wanglab/gogpt-training-data huggingface dataset:
Protein: Polyketide synthase PltC (Q4KCY8)
Organism: Pseudomonas fluorescens (strain ATCC BAA-477 / NRRL B-23932 / Pf-5)
Interaction partners:
- L-proline--[L-prolyl-carrier protein] ligase
- AMP-binding enzyme
- AMP-binding protein
- Thioesterase PltG
- L-cysteine--[L-cysteinyl-carrier protein] ligase
- Non-ribosomal peptide synthetase PvdJ
- L-cysteine--[L-cysteinyl-carrier protein] ligase
- Polyketide synthase/nonribosomal peptide synthetase hybrid RzxA
- Non-ribosomal peptide synthetase OfaA
- Non-ribosomal peptide synthetase OfaC
Sequence:
MDNDVRDVSKEQLQESLAQAITTIRALKEKVAGKSSAPVEPIAVVGLGCRLPGSADTPKRLWSLLKHATDAVGDMPSDRLYGTDYYHPDPQAPGKAYVMRGGFIEGVDQFDPGFFGISPKEAEGMDPQQRLALEVAWEALENAAIAPDSLHGKKLGVFMGVSTNDYVRLRQQLGAVEDVNAYQFYGETSFVAGRIAYTLGSRGPAVVLDTSCSSSLVALHQACNSLRSRESELALAGGVNLILSPYGFILVSKLRAVAPDGRCKTFDAAADGYGRAEGCVILALKRLSDAVRDQDPVLAVIEGSAVNNDGASSGITVPNIHAQEEVIRLALGQAGLQGSEVDYVEAHGTGTALGDPIELHALHAVLGKQRPVDAPLLVGSIKANMGHLEPVAGVTGLAKVLLCLQQEALVPQVHFNTPNPRIEWDRLALKVVTESTPWPRQGKARHAGVSSFGVTGTNAHVLVGDAPLRERAQGRDNPWQLITLSAKGETPRRQIAGRYERFIADNSQLELKDLCYTANVGRAHFGHRFAAVADSREGLREQLAAYASRKVVGHVFEGRCQGAAAPLVMLFPGQGCQYRAMAQALYDSEPFFKAQIDECRALLQPLMDVDLLTLVLDAGAASDSYLQQTRYAQPAIFAVEYALARLWMHWGVAADALFGHSFGEISAICVAGAVSLADALRMVEARGRLAQQLMTAGGAMYALGMSEAQLLELLKDRPGSAIELAAVNSPQDVVVAGPQAEVQALAEAALASGCKVKKLAVSHAFHTAATEPMLEAFRQTVAQITFSEPRLPVISSVTGRVHTLSSLSSPDYWCTHTRQAVRFCEGVNTLIAELGVKTFLEVASDAVLTPLIGRHPLADGSLVLASLRRAGDPSRDLRLAAAQLYVGGHNLDWARLHEHDGALRQALPGYAFQRQRYWFDNASGSPLQQVAAGAVGRLLGHSVNAPTPAFESTLDSALLQVVGGEIRDDLALLRPDRLLAALSDELAGHLQLDTYGVSLASITPALAFHVDDQLHLFTELKPLSGAAWEVNCSALSAAAKVAGADWQPVLSLTLEGLPAAVRGGLPDPGHAATQDAGFVYHMQLPAEPDPHGNHLGQVLEYLGQAVPGDAPGSISGIRRWVASRSASPRAQSLVIATSQAHPQQFDCALYDAHGQCVGSLEGLTLAAAPSEEALRGMLYQPDVLYSLDWLERPRQRAEVPQQDRLFTLVSRSPETAAPLVEHLQRGGHRARVLCPQQLLDSARRVLAQDPSQALTDEGEALAADIIVLDGKDIEDAGSTTLQSLSSLQATLFHPLLEMVQALIELGPRGGRLWLVTQGANPVGLDRDQPLQVATGPLWGLGKTLALEHPEHWRGLIDLAPDDPHWARALAEEVSDSDGDDKICLRPGKRYVQRLNHFSAAQLPAQAYAPCPQGSYLITGGMGGIGLAMAQWLLDKGAGAVLITGRRPLEDVATGLERFGAAASRVSYVQADITSPQDMQRLFCGLEASGASLKGIFHAAGISIPQDLKDVDRDSFDQVMRPKVEGTWLLHELSLGLDLDFFVLCSSIASVWGSQHVASYAAANQFLDSLAWQRRAMGLSALVIDWGLWAGGSHLFDEQVLNFLTSVGLKQIAPVQNVGLLSRILASELPQMVVSGVDWNRFKPLLESRGPQPLLQYIRSQAPTARAGDSSNVEILQQLAGADEAAALALLDDYVWEQYAQLLGVKTEQVRAKLEDGGSLMDYGLDSLLVMDMVARCRRDLKLEIKAREFLECPGLMWPDFLARSIKEQGCVAEA
Protein: Phosphatidylinositol 3,4,5-trisphosphate 3-phosphatase and protein-tyrosine-phosphatase PTEN2A (EC 3.1.3.48) (EC 3.1.3.67) (Protein PHOSPHATASE AND TENSIN HOMOLOG 2-a) (AtPTEN2) (AtPTEN2a) (Q9LT75)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Binds phosphatidic acid. Protein tyrosine phosphatase that exhibits also lipid phosphatase activity. Hydrolyzed poorly p-nitrophenyl phosphate (p-NPP). Can use PtdIns isomers as substrates. Removes efficiently phosphate from the D3 position of the inositol ring, less from the D4 position and not at all from the D5 position on monophosphorylated PtdIns isomers (PIPs). The presence of a phosphate group in the D5 position on PIP(2) isomers reduces lipid phosphatase activity. Mostly active on PtdIns(3)P and PtdIns(3,4)P(2), to a lower extent, on PtdIns(4)P and PtdIns(3,5)P(2), but barely against PtdIns(3,4,5)P(3) as substrate.
Interaction partners:
- Phosphoinositide phosphatase SAC7
- Phosphoinositide phosphatase SAC6
- Putative 1-phosphatidylinositol-3-phosphate 5-kinase FAB1D
- Phosphoinositide phosphatase SAC8
- Phosphatidylinositol 3-kinase VPS34
- Putative 1-phosphatidylinositol-3-phosphate 5-kinase FAB1C
- Phosphatidylinositol 4-kinase alpha 1
- 1-phosphatidylinositol-3-phosphate 5-kinase FAB1B
- 1-phosphatidylinositol-3-phosphate 5-kinase FAB1A
- CDP-diacylglycerol--inositol 3-phosphatidyltransferase 1
Sequence:
MSSESPNLPAAAGTVPDNHPPPPPVVTAAEAGSDDSPKGVASKLSAAGISNWAKNLKVPQPFASTQNDSGVENTEKSAFAKFTSGLGIRLSPKSPQTNDTTTEGTSSATESSFIGTITKGLVDTSKNAVKAVQVKARHAVSQNKRRYQEGGFDLDLTYITENIIAMGFPAGDMSSGFFGYVEGFYRNQMEEVINFLETQHKGKYKVYNLCSERLYDVSLFEGKVASFPFDDHNCPPIHLVTSFCQSAYSWLKEDIENVVVVHCKAGMARTGLMICSLLLYLKFFPTAEECMDFYNQKRCVDGKGLVLPSQIRYVKYFERILTYFNGENQPGRRCMLRGFRLHRCPYWIRPSITISDHNGVLFTTKKHPRTKDLSPEDFWFSAPKKGVMVFALPGEPGLTELAGDFKIQFHDRQGDFYCWLNTTMMENRVILKTSELDGFDKRKLPSPGFMVEVVLADINATIPTNPSSETASKTPEETSAANSSPVDGSASVPGPDKETENPDKDDVFSDNEGDSTGPTKTTSSASSQTPEAKKSADETAVLTKATEKVSISGNKGSSQPVQGVTVSKGEATEKPSGAGVNASSSSESEFKVMAADASVFSFGDEDDFESD
Protein: At2g01710/T8O11.12 (Chaperone DnaJ-domain superfamily protein) (Expressed protein) (Q9ZU99)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
Sequence:
MGDNNPNRSEAERLLGIAEKLLESRDLNGSKEFAILAQETEPLLEGTDQILAVVDVLLSSAPENRIKNQPNWYKILQIEDLTESSTDNDLIKKQYRRLALLLHPDKNRFPFADQAFRFVLDAWEVLSTPTKKSQFDGDLNLIFTKVNLNTQKSKKKTTTNEKMSTFWTACPYCYSLHEYPRVYQEYCIRCQNCQRAFHAASIPQLPPLIPGKDEYYCCWGFFPMGFVGGKGGEAAIANGVDAAKFPNWMPPVFSSGGVAAPPSGNGVSFDGWSGGAAKRDNEAVRSNNGVGVNSDGTPKKRGRGRPKKNPV
Protein: Conserved protein (P71734)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Interaction partners:
- Conserved protein
- Uncharacterized protein Rv2411c
- Uncharacterized protein Rv2567
Sequence:
MWRTRVVHTTGYVYQSPVTASYNEARLTPRSSSRQNLVLNRVETIPATRSYRYIDYWGTAVTAFDLHAPHTELTVTSSSVVETERPEPLAAKATWADLQSTAVIDRFDEVLRPTPHTPASARVDAVGRRIRKCHEPSEAVVAAARWARSELDYIPGTTSVHSSGLDALEQGKGVCQDFVHLSLMVLRSMGIPCRYVSGYLHPKRDAVVGKTVDGRSHAWVQAWTGGWWHYDPTNDNEITEQYISVGVGRDYTDVSPLKGIYSGEGVTDLDVVVEITRLA
Protein: cAMP-dependent protein kinase type I-beta regulatory subunit (P81377)
Organism: Rattus norvegicus (Rat)
Function: Regulatory subunit of the cAMP-dependent protein kinases involved in cAMP signaling in cells.
Subcellular location: Cell membrane {ECO:0000250}.
Interaction partners:
Sequence:
MASPSCFHSEDEDSLKGCEMYVQKHGIQQVLKECIVHLCVAKPDRPLRFLREHFEKLEKEENRQILARQKSNSQCDSHDEEISPTPPNPVVKARRRRGGVSAEVYTEEDAVSYVRKVIPKDYKTMTALAKAISKNVLFSHLDDNERSDIFDAMFPVTHIDGETVIQQGNEGDNFYVIDQGEVDVYVNGEWVTNISEGGSFGELALIYGTPRAATVKAKTDLKLWGIDRDSYRRILMGSTLRKRKMYEEFLSKVSILESLEKWERLTVADALEPVQFEDGEKIVVQGEPGDDFYIITEGTASVLQRRSPNEEYVEVGRLGPSDYFGEIALLLNRPRAATVVARGPLKCVKLDRPRFERVLGPCSEILKRNIQRYNSFISLTV
Protein: Ribosomal RNA-processing protein 17 (Q04031)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Essential protein involved in ribosomal RNA processing.
Subcellular location: Nucleus, nucleolus {ECO:0000269|PubMed:14562095}.
Interaction partners:
- Ribosome biogenesis protein 15
- Ribosome biogenesis protein BRX1
- rRNA-processing protein EBP2
- ATP-dependent rRNA helicase SPB4
- 25S rRNA
- Ribosome biogenesis protein ERB1
- 27S pre-rRNA
- Ribosome biogenesis protein RLP7
- Proteasome-interacting protein CIC1
- ATP-dependent RNA helicase HAS1
Sequence:
MAVHTNRQILTRGKNYATKQSKKFGTDEVTFDKDSRLDYLTGFHKRKLQRQKKAQEFIKEQERLRKIEERQKIRQERKEVMEEQLKTFKESLNLEAEIEDAKNDKTEDLQVESDESWHGFDSDKDDGDNDNNESSVKPILKKGAITEIYDDSTTVELETLEPNDNFEYLAQLNNVKLEKAEKVLKQSINRATKYAKFLGVDEKQKKKPRVKKFRYLTKNERRINQRKANDNKRRR
Protein: Zinc finger protein 111 (G3V9G6)
Organism: Rattus norvegicus (Rat)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- Large ribosomal subunit protein eL37
Sequence:
MEAVTFRDVAVVFSKEEMGLLDAAQRKLYHDVMLENLRNLLAVGGQSPNKMKTVDATGIRCLLLGQLLYWEITGHDANKLARAPEAVVNTQGKGSHFLEQGHSSCHREAEEPPRASEDDSSLDSLTRDHSSTTENQEFLSGRAQGSWCKTHLRKRQNHQKHCLQTLMKNKPELLTQHSPVQRTQEDSRHSSSVPIQQSVHPGRKRYWCHECGKGFSQSSALQTHRRVHTGEKPCRDNSCRKSFSRSSGLSIHRQVHTGERPYRCKVCGKGFLRWSHLQAHERIHTGEKPYKCGECGKRFSCISNLHTHQRFHSKEKPYKCDKCGKCFSLNFNLHIHQRVHTGEKPYKCEECGKCFSLSFNLHSHQRVHTGEKPYKCEECGKCFSSASSFQRHRQIHIKEKTLHRDVCGKGSSRDSNLQTHQRVHIQEKPYRCNSCGKSFRCSMDLNIHRRVHTGEKPYKCEVCGKGFNYLSHLQAHEKIHADQKPYKCEYCGRRFSYSSNLHTHQRVHTGEKPYKCEECGKSFSLASSLQAHQRVQTGKKPFKCNACQKRFSQAWNLQAHQRVHTGEKPYKCDTCGKAFGQRSSLQIHQRIHTGEKPFKCEECGKEFSLNSGLTAHRRVHTGEKPYECTECGKGFSLASSLRTHQRIHTGEKPFQCNECQKRFSQVSHLQSHQRVHTGEKPYKCDTCGKAFSQKSGLQVHRRIHTGEKPFKCEECGKEFIWSSGLSAHRRVHTGEKTLHG
Protein: Retinal rod rhodopsin-sensitive cGMP 3',5'-cyclic phosphodiesterase subunit delta (GMP-PDE delta) (O55057)
Organism: Mus musculus (Mouse)
Function: Promotes the release of prenylated target proteins from cellular membranes. Modulates the activity of prenylated or palmitoylated Ras family members by regulating their subcellular location. Required for normal ciliary targeting of farnesylated target proteins, such as INPP5E (By similarity). Modulates the subcellular location of target proteins by acting as a GTP specific dissociation inhibitor (GDI). Increases the affinity of ARL3 for GTP by several orders of magnitude. Stabilizes ARL3-GTP by decreasing the nucleotide dissociation rate.
Subcellular location: Cytoplasm, cytosol {ECO:0000269|PubMed:22179043}. Cytoplasmic vesicle membrane {ECO:0000250|UniProtKB:O43924}; Peripheral membrane protein {ECO:0000250|UniProtKB:O43924}. Cytoplasm, cytoskeleton, cilium basal body {ECO:0000250|UniProtKB:O43924}.
Interaction partners:
- ADP-ribosylation factor-like protein 2
- GTPase KRas
- ADP-ribosylation factor-like protein 13B
- ADP-ribosylation factor-like protein 3
- Phosphatidylinositol polyphosphate 5-phosphatase type IV
- GTP-binding protein Rheb
- X-linked retinitis pigmentosa GTPase regulator
- Protein unc-119 homolog A
- GMP synthase
- Guanylate kinase
Sequence:
MSAKDERARDILRGFKLNWMNLRDAETGKILWQGTEDLSVPGVEHEARVPKKILKCKAVSRELNFSSAEQMEKFRLEQKVYFKGQCLEEWFFEFGFVIPNSTNTWQSLIEAAPESQMMPASVLTGNVIIETKFFDDDLLVSTSKVRLFYV
Protein: Homeobox protein Nkx-2.6 (Homeobox protein NK-2 homolog F) (P43688)
Organism: Mus musculus (Mouse)
Function: Acts as a transcriptional activator (By similarity). In conjunction with NKX2-5, may play a role in both pharyngeal and cardiac embryonic development.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
Sequence:
MLSSPVASTPFSVADILRLECQQKDSKTLSQWELHRNPVKPRYLRMNQESGWFESSDRAQAVPFRCTWETVLEMGSNPVGEPQTPPGTISRLGARNPMTDRGVGNLSGDMRRGGPVSTRTRPQRKSRVLFSQAQVLALERRFKQQRYLTAPEREHLASALQLTSTQVKIWFQNRRYKSKSQRQDQTLELAGHPLAPRRVAVPVLVLDGKPCLDPDVAAFLGPYKATSPYSCFGGYAGTPYDASYASRCTSASAGPGPLTPLASSGFSPGGQSAAPQGHLPATPQGVTAW
Protein: mRNA-binding protein (A0A1D8PMA5)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Interaction partners:
- CCR4-NOT core DEDD family RNase subunit
- CCR4-Not complex 3'-5'-exoribonuclease subunit Ccr4
- Copper metallochaperone
- ATP-dependent RNA helicase DHH1
- Tif3p
- Lhp1p
Sequence:
MSSETIWSSGHNSPIQNNLSLASTTTNNTSQYKSVIDQVDPDVIRLFANSNSFDPLSSSTGPGTTGHTSGLTSGTDRRLSFNDGSDIIESDFFGFKRGALSAITAPVVGNGNNGRHHNQVTNKNFGTASISGGIANRHPPQDSFLQKFSSVADATREIELGRLSLDDRNNGNNQVSSVNEIKMVNTSAFTSPHGSLNENLNMPVPTRGGSRHQSISEKIDNYNNNSPIQTAAALSINSDLNSDTVNINSTTTNSNHDATKNQGNYSHNFWNPAAATSFTPVGAIPTPNYFIDANGLPIPPLPMPPQGFYPPRGGNASNSGGANSISPPPPFMIPSPPPPFLDPSVYSMMYGGNFPPPPPPPPSQQQQQQQPSQQQQPSHSNQDKKANETNSKSKETKYSDTESHEEDNEKQDNYHGPGPVPGPGPGPGPIGVGLMNRQFSPASFMFHPFNPYSMYQSSPPLVPPEAALGGMASPPPPPPLPQQQQPQQQSAPSSQGKSTSGVSGSSTSTSTSHHSQSKHHHHHNNNNNNNNNSSSSGSTPGVGSKRKGNFKGKNNTTNGGGNHIYRSPLLEEVRSNPKPYQLKDIYGHAIEFTKDQHGSRFIQQKLPEATEEEKETIFNEIWEISYELMTDVFGNYVIQKYFEYGTTTQKQVLLESMIGHIHELSLQMYGCRVVQRALEAIDNEGQLRIIEELKDHILICCKDQNGNHVIQKSIEKIKPFSQIRYILTSLDNQIYHLSTHPYGCRVIQRLLEYSDIDDQKLILSQLNNFLYYLILDQYGNYVIQHILENGTQEEKEPILEIVLGSVVQFSKHKFASNVIEKCIKFGDINQRKRILHEVMLGNETILGDDDIDGEPVKEDSPLALMVKDQFGNYVIQKLVEAFDGDERKLLIIKIKKCLSLSSNNLASIRNIRNIIDHVSESNSDLKVES
Protein: Chitinase-3-like protein 1 (Cartilage glycoprotein 39) (CGP-39) (GP-39) (Q9WTV1)
Organism: Rattus norvegicus (Rat)
Function: Carbohydrate-binding lectin with a preference for chitin. Has no chitinase activity. May play a role in tissue remodeling and in the capacity of cells to respond to and cope with changes in their environment. Plays a role in T-helper cell type 2 (Th2) inflammatory response and IL-13-induced inflammation, regulating allergen sensitization, inflammatory cell apoptosis, dendritic cell accumulation and M2 macrophage differentiation. Facilitates invasion of pathogenic enteric bacteria into colonic mucosa and lymphoid organs. Mediates activation of AKT1 signaling pathway and subsequent IL8 production in colonic epithelial cells. Regulates antibacterial responses in lung by contributing to macrophage bacterial killing, controlling bacterial dissemination and augmenting host tolerance. Also regulates hyperoxia-induced injury, inflammation and epithelial apoptosis in lung (By similarity).
Subcellular location: Secreted, extracellular space {ECO:0000250}. Cytoplasm {ECO:0000250}. Cytoplasm, perinuclear region {ECO:0000250}. Endoplasmic reticulum {ECO:0000250}.
Interaction partners:
- Cytochrome c oxidase subunit 3
- Cytochrome c oxidase subunit 2
Sequence:
MTLQLPGFAVLMLLQSCSAYKLVCYYTNWSQYREGNGSCFPDALDHSLCTHIIYSFANISNNKLSTSEWNDVTLYGMLNTLKTRNPRLKTLLSVGGWSFGSERFSRIVSNAKSRKTFVQSVAPFLRTYGFDGLDLAWLYPGPKDKQHFTTLIKELKAEFTKEVQPGTEKLLLSAAVSAGKVTLDSGYDVAQIAQHLDFINLMTYDFHGTWRHTTGHHSPLFRGQQDTGPDRFSNVDYGVGYMLRLGAPTNKLVMGIPTFGKSFTLASSENQVGAPITGSGLPGRYTKEKGTLAYYEICDFLRGAEVHRILGQQVPFATKGNQWVGYDDPESVKNKVKYLKNKQLAGAMVWAVDLDDFRGSFCGHNVHFPLTNAIKEALAVA
Protein: Uncharacterized protein (Q38E81)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MSLLNTTLQTLVVRLRDMSGNVTQQKLHNRVFDAYEAKSLVFEAITPEQQTVMRQYGAIPPQHPVGQPLLIDDWAELVSIHKDDNLYQLLPRRAKSNASYNTMRAICCSAGSPFTMDHRVDPIDYKFVFRAADLEVRNQFNAKSPDKIPTTIWFDGILSAPNDSGLVSCHNTLSPAQINNLAGACQFLKEWSKEPPEGDRHRQLKQLYAQLLSKRSHLFIGTTAVPSREILNYAKTKSVFVYAKRGMHYIFHA
Protein: Tyrosine-protein kinase Drl (EC 2.7.10.1) (Protein derailed) (Q27324)
Organism: Drosophila melanogaster (Fruit fly)
Function: Probable coreceptor of Wnt proteins. Involved in neuronal pathway recognition and ventral muscle attachment site selection. Non-vital for development. May be part of a signal transduction cascade involved in learning and possibly memory.
Subcellular location: Cell membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}.
Interaction partners:
- Protein Wnt-5
- Frizzled
- Tyrosine-protein kinase Dnt
- Frizzled-3
- Frizzled-2
- Frizzled-4
- Roundabout 1, isoform A
- Hibris, isoform B
Sequence:
MAPNLLTIGLLLTLIASGQAHLNIFLNLHEVLRLIGVSAELYYVREGAINDYALNFAVPVPANISDVTFTWQSLVDHPLPYSINIATSDTEVLPRPILNISRIGDVPVEPQTWGIALKCSGTRNAEVTVTINVEVILDRATNNNTNLIFKRKKICLREEQDSAHEEYDDDDLDLLQTARKGHGGDIHYVDRNDEHVVANGHQAPEKQRPVVTESPVGRGNSGGSKRDFDPMLRENLVPPASGLVTLIVGGILALVLVSTLILIAYCAKGPSKRHPSNGVHLIKTSSFQRLPTISSTAHNSIYVCPSTITPTYATLTRPFREYEHEPEEFNRRLQELTVQKCRVRLSCLVQEGNFGRIYRGTYNDCQEVLVKTVAQHASQLQVNLLLQESMMLYEASHPNVLSVLGISIEDYATPFVLYAATGSVRNLKSFLQDPSYARSVTTIQTVLMGSQLAMAMEHLHNHGVIHKDIAARNCVIDDQLRVKLTDSALSRDLFPGDYNSLGDGEYRPIKWLSLEALQKSHYNEGSDVWSFGVLMWEMCTLGKLPYAEIDPYEMEHYLKDGYRLAQPFNCPDELFTIMAYCWASMPAERPSFSQLQICLSEFHTQITRYV
Protein: General regulatory factor 8 (F4KHY7)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
Sequence:
MATTLSRDQYVYMAKLAEQAERYEEMVQFMEQLVSGATPAGELTVEERNLLSVAYKNVIGSLRAAWRIVSSIEQKEESRKNEEHVSLVKDYRSKVETELSSICSGILRLLDSHLIPSATASESKVFYLKMKGDYHRYLAEFKSGDERKTAAEDTMIAYKAAQDVAVADLAPTHPIRLGLALNFSVFYYEILNSSEKACSMAKQAFEEAIAELDTLGEESYKDSTLIMQLLRDNLTLWTSDMQVCPILYFHIQLHHQKLAY
Protein: Stress-induced-phosphoprotein 1 (STI1) (Hsc70/Hsp90-organizing protein) (Hop) (O35814)
Organism: Rattus norvegicus (Rat)
Function: Acts as a co-chaperone for HSP90AA1 (By similarity). Mediates the association of the molecular chaperones HSPA8/HSC70 and HSP90.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:Q60864}. Nucleus {ECO:0000250|UniProtKB:Q60864}. Dynein axonemal particle {ECO:0000250|UniProtKB:Q7ZWU1}.
Interaction partners:
- Major prion protein
- Heat shock protein HSP 90-beta
- Heat shock 70 kDa protein 4
- Hsp90 co-chaperone Cdc37
- Activator of 90 kDa heat shock protein ATPase homolog 1
- DnaJ heat shock protein family
- T-complex protein 1 subunit gamma
- Prostaglandin E synthase 3
- Heat shock protein HSP 90-alpha
- Heat shock cognate 71 kDa protein
Sequence:
MEQVNELKEKGNKALSAGNIDDALQCYSEAIKLDPQNHVLYSNRSAAYAKKGDYQKAYEDGCKTVDLKPDWGKGYSRKAAALEFLNRFEEAKRTYEEGLKHEANNLQLKEGLQNMEARLAERKFMNPFNLPNLYQKLENDPRTRTLLSDPTYRELIEQLQNKPSDLGTKLQDPRVMTTLSVLLGVDLGSMDEEEEAATPPPPPPPKKEAKPEPMEEDLPENKKQALKEKELGNDAYKKKDFDKALKHYDKAKELDPTNMTYITNQAAVHFEKGDYNKCRELCEKAIEVGRENREDYRQIAKAYARIGNSYFKEERYKDAIHFYNKSLAEHRTPDVLKKCQQAEKILKEQERLAYINPDLALEEKNKGNECFQKGDYPQAMKHYTEAIKRNPRDAKLYSNRAACYTKLLEFQLALKDCEECIQLEPTFIKGYTRKAAALEAMKDYTKAMDVYQKALDLDSSCKEAADGYQRCMMAQYNRHDSPEDVKRRAMADPEVQQIMSDPAMRLILEQMQKDPQALSEHLKNPVIAQKIQKLMDVGLIAIR
Protein: Large ribosomal subunit protein uL6 (50S ribosomal protein L6) (P0AG55)
Organism: Escherichia coli (strain K12)
Function: This protein binds directly to at least 2 domains of the 23S ribosomal RNA, thus is important in its secondary structure. It is located near the subunit interface in the base of the L7/L12 stalk, and near the tRNA binding site of the peptidyltransferase center.
Interaction partners:
- Large ribosomal subunit protein uL11
- Large ribosomal subunit protein uL5
- Small ribosomal subunit protein uS8
- Large ribosomal subunit protein uL10
- Large ribosomal subunit protein bL19
- Large ribosomal subunit protein bL12
- Large ribosomal subunit protein uL29
- Protein translocase subunit SecY
- Small ribosomal subunit protein uS9
- Large ribosomal subunit protein uL1
Sequence:
MSRVAKAPVVVPAGVDVKINGQVITIKGKNGELTRTLNDAVEVKHADNTLTFGPRDGYADGWAQAGTARALLNSMVIGVTEGFTKKLQLVGVGYRAAVKGNVINLSLGFSHPVDHQLPAGITAECPTQTEIVLKGADKQVIGQVAADLRAYRRPEPYKGKGVRYADEVVRTKEAKKK
Protein: Peroxisomal membrane protein PEX16 (Q5FVJ9)
Organism: Rattus norvegicus (Rat)
Subcellular location: Peroxisome membrane {ECO:0000256|RuleBase:RU365003}.
Interaction partners:
Sequence:
MRKLGGNLDLPFKVASPIPTSCLSWCTLPLTCLCCSMTGSFGRSFEKKLPVSLSQQKLLTWLSVLECVEVFMEMGAAKVWGEVGRWLVIALIQLAKAVLRMFLLIWFKTGIQTSPPIVPLDRETQAQPLDGDHNLGSPEPSYVGKRSNRVVRTLQNSPSLHSRHWGAPQQREIRQKQQQEELSTPPTPLGLQETIAESLYIARPLLHLLSLGLWGQRSWAPWLLSGVVDMTSLSLLSDRKNLTRRERLELRRRTILLLYYLLRSPFYDRFSEAKILFLLQLLADHIPGIGLVARPLMDYLPSWQKIYFYSWG
Protein: TNF receptor-associated factor 6 (EC 2.3.2.27) (E3 ubiquitin-protein ligase TRAF6) (Interleukin-1 signal transducer) (RING finger protein 85) (RING-type E3 ubiquitin transferase TRAF6) (Q9Y4K3)
Organism: Homo sapiens (Human)
Function: E3 ubiquitin ligase that, together with UBE2N and UBE2V1, mediates the synthesis of 'Lys-63'-linked-polyubiquitin chains conjugated to proteins, such as IKBKG, IRAK1, AKT1 and AKT2. Also mediates ubiquitination of free/unanchored polyubiquitin chain that leads to MAP3K7 activation. Leads to the activation of NF-kappa-B and JUN. Seems to also play a role in dendritic cells (DCs) maturation and/or activation (By similarity). Represses c-Myb-mediated transactivation, in B-lymphocytes. Adapter protein that seems to play a role in signal transduction initiated via TNF receptor, IL-1 receptor and IL-17 receptor. Regulates osteoclast differentiation by mediating the activation of adapter protein complex 1 (AP-1) and NF-kappa-B, in response to RANK-L stimulation (By similarity). Together with MAP3K8, mediates CD40 signals that activate ERK in B-cells and macrophages, and thus may play a role in the regulation of immunoglobulin production (By similarity). Participates also in the TCR signaling by ubiquitinating LAT.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:18093978, ECO:0000269|PubMed:23514740, ECO:0000269|PubMed:24586164}. Cytoplasm, cell cortex {ECO:0000269|PubMed:18093978}. Nucleus {ECO:0000269|PubMed:18093978}. Lipid droplet {ECO:0000250|UniProtKB:P70196}. Note=Found in the nuclei of some aggressive B-cell lymphoma cell lines as well as in the nuclei of both resting and activated T- and B-lymphocytes. Found in punctate nuclear body protein complexes. Ubiquitination may occur in the cytoplasm and sumoylation in the nucleus. RSAD2/viperin recruits it to the lipid droplet (By similarity). {ECO:0000250}.
Interaction partners:
- Mucosa-associated lymphoid tissue lymphoma translocation protein 1
- Toll-like receptor 4
- TRAF-interacting protein with FHA domain-containing protein A
- Interferon regulatory factor 7
- Myeloid differentiation primary response protein MyD88
- Serine/threonine-protein kinase TBK1
- Toll-like receptor 3
- Interferon regulatory factor 5
- TGF-beta-activated kinase 1 and MAP3K7-binding protein 3
- Tumor necrosis factor receptor superfamily member 5
Sequence:
MSLLNCENSCGSSQSESDCCVAMASSCSAVTKDDSVGGTASTGNLSSSFMEEIQGYDVEFDPPLESKYECPICLMALREAVQTPCGHRFCKACIIKSIRDAGHKCPVDNEILLENQLFPDNFAKREILSLMVKCPNEGCLHKMELRHLEDHQAHCEFALMDCPQCQRPFQKFHINIHILKDCPRRQVSCDNCAASMAFEDKEIHDQNCPLANVICEYCNTILIREQMPNHYDLDCPTAPIPCTFSTFGCHEKMQRNHLARHLQENTQSHMRMLAQAVHSLSVIPDSGYISEVRNFQETIHQLEGRLVRQDHQIRELTAKMETQSMYVSELKRTIRTLEDKVAEIEAQQCNGIYIWKIGNFGMHLKCQEEEKPVVIHSPGFYTGKPGYKLCMRLHLQLPTAQRCANYISLFVHTMQGEYDSHLPWPFQGTIRLTILDQSEAPVRQNHEEIMDAKPELLAFQRPTIPRNPKGFGYVTFMHLEALRQRTFIKDDTLLVRCEVSTRFDMGSLRREGFQPRSTDAGV
Protein: Thylakoid lumenal protein TL20.3, chloroplastic (Q8H1Q1)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Pentapeptide repeat protein of unknown function. Subject to degradation when reduced.
Subcellular location: Plastid, chloroplast thylakoid lumen {ECO:0000269|PubMed:18431481, ECO:0000269|PubMed:20049866}.
Interaction partners:
- Peptidyl-prolyl cis-trans isomerase FKBP17-2, chloroplastic
- Peptidyl-prolyl cis-trans isomerase CYP26-2, chloroplastic
- Protein PHOTOSYSTEM I ASSEMBLY 2, chloroplastic
- Peptidyl-prolyl cis-trans isomerase CYP37, chloroplastic
- Peptidyl-prolyl cis-trans isomerase FKBP13, chloroplastic
- Peptidyl-prolyl cis-trans isomerase FKBP17-1, chloroplastic
- Peptidyl-prolyl cis-trans isomerase FKBP16-4, chloroplastic
- Pentatricopeptide repeat-containing protein At1g01970
- Photosynthetic NDH subunit of lumenal location 4, chloroplastic
- Thioredoxin-like protein HCF164, chloroplastic
Sequence:
MAFSSLSPLPMKSLDISRSSSSVSRSPYHFQRYLLRRLQLSSRSNLEIKDSSNTREGCCSSAESNTWKRILSAAMAAAVIASSSGVPAMAELNRFEADTRGEFGIGSAAQYGSADLSKTVHSNENFRRANFTSADMRESDFSGSTFNGAYLEKAVAYKANFSGADLSDTLMDRMVLNEANLTNAVLVRSVLTRSDLGGAKIEGADFSDAVIDLLQKQALCKYATGTNPLTGVDTRKSLGCGNSRRNAYGSPSSPLLSAPPQRLLGRDGFCDEKTGLCDVK
Protein: Epididymis secretory protein Li 85 (Poly(RC) binding protein 1) (Q53SS8)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MDAGVTESGLNVTLTIRLLMHGKEVGSIIGKKGESVKRIREESGARINISEGNCPERIITLTGPTNAIFKAFAMIIDKLEEDINSSMTNSTAASRPPVTLRLVVPATQCGSLIGKGGCKIKEIRESTGAQVQVAGDMLPNSTERAITIAGVPQSVTECVKQICLVMLETLSQSPQGRVMTIPYQPMPASSPVICAGGQDRCSDAAGYPHATHDLEGPPLDAYSIQGQHTISPLDLAKLNQVARQQSHFAMMHGGTGFAGIDSSSPEVKGYWASLDASTQTTHELTIPNNLIGCIIGRQGANINEIRQMSGAQIKIANPVEGSSGRQVTITGSAASISLAQYLINARLSSEKGMGCS
Protein: Germ cell nuclear acidic-1 protein (Germ cell nuclear acidic-1 peptidase) (Q23462)
Organism: Caenorhabditis elegans
Function: May play a role in DNA-protein cross-links (DPCs) clearance through a SUMO-dependent recruitment to sites of DPCs, ensuring the genomic stability by protecting germ cells and early embryos from various sources of damage. May resolve the topoisomerase II (top-2) DPCs. Limits replication stress and DNA double-strand breaks.
Subcellular location: Chromosome {ECO:0000269|PubMed:31839538}. Note=Localizes on condensed chromosomes in spermatocytes in G2 and M during meiotic prophase (PubMed:31839538). Colocalizes with top-2 on condensed chromosomes during embryonic cell divisions (PubMed:31839538). {ECO:0000269|PubMed:31839538}.
Interaction partners:
- DNA-dependent metalloprotease dvc-1
- DNA topoisomerase 2 top-2
- 5' exonuclease Apollo
- Small ubiquitin-related modifier
- DNA topoisomerase 1
Sequence:
MPTPFRDLHNKSNASASSYETAWSSSFSSRRSTNNDSKSNLKEIKDEPISNLDESISILENNISMMSVSSPTPAYRTPARVIAREAPMTPGDRLLQKIEKEDERDMLRQLYPEMFDSNQKPRQKPKEVKKALKVESLSDYENDDKENVPPCGKPSKEKEEKKQRTKKIVISSDSEDDGNFENYLKTLREKPTEPAKPERKIPVKKDFVVDDDYISEESSEEESEEEEEDVDDEEYRESSPEVEAKISYSDRKQKKRPTDEEEWFLLSLSEKFSGPIHEDAKVYIKETSLRYKKHRESLLTRLQDILVRRIFSAIPSEKLKVIWNARLRKSAGQCRNHSNGNSTVEMSPVVCTTAERVRDTLIHELCHAATWVVDRLHKEGHGPGWKRWGARCSSVFKSLPFIERCHSYEIEAKFFYVCEKDGCDVEIKRQSKSLDTSRKACGRCFGRFILYRYCRRTNTRIRIEDPKAKPVGPILSNSSKPSPPAPRRIVSEHPEGFKEYSEEHYWKYTAQGLKHSDVMGKLLKEFKELKQL