wanglab/gogpt-training-data huggingface dataset:
Protein: Muscle LIM protein Mlp84B (Q24400)
Organism: Drosophila melanogaster (Fruit fly)
Function: Plays a role in cell differentiation late in myogenesis. Transcription factor Mef2 is essential for expression.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:8794860}. Nucleus {ECO:0000269|PubMed:8794860}.
Interaction partners:
- Tropomyosin-2
- Muscle-specific protein 20
- Myosin heavy chain, muscle
- Myosin regulatory light chain 2
- Myosin light chain alkali
- Troponin T, skeletal muscle
- Troponin C, isoform 2
- Actin-87E
- Paramyosin, long form
- Troponin I
Sequence:
MPSFQPIEAPKCPRCGKSVYAAEERLAGGYVFHKNCFKCGMCNKSLDSTNCTEHERELYCKTCHGRKFGPKGYGFGTGAGTLSMDNGSQFLRENGDVPSVRNGARLEPRAIARAPEGEGCPRCGGYVYAAEQMLARGRSWHKECFKCGTCKKGLDSILCCEAPDKNIYCKGCYAKKFGPKGYGYGQGGGALQSDCYAHDDGAPQIRAAIDVDKIQARPGEGCPRCGGVVYAAEQKLSKGREWHKKCFNCKDCHKTLDSINASDGPDRDVYCRTCYGKKWGPHGYGFACGSGFLQTDGLTEDQISANRPFYNPDTTSIKARDGEGCPRCGGAVFAAEQQLSKGKVWHKKCYNCADCHRPLDSVLACDGPDGDIHCRACYGKLFGPKGFGYGHAPTLVSTSGESTIQFPDGRPLAGPKTSGGCPRCGFAVFAAEQMISKTRIWHKRCFYCSDCRKSLDSTNLNDGPDGDIYCRACYGRNFGPKGVGYGLGAGALTTF
Protein: Xaa-Pro aminopeptidase (EC 3.4.11.9) (Aminoacylproline aminopeptidase) (Aminopeptidase P II) (APP-II) (X-Pro aminopeptidase) (P15034)
Organism: Escherichia coli (strain K12)
Subcellular location: Cytoplasm.
Interaction partners:
- 2-octaprenyl-6-methoxyphenol hydroxylase
- Cytosol non-specific dipeptidase
- UPF0149 protein YgfB
- 2-octaprenylphenol hydroxylase
- Aminopeptidase N
- GMP reductase
- Bifunctional protein FolD
- Cytosol aminopeptidase
Sequence:
MSEISRQEFQRRRQALVEQMQPGSAALIFAAPEVTRSADSEYPYRQNSDFWYFTGFNEPEAVLVLIKSDDTHNHSVLFNRVRDLTAEIWFGRRLGQDAAPEKLGVDRALAFSEINQQLYQLLNGLDVVYHAQGEYAYADVIVNSALEKLRKGSRQNLTAPATMIDWRPVVHEMRLFKSPEEIAVLRRAGEITAMAHTRAMEKCRPGMFEYHLEGEIHHEFNRHGARYPSYNTIVGSGENGCILHYTENECEMRDGDLVLIDAGCEYKGYAGDITRTFPVNGKFTQAQREIYDIVLESLETSLRLYRPGTSILEVTGEVVRIMVSGLVKLGILKGDVDELIAQNAHRPFFMHGLSHWLGLDVHDVGVYGQDRSRILEPGMVLTVEPGLYIAPDAEVPEQYRGIGIRIEDDIVITETGNENLTASVVKKPEEIEALMVAARKQ
Protein: F-box only protein 44 (F-box protein FBX30) (F-box/G-domain protein 3) (Q9H4M3)
Organism: Homo sapiens (Human)
Function: Substrate-recognition component of the SCF (SKP1-CUL1-F-box protein)-type E3 ubiquitin ligase complex.
Interaction partners:
Sequence:
MAVGNINELPENILLELFTHVPARQLLLNCRLVCSLWRDLIDLVTLWKRKCLREGFITEDWDQPVADWKIFYFLRSLHRNLLHNPCAEEGFEFWSLDVNGGDEWKVEDLSRDQRKEFPNDQVKKYFVTSYYTCLKSQVVDLKAEGYWEELMDTTRPDIEVKDWFAARPDCGSKYQLCVQLLSSAHAPLGTFQPDPATIQQKSDAKWREVSHTFSNYPPGVRYIWFQHGGVDTHYWAGWYGPRVTNSSITIGPPLP
Protein: Death effector domain-containing protein (DEDPro1) (Death effector domain-containing testicular molecule) (FLDED-1) (O75618)
Organism: Homo sapiens (Human)
Function: A scaffold protein that directs CASP3 to certain substrates and facilitates their ordered degradation during apoptosis. May also play a role in mediating CASP3 cleavage of KRT18. Regulates degradation of intermediate filaments during apoptosis. May play a role in the general transcription machinery in the nucleus and might be an important regulator of the activity of GTF3C3. Inhibits DNA transcription in vitro (By similarity).
Subcellular location: Cytoplasm. Nucleus, nucleolus {ECO:0000250}. Note=Translocated to the nucleus during CD95-mediated apoptosis where it is localized in the nucleoli (By similarity). Following apoptosis induction, the mono and/or diubiquitination form increases and forms filamentous structures that colocalize with KRT8 and KRT18 intermediate filament network in simple epithelial cells. {ECO:0000250}.
Interaction partners:
- 3'-5' exoribonuclease 1
- Beclin-1
- Histone RNA hairpin-binding protein
- FAS-associated death domain protein
- Caspase-8
- Keratin, type I cytoskeletal 18
- E3 ubiquitin-protein ligase RNF34
Sequence:
MAGLKRRASQVWPEEHGEQEHGLYSLHRMFDIVGTHLTHRDVRVLSFLFVDVIDDHERGLIRNGRDFLLALERQGRCDESNFRQVLQLLRIITRHDLLPYVTLKRRRAVCPDLVDKYLEETSIRYVTPRALSDPEPRPPQPSKTVPPHYPVVCCPTSGPQMCSKRPARGRATLGSQRKRRKSVTPDPKEKQTCDIRLRVRAEYCQHETALQGNVFSNKQDPLERQFERFNQANTILKSRDLGSIICDIKFSELTYLDAFWRDYINGSLLEALKGVFITDSLKQAVGHEAIKLLVNVDEEDYELGRQKLLRNLMLQALP
Protein: ELAV-like protein 2 (Hu-antigen B) (HuB) (Q8CH84)
Organism: Rattus norvegicus (Rat)
Function: RNA-binding protein that binds to the 3' untranslated region (3'UTR) of target mRNAs (By similarity). Seems to recognize a GAAA motif (By similarity). Can bind to its own 3'UTR, the FOS 3'UTR and the ID 3'UTR (By similarity).
Interaction partners:
Sequence:
METQLSNGPTCNNTANGPTTVNNNCSSPVDSGNTEDSKTNLIDNYLPQNMTQEELKSLFGSIGEIESCKLVRDKITGQSLGYGFVNYIDPKDAEKAINTLNGLRLQTKTIKVSYARPSSASIRDANLYVSGLPKTMTQKELEQLFSQYGRIITSRILVDQVTGISRGVGFIRFDKRIEAEEAIKGLNGQKPPGATEPITVKFANNPSQKTNQAILSQLYQSPNRRYPGPLAQQAQRFRLDNLLNMAYGVKRFSPMTIDGMTSLAGINIPGHPGTGWCIFVYNLAPDADESILWQMFGPFGAVTNVKVIRDFNTNKCKGFGFVTMTNYDEAAMAIASLNGYRLGDRVLQVSFKTNKTHKA
Protein: Protocadherin alpha-3 (PCDH-alpha-3) (Q9Y5H8)
Organism: Homo sapiens (Human)
Function: Potential calcium-dependent cell-adhesion protein. May be involved in the establishment and maintenance of specific neuronal connections in the brain.
Subcellular location: Cell membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}.
Interaction partners:
- Protocadherin alpha-6
- Protocadherin alpha-1
- Protocadherin alpha-2
- Protocadherin alpha-11
Sequence:
MLFSWREDPGAQCLLLSLLLLAASEVGSGQLHYSVSEEAKHGTFVGRIAQDLGLELAELVPRLFRVASKRHGDLLEVNLQNGILFVNSRIDREELCGRSAECSIHLEVIVDRPLQVFHVEVEVKDINDNAPVFPMAVKNLFISESRQPGSRFSLEGASDADIGTNSLLTYSLDSTEYFTLDVKRNDEEIKSLGLVLKKNLNREDTPKHYLLITAIDGGKPELTGTTQLKITVLDVNDNAPAFERTIYKVRLLENAPNGTLVVTVNATDLDEGVNKDIAYSFNTDMSADILSKFHLDPVNGQISVKGNIDFEESKSYEIQVEATDKGNPPMSDHCTVLLEIVDINDNVPELVIQSLSLPVLEDSPLSTVIALISVSDRDSGVNGQVTCSLTPHVPFKLVSTFKNYYSLVLDSPLDRESVSAYELVVTARDGGSPSLWATASVSVEVADVNDNAPAFSQSEYTVFVKENNPPGCHIFTVSARDADAQENALVSYSLVERRVGERALSSYVSVHAESGKVYALQPLDHEELELLQFQVSARDAGVPPLGSNVTLQVFVLDENDNAPALLMPRVGGIGGAVSELVPRSVGAGHVVAKVRAVDADSGYNAWLSYELQPGTGGARIPFRVGLYTGEISTTRALDEVDAPRHRLLVLVKDHGEPSLTATATVLVSLVESGQAPKASSQASAGATGPEAALVDVNVYLIVAICAVSSLLVLTLLLYTALRCSAPPTEGDCGPGKPTLVCSSAVGSWSYSQQRQQRVCSGEGLPKTDLMAFSPSLPPCPISRDREEKQDVDVDLSAKPRQPNPDWRYSASLRAGMHSSVHLEEAGILRAGPGGPDQQWPTVSSATPEPEAGEVSPPVGAGVNSNSWTFKYGPGNPKQSGPGELPDKFIIPGSPAIISIRQEPTNSQIDKSDFITFGKKEETKKKKKKKKGNKTQEKKEKGNSTTDNSDQ
Protein: Very long chain fatty acid elongase 1 (EC 2.3.1.199) (3-keto acyl-CoA synthase Elovl1) (ELOVL fatty acid elongase 1) (ELOVL FA elongase 1) (Elongation of very long chain fatty acids protein 1) (Very long chain 3-ketoacyl-CoA synthase 1) (Very long chain 3-oxoacyl-CoA synthase 1) (Q9JLJ5)
Organism: Mus musculus (Mouse)
Function: Catalyzes the first and rate-limiting reaction of the four reactions that constitute the long-chain fatty acids elongation cycle. This endoplasmic reticulum-bound enzymatic process allows the addition of 2 carbons to the chain of long- and very long-chain fatty acids (VLCFAs) per cycle. Condensing enzyme that exhibits activity toward saturated and monounsaturated acyl-CoA substrates, with the highest activity towards C22:0 acyl-CoA. May participate in the production of both saturated and monounsaturated VLCFAs of different chain lengths that are involved in multiple biological processes as precursors of membrane lipids and lipid mediators. Important for saturated C24:0 and monounsaturated C24:1 sphingolipid synthesis. Indirectly inhibits RPE65 via production of VLCFAs.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000255|HAMAP-Rule:MF_03201}; Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_03201}.
Interaction partners:
- Very-long-chain 3-oxoacyl-CoA reductase
- Very long chain fatty acid elongase 3
- Very long chain fatty acid elongase 4
- Very long chain fatty acid elongase 7
- Ceramide synthase 2
- ATP-binding cassette sub-family D member 1
Sequence:
MEAVVNLYHELMKHADPRIQSYPLMGSPLLITSILLTYVYFILSLGPRIMANRKPFQLRGFMIVYNFSLVILSLYIVYEFLMSGWLSTYTWRCDPIDFSNSPEALRMVRVAWLFMLSKVIELMDTVIFILRKKDGQVTFLHVFHHSVLPWSWWWGIKIAPGGMGSFHAMINSSVHVVMYLYYGLSALGPVAQPYLWWKKHMTAIQLIQFVLVSLHISQYYFMPSCNYQYPIIIHLIWMYGTIFFILFSNFWYHSYTKGKRLPRAVQQNGAPATTKVKAN
Protein: Annexin (Q27473)
Organism: Caenorhabditis elegans
Interaction partners:
- Actin
- Calreticulin
- SCP domain-containing protein
- SCP domain-containing protein
- Tetraspanin
- Tetraspanin
- Tetraspanin
- Sperm vesicle fusion protein fer-1
Sequence:
MATAKIHFKPYFDEVAASEQLEKALRNKEKLKILEILVSVNNTQRQMIRTPYKTRYGKDLEDEIKKAFSGDFEDFLVALLQTPTKLDVTELNRSVKGLGTNEKNLIEILTTRTNEEIEAAKNTYFMTYSKSLEDAISADTSGDFRRLLIVILQAKREEGGFADTFKVGPHAAQILKSFDKKSGVEKFDAFKIFATCNGAHIQKVIEEVERQSGKEFQKLIDKELSGDFKNLVLSLIETSRNKPRYFANSIHLATKGMGTRDKDLIRILVSRSENDLVIIEHEFQTLFGKPLTQLIKEECKAEYRDGLTMLVKGNPRP
Protein: L-lactate dehydrogenase (EC 1.1.1.27) (C0HAI2)
Organism: Salmo salar (Atlantic salmon)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
Sequence:
MSSVMQKLITPMASGPAEPPRNKVTVVGVGMVGMACAVSILLRDLADELALVDVMEDKLKGEMMDLQHGSLFLKTSKIVADKDYAVTANSRIVVVTAGVRQQEGESRLNLVQRNVNIFKHIIPQIVKHSPNCTLIVVSNPVDVLTYVTWKLSGLPKHRVIGSGTNLDSARFRFLMAERLGIHATSFNGWVLGEHGDTSVPVWSGVSVAGVNLQKLNPEFGLDGDKEDWKATHKEVVDSAYEVIKLKGYTNWAIGLSVADLTESIIKNMSRIHPVSTMVKDMYGIGEEVFLSLPCVLNSNGVGSVINMTLTDAEVGQLKKSADTLWGIQKDLKDV
Protein: Murein peptide amidase A (EC 3.4.17.-) (Gamma-D-Glu-Dap amidase) (Zinc metallocarboxypeptidase MpaA) (A7N805)
Organism: Vibrio campbellii (strain ATCC BAA-1116)
Function: Involved in muropeptide degradation. Catalyzes the hydrolysis of the gamma-D-glutamyl-diaminopimelic acid (gamma-D-Glu-Dap) amide bond in the murein tripeptide L-alanyl-gamma-D-glutamyl-meso-diaminopimelic acid, leading to the formation of L-Ala-gamma-D-Glu and Dap. Has weak activity with L-Ala-gamma-D-Glu-L-Lys, MurNAc-tripeptide and gamma-D-Glu-meso-Dap. Cannot hydrolyze murein tetrapeptide.
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_02211}.
Interaction partners:
Sequence:
MNRYYSNNQEITVSLIPRTERAAFLITPTSYGKSVLGAPLLYFPAQVESNSRGLILAGTHGDETASIAGLSCALRSLPAECLKHDVILSMNPDANQLGTRANANQVDLNRAFPTQNWTEHGTVYRWSSHTPVRDVKVKTGDKEQLEPEVDALISLIELRRPKFVVSFHEPLAFVDDPAHSDLAKWLGKQFNLPIVDDVDYETPGSFGTWCNERQLPCITVELPPISADLTIEKHLDAFIALLQHDPDL
Protein: Floral homeotic protein GLOBOSA (Q03378)
Organism: Antirrhinum majus (Garden snapdragon)
Function: Transcription factor involved in the genetic control of flower development. Acts in conjunction with DEFICIENS (defA).
Subcellular location: Nucleus.
Interaction partners:
Sequence:
MGRGKIEIKRIENSSNRQVTYSKRRNGIMKKAKEISVLCDAHVSVIIFASSGKMHEFCSPSTTLVDMLDHYHKLSGKRLWDPKHEHLDNEINRVKKENDSMQIELRHLKGEDITTLNYKELMVLEDALENGTSALKNKQMEFVRMMRKHNEMVEEENQSLQFKLRQMHLDPMNDNVMESQAVYDHHHHQNIADYEAQMPFAFRVQPMQPNLQERF
Protein: Transitional endoplasmic reticulum ATPase (TER ATPase) (EC 3.6.4.6) (Protein CDC48) (Valosin-containing protein) (VCP) (Q7ZU99)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: Necessary for the fragmentation of Golgi stacks during mitosis and for their reassembly after mitosis. Involved in the formation of the nuclear envelope, and of the transitional endoplasmic reticulum (tER). The transfer of membranes from the endoplasmic reticulum to the Golgi apparatus occurs via 50-70 nm transition vesicles which derive from part-rough, part-smooth transitional elements of the endoplasmic reticulum (tER). Vesicle budding from the tER is an ATP-dependent process. Also involved in DNA damage response: recruited to double-strand breaks (DSBs) sites and promotes the recruitment of tp53bp1 at DNA damage sites (By similarity). Together with sprtn metalloprotease, involved in the repair of covalent DNA-protein cross-links (DPCs) during DNA synthesis (By similarity). Involved in interstrand cross-link repair in response to replication stress by mediating unloading of the ubiquitinated CMG helicase complex (By similarity). Enhances cell cycle progression and inhibits apoptosis at low temperatures. Essential for the maturation of ubiquitin-containing autophagosomes and the clearance of ubiquitinated protein by autophagy (By similarity). Acts as a negative regulator of type I interferon production by promoting ubiquitination of RIGI (By similarity). May play a role in the ubiquitin-dependent sorting of membrane proteins to lysosomes where they undergo degradation (By similarity). May more particularly play a role in caveolins sorting in cells (By similarity). By controlling the steady-state expression of the IGF1R receptor, indirectly regulates the insulin-like growth factor receptor signaling pathway (By similarity).
Subcellular location: Cytoplasm, cytosol {ECO:0000250|UniProtKB:P23787}. Endoplasmic reticulum {ECO:0000250|UniProtKB:P55072}. Nucleus {ECO:0000250|UniProtKB:P23787}.
Interaction partners:
- UBX domain protein 7.
- UBX domain-containing protein 6
- Nuclear protein localization protein 4 homolog
- NSFL1
- UBX domain protein 2A
- UBX domain protein 4.
- Ubiquitin thioesterase OTU1
- UBX domain-containing protein 1
- Protein N-lysine methyltransferase METTL21D isoform X1 methyltransferase)
- Derlin
Sequence:
MASGGESKNDDLSTAILKQKNRPNRLIVDESINEDNSVVSLSQAKMDELQLFRGDTVLLKGKKRRETVCIVLSDDTCSDEKVRMNRVVRNNLRVRLGDVISIQPCPDVKYGKRIHVLPIDDTVEGITGNLFEVYLKPYFLEAYRPIRKGDIFLVRGGMRAVEFKVVETDPSPYCIVAPDTVIHCEGEPIKREDEEESLNEVGYDDIGGVRKQLAQIKEMVELPLRHPALFKAIGVKPPRGILLYGPPGTGKTLIARAVANETGAFFFLINGPEIMSKLAGESESNLRKAFEEAEKNAPAIIFIDELDAIAPKREKTHGEVERRIVSQLLTLMDGLKQRAHVIVMAATNRPNSIDPALRRFGRFDREVDIGIPDATGRLEILQIHTKNMKLADDVDLEQVANETHGHVGADLAALCSEAALQAIRKKMDLIDLEDETIDAEVMNSLAVTMDDFRWALSQSNPSALRETVVEVPNITWEDIGGLDDVKRELQELVQYPVEHPDKFLKFGMTPSKGVLFYGPPGCGKTLLAKAIANECQANFISIKGPELLTMWFGESEANVREIFDKARQAAPCVLFFDELDSIAKARGGNVGDGGGAADRVINQILTEMDGMSSKKNVFIIGATNRPDIIDPAILRPGRLDQLIYIPLPDEKSRIAILKANLRKSPISKDVDLDFLAKMTNGFSGADLTEICQRACKLAIRESIENEIRRERERQTNPSAMEVEEDDPVPEIRKDHFEEAMRFARRSVSDNDIRKYEMFAQTLQQSRGFGSFRFPSSNQGGSGPSQGSSGGGGGNVFNEDNDDDLYG
Protein: Transcriptional adapter 2 (Q9P7J7)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Functions as component of the transcription regulatory histone acetylation (HAT) complexes SAGA, SALSA and ADA. SAGA is involved in RNA polymerase II-dependent transcriptional regulation. At the promoters, SAGA is required for recruitment of the basal transcription machinery. It influences RNA polymerase II transcriptional activity through different activities such as TBP interaction and promoter selectivity, interaction with transcription activators, and chromatin modification through histone acetylation (gcn5) and deubiquitination (ubp8). SAGA acetylates nucleosomal histone H3 to some extent (to form H3K9ac, H3K14ac, H3K18ac and H3K23ac). SAGA interacts with DNA via upstream activating sequences (UASs). SALSA, an altered form of SAGA, may be involved in positive transcriptional regulation. SLIK is proposed to have partly overlapping functions with SAGA. It preferentially acetylates methylated histone H3. ADA preferentially acetylates nucleosomal histones H3 (to form H3K14ac and H3K18ac) and H2B (By similarity). Required for full activation of chromatin alteration and meiotic recombination at meiotic recombination hot spot ade6-M26. Also required for the regulation of transcription and chromatin structure around ade6-M26 in response to osmotic stress. Needed for hyperacetylation of histone H3 around ade6-M26.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00624, ECO:0000269|PubMed:16823372}.
Interaction partners:
- Histone acetyltransferase gcn5
- SAGA complex subunit Ngg1
- SAGA complex subunit Sgf29
- SAGA complex/transcription factor TFIID complex subunit Taf12
- SAGA complex/transcription factor TFIID complex subunit Taf9
- SAGA complex subunit Spt7
- SAGA complex subunit Spt3
- SAGA complex/transcription factor TFIID complex subunit Taf10
- SAGA complex subunit Sus1
- SAGA complex/transcription factor TFIID complex subunit Taf6
Sequence:
MPPQKYHCNVCAQDITRSIHIRCVECVDFDLCIPCFTSGASLGTHHPSHPYRIIETNSYPIFDENWGADEELLLIDACETLGLGNWADIADYVGNARTKEECRDHYLKTYIESDCYPLASVELPGPVDRIAFAARKRARIEAFQPPPIIPQKPLASTPQCHEIQGYMPGRLEFDQEYMNEAELPIKDMNFDDDLHESAKHEMQLKLTMLNIYNSRLTRRAVRKQTIFNHNLLDYRRLQANEKRMSKEERNLLNKTKAFARLLTGPDYQKFVNSYHEQITLKKQISDLQEWRQMGLTTLEQGHKYERDKTQKFLLSKASASYDKQLRHVKSFNQTTSAPFQVRDIQKIVPRKPATPTMFSASADRQLLSEDEQALCSKLQIFPKPFLALKFALISASLTSKKPFQKTDAVNLFKHLDANKVEQVYDFFHNARWIGAPT
Protein: Serine/threonine-protein kinase/endoribonuclease ireA (Endoplasmic reticulum-to-nucleus signaling A) [Includes: Serine/threonine-protein kinase (EC 2.7.11.1); Endoribonuclease (EC 3.1.26.-)] (Q4WKP8)
Organism: Aspergillus fumigatus (strain ATCC MYA-4609 / CBS 101355 / FGSC A1100 / Af293) (Neosartorya fumigata)
Function: Senses unfolded proteins in the lumen of the endoplasmic reticulum (ER) via its N-terminal domain which leads to enzyme auto-activation (By similarity). The active endoribonuclease domain responds by cleaving an intron from the downstream cytoplasmic mRNA hacA, allowing for the translation of a transcription factor that coordinates a series of adaptive responses that are collectively known as the unfolded protein response (UPR). In the absence of ER stress, ireA controls dual signaling circuits that are both hacA-dependent and hacA-independent and which contribute to the expression of traits that are essential for virulence.
Subcellular location: Membrane {ECO:0000255}; Single-pass type I membrane protein {ECO:0000255}.
Interaction partners:
- Endoplasmic reticulum chaperone BiP
- Translation initiation factor RLI1
- RING-type E3 ubiquitin transferase
- Transcriptional regulator of the unfolded protein response hacA
Sequence:
MRWRLPGARTTLPASVALLLLPILVAPQQLQEHDDLPSTLSVPLSPTQRSFDHHPLPTINVKSNDASALATMALAGPGRAVRARPAQASSSSAGLAPQLHARSLQDWEVEDFVLLATVDGSIHARDRRTGAARWALEVPSSPMVESIYHRANRSSFDRAQPEDDFLWIVEPSQDGNLYIYSPGPDAGLQKLGLTVKELVEQTPYSGTDPAVTYTARKETTLYTVDARTGNILQVFSSRGPITSGHGCRKVDGFDLEAEECDTPSGTLVLGRVEYAVAIQNTETGDPICTLKYSEWTANNRDMDLQSQYFRTMDQSHIYSMHDGVVLGFDHSRMDRPRYTQRFSSPVVRVFDVARPINVESPEAATPLVLLSQPLQPPDPDYGSLDDRDARVFVDCTSAGGWFAMSEETYPLVTGRAKMAQCYEKDYLRHGQPLTSLPTSQQRDALAGVHSLNGPRVVRNTPSISGPSPLELANDTPRELMRSPSELALPPALRHSTIIRKGWDNAVDIFVTILLLFFGAFIYFNSHNIQELAKQKLDVKNIIASYAQPPLSTPSTPVVESTHFKRDSSPSRPISNLTVEVTVPEEQQEGDATPKPKRDRSAVGPDSTPRVKIREPSRGPDSDDDVEELDQAASPEKPKKKARRGRRGGKNHRRGKKPDSEGESKDQADRVVDQVNNLQPQSRLEPDLQLVRTVSNDIIEMDGVLQIGRLRVFSDVVLGHGSHGTVVYRGSFDGRDVAVKRMLVEFYDIASHEVGLLQESDDHNNVIRYFCREQAAGFLYIALELCPASLQDLIERPGDYPQLVQGGLDMPDILRQIIAGVRYLHSLKIVHRDLKPQNILVAMPRGRTGSRSLRLLISDFGLCKKLDDNQSSFRATTAHAAGTSGWRAPELLVDDDNRSAIQGGESQHTESSEPAVVDPQTNRRATRAIDIFSLGCVFYYVLTRGSHPFDKNGKFMREANIVKGNFNLDELQRLGDYAFEADDLIRSMLSLDPRKRLAPLCSSLAFRLFTDLFPRPDASAVLMHPFFWNPSDRLSFLCDVSDHFEFEPRDPPSDALLCLESVACRVMGPEMDFLRLLPKDFKDNLGKQRKYTGSKMLDLLRALRNKRNHYNDMPAHLKAHIGGLPEGYLNFWTVRFPSLLMSCHSVIVELRLTKIDRFKRYFTPVE
Protein: Palmitoyltransferase (EC 2.3.1.225) (B4DRN8)
Organism: Homo sapiens (Human)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
Sequence:
MFVWSYWMTIFTSPASPSKEFYLSNSEKERYEKEFSQERQQEILRRAARALPIYTTSASKTIRYCEKCQLIKPDRAHHCSACDSCILKMDHHCPWVNNCVGFSNYKFFLLFLLYSLLYCLFVAATVLEYFIKFWTNELTDTRAKFHVLFLFFVSAMFFISVLSLFSYHCWLVGKNRTTIESFRAPTFSYGPDGNGFSLGCSKNWRQVFGDEKKYWLLPIFSSLGDGCSFPTRLVGMDPEQASVTNQNEYARSSGSNQPFPIKPLSESKNRLLDSESQWLENGAEEGIVKSGV
Protein: Metallothionein-like protein 2A (MT-2A) (MT-K) (MT-1G) (P25860)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Metallothioneins have a high content of cysteine residues that bind various heavy metals (Probable). Functions as metal chelator of copper (Cu) and zinc (Zn). Plays a role in Cu homeostasis, specifically in the remobilization of Cu from senescing leaves. The mobilization of Cu from internal sources is important for seed development.
Interaction partners:
- Metallothionein-like protein 1A
- Metallothionein-like protein 4A
- Metallothionein-like protein 1C
- Metallothionein-like protein 3
- Putative metallothionein-like protein 1B
- Metallothionein-like protein 4B
- NADH dehydrogenase 1 beta subcomplex subunit 3-A
- Probable pectinesterase 55
- Heavy metal-associated isoprenylated plant protein 24
- Polyadenylate-binding protein 3
Sequence:
MSCCGGNCGCGSGCKCGNGCGGCKMYPDLGFSGETTTTETFVLGVAPAMKNQYEASGESNNAENDACKCGSDCKCDPCTCK
Protein: Multiple drug resistance-associated protein-like transporter 1 (MRP-like transporter 1) (Vacuolar multi-drug resistance ABC transporter MTL1) (Q5A762)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Function: Vacuolar multi-drug resistance ABC transporter that may be involved in the transport of bilirubin and glutathione conjugates (By similarity). Plays an important role in virulence.
Subcellular location: Vacuole membrane; Multi-pass membrane protein {ECO:0000269|PubMed:11929516, ECO:0000269|PubMed:16254441}. Note=Associates with lipid rafts in a RTA2-dependent manner. {ECO:0000269|PubMed:22662216}.
Interaction partners:
- ATP-binding cassette transporter
Sequence:
MNESNRELILGLSPVHLSLFNSESLLHTFNFFGVGDGQANIASNYVTASKFVIPQPLYSPHGNALNPAFVELIGQAVNTFFAIFMLFQLTRLLLTKKKSHRIYTPTPFSQTLKISLVLLQVILVASLYFLNKNSYFIGGIAATVLALILHLVEFRRSPIAIESLLTYWSANTAFTFAVFIQDSYSKHKIYANSGPAYVIEIISLVNSFLIFVFEVGYYKPGFEITNEKFLDTVNLFSYFTFYYLQPLINKIYATDDVQLTDLPDILGNITCDDTKAKVAKAWEEELKRTKKPGLVSKVWSFVTRRKVNSKPQMFLAIAKAFFDKFAISITLAIIVTGLSFLQPFLLRKFIQFFSTYFYSVEKPPIIIGYFWASVMFLTSVANFIAFNQAFKTQFDLGYEIQSSLTTLIYEKALRLSPQSRKNKPTGDIINHITMDIDIIFWFCWQLGEYLASPLKLAVCLAALYKLFSNATWAGVITAIIVAPLATLVNASMSKNYIQLMKDKDERTSLITEILNSAKSIKFYSWEKPMLARLSHIRNDRELNNIKKIGVVSALAQFLWSCIPFFISCATYATYAYFYNVPLTPDIVFPALALFDLLSEPMLLIPSFIVEVIEVSTSLARIGELLCLDELADDQHGYVKRDPEPNDNSIYSVIVKDATFVWSEETQQKQYTDEESEVQEVPASNVALKNINFSARKGELACIVGKVGSGKSTLIKAILGDVPIKIPSYSDDSTNPTPSVETFGSIAYCPQNPWILNGTVKENILFGHKYDAEFYQKTIDACELISDFKNLPDGDQTVVGEKGISLSGGQKARISLARSVYTRADIYLLDDILSAVDAHVGKNIIKKVLSNEGLIGNRCRILATNSVPVLHEANDIYLIAGGAFVEHGKFKEVMKRNGDLAKLIKEYGRKKDEPTEEETTEASTEPKEEDHSNGKSDTAVHDELDTDELVDEIVDYVGEQNRGVVEQAILRRASVVSYGHNYENDEADNGQIRKTRHEQEESRKGTVPWDIFKQYIIACDYKYFSFYVAATFSVVLISAGEKYLLSYWSQLNSEQNDTVEPVFFLGTYATLGVVSGFLTYMGALVIWSYCIVKGSTYFHNKMAESVLRSPMSFFDTTPIGRILNRFTEDIGKIDMNLPWTIISFITTLLNGFVTFGVILSFLPLMLVVIVSLLFVYNYFRIRFVPTTRELKRLESIAKSPVLATIQESINGVETIKAFHQRERFVYKSKKLIDEKTLIGVVQQNCNRWLSMRLQTISSSIMFFTALLAVVTLGGKHPILPSILGFVMTYSMSITYILNSLVRIWAEMQAGGVAIERIIEYCDLPSEAPMIIEDKRPQDSWPAHGVVKFKKYSTAYRKHLDPVLREIELTINSKEKVGIVGRTGAGKSSLTLALFRIIEATGGNIEIDGVDTSQIGLYDLRHHLTIIPQEAHTFRASVRENLDPFGEYSDDKLWKVLELAHLKEHVTKMETDPTEEEKKASKNPDELSKKVGLDAQIEEGGSNLSSGQKQLLCLARALLNETSKILVLDEATAAVDFQTDKIIQETIRTEFKDKTILTIAHRIDTIMDSDKILVLDSGKVAEFDSPQNLLKNKDSIFYSLAKEGGYID
Protein: Protein RecT (P33) (P33228)
Organism: Escherichia coli (strain K12)
Function: Binds to single-stranded DNA and also promotes the renaturation of complementary single-stranded DNA. Function in recombination. Has a function similar to that of lambda RedB.
Interaction partners:
- Exodeoxyribonuclease 8
- Protein RecA
- Single-stranded DNA-binding protein
- Double-strand break reduction protein
- Endodeoxyribonuclease toxin RalR
- Uncharacterized protein YdaQ
Sequence:
MTKQPPIAKADLQKTQGNRAPAAVKNSDVISFINQPSMKEQLAAALPRHMTAERMIRIATTEIRKVPALGNCDTMSFVSAIVQCSQLGLEPGSALGHAYLLPFGNKNEKSGKKNVQLIIGYRGMIDLARRSGQIASLSARVVREGDEFSFEFGLDEKLIHRPGENEDAPVTHVYAVARLKDGGTQFEVMTRKQIELVRSLSKAGNNGPWVTHWEEMAKKTAIRRLFKYLPVSIEIQRAVSMDEKEPLTIDPADSSVLTGEYSVIDNSEE