wanglab/gogpt-training-data huggingface dataset:
Protein: (DL)-glycerol-3-phosphatase 1, mitochondrial (EC 3.1.3.21) (5-amino-6-(5-phospho-D-ribitylamino)uracil phosphatase) (AtGpp1/PyrP3) (EC 3.1.3.104) (5-amino-6-ribitylamino-2,4(1H,3H)-pyrimidinedione 5'-phosphate phosphatase) (ARPP phosphatase) (Glycerol-1-phosphatase 1) (AtGPP1) (Haloacid dehalogenase-like hydrolase domain-containing protein GPP1) (F4JTE7)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Acts as a glycerol-3-phosphatase with higher stereospecificity for L-glycerol-3-phosphate than DL-glycerol-3-phosphate. Can also dephosphorylate in vitro 5-amino-6-(5-phospho-D-ribitylamino)uracil, also known as ARPP.
Subcellular location: Mitochondrion {ECO:0000269|PubMed:27490826}.
Interaction partners:
- Glycerol kinase
- 
- Aldo-keto reductase family 4 member C10
- Alpha/beta-Hydrolases superfamily protein
- Alpha/beta-Hydrolases superfamily protein
- Alpha/beta-Hydrolases superfamily protein
- Gamma-glutamyl peptidase 2
- Haloacid dehalogenase-like hydrolase domain-containing protein At2g33255
- Phosphomannomutase
- Gamma-glutamyl peptidase 1
Sequence:
MLTTPTRFVALRIPFRSSNKIPISIAPSPKVFPRKPVIRVPASLRFVATMSTPAAAVNATVTVTDAGRGSITHVIFDMDGLLLDTEKFYTEVQEKILARYNKTFDWSLKAKMMGRKAIEAARLFVDESGISDSLSAEDFIVERESMLQDLFPTSDLMPGASRLLRHLHGKGIPICIATGTHTRHFDLKTQRHRELFSLMHHVVRGDDPEVKEGKPAPDGFLAASRRFEDGPVDPRKVLVFEDAPSGVQAAKNAGMNVIMVPDSRLDKSYCNVADQVLASLLDFKPEEWGLPSFQDSHN
Protein: Urea amidolyase [Includes: Urea carboxylase (EC 6.3.4.6); Allophanate hydrolase (EC 3.5.1.54)] (P32528)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Hydrolysis of urea to ammonia and CO(2).
Interaction partners:
- Arginase
- Glutamyl-tRNA
- Allantoicase
- Ureidoglycolate lyase
- Allantoinase
- Transcriptional activator protein DAL81
- Protein DAL82
- Urea active transporter
- Glutamine synthetase
- Acetyl-CoA carboxylase
Sequence:
MTVSSDTTAEISLGWSIQDWIDFHKSSSSQASLRLLESLLDSQNVAPVDNAWISLISKENLLHQFQILKSRENKETLPLYGVPIAVKDNIDVRGLPTTAACPSFAYEPSKDSKVVELLRNAGAIIVGKTNLDQFATGLVGTRSPYGKTPCAFSKEHVSGGSSAGSASVVARGIVPIALGTDTAGSGRVPAALNNLIGLKPTKGVFSCQGVVPACKSLDCVSIFALNLSDAERCFRIMCQPDPDNDEYSRPYVSNPLKKFSSNVTIAIPKNIPWYGETKNPVLFSNAVENLSRTGANVIEIDFEPLLELARCLYEGTWVAERYQAIQSFLDSKPPKESLDPTVISIIEGAKKYSAVDCFSFEYKRQGILQKVRRLLESVDVLCVPTCPLNPTMQQVADEPVLVNSRQGTWTNFVNLADLAALAVPAGFRDDGLPNGITLIGKKFTDYALLELANRYFQNIFPNGSRTYGTFTSSSVKPANDQLVGPDYDPSTSIKLAVVGAHLKGLPLHWQLEKVNATYLCTTKTSKAYQLFALPKNGPVLKPGLRRVQDSNGSQIELEVYSVPKELFGAFISMVPEPLGIGSVELESGEWIKSFICEESGYKAKGTVDITKYGGFRAYFEMLKKKESQKKKLFDTVLIANRGEIAVRIIKTLKKLGIRSVAVYSDPDKYSQHVTDADVSVPLHGTTAAQTYLDMNKIIDAAKQTNAQAIIPGYGFLSENADFSDACTSAGITFVGPSGDIIRGLGLKHSARQIAQKAGVPLVPGSLLITSVEEAKKVAAELEYPVMVKSTAGGGGIGLQKVDSEEDIEHIFETVKHQGETFFGDAGVFLERFIENARHVEVQLMGDGFGKAIALGERDCSLQRRNQKVIEETPAPNLPEKTRLALRKAAESLGSLLNYKCAGTVEFIYDEKKDEFYFLEVNTRLQVEHPITEMVTGLDLVEWMIRIAANDAPDFDSTKVEVNGVSMEARLYAENPLKNFRPSPGLLVDVKFPDWARVDTWVKKGTNISPEYDPTLAKIIVHGKDRDDAISKLNQALEETKVYGCITNIDYLKSIITSDFFAKAKVSTNILNSYQYEPTAIEITLPGAHTSIQDYPGRVGYWRIGVPPSGPMDAYSFRLANRIVGNDYRTPAIEVTLTGPSIVFHCETVIAITGGTALCTLDGQEIPQHKPVEVKRGSTLSIGKLTSGCRAYLGIRGGIDVPKYLGSYSTFTLGNVGGYNGRVLKLGDVLFLPSNEENKSVECLPQNIPQSLIPQISETKEWRIGVTCGPHGSPDFFKPESIEEFFSEKWKVHYNSNRFGVRLIGPKPKWARSNGGEGGMHPSNTHDYVYSLGAINFTGDEPVIITCDGPSLGGFVCQAVVPEAELWKVGQVKPGDSIQFVPLSYESSRSLKESQDVAIKSLDGTKLRRLDSVSILPSFETPILAQMEKVNELSPKVVYRQAGDRYVLVEYGDNEMNFNISYRIECLISLVKKNKTIGIVEMSQGVRSVLIEFDGYKVTQKELLKVLVAYETEIQFDENWKITSNIIRLPMAFEDSKTLACVQRYQETIRSSAPWLPNNVDFIANVNGISRNEVYDMLYSARFMVLGLGDVFLGSPCAVPLDPRHRFLGSKYNPSRTYTERGAVGIGGMYMCIYAANSPGGYQLVGRTIPIWDKLCLAASSEVPWLMNPFDQVEFYPVSEEDLDKMTEDCDNGVYKVNIEKSVFDHQEYLRWINANKDSITAFQEGQLGERAEEFAKLIQNANSELKESVTVKPDEEEDFPEGAEIVYSEYSGRFWKSIASVGDVIEAGQGLLIIEAMKAEMIISAPKSGKIIKICHGNGDMVDSGDIVAVIETLA
Protein: Gephyrin a (Gephyrin1 isoform) (D3KYK8)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
Sequence:
MASDGMILTNHDHQIRVGILTVSDSCFRNLAEDRSGINLKDLVHDPSLLGGIISAYKIVPDEIDEIKEILVDWCDEKELNLILTTGGTGFAPRDVTPEATREVIEREAPGMALAMLMGSLNVTPLGMLSRPVCGIRGKTLIINLPGSKKGSQECFQFILPALPHAIDLLRDAIVKVKEVHDALEDLPSPPPPLSPPPTTSPHKQTEDKGVQCEEEDEEKKDSGVASTEDSGSSHITAAAIAAKSMTSHLSHAVVMAKGGQPLSGFIPSTSIPSHFTCSCSDTIPESIISRGVQVLPRDTASLSTTPSESPCAQQSRLSTASCPTPKVQSRCSSKENILRASHSAVDITKVARRHRMSPFPLTSMDKAFITVLEMTPVLGTEIINYRDGMGRVLAQDVYAKDNLPPFPASVKDGYAVRAADGPGDRFIIGESQAGEQPTLTVMPGQVMRVTTGAPIPCGADAVVQVEDTELLRESEDGTEELEVRILVQARPGQDIRPIGHDIKRGECVLAKGTHMGPSEIGLLATVGVTEVEVQKFPVVAVMSTGNELLNPEDDLHPGKIRDSNRSTLLATIQEHGYPTINLGIVGDNPDDLLNALNEGISRADVIITSGGVSMGEKDYLKQVLDIDLHAQIHFGRVFMKPGLPTTFATLDIDGARKLIFALPGNPVSAVVTCNLFVIPALRKMQGILDPRPTIIKARLSCDVKLDPRPEYHRCILTWHHQEPLPWAQSTGNQMSSRLMSMRSANGLLMLPPKTEQYVELHKGEVVDVMVIGRL
Protein: UL16-binding protein 1 (ALCAN-beta) (NKG2D ligand 1) (N2DL-1) (NKG2DL1) (Retinoic acid early transcript 1I) (Q9BZM6)
Organism: Homo sapiens (Human)
Function: Binds and activates the KLRK1/NKG2D receptor, mediating natural killer cell cytotoxicity.
Subcellular location: Cell membrane {ECO:0000269|PubMed:12782710}; Lipid-anchor, GPI-anchor {ECO:0000269|PubMed:12782710}. Endoplasmic reticulum {ECO:0000269|PubMed:12782710}. Note=In CMV-infected fibroblasts, detected in the endoplasmic reticulum/cis-Golgi. {ECO:0000269|PubMed:12782710}.
Interaction partners:
- NKG2-D type II integral membrane protein
- MHC class I polypeptide-related sequence B
- UL16-binding protein 3
- Hematopoietic cell signal transducer
- UL16-binding protein 2
- CD226 antigen
- Natural cytotoxicity triggering receptor 1
- Natural cytotoxicity triggering receptor 3
- MHC class I polypeptide-related sequence A
- Leukocyte immunoglobulin-like receptor subfamily B member 1
Sequence:
MAAAASPAFLLCLPLLHLLSGWSRAGWVDTHCLCYDFIITPKSRPEPQWCEVQGLVDERPFLHYDCVNHKAKAFASLGKKVNVTKTWEEQTETLRDVVDFLKGQLLDIQVENLIPIEPLTLQARMSCEHEAHGHGRGSWQFLFNGQKFLLFDSNNRKWTALHPGAKKMTEKWEKNRDVTMFFQKISLGDCKMWLEEFLMYWEQMLDPTKPPSLAPGTTQPKAMATTLSPWSLLIIFLCFILAGR
Protein: STRUBBELIG-receptor family 6 (A8MQH3)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004370}.
Interaction partners:
Sequence:
MRENWAVVALFTLCIVGFELRFIHGATDASDTSALNTLFSGMHSPAQLTQWTAAAGDPCGQNWRGVTCSGSRVTQIKLSGLELSGTLGGYMLDKLTSLTELDLSSNNLGGDLPYQFPPNLQRLNLANNQFTGAASYSLSQITPLKYLNLGHNQFKGQIAIDFSKLDSLTTLDFSFNSFTNSLPATFSSLTSLKSLYLQNNQFSGTVDVLAGLPLETLNIANNDFTGWIPSSLKGITLIKDGNSFNTGPAPPPPPGTPPIRGSPSRKSGGRESRSSDESTRNGDSKKSGIGAGAIAGIIISLLVVTALLVAFFLFRRKKSKRSSPMDIEKTDNQPFTLASNDFHENNSIQSSSSVETKKLDTSLSINLRPPPIDRNKSFDDEDSTRKPIAVKKSTVVVPSNVRLYSVADLQIATGSFSVDNLLGEGTFGRVYRAEFDDGKVLAVKKIDSSALPHGMTDDFIEMVSKIANLDHPNVTKLVGYCAEHGQHLVVYEFHKNGSLHDFLHLSEEESKALVWNSRVKIALGTARALEYLHEVCSPSIVDKNIKSANILLDSELNPHLSDSGLASFLPTANELLNQTDEGYSAPEVSMSGQYSLKSDIYSFGVVMLELLTGRKPFDSSTRSRSEQSLVRWATPQLHDIDALAKMVDPALKGLYPVKSLSRFADVIALCVQPEPEFRPPMSEVVQALVVLVQRANMSKRTVGVDPSQRAGSADTTSDYM
Protein: Uncharacterized protein C17orf67 (Q0P5P2)
Organism: Homo sapiens (Human)
Subcellular location: Secreted {ECO:0000305}.
Interaction partners:
Sequence:
MKTLPVLVLSLTLLTVFSETSPILTEKQAKQLLRSRRQDRPSKPGFPDEPMREYMHHLLALEHRAEEQFLEHWLNPHCKPHCDRNRIHPV
Protein: Helper of Tim protein 13 (P36078)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Required for the assembly or recycling of the small Tim proteins in the mitochondrial intermembrane, thereby participating in the import and insertion of multi-pass transmembrane proteins into the mitochondrial inner membrane. Probably acts by facilitating the formation of disulfide bonds in small Tim proteins.
Subcellular location: Mitochondrion intermembrane space {ECO:0000269|PubMed:15294910}. Mitochondrion membrane {ECO:0000269|PubMed:15294910}; Peripheral membrane protein {ECO:0000269|PubMed:15294910}.
Interaction partners:
- Mitochondrial intermembrane space import and assembly protein 40
- Mitochondrial FAD-linked sulfhydryl oxidase ERV1
- Mitochondrial import inner membrane translocase subunit TIM8
- Mitochondrial import inner membrane translocase subunit TIM13
- Mitochondrial import inner membrane translocase subunit TIM10
Sequence:
MIETAIYGKTVDDQSRCVHWHLPKDVIAIRFKCCDKYYACFECHQELSSHPLEKYDLLDDANKHLIICGVCRHEMTFAEYYDYNSNLICPNCRSPFNPGCKLHYHLYFQNPPPAMC
Protein: Probable vinculin (Ddalpha-catenin) (Q54MH2)
Organism: Dictyostelium discoideum (Social amoeba)
Function: Involved in cell adhesion. Thought to play an important role in cytokinesis B, probably by providing substrate adhesion and traction forces. Required to organize and polarize the tip epithelium during cytokinesis. Required for the normal distribution of myosin in the tip epithelium. Involved in the localization of ctxA, ctxB, dcsA, exoc6 and rgaA. Thought to form a complex with ctxA, ctxB, and rgaA which regulates myosin accumulation to the apical plasma membrane.
Subcellular location: Cytoplasm, cell cortex {ECO:0000269|PubMed:19065153}. Cell junction {ECO:0000269|PubMed:21393547}. Note=Localized during interphase over the cell basal surface with levels decreasing at the basal surface when cells enter the mitotic phase. At this time, there is intense localization along the polar edges (PubMed:19065153). Also found at cell-cell contacts in the slug and fruiting body and in columnar cells of the tip epithelium (PubMed:21393547). {ECO:0000269|PubMed:19065153, ECO:0000269|PubMed:21393547}.
Interaction partners:
- Talin-B
- LIM domain-containing protein DDB_G0271356
- Paxillin-B
- Protein VASP homolog
- Cofilin-1A
Sequence:
MDEVLEMIADAVSSLVVAITDSEEKNTLFGDMVPGVELIQQAVNGMAEAAEETVSLIDEEFIGQLESTSKQLKNSAGQLYVHAVRAREDPWNRVPQKDAIKAAKQILQNVVLLVLIEEQSNIKVLVNIAKKAAEGVRRIDEIENIKQLDVMIGDVNQLQNELVKRSQRRSEGSHNPELRSKLEDIATMVNILSEQHQASARDVCRNPREETLRSKRSELSSKLLSAIDDLIYTIKLIFENNTKFVDLAFKWKPVRTMAEDEVTRASAVLIDNLRTLPKSIEAGNGPAAAREIVNAANLQISNAIIVANRCQDPVKKKMLLKQIEELKKLTPMLISAMKPVLENPNDQEAQKHLESVIYSTQKASEALATAVVSSPAEIVAASGVSLARDLDSLEEAIASGDKKRAQVILSHIPSAIDKHIELANALLETITDPGQRHQIKQSIERLQTLKPRIIENANRAIANPNDHEARKNLSSDIKEAKKAIGQISQPYEVVSALNTKIHNDLDSLIKCIDEGGPDMQVKGVQYAKDIANSIKKQIEAAEAYAQTITDPDRKKQVLDSIEQLKKLTPQLLEAIRACLANPDDKEARKRLDDVVRRVKEASSNLSQVIQPTADELKEEKRKRNEEIARIEAEEKAKARALLKAAELARIEAEEEKKRLAIIEEEKKRLAAEEEERKRAPKLVVPEGPVNKAVFGAAADVAQALESKVRDGTPLGILVQLSDEIAQQMALIASFAMNGDVKGMITAARKIADTIKQVQTQAKHIADNCTDPRLKQNVLTYCDCGGNFSTQLKILCAVKSNDFNDPTAEEQLVTCAKGLSGAVINLVKSSEAASIKQRKVPQQ
Protein: Intermediate filament protein B (IF-B) (P23731)
Organism: Ascaris suum (Pig roundworm) (Ascaris lumbricoides)
Subcellular location: Cytoplasm.
Interaction partners:
Sequence:
SLKQSQESSEYEIAYRSTIQPRTAVRTQSRQSGAYSTGAVSGGGGRVLKMVTEMGSASIGGISPALSANAAKSFLEATDKEKKEMQGLNDRLGNYIDRVKKLEEQNRKLVADLDELRGRWGKDTSEIKIQYSDSLRDARKEIDDGARRKAEIDVKVARLRDDLAELRNRYEDVQHRRESDREKINQWQHAIEDAQSELEMLRARWRQLTEEEKRLNGDNARIWEELQKARNDLDEETLGRIDFQNQVQTLMEELEFLRRVHEQEVKELQALLAQAPADTREFFKNELALAIRDIKDEYDYIAKQGKQDMESWYKLKVSEVQGSANRANMESSYQREEVKRMRDNIGDLRGKLGDLEAKNALLEKEVQNLNYQLNDDQRQYEAALNDRDATLRRMREECQTLVAELQALLDTKQMLDAEIAIYRKMLEGEESRVGLRQMVEQVVKTHSLQQQEDTDSTRNVRGEVSTKTTFQRSAKGNVTISECDPNGKFITLENTHRSKDENLGEHRLKRKLDNRREIVYTIPPNTVLKAGRTMKIYARDQGGIHNPPDTLVFDGENTWGIGANVVTSLINKDGDERATHTQKTIQTGQ
Protein: Signal recognition particle receptor alpha subunit, putative (Q383U0)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Endoplasmic reticulum membrane {ECO:0000256|ARBA:ARBA00004397}; Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004397}; Cytoplasmic side {ECO:0000256|ARBA:ARBA00004397}.
Interaction partners:
- Signal recognition particle 54 kDa protein
- Signal recognition particle receptor subunit beta
- Signal recognition particle subunit SRP72
- Signal recognition particle subunit SRP68
- 60S ribosomal protein L5, putative
- SRP19 protein
- Large ribosomal subunit protein uL5
- 60S ribosomal protein L17, putative
- 60S ribosomal protein L35, putative
- Pretranslocation protein, alpha subunit, putative
Sequence:
MIDTLSIVSNGGIVLWERSSDVSRKCSIINQVIQEFLLEDRAGMHETVIGDYKVHWMLENDAHFFVVAIHPKFVSYPQMCAFLRTIARCFVKKYGRVRDNVLVEYDFSAEYAETLSMLDAGVPGVDALGGGDQISNGDTEGEEEDEDLLEDAADREPQGEGECSAAGAASGAYQGPDTFVTKSGHVIGRKGKKLAGSKSTTATSQKRSKQVKRATRWDEPSADSAVEEQRGQGTRPTEEELEVQTALQRAAFIKRLPNGSVAPVREKEWEGQQRGLLANWLRSYVGRRELDSQDFNNVIPGLREKLITKNVAVEVAEHVCKSVEASLTGKVLGTFESLHQCIEAAMISALRRILQPKHEINILRAVASSRGRNKPYSIVLCGVNGVGKSTTLAKITYWLQQNGHTVMIAAGDTFRHGAVEQLEVHGRCLGVDVFQMGYGTDPSAVAAAAISRATRDGCDVVMIDTAGRMQDHESRMRALAKLIHDNQPDLVLFVGEALVGNTGVDQLRRFNQCLVDFVPVGSVPRGIDGIVLTKFDTIDDKVGAAVSMVYELGQPIVFVGAGQTYQDLKVMEPDVVVSALMA
Protein: Glycosyltransferases (EC 2.4.-.-) (Q6V9S8)
Organism: Gossypium hirsutum (Upland cotton) (Gossypium mexicanum)
Subcellular location: Golgi apparatus membrane {ECO:0000256|ARBA:ARBA00004323, ECO:0000256|RuleBase:RU363127}; Single-pass type II membrane protein {ECO:0000256|ARBA:ARBA00004323, ECO:0000256|RuleBase:RU363127}.
Interaction partners:
Sequence:
MGSAERTKKEVQLWKKAIVHFSLCFVMGFFTGFAPTGKDSIFSSPAVATHNKSHISQPPVNQSVTPAVHSSNVNQSLRAETPVPVPVPAKSNELESPKQVDGTVVHEVKLPSRRLVIVVTPTSTKDQFQGVFLRRLANTIRLVPQPLLWIVVEGQSDSNELSEILRKTGIMYRHLVFKENFTDPEAELNHQRNVALKHVEQHKLSGIVHFAGLTNVYDLDFFKELRQIEVFGTWPMALLSANERRVVIEGPVCDSSQVIGWHLRKMNNQTDAETDADTKPPIHISSFAFNSSILWDPERWGRLTSVQGTSQNSLKFVKQIVMEDEGKLKGIPPEECSKIMLWRLHFPIGVVPRNLVKTSSLFDVITQL
Protein: E-cadherin (Q95LE0)
Organism: Canis lupus familiaris (Dog) (Canis familiaris)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004236}.
Interaction partners:
Sequence:
MGPRYGGAPALLLPLLLLLQVSSGLCQEPEPCRPGFGADSYTFTVPRRHLERGRVLGRVSFEGCTGLPRTAYVSDDTRFKVGTDGVITVKRPLQLHKPEISFLVHAWDSSRRKLSTRVRLKAATHHHHHHHDAPSKTQTEVLTFPSSQHGLRRQKRDWVIPPISCPENEKGPFP
Protein: Ubl carboxyl-terminal hydrolase 18 (EC 3.4.19.12) (43 kDa ISG15-specific protease) (hUBP43) (ISG15-specific-processing protease) (Ubl thioesterase 18) (Q9UMW8)
Organism: Homo sapiens (Human)
Function: Interferon-induced ISG15-specific protease that plays a crucial role for maintaining a proper balance of ISG15-conjugated proteins in cells. Regulates protein ISGylation by efficiently cleaving ISG15 conjugates linked via isopeptide bonds. Regulates T-cell activation and T-helper 17 (Th17) cell differentiation by deubiquitinating TAK1, likely to keep TAK1-TAB complexes in steady conditions. In turn, restricts activation of NF-kappa-B, NFAT, and JNK as well as expression of IL2 in T-cells after TCR activation. Acts as a molecular adapter with USP20 to promote innate antiviral response through deubiquitinating STING1. Involved also in the negative regulation of the inflammatory response triggered by type I interferon. Upon recruitment by STAT2 to the type I interferon receptor subunit IFNAR2 interferes with the assembly of the ternary interferon-IFNAR1-IFNAR2 complex and acts as a negative regulator of the type I interferon signaling pathway.
Subcellular location: [Isoform 1]: Cytoplasm {ECO:0000269|PubMed:22170061}.; SUBCELLULAR LOCATION: [Isoform 2]: Nucleus {ECO:0000269|PubMed:22170061}. Cytoplasm {ECO:0000269|PubMed:22170061}.
Interaction partners:
- Ubiquitin-like protein ISG15
- Interferon alpha/beta receptor 2
- 2'-5'-oligoadenylate synthase 1
- Interferon-induced GTP-binding protein Mx1
- Signal transducer and activator of transcription 2
- E3 ISG15--protein ligase HERC5
- S-adenosylmethionine-dependent nucleotide dehydratase RSAD2
- Antiviral innate immune response effector IFIT1
- Antiviral innate immune response receptor RIG-I
- Interferon-induced protein 44
Sequence:
MSKAFGLLRQICQSILAESSQSPADLEEKKEEDSNMKREQPRERPRAWDYPHGLVGLHNIGQTCCLNSLIQVFVMNVDFTRILKRITVPRGADEQRRSVPFQMLLLLEKMQDSRQKAVRPLELAYCLQKCNVPLFVQHDAAQLYLKLWNLIKDQITDVHLVERLQALYTIRVKDSLICVDCAMESSRNSSMLTLPLSLFDVDSKPLKTLEDALHCFFQPRELSSKSKCFCENCGKKTRGKQVLKLTHLPQTLTIHLMRFSIRNSQTRKICHSLYFPQSLDFSQILPMKRESCDAEEQSGGQYELFAVIAHVGMADSGHYCVYIRNAVDGKWFCFNDSNICLVSWEDIQCTYGNPNYHWQETAYLLVYMKMEC
Protein: Protein translocase subunit SecA 2 (EC 7.4.2.8) (P9WGP3)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: Part of the Sec protein translocase complex. Interacts with the SecYEG preprotein conducting channel. Has a central role in coupling the hydrolysis of ATP to the transfer of proteins into and across the cell membrane, serving as an ATP-driven molecular motor driving the stepwise translocation of polypeptide chains across the membrane.
Subcellular location: Cell membrane {ECO:0000255|HAMAP-Rule:MF_01382}; Peripheral membrane protein {ECO:0000255|HAMAP-Rule:MF_01382}; Cytoplasmic side {ECO:0000255|HAMAP-Rule:MF_01382}. Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01382}. Note=Distribution is 50-50. {ECO:0000255|HAMAP-Rule:MF_01382}.
Interaction partners:
- Protein translocase subunit SecY
- Probable protein-export membrane protein SecG
- Protein translocase subunit SecE
- Signal recognition particle receptor FtsY
- Sec translocon accessory complex subunit YajC
- Signal recognition particle protein
- Membrane protein insertase YidC
- Protein translocase subunit SecA 1
- NADH-quinone oxidoreductase subunit G
- Superoxide dismutase
Sequence:
MNVHGCPRIAACRCTDTHPRGRPAFAYRWFVPKTTRAQPGRLSSRFWRLLGASTEKNRSRSLADVTASAEYDKEAADLSDEKLRKAAGLLNLDDLAESADIPQFLAIAREAAERRTGLRPFDVQLLGALRMLAGDVIEMATGEGKTLAGAIAAAGYALAGRHVHVVTINDYLARRDAEWMGPLLDAMGLTVGWITADSTPDERRTAYDRDVTYASVNEIGFDVLRDQLVTDVNDLVSPNPDVALIDEADSVLVDEALVPLVLAGTTHRETPRLEIIRLVAELVGDKDADEYFATDSDNRNVHLTEHGARKVEKALGGIDLYSEEHVGTTLTEVNVALHAHVLLQRDVHYIVRDDAVHLINASRGRIAQLQRWPDGLQAAVEAKEGIETTETGEVLDTITVQALINRYATVCGMTGTALAAGEQLRQFYQLGVSPIPPNKPNIREDEADRVYITTAAKNDGIVEHITEVHQRGQPVLVGTRDVAESEELHERLVRRGVPAVVLNAKNDAEEARVIAEAGKYGAVTVSTQMAGRGTDIRLGGSDEADHDRVAELGGLHVVGTGRHHTERLDNQLRGRAGRQGDPGSSVFFSSWEDDVVAANLDHNKLPMATDENGRIVSPRTGSLLDHAQRVAEGRLLDVHANTWRYNQLIAQQRAIIVERRNTLLRTVTAREELAELAPKRYEELSDKVSEERLETICRQIMLYHLDRGWADHLAYLADIRESIHLRALGRQNPLDEFHRMAVDAFASLAADAIEAAQQTFETANVLDHEPGLDLSKLARPTSTWTYMVNDNPLSDDTLSALSLPGVFR
Protein: Uncharacterized protein (Q38CG5)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MLNSCLCKIFMFVRFLVLIVFALCTNILSAGAKECKLMGEMEAWKHDGGSFIHDEKSGTWHELNSDGESVASFVEFTRKDDTVVLRDESRHLFLLLRPDLAAIMNNGDDNFQPLFQGRFVSSVSCA
Protein: Chaperonin GroEL 1 (EC 5.6.1.7) (60 kDa chaperonin 1) (Chaperonin-60 1) (Cpn60 1) (P9WPE9)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: Prevents aggregation of substrate proteins and promotes their refolding. In vitro, activity may be independent of the presence or absence of the GroES co-chaperonin or ATP. Shows weak ATPase activity.
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00600}.
Interaction partners:
- Co-chaperonin GroES
- Chaperone protein DnaK
- Chaperonin GroEL 2
- Protein GrpE
- Chaperone protein DnaJ 1
- Possible formate hydrogenase HycE
- Chaperone protein HtpG
- Chaperone protein DnaJ 2
- Heat-inducible transcription repressor HrcA
- Conserved hypothetical proline rich protein
Sequence:
MSKLIEYDETARRAMEVGMDKLADTVRVTLGPRGRHVVLAKAFGGPTVTNDGVTVAREIELEDPFEDLGAQLVKSVATKTNDVAGDGTTTATILAQALIKGGLRLVAAGVNPIALGVGIGKAADAVSEALLASATPVSGKTGIAQVATVSSRDEQIGDLVGEAMSKVGHDGVVSVEESSTLGTELEFTEGIGFDKGFLSAYFVTDFDNQQAVLEDALILLHQDKISSLPDLLPLLEKVAGTGKPLLIVAEDVEGEALATLVVNAIRKTLKAVAVKGPYFGDRRKAFLEDLAVVTGGQVVNPDAGMVLREVGLEVLGSARRVVVSKDDTVIVDGGGTAEAVANRAKHLRAEIDKSDSDWDREKLGERLAKLAGGVAVIKVGAATETALKERKESVEDAVAAAKAAVEEGIVPGGGASLIHQARKALTELRASLTGDEVLGVDVFSEALAAPLFWIAANAGLDGSVVVNKVSELPAGHGLNVNTLSYGDLAADGVIDPVKVTRSAVLNASSVARMVLTTETVVVDKPAKAEDHDHHHGHAH
Protein: Alpha-synuclein (Non-A beta component of AD amyloid) (Non-A4 component of amyloid precursor) (NACP) (P37840)
Organism: Homo sapiens (Human)
Function: Neuronal protein that plays several roles in synaptic activity such as regulation of synaptic vesicle trafficking and subsequent neurotransmitter release. Participates as a monomer in synaptic vesicle exocytosis by enhancing vesicle priming, fusion and dilation of exocytotic fusion pores. Mechanistically, acts by increasing local Ca(2+) release from microdomains which is essential for the enhancement of ATP-induced exocytosis. Acts also as a molecular chaperone in its multimeric membrane-bound state, assisting in the folding of synaptic fusion components called SNAREs (Soluble NSF Attachment Protein REceptors) at presynaptic plasma membrane in conjunction with cysteine string protein-alpha/DNAJC5. This chaperone activity is important to sustain normal SNARE-complex assembly during aging. Also plays a role in the regulation of the dopamine neurotransmission by associating with the dopamine transporter (DAT1) and thereby modulating its activity.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:19762560, ECO:0000269|PubMed:24936070, ECO:0000269|PubMed:25561023, ECO:0000269|PubMed:26442590, ECO:0000269|PubMed:31034892, ECO:0000269|PubMed:33657088}. Membrane {ECO:0000269|PubMed:24936070}. Nucleus {ECO:0000269|PubMed:12859192, ECO:0000269|PubMed:24936070}. Synapse {ECO:0000269|PubMed:15282274}. Secreted {ECO:0000269|PubMed:24936070}. Cell projection, axon {ECO:0000250|UniProtKB:O55042}. Note=Membrane-bound in dopaminergic neurons (PubMed:15282274). Expressed and colocalized with SEPTIN4 in dopaminergic axon terminals, especially at the varicosities (By similarity). {ECO:0000250|UniProtKB:O55042, ECO:0000269|PubMed:15282274}.
Interaction partners:
- Synphilin-1
- E3 ubiquitin-protein ligase parkin
- Tyrosine 3-monooxygenase
- Sodium-dependent dopamine transporter
- Apolipoprotein E
- Calmodulin-1
- Microtubule-associated protein tau
- TAR DNA-binding protein 43
- Heat shock 70 kDa protein 4
- Parkinson disease protein 7
Sequence:
MDVFMKGLSKAKEGVVAAAEKTKQGVAEAAGKTKEGVLYVGSKTKEGVVHGVATVAEKTKEQVTNVGGAVVTGVTAVAQKTVEGAGSIAAATGFVKKDQLGKNEEGAPQEGILEDMPVDPDNEAYEMPSEEGYQDYEPEA
Protein: Sex-determining protein fem-1 (Feminization of XX and XO animals protein 1) (P17221)
Organism: Caenorhabditis elegans
Function: Substrate-recognition component of the cullin-RING-based CBC(fem-1) (Cul2-ElonginB-ElonginC) E3 ubiquitin-protein ligase complex of the DesCEND (destruction via C-end degrons) pathway, which recognizes a C-degron located at the extreme C terminus of target proteins, leading to their ubiquitination and degradation (By similarity). The C-degron recognized by the DesCEND pathway is usually a motif of less than ten residues and can be present in full-length proteins, truncated proteins or proteolytically cleaved forms (By similarity). Sex-determining protein; essential for the adoption of the male sexual fate in all tissues. The CBC(fem-1) complex mediates the ubiquitination and subsequent proteasomal degradation of tra-1. Promotes ubiquitination and degradation of cdl-1. May be involved in turnover of neuronal substrates, thereby impacting synaptic acetylcholine release and neuromuscular transmission.
Subcellular location: Cytoplasm {ECO:0000305}.
Interaction partners:
- Protein phosphatase fem-2
- Cullin-2
- Sex-determination protein fem-3
- Elongin-C
- RING-box protein 1
- RNA polymerase II transcription factor SIII p18 subunit
- Early embryogenesis protein zyg-11
- Leucine-Rich Repeat protein
- Zyg eleven-related protein 1
- Valine--tRNA ligase
Sequence:
MTPNGHHFRTVIYNAAAVGNLQRIKVFTINSRNDRQWIIDCFNSDQDGRYPLVIAARNGHANVVEYLLEIGADPSVRGVVEFDNENIQGTPPLWAASAAGHIEIVKLLIEKANADVNQATNTRSTPLRGACYDGHLDIVKYLLEKGADPHIPNRHGHTCLMIASYRNKVGIVEELLKTGIDVNKKTERGNTALHDAAESGNVEVVKILLKHGSVLMKDIQGVDPLMGAALSGFLDVLNVLADQMPSGIHKRDALKLLGSTLLDKKMDAMSAMNCWKQSMEVPLHADDLRLVREMETFFEPQEVYEYQREAQNIAQVELLDGNIEAQRMQALVIRERILGGAHTDVHYYLRFRGAVYCDMGQMNRCYDLWKHALELQQKHFAPLYYGTITTLQSFHETFSMSLNDFVNNHHANRNLRVRSSWVKYVFNGVCLELERAAAWTGAPLLEDTECCGKERCQHATEESEYKKLVYVAVHLVNVLERLSLPSAHIDDSDEEKEPKADVRRLMIVCHELHIPLLHHTLEERIPDSNSAELGLPKAAVLEQLLELDLDVNATDKNNDTPMHILLRAREFRKSLVRALLVRGTWLFARNRHGDVVLNVMKRMKALNHANFDDLPLGRHITLAGLVANAMRVKYPKKFVGVEEQMPLELRRFYLAH
Protein: AT07759p (Q8IHF3)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
HGCHGVCCRWQDSLTICPKFLISGGAEGAIYLWDIETGARLQEIVQKGTEYVTISCSTNDPLTIYAGTSIGTIREFQDSTLVREITIPSRTKGSVSDVCLARSDLIMFVADHEGNLFNMQLPFLEAGGGTFTNFRFFDGPVNKLRFSYDGTLLFAISNKGTLAIWAMDNIEGKVPYMDQDLMRSQEVLIPRSQLNDKIEQIANLELRLKQQAEEFQYQLSQNEIFDGQQLQEVHRSYCSALEELKELNNEIEARHTEEMNHITFQINSIREEHRIQLDTLATQYSERMLIEYQKFTNLRENMLELRESYEDKLKNSTGTLQDTVEALENNYKQQLNERKELIRDLMKEMQDKKAEFIEYCREVELENDRNMVSTQTEYENKLTTERNETQMWRGKAGVLQKKFESQSREIDNLLEEVEILKEEHHKSQRNIQKQMRNIEDLQKDIADRDYAINGKEKRIQDLLHKNQELDKYKQVLGHKIAELKAQIEPREFQINDKRKHIIEMEAELEGLNQNNVQLELQLKEMRDKYLSNVAELRTERHRAKASRECLHSICSDIYYVAGEINSAEALKKAVKELFRKHASDDELKRFVTLDAEVRDEFMRQRRQIENVLDRYKSVAEDKSVQKKYDKLFKENVILIEEIEKLNETNKMLRSKVKEDLRRSTKTIHK