wanglab/gogpt-training-data huggingface dataset:
Protein: Interferon regulatory factor 3 (Q5XIB0)
Organism: Rattus norvegicus (Rat)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- Histone lysine acetyltransferase CREBBP
- Serine/threonine-protein kinase TBK1
- Interferon regulatory factor 7.
- Inhibitor of nuclear factor kappa-B kinase subunit epsilon
- Interferon beta
- Ubiquitin-like protein ISG15
- Mitochondrial antiviral-signaling protein
- histone acetyltransferase
- Z-DNA-binding protein 1
- Stimulator of interferon genes protein
Sequence:
MGTPKPLILPWLVSQLDLGQLKGVAWLDESRTKFRIPWKHGLRQDAQMADFGIFQAWAEASGAYTPGKDKPDLSTWKRNFRSALNRKEVLRLAEDRSKDPFDPHKVYEFVTPGGARDFVHLDTSPDTNGKSSLSDHQEDLLELLDHMALGPLPDEGSSDLPIASDPSQPPLSPIVNNFPNPAPQENPLRQLLAEEQWEFEVTAFYRGRQVFQQTLFCPGGLRLVGSTSDNGTLPWQPVTLPDPEEFLTDRLVREYVRQVLKGLGKGLVLWRAGQCLWAQRLGHSHSFWALGEELLPDSGRGPDGEVPKDKNGVVFDLRPFVADLIAFMEGSRHSPRYTLWFCVGESWPQDQPWVKRLVMVKVVPTCLKELLEMAREGGASSLKTVDLHISNSQPISLTSDQYKACLQDLVEDMDFQATGET
Protein: Telomere length regulation protein TEL2 (P53038)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Part of the TTT complex that is required to stabilize protein levels of the phosphatidylinositol 3-kinase-related protein kinase (PIKK) family proteins (By similarity). Required for telomere length regulation and telomere position effect. Regulates telomere length and participates in gene silencing at subtelomeric regions. Binds to telomeric DNA repeats.
Subcellular location: Nucleus {ECO:0000305}. Chromosome, telomere {ECO:0000305}.
Interaction partners:
- TEL2-interacting protein 1
- RuvB-like protein 2
- TEL2-interacting protein 2
- RuvB-like protein 1
- SAGA complex/NuA4 acetyltransferase complex subunit TRA1
- ASTRA-associated protein 1
- Serine/threonine-protein kinase TOR2
- Serine/threonine-protein kinase TOR1
- DNA repair protein RAD1
- Serine/threonine-protein kinase MEC1
Sequence:
MVLETLKQGLDSSQIHEALIQLDSYPREPVDLDASMVLIKFVIPVYPSLPERSKVILRRLASKSFTFLCQIVTFSRTISGRDGLQEIRIYQEILEDIISFEPGCLTFYLKASTTSKADRDSIKALFFGSKLFNVLANRIDMAKYLGYLRLQWKFLLESNETDPPGFLGEWLVSSFLLNPVLAADMLLGELFLLKESYFFSFQKIISASSLIDQKRLIAKFLLPYIQVIVTLENLNDVRKILRRFDLDKIISLSVLFEIQSLPLKEVIVRLMSNHSSTKFVSALVSKFADFTDEEVDTKTCELLVLFAVHNLNHSQREEIAHDERFLNGVTKHLGSNEREARERAMFIAKLLSGGHLKYESDFKINIPNVKFESNSDDKIIDFQSLKNPSICNTQTDVGKDKITEVSGHVQSLTLDCSDSDDEDENDEREIVKRIVFLKDLMKEYEKTGESRKAPLIPLLKQTVKLIRQKADFQLEVGYYAQGILSSIVCLNNEFDEPLFEQWRINALTSILVVLPEKVNGAINILFNSELSLQQRMSLLSALGLSARELRGLDDPTIVKPKFDFPTNRLPWDDQSHHNSRLVEVQESTSMIKKTKTVWKSRKLGKDREKGTQNRFRKYAGLFFYPLAHGWLNGIDVGTYNQLFKSHYLTTLRIIYSCANPVHDFESMTELMNHIISSAIEEGISLNKG
Protein: Putrescine transport ATP-binding protein PotG (EC 7.6.2.16) (P31134)
Organism: Escherichia coli (strain K12)
Function: Part of the ABC transporter complex PotFGHI involved in putrescine uptake. Responsible for energy coupling to the transport system. Imports putrescine for maintenance of the optimal concentration of polyamines necessary for cell growth in the presence of glucose.
Subcellular location: Cell inner membrane {ECO:0000305}; Peripheral membrane protein {ECO:0000305}.
Interaction partners:
- Putrescine transport system permease protein PotI
- Putrescine transport system permease protein PotH
- Putrescine-binding periplasmic protein PotF
- Spermidine/putrescine transport system permease protein PotB
- Spermidine/putrescine transport system permease protein PotC
- ATP-dependent lipid A-core flippase
- Maltose/maltodextrin import ATP-binding protein MalK
- sn-glycerol-3-phosphate import ATP-binding protein UgpC
- Maltose/maltodextrin transport system permease protein MalG
- sn-glycerol-3-phosphate transport system permease protein UgpE
Sequence:
MNDAIPRPQAKTRKALTPLLEIRNLTKSYDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPSAGQIMLDGVDLSQVPPYLRPINMMFQSYALFPHMTVEQNIAFGLKQDKLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLLDEPMGALDKKLRDRMQLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEIYEHPTTRYSAEFIGSVNVFEGVLKERQEDGLVLDSPGLVHPLKVDADASVVDNVPVHVALRPEKIMLCEEPPANGCNFAVGEVIHIAYLGDLSVYHVRLKSGQMISAQLQNAHRHRKGLPTWGDEVRLCWEVDSCVVLTV
Protein: ATP synthase peripheral stalk subunit F6, mitochondrial (ATPase subunit F6) (ATP synthase peripheral stalk subunit F6) (P97450)
Organism: Mus musculus (Mouse)
Function: Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Part of the complex F(0) domain and the peripheric stalk, which acts as a stator to hold the catalytic alpha(3)beta(3) subcomplex and subunit a/ATP6 static relative to the rotary elements. Also involved in the restoration of oligomycin-sensitive ATPase activity to depleted F1-F0 complexes.
Subcellular location: Mitochondrion. Mitochondrion inner membrane.
Interaction partners:
- ATP synthase F
- ATP synthase peripheral stalk subunit OSCP, mitochondrial
- ATP synthase peripheral stalk subunit b, mitochondrial
- ATP synthase F
- ATP synthase peripheral stalk subunit d, mitochondrial
- ATP synthase F
- ATP synthase F
- ATP synthase F
- ATP synthase F
- ATP synthase F
Sequence:
MVLQRIFRLSSVLRSAVSVHLKRNIGVTAVAFNKELDPVQKLFVDKIREYKSKRQASGGPVDIGPEYQQDLDRELYKLKQMYGKGEMDTFPTFKFDDPKFEVIDKPQS
Protein: Neprilysin (EC 3.4.24.11) (Atriopeptidase) (Common acute lymphocytic leukemia antigen) (CALLA) (Enkephalinase) (Neutral endopeptidase 24.11) (NEP) (Neutral endopeptidase) (Skin fibroblast elastase) (SFE) (CD antigen CD10) (P08473)
Organism: Homo sapiens (Human)
Function: Thermolysin-like specificity, but is almost confined on acting on polypeptides of up to 30 amino acids. Biologically important in the destruction of opioid peptides such as Met- and Leu-enkephalins by cleavage of a Gly-Phe bond. Catalyzes cleavage of bradykinin, substance P and neurotensin peptides. Able to cleave angiotensin-1, angiotensin-2 and angiotensin 1-9. Involved in the degradation of atrial natriuretic factor (ANF) and brain natriuretic factor (BNP(1-32)). Displays UV-inducible elastase activity toward skin preelastic and elastic fibers.
Subcellular location: Cell membrane {ECO:0000269|PubMed:20876573}; Single-pass type II membrane protein {ECO:0000255}.
Interaction partners:
- Angiotensin-converting enzyme 2
- Dipeptidyl peptidase 4
- Angiotensinogen
- B-lymphocyte antigen CD19
- Lysosomal Pro-X carboxypeptidase
- Insulin-degrading enzyme
- Xaa-Pro aminopeptidase 2
- B-cell lymphoma 6 protein
- Meprin A subunit beta
- T-cell surface glycoprotein CD5
Sequence:
MGKSESQMDITDINTPKPKKKQRWTPLEISLSVLVLLLTIIAVTMIALYATYDDGICKSSDCIKSAARLIQNMDATTEPCTDFFKYACGGWLKRNVIPETSSRYGNFDILRDELEVVLKDVLQEPKTEDIVAVQKAKALYRSCINESAIDSRGGEPLLKLLPDIYGWPVATENWEQKYGASWTAEKAIAQLNSKYGKKVLINLFVGTDDKNSVNHVIHIDQPRLGLPSRDYYECTGIYKEACTAYVDFMISVARLIRQEERLPIDENQLALEMNKVMELEKEIANATAKPEDRNDPMLLYNKMTLAQIQNNFSLEINGKPFSWLNFTNEIMSTVNISITNEEDVVVYAPEYLTKLKPILTKYSARDLQNLMSWRFIMDLVSSLSRTYKESRNAFRKALYGTTSETATWRRCANYVNGNMENAVGRLYVEAAFAGESKHVVEDLIAQIREVFIQTLDDLTWMDAETKKRAEEKALAIKERIGYPDDIVSNDNKLNNEYLELNYKEDEYFENIIQNLKFSQSKQLKKLREKVDKDEWISGAAVVNAFYSSGRNQIVFPAGILQPPFFSAQQSNSLNYGGIGMVIGHEITHGFDDNGRNFNKDGDLVDWWTQQSASNFKEQSQCMVYQYGNFSWDLAGGQHLNGINTLGENIADNGGLGQAYRAYQNYIKKNGEEKLLPGLDLNHKQLFFLNFAQVWCGTYRPEYAVNSIKTDVHSPGNFRIIGTLQNSAEFSEAFHCRKNSYMNPEKKCRVW
Protein: Bone marrow proteoglycan (BMPG) (Proteoglycan 2) [Cleaved into: Eosinophil granule major basic protein (EMBP) (MBP)] (Q61878)
Organism: Mus musculus (Mouse)
Function: Cytotoxin and helminthotoxin. MBP also induces non-cytolytic histamine release from basophils. It is involved in antiparasitic defense mechanisms and immune hypersensitivity reactions (By similarity).
Subcellular location: Secreted {ECO:0000250|UniProtKB:P13727}.
Interaction partners:
- Pappalysin-1
- Eosinophil peroxidase
- Proteoglycan 3
Sequence:
MKFPLLLALLVGGASALHLSSETSDSKSPLMDENLPRDAEISGPEGEECPPGEELMPLEGEKEEGSGSEGVPGDEGAVSGQDVTDVDLQCPKEEDTTSLMGDSGCKTCRYLLVRRAECFDKAQSVCRRCYRGTLASIHSFSVNFGIQSAVRGINQGQVWIGGRIKGWGRCKRFRWVDGSSWNFAYWAAGQPCPGGGRCVTLCTQGGHWRLSHCVKRRPFICSY
Protein: Embryonic mRna (mRNA) Anterior (O45146)
Organism: Caenorhabditis elegans
Interaction partners:
- Inactive protein-tyrosine phosphatase egg-5
- RNA-binding protein pos-1
- Chondroitin proteoglycan 4 domain-containing protein
- Pumilio domain-containing protein 7
- Protein lilliputian
- Chitin-binding domain protein cbd-1
- glutamine synthetase
- PUM-HD domain-containing protein
- C-type lectin domain-containing protein 87
- DNA-dependent metalloprotease dvc-1
Sequence:
MADLTALIAIIRDWYSASVQRRQMIENSHIIPSSEFNIFRSARMAGDDVPSTSGAPPGSSSAPTPAGNQVAPMPATRPREAESQNAAQPGLSTQIWRAICPLCGSNRVSNTEENTNVPVTGNVTPRDVQTDQPVADLQSPPLSPSSSVEQSGSLPPLPESPASQANRESTSAQPRLDQIPEDPSEASMANQTPSEQSSRDRDSQCSCPSRAPVEDPVASFELNDKDSISIPSDSGASLRTGSAGSGGEPEVPLAQNNPEARGRREWLQHQNAVGSGDTPSTRPSTAENNSDHGEGPSEPQNRPPSRPEDDDDDSNKPSTSGFIRKGKSLSRQMKVSVAHFWNEYKTVYPSERLPAPTTSPGSPKINDGKECWLDSFKNRTIEQDLFTF
Protein: B3 domain-containing protein IDEF1 (Protein IRON DEFICIENCY-RESPONSIVE ELEMENT FACTOR 1) (Q6Z1Z3)
Organism: Oryza sativa subsp. japonica (Rice)
Function: Transcription regulator involved in iron deficiency response and tolerance. May regulate directly iron transporters or other transcription factors involved in iron-deficiency response. Binds specifically to the DNA sequence 5'-CATGC-3' of the IDE1 element found in the promoter of the barley iron deficiency-inducible gene IDS2.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00326, ECO:0000269|PubMed:18025467}.
Interaction partners:
Sequence:
MGQMDGGDGGGGGHPYHYQALLAAVHQQTVPFPNPFPAPSSGAEPPHPHNHNHNHNHNHNIHNSHNHNHNHNAAPHPCHTPTPTPTPRGFADWSASTSAFTSLAAHSSTAPSNAVHYSFSPCYAFWTHYMLNKNAYPTSFPAPHDDHLRLANNNHPRDAPGPASSYGVESFTSPSMAPNICTHMPPIEGPISAKEDKKPEILPRVVKSSDELETRNSNVEFHSETVGTLPESKQGHDSRATKLLNSGEYQVILRKELTKSDVGNVGRIVLPKKDAEASLPPLLQRDPLILHMDDMVLPVTWKFKYRYWPNNKSRMYILDSAGEFLKTHGLQAGDVIIIYKNLAPGKFIIRGEKAIHQQTTNP
Protein: Retinoic acid early-inducible protein 1-gamma (RAE-1-gamma) (O08604)
Organism: Mus musculus (Mouse)
Function: Acts as a ligand for KLRK1.
Subcellular location: Cell membrane {ECO:0000269|PubMed:10894171, ECO:0000269|PubMed:8982867}; Lipid-anchor, GPI-anchor {ECO:0000269|PubMed:10894171, ECO:0000269|PubMed:8982867}.
Interaction partners:
Sequence:
MAKAAVTKRHHFMIQKLLILLSYGYTNGLDDAHSLRCNLTIKAPTPADPLWYEAKCLVDEILILHLSNINKTMTSGDPGETANATEVGECLTQPVNDLCQKLRDKVSNTKVDTHKTNGYPHLQVTMIYPQSQGQTPSATWEFNISDSYFFTFYTENMSWRSANDESGVIMNKWNDDGDLVQRLKYFIPECRQKIDEFLKQSKEKPRSTSRSPSITQLTSTSPLPPPSHSTSKKGFISVGLIFISLLFAFAFAM
Protein: Nitric oxide synthase (EC 1.14.13.39) (A2BIN8)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Cytoplasm, cytosol {ECO:0000256|ARBA:ARBA00004514}.
Interaction partners:
- Argininosuccinate lyase
- Calmodulin
- Arginase
- Arginase
- non-specific serine/threonine protein kinase
- V-akt murine thymoma viral oncogene homolog 2,-like.
- non-specific serine/threonine protein kinase
- Non-specific serine/threonine protein kinase.
- non-specific serine/threonine protein kinase
- Calmodulin-like protein 4
Sequence:
MGRQAQTTIIENEKQTVQSKRPVDRPIRCPFAVQLRNYKDGSTHQDSLHHKAAKNTPCNSKTCEGSIMNPKPLIRGPSKITPSPDDMLSQAEDFIDQYYKSLKIPGSTEQQARIDRIALEITLTGTYSLTTEELAFGAKQAWRNAPRCIGRIQWSNLQLFDARDCKTAEDMFHALCTHLKYATNGGNLRSAITVFPQRTDEGHDFRVWNGQLIKYAGYQMDDGSVIGDPAGVDFTQVCIQLGWKPKYGRFDVLPLVLQANGEDPEVFEIPPELILEVPIEHPEYEWFKDLDLKWYAIPAVANMLMEVGGLEFTACPFNGWYMGTEIGVRDFCDSQRYNILERVGQLMGLETRKLSSLWKDQALVAINVAVIHSYQKNKVTITDHHSASESFMQHLETEVRLRGGCPADWVWLVPPMSGSLTPVYHQELLNYILSPFFYYQTDPWLTHKWKDEKKGLRRCKVSFKGLIRAVFFSQTLIKAVLAKRVRCTVLYATETGKSLSFAKKLNTMLNRAFDSRLVCMEEYDFSELETETLLMVVTSTFGNGESPGNGVTFRKQLFSLQKVKNTIRYGVFGLGSRVYPQFCAFAHAVDDKLAELGAKRMTATGEGDELNGQDEAFSAWACTAFKDACEEFNIKKQLKAVEEQTEGWDPQRYRVQQDSCTLDPITALSALHSKTVFPMTLKRRQKLQSAQSSRSTILVELKTDGNTDALKFAPGDHVGIFPENSSELVHGIVKHLPDATPDNQSLRLETLSESSHEGKRWQTDERLPACTLVQALTYFLDVTTPPSQSLLRKLSTVADQEEDRKRLEALASDFQEYSTWKDFYRPTFLEVLEEFPSLKVPSAFILSQIPLLKPRLYSVSSSLDHHPNELHLTISVVEYQTQGGAGPMHFGTCSTWFNTIKRGHTVPCFVHRSGGFHLPEDPSTPVLLIGAGSGIAPFRSFWQQRTQDVKKTGQQISPMTLLFGCRDSETDHLYKVETLKLRLNGILGNVNTAYSRQPGKPKMYVQDVLKEQLVEKALEVLHKSAGHLYVCGGMNMAKDVAQTLKDILVNNTIMSEVEAGEYMDMLKVEKRYHEDIFGA
Protein: Cytoplasmic linker associated protein 2 (A0A0U1RQI6)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MRRLICKRICDYKSFDDEESVDGNRPSSAASAFKVPAPKTSGNPANSARKPGSAGGPKVGGASKEGGAGAVDEDDFIKAFTDVPSIQIYSSRELEETLNKIREILSDDKHDWDQRANALKKIRSLLVAGAAQYDCFFQHLRLLDGALKLSAKDLRSQVVREACITVAHLSTVLGNKFDHGAEAIVPTLFNLVPNSAKVMATSGCAAIRFIIRHTHVPRLIPLITSNCTSKSVPVRRRSFEFLDLLLQEWQTHSLERHAAVLVETIKKGIHDADAEARVEARKTYMGLRNHFPGEAETLYNSLEPSYQKSLQTYLKSSGSVASLPQSDRSSSSSQESLNRPFSSKWSTANPSTVAGRVSAGSSKASSLPGSLQRSRSDIDVNAAAGAKAHHAAGQSVRSGRLGAGALNAGSYASLEDTSDKLDGTASEDGRVRAKLSAPLAGMGNAKADSRGRSRTKMVSQSQRSSSPDKNEGSQSANTIGAGSRSGSPGRVLTTTALSTVSSGVQRVLVNSASAQKRSKIPRSQGCSREASPSRLSVARSSRIPRPSVSQGCSREASRESSRDTSPVRSFQPLGPGYGISQSSRLSSSVSAMRVLNTGSDVEEAVADALLLGDIRTKKKPARRRYESYGMHSDDDANSDASSACSERSYSSRNGSIPTYMRQTEDVAEVLNRCASSNWSERKEGLLGLQNLLKNQRTLSRVELKRLCEIFTRMFADPHGKVFSMFLETLVDFIQVHKDDLQDWLFVLLTQLLKKMGADLLGSVQAKVQKALDVTRESFPNDLQFNILMRFTVDQTQTPSLKVKVAILKYIETLAKQMDPGDFINSSETRLAVSRVITWTTEPKSSDVRKAAQSVLISLFELNTPEFTMLLGALPKTFQDGATKLLHNHLRNTGNGTQSSMGSPLTRPTPRSPANWSSPLTSPTNTSQNTLSPSAFDYDTENMNSEDIYSSLRGVTEAIQNFSFRSQEDMNEPLKRDSKKDDGDSMCGGPGMSDPRAGGDATDSSQTALDNKASLLHSMPTHSSPRSRDYNPYNYSDSISPFNKSALKEAMFDDDADQFPDDLSLDHSDLVAELLKELSNHNERVEERKIALYELMKLTQEESFSVWDEHFKTILLLLLETLGDKEPTIRALALKVLREILRHQPARFKNYAELTVMKTLEAHKDPHKEVVRSAEEAASVLATSISPEQCIKVLCPIIQTADYPINLAAIKMQTKVIERVSKETLNLLLPEIMPGLIQGYDNSESSVRKACVFCLVAVHAVIGDELKPHLSQLTGSKMKLLNLYIKRAQTGSGGADPTTDVSGQS
Protein: Allergen Pet c 1 (allergen Allergen Pet c 1.0201) (C0HKF5)
Organism: Petroselinum crispum (Parsley) (Petroselinum hortense)
Interaction partners:
Sequence:
GVQKTVVEAPSTVSAEKMYGFLLDMDTVFPKVLPQLIGKSVEILEGDGSVGTVKLVHLGEATEYTTMKQRVDVIDKAGLAYTYTTIGGDILVEVLESVVNEFVVVPTDGGCIVKNTTIYNTKGDAVLPEDKVKEATEKSALAFKAVEAYLLAN
Protein: Probable cyclin-dependent kinase 8 (EC 2.7.11.22) (EC 2.7.11.23) (Ddcdk8) (Q95YH0)
Organism: Dictyostelium discoideum (Social amoeba)
Function: Component of the Mediator complex, a coactivator involved in regulated gene transcription of nearly all RNA polymerase II-dependent genes. Mediator functions as a bridge to convey information from gene-specific regulatory proteins to the basal RNA polymerase II transcription machinery. Mediator is recruited to promoters by direct interactions with regulatory proteins and serves as a scaffold for the assembly of a functional pre-initiation complex with RNA polymerase II and the general transcription factors. Phosphorylates the CTD (C-terminal domain) of the large subunit of RNA polymerase II (RNAp II), which may inhibit the formation of a transcription initiation complex (By similarity). Involved in cell aggregation, but not growth. Required for starvation-induced expression of genes essential for early development of acaA and/or other genes.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- Cyclin-C
- Putative mediator of RNA polymerase II transcription subunit 14
- Putative mediator of RNA polymerase II transcription subunit 7
- Putative mediator of RNA polymerase II transcription subunit 6
- Putative mediator of RNA polymerase II transcription subunit 31
- Putative mediator of RNA polymerase II transcription subunit 18
- Putative mediator of RNA polymerase II transcription subunit 21
- Putative mediator of RNA polymerase II transcription subunit 12
- Large ribosomal subunit protein uL6
- Putative mediator of RNA polymerase II transcription subunit 27
Sequence:
MNTHNQSSNQNGGGSGGGGGGGGSSTFSPIVLTSTYRLDVQEKYTFSYEIGSGTYGMVYKADDKKRPNNKVAVKKFRSTKEGEGLSLTAYREIGLLKELSNENIVKLLDVCLNPKDKLLYLIFDYAEFDLFGIIKYHRENGSHFSDATIKSLIWQVLNGIHYLHSNWVIHRDLKPSNILVMGEGKECGTVKIGDFGLARIFQSPLKPLNENGVVVTIWYRSPELLLGSKHYTRAVDIWAIGCIFAELITTKPLFPGKEKDPKIPSLFQDDQVEKIIRVLGKPTLDMWPDIKHLPEWKRLSSMEAFPNSLAKCVGIDENSQAYDLLSKMILYDPSKRITASEALDHPYFKELPLPLPNAFSKPIPYPPRLPINKKKREFDD
Protein: Small ribosomal subunit protein eS7 (40S ribosomal protein S7) (P62084)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250|UniProtKB:P62081}. Cytoplasm {ECO:0000250|UniProtKB:P62081}. Nucleus {ECO:0000250|UniProtKB:P62081}.
Interaction partners:
- Small ribosomal subunit protein eS8
- Large ribosomal subunit protein eL39
- FAU ubiquitin-like and ribosomal protein S30 fusion b
- Small ribosomal subunit protein eS17
- Small ribosomal subunit protein eS1
- Small ribosomal subunit protein uS12
- Large ribosomal subunit protein eL13
- Ribosomal protein S10
- Large ribosomal subunit protein uL16
- Small ribosomal subunit protein uS2
Sequence:
MFSTSAKIVKPNGEKPDEFESGISQALLELEMNSDLKAQLRELHITAAKEIEVGGSRKAIIIFVPVPQLKSFQKIQVRLVRELEKKFSGKHVVFIAQRRILPKPTRKSRTKNKQKRPRSRTLTNVHDAILEDLVFPSEIVGKRIRVKLDSSRLIKVHLDKAQQNNVEHKVETFAGVYKKLTGKDVIFEFPEFQL
Protein: UDP-N-acetylglucosamine transferase subunit ALG13 (EC 2.4.1.141) (Asparagine-linked glycosylation protein 13) (P53178)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Involved in protein N-glycosylation. Essential for the second step of the dolichol-linked oligosaccharide pathway.
Subcellular location: Endoplasmic reticulum {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:16100110}.
Interaction partners:
- Chitobiosyldiphosphodolichol beta-mannosyltransferase
- UDP-N-acetylglucosamine transferase subunit ALG14
- UDP-N-acetylglucosamine--dolichyl-phosphate N-acetylglucosaminephosphotransferase
- GDP-Man:Man
- Dolichyl pyrophosphate Glc1Man9GlcNAc2 alpha-1,3-glucosyltransferase
- Dol-P-Man:Man
- Dolichyl pyrophosphate Man9GlcNAc2 alpha-1,3-glucosyltransferase
- Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit STT3
- Dol-P-Man:Man
- Dolichol-phosphate mannosyltransferase
Sequence:
MGIIEEKALFVTCGATVPFPKLVSCVLSDEFCQELIQYGFVRLIIQFGRNYSSEFEHLVQERGGQRESQKIPIDQFGCGDTARQYVLMNGKLKVIGFDFSTKMQSIIRDYSDLVISHAGTGSILDSLRLNKPLIVCVNDSLMDNHQQQIADKFVELGYVWSCAPTETGLIAGLRASQTEKLKPFPVSHNPSFERLLVETIYS
Protein: Peroxisome biogenesis protein 20 (Peroxin-20) (Pppex20) (Q2VUH8)
Organism: Komagataella pastoris (Yeast) (Pichia pastoris)
Function: Coreceptor required for the peroxisomal import of proteins containing a C-terminal PTS2-type peroxisomal targeting signal, such as 3-oxoacyl-CoA thiolase. Acts via its interaction with PEX7, promoting association between PEX7 bound to cargo proteins and the PEX13-PEX14 docking complex. PEX20 along with PEX7 and PTS2-containing cargo proteins are tranlocated into peroxisomes by passing through the PEX13-PEX14 docking complex. PEX20 coreceptor is then retrotranslocated into the cytosol, leading to release of bound cargo in the peroxisome matrix, and reset for a subsequent peroxisome import cycle. Also mediates peroxisomal import of proteins that do not contain PTS1- or PTS2-type peroxisomal targeting signals, such as acyl-CoA oxidases (Aox) izozymes (By similarity). Import of acyl-CoA oxidases (Aox) izozymes is independent of PEX7 (By similarity). Required for PEX7 ubiquitination.
Subcellular location: Cytoplasm, cytosol {ECO:0000269|PubMed:16390998, ECO:0000269|PubMed:17209040, ECO:0000269|PubMed:23344950}. Peroxisome matrix {ECO:0000269|PubMed:16390998, ECO:0000269|PubMed:17209040, ECO:0000269|PubMed:23344950}. Note=Cycles between the cytosol and the peroxisome matrix (PubMed:16390998, PubMed:17209040, PubMed:23344950). Following binding to cargo proteins in the cytosol, recruited to the docking complex, composed of PEX13 and PEX14, leading to translocation into the peroxisome matrix along with cargo proteins (PubMed:16390998). Export and recycling to the cytosol is initiated by binding to the PEX2-PEX10-PEX12 retrotranslocation channel (PubMed:16390998). Cys-8 of PEX20 is then monoubiquitinated by PEX2, promoting its extraction from peroxisomal membrane by the PEX1-PEX6 AAA ATPase complex (PubMed:23344950). Extraction is accompanied by release of bound cargo in the peroxisome matrix (By similarity). {ECO:0000250|UniProtKB:P50542, ECO:0000269|PubMed:16390998, ECO:0000269|PubMed:17209040, ECO:0000269|PubMed:23344950}.
Interaction partners:
Sequence:
MFTSNGSCGPATALDNLSKRVGQDRTLENDHVARFRDQNSSQNRAFRAESSFNTTAGAEFGQFQNTSVQRNYFPSAELIRKNTRFGDNWSSEFRQQQENNKWVEDFGAMNLENVRMEQEQSFQTMDQRTNMQAMSSTANAWTQEFNHMQHNKEMEYEMRIRETQRLVNAPAREVFSMVNQHSQQHNQNFTHNQTQLGDQSHYMTNLAFERQFETVQNEIDGMDMFSDSEQVEQQKELQKEDDNNDIETTKFAEIAQQVFNQMNNVDTTVSQNTEHKFKQSNFLRLMDKVAQREVEINGSGDRFIDKTGNDIRDYLPDPLSDLR
Protein: Proteasome regulatory non-ATP-ase subunit 3 (Q386U6)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Proteasome regulatory ATPase subunit 3
- Protease regulatory ATPase subunit 4
- Proteasome regulatory non-ATP-ase subunit 2
- Proteasome regulatory non-ATP-ase subunit 10
- Proteasome regulatory non-ATP-ase subunit 7
- Proteasome regulatory non-ATP-ase subunit 9
- Proteasome regulatory ATPase subunit 1
- Proteasome regulatory ATPase subunit 5
- Proteasome subunit beta
- Proteasome regulatory non-ATPase subunit 8
Sequence:
MQTTGELTLKQQLQQSGSKGNDELLGRLMSLYRALCVRHDEVGQEMLLNDILALLTLNHQHDLAERVIATCEISLPHRSNNQAARYFYYVGLTHALRLGYVEADQFLQYALRKAPERASGFRVAATKLSLVVQLLLGEIPPRSDFLQKDMRECLSPYLQLTSCVRFGQLGRFMSILQQHKAIFEHDRTYSLILRVRQHVIRTGLRRICQAYSRISIPDVCAKLSMENPDDAEYIIAKAIRSGVIDAVIDHEQRHLISSETVDVYSTSEPLLALQRRIQFLNATHNEVKRSMRYSAADPDLEEERRKVDREEMDSLLRAIEDEELGGADFEDGLP
Protein: Potassium voltage-gated channel protein Shaker (Protein minisleep) (P08510)
Organism: Drosophila melanogaster (Fruit fly)
Function: Voltage-gated potassium channel that mediates transmembrane potassium transport in excitable membranes. The channel alternates between opened and closed conformations in response to the voltage difference across the membrane. Forms rapidly inactivating tetrameric potassium-selective channels through which potassium ions pass in accordance with their electrochemical gradient and may contribute to A-type currents. Plays a role in the regulation of sleep need or efficiency. Plays a role in sexual behavior, where it is important for male sex discrimination.
Subcellular location: Cell membrane {ECO:0000269|PubMed:2448636}; Multi-pass membrane protein {ECO:0000305}. Membrane raft {ECO:0000269|PubMed:21813698}; Multi-pass membrane protein {ECO:0000305}. Cell projection, neuron projection {ECO:0000269|PubMed:20010822}. Perikaryon {ECO:0000269|PubMed:20010822}. Note=Localizes to both neuronal cell body and cell projections but requires qvr/quiver/sleepless for targeting to or retention in cell projections. {ECO:0000269|PubMed:20010822}.
Interaction partners:
- Hyperkinetic, isoform M
- Disks large 1 tumor suppressor protein
- Large ribosomal subunit protein eL31
- Large ribosomal subunit protein eL43
- 40S ribosomal protein S24
- Large ribosomal subunit protein eL21
- FI01658p
- Large ribosomal subunit protein eL38
- Small ribosomal subunit protein eS6
- Small ribosomal subunit protein eS17
Sequence:
MAAVAGLYGLGEDRQHRKKQQQQQQHQKEQLEQKEEQKKIAERKLQLREQQLQRNSLDGYGSLPKLSSQDEEGGAGHGFGGGPQHFEPIPHDHDFCERVVINVSGLRFETQLRTLNQFPDTLLGDPARRLRYFDPLRNEYFFDRSRPSFDAILYYYQSGGRLRRPVNVPLDVFSEEIKFYELGDQAINKFREDEGFIKEEERPLPDNEKQRKVWLLFEYPESSQAARVVAIISVFVILLSIVIFCLETLPEFKHYKVFNTTTNGTKIEEDEVPDITDPFFLIETLCIIWFTFELTVRFLACPNKLNFCRDVMNVIDIIAIIPYFITLATVVAEEEDTLNLPKAPVSPQDKSSNQAMSLAILRVIRLVRVFRIFKLSRHSKGLQILGRTLKASMRELGLLIFFLFIGVVLFSSAVYFAEAGSENSFFKSIPDAFWWAVVTMTTVGYGDMTPVGVWGKIVGSLCAIAGVLTIALPVPVIVSNFNYFYHRETDQEEMQSQNFNHVTSCPYLPGTLGQHMKKSSLSESSSDMMDLDDGVESTPGLTETHPGRSAVAPFLGAQQQQQQPVASSLSMSIDKQLQHPLQQLTQTQLYQQQQQQQQQQQNGFKQQQQQTQQQLQQQQSHTINASAAAATSGSGSSGLTMRHNNALAVSIETDV