of ten acidic hydrolases considered as key virulence factors. These enzymes supply the fungus with nutrient amino acids as well as are able to degrade the selected host's proteins involved in the immune defense. Serves as a major regulator of MSB2-processing which activates CEK1 MAPK-signaling affecting biofilm formation and oropharyngeal candidiasis. Moreover, acts toward human hemoglobin though limited proteolysis to generate a variety of antimicrobial hemocidins, enabling to compete with the other microorganisms of the same physiological niche using the microbicidal peptides generated from the host protein.
Subcellular location: Secreted {ECO:0000250|UniProtKB:P0CY27}.
Interaction partners:
Sequence:
MVSIITFTKNVLVTLAFALLAQGLAIPEDIDKRAEKVVSLDFTVTRKPFNATAHGQHHQSQQQQQQQQQQPAQKRGTVQTSLINEGPSYAATITVGSNKQQQTVIVDTGSSDLWVVDSAAVCQVTYPGQSPTFCKQDGTYKPSSSTTSQNLGKAFSIRYEDGSSSQGTVYKDTVGLGGASITNQQFADVTTTSVDQGILGIGFTGDESSPTYDNVPVTLKKQGIINKNAYSLYLNSASASSGTIIFGGVDNAKYTGSLTALPITSSNELRVQLSTINIAGTTVSASTTPVLDSGTTLTYFSQTIADKLAAAVGAKWNSYYQLYTSSCNLAGNIVFNFAKGVTISVPLSEFVLQDGNSCYFGVSRDSATILGDNFLRRAYAVYDLDGNTISLAQVKYTTSSSISTL
Protein: E3 ubiquitin-protein ligase RNF146 (EC 2.3.2.27) (Dactylidin) (Iduna) (RING finger protein 146) (RING-type E3 ubiquitin transferase RNF146) (Q9NTX7)
Organism: Homo sapiens (Human)
Function: E3 ubiquitin-protein ligase that specifically binds poly-ADP-ribosylated (PARsylated) proteins and mediates their ubiquitination and subsequent degradation. May regulate many important biological processes, such as cell survival and DNA damage response. Acts as an activator of the Wnt signaling pathway by mediating the ubiquitination of PARsylated AXIN1 and AXIN2, 2 key components of the beta-catenin destruction complex. Acts in cooperation with tankyrase proteins (TNKS and TNKS2), which mediate PARsylation of target proteins AXIN1, AXIN2, BLZF1, CASC3, TNKS and TNKS2. Recognizes and binds tankyrase-dependent PARsylated proteins via its WWE domain and mediates their ubiquitination, leading to their degradation. Different ubiquitin linkage types have been observed: TNKS2 undergoes ubiquitination at 'Lys-48' and 'Lys-63', while AXIN1 is only ubiquitinated at 'Lys-48'. May regulate TNKS and TNKS2 subcellular location, preventing aggregation at a centrosomal location. Neuroprotective protein. Protects the brain against N-methyl-D-aspartate (NMDA) receptor-mediated glutamate excitotoxicity and ischemia, by interfering with PAR-induced cell death, called parthanatos (By similarity). Prevents nuclear translocation of AIFM1 in a PAR-binding dependent manner (By similarity). Does not affect PARP1 activation (By similarity). Protects against cell death induced by DNA damaging agents, such as N-methyl-N-nitro-N-nitrosoguanidine (MNNG) and rescues cells from G1 arrest (By similarity). Promotes cell survival after gamma-irradiation. Facilitates DNA repair.
Subcellular location: Cytoplasm, cytosol. Nucleus. Note=Translocates to the nucleus after DNA damage, such as laser-induced DNA breaks, and concentrates at DNA breaks. This translocation requires PARP1 activation and PAR-binding.
Interaction partners:
- Poly [ADP-ribose] polymerase tankyrase-1
- Ubiquitin-conjugating enzyme E2 D1
- Poly [ADP-ribose] polymerase tankyrase-2
- Poly [ADP-ribose] polymerase 1
- Axin-2
- Axin-1
- Poly [ADP-ribose] polymerase 2
- Chromodomain-helicase-DNA-binding protein 1-like
- SH3 domain-binding protein 2
- FACT complex subunit SPT16
Sequence:
MMAGCGEIDHSINMLPTNRKANESCSNTAPSLTVPECAICLQTCVHPVSLPCKHVFCYLCVKGASWLGKRCALCRQEIPEDFLDKPTLLSPEELKAASRGNGEYAWYYEGRNGWWQYDERTSRELEDAFSKGKKNTEMLIAGFLYVADLENMVQYRRNEHGRRRKIKRDIIDIPKKGVAGLRLDCDANTVNLARESSADGADSVSAQSGASVQPLVSSVRPLTSVDGQLTSPATPSPDASTSLEDSFAHLQLSGDNTAERSHRGEGEEDHESPSSGRVPAPDTSIEETESDASSDSEDVSAVVAQHSLTQQRLLVSNANQTVPDRSDRSGTDRSVAGGGTVSVSVRSRRPDGQCTVTEV
Protein: Uncharacterized protein, isoform B (Q8IQI3)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Double-strand break repair protein
- Mutagen-sensitive 101
- Nibrin
- Regulator of telomere elongation helicase 1 homolog
- Breast cancer type 2 susceptibility protein homolog
- DNA repair protein RAD50
- Ubiquitin-ribosomal protein eL40 fusion protein
- Ubiquitin-ribosomal protein eS31 fusion protein
- Cleavage stimulation factor subunit 1
Sequence:
MPPPRPKGIGFNTGATQPRSNSNTPMSERQQMALLIQMTANSSTVQSQSLELLLVGLNFNLHHSSRTTLKKNECKKGDAETDEGSLNEKQEVLDTKDKSSAEESSNDGKSSDTNHQGTSAAKRCYSDIEEDYEESGEDVKKKKRKDSEHGKDVKGASLKLTSRVEKSSKLAATKGSPSGNKSSASNAEKEPAETSKNVDIENETECSDDYKSNDSLYNGGLKVPPLKIVIPQQNCSIDTEGNVLRTGKVTASRNAALPYVVSSNSDSIDTVITNQSISPHESPQKSNSICSTALDDKNIKLFNDEKNLRVLRSSHRTGVTSVERSSNNSSPQMQSSSPSPASSNHANDPADVKLSYSNMTSSPIPQGHQFDQEAITNVPSPSTSSTSSSKDINPSNVELHPRKRKIRPKNTDDSSKNSNAADSGVNSEESHPHDHPFTNGFQMFLSIRRQIEKKWKSLYPVKPRPPQGYNEYLLTKKSYLLRRNATISVPDIPRTVPQAMERIYQDQEKARRDLIEAHTVEREKLCMNVEQEIIRVHSKAARSISGQPAPYSVCTYLKDDEVYNMITPEQDEKEKSARCRFNGRLLLSWLQDVDDKWEKIKESMVLRHHNEAESLHAVQVMDWNIFAKRNRLCDNPIEVNLEHVPIVSVGDDFDTLPT
Protein: Transporter (Q9V4E7)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
- cathepsin L
- Protein dpy-30 homolog
Sequence:
MYTNSASDGDGGGDVCKHESIEMSKELGHTTSLQSSSPTTTDTSNKQQLVKIEQLPDRGSWSSKMDFILSVVGLAIGLGNVWRFPYLCYKNGGGAFILPYIITLFLAGIPMFFMELALGQMLTIGGLGVFKIAPIFKGIGYAAAVMSCWMNVYYIVILAWAVFYFFMSMRADVPWRTCNNWWNTVNCVSQYERKNLHCWDKIINGTTQKVCSVSALNITSLELTDPVKEFWERRALQISHGIEEIGNIRWELAGTLLLVWILCYFCIWKGVKWTGKVVYFTALFPYVLLTILLVRGITLPGALEGIKFYIIPNFSKLTNSEVWIDAVTQIFFSYGLGLGTLVALGSYNKFTNNVYKDALIVCTVNSSTSMFAGFVIFSVIGFMAHEQQRPVADVAASGPGLAFLVYPSAVLQLPGSPMWSCLFFFMLLLIGLDSQFCTMEGFITAIIDEWPQLLRKRKEIFIAIVCALSYLVGLTCITQGGMYIFQILDSYAVSGFCLLWLIFFECVSISWCYGVDRFYDGIKDMIGYYPTVWWKFCWCVTTPAICLGVFFFNIVQWTPVKYLDYSYPWWAHAFGWFTALSSMLYIPLYMFWLWKRTPGELSEKIRALVRIDEDVTRLREKMLREAYAKEIEFNSL
Protein: Transmembrane protein 17 (Q86X19)
Organism: Homo sapiens (Human)
Function: Transmembrane component of the tectonic-like complex, a complex localized at the transition zone of primary cilia and acting as a barrier that prevents diffusion of transmembrane proteins between the cilia and plasma membranes. Required for ciliogenesis and sonic hedgehog/SHH signaling (By similarity).
Subcellular location: Cell projection, cilium membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Note=Localizes to the transition zone of primary cilia. {ECO:0000250}.
Interaction partners:
- Transmembrane protein 231
- B9 domain-containing protein 1
- Coiled-coil and C2 domain-containing protein 2A
- Transmembrane protein 216
- B9 domain-containing protein 2
- Tectonic-1
- Meckelin
- Tectonic-2
- Transmembrane protein 107
- Tectonic-like complex member MKS1
Sequence:
MELPDPVRQRLGNFSRAVFSDSNRTGPESNEGPENEMVSSLALQMSLYFNTYYFPLWWVSSIMMLHMKYSILPDYYKFIVITVIILITLIEAIRLYLGYVGNLQEKVPELAGFWLLSLLLQLPLILFLLFNEGLTNLPLEKAIHIIFTLFLAFQVVAAFLTLRKMVNQLAVRFHLQDFDRLSANRGDMRRMRSCIEEI
Protein: Proteasome subunit alpha type-2-A (20S proteasome alpha subunit B-1) (Proteasome component 3) (O23708)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: The proteasome is a multicatalytic proteinase complex which is characterized by its ability to cleave peptides with Arg, Phe, Tyr, Leu, and Glu adjacent to the leaving group at neutral or slightly basic pH. The proteasome has an ATP-dependent proteolytic activity.
Subcellular location: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
Interaction partners:
- Proteasome subunit alpha type-3
- Proteasome subunit beta type-3-A
- Proteasome subunit beta type-1
- Proteasome subunit beta type-6
- Proteasome subunit beta type-4
- Proteasome subunit beta type-2-B
- Proteasome subunit alpha type-7-B
- Proteasome subunit alpha type-1-B
- Proteasome subunit beta type-2-A
- Proteasome subunit beta type-3-B
Sequence:
MGDSQYSFSLTTFSPSGKLVQIEHALTAVGSGQTSLGIKASNGVVIATEKKLPSILVDEASVQKIQHLTPNIGVVYSGMGPDFRVLVRKSRKQAEQYLRLYKEPIPVTQLVRETATVMQEFTQSGGVRPFGVSLLVAGYDDKGPQLYQVDPSGSYFSWKASAMGKNVSNAKTFLEKRYTEDMELDDAIHTAILTLKEGFEGEISSKNIEIGKIGADKVFRVLTPAEIDDYLAEVE
Protein: Catalase B (EC 1.11.1.6) (Antigenic catalase) (Slow catalase) (Q92405)
Organism: Aspergillus fumigatus (strain ATCC MYA-4609 / CBS 101355 / FGSC A1100 / Af293) (Neosartorya fumigata)
Function: Occurs in almost all aerobically respiring organisms and serves to protect cells from the toxic effects of hydrogen peroxide.
Subcellular location: Secreted {ECO:0000305}.
Interaction partners:
- FMN-dependent dehydrogenase family protein
- 3-hydroxyanthranilate 3,4-dioxygenase 1
- Kynureninase 1
- Kynureninase 2
- Superoxide dismutase
- Glutathione peroxidase
- propanoyl-CoA C-acyltransferase
Sequence:
MRLTFIPSLIGVANAVCPYMTGELNRRDEISDGDAAAATEEFLSQYYLNDNDAFMTSDVGGPIEDQNSLSAGERGPTLLEDFIFRQKIQRFDHERVPERAVHARGAGAHGVFTSYGDFSNITAASFLAKEGKQTPVFVRFSTVAGSRGSSDLARDVHGFATRFYTDEGNFDIVGNNIPVFFIQDAILFPDLIHAVKPRGDNEIPQAATAHDSAWDFFSQQPSTMHTLLWAMSGHGIPRSFRHVDGFGVHTFRFVTDDGASKLVKFHWKSLQGKASMVWEEAQQTSGKNPDFMRQDLHDAIEAGRYPEWELGVQIMDEEDQLRFGFDLLDPTKIVPEEFVPITKLGKMQLNRNPRNYFAETEQVMFQPGHIVRGVDFTEDPLLQGRLFSYLDTQLNRHGGPNFEQLPINQPRVPVHNNNRDGAGQMFIPLNPHAYSPKTSVNGSPKQANQTVGDGFFTAPGRTTSGKLVRAVSSSFEDVWSQPRLFYNSLVPAEKQFVIDAIRFENANVKSPVVKNNVIIQLNRIDNDLARRVARAIGVAEPEPDPTFYHNNKTADVGTFGTKLKKLDGLKVGVLGSVQHPGSVEGASTLRDRLKDDGVDVVLVAERLADGVDQTYSTSDAIQFDAVVVAAGAESLFAASSFTGGSANSASGASSLYPTGRPLQILIDGFRFGKTVGALGSGTAALRNAGIATSRDGVYVAQSVTDDFANDLKEGLRTFKFLDRFPVDH