wanglab/gogpt-training-data huggingface dataset:
Protein: DnaJ homolog subfamily C member 11 (Q5U458)
Organism: Mus musculus (Mouse)
Function: Required for mitochondrial inner membrane organization. Seems to function through its association with the MICOS complex and the mitochondrial outer membrane sorting assembly machinery (SAM) complex.
Subcellular location: Mitochondrion {ECO:0000250|UniProtKB:Q9NVH1, ECO:0000269|PubMed:25111180}. Mitochondrion outer membrane {ECO:0000250|UniProtKB:Q9NVH1}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q9NVH1}.
Interaction partners:
- MICOS complex subunit Mic60
- MICOS complex subunit Mic19
- MICOS complex subunit Mic27
- MICOS complex subunit Mic26
- Metaxin-1
- MICOS complex subunit Mic25
- Metaxin-2
- Sorting and assembly machinery component 50 homolog
- MICOS complex subunit MIC13
- Coiled-coil-helix-coiled-coil-helix domain containing 10
Sequence:
MATALSEEELDNEDYYSLLNVRREASSEELKAAYRRLCMLYHPDKHRDPELKSQAERLFNLVHQAYEVLSDPQTRAIYDIYGKRGLEMEGWEVVERKRTPAEIREEFERLQREREERRLQQRTNPKGTISVGVDATDLFDRYDEEYEDVSGSGFPQIEINKMHISQSIEAPLTATDTAILSGSLSTQNGNGGGSVNFALRRVTSAKGWGELEFGAGDLQGPLFGLKLFRNLTPRCFVTTNCALQFSSRGIRPGLTTVLARNLDKNTVGYLQWRWGIQSAMNTSIVRDTKTCHFTVALQLGIPHSFALISYQHKFQDDDQTRVKGSLKAGFFGTIVEYGAERKISRHSVLGAAVSIGVPQGVSLKVKLNRASQTYFFPIHLTDQLLPSAVFYATVGPLVVYLAVHRLIIRPYLRAQKEKELEKQRENTASDILQKKQEAEAAVRLMQESVRRIIEAEESRMGLIIVNAWYGKFVNDKSRKNEKVKVIDVTVPLQCLVKDSKLILTEASKAGLPGFYDPCVGEEKSLRVLYQFRGVLHQVMVPDSEALRIPKQSHRIDTDG
Protein: Predicted gene, 20814 (Predicted gene, 20855) (Predicted gene, 20905) (Predicted gene, 20906) (Predicted gene, 20908) (Predicted gene, 20920) (Predicted gene, 20931) (Predicted gene, 21317) (Predicted gene, 21366) (Sycp3 like Y-linked) (A0A087WRK1)
Organism: Mus musculus (Mouse)
Interaction partners:
- Y-linked testis-specific protein 1
Sequence:
MRRMALKKLKVIPKEGYLLLLDFDDEDDDIKVSEEALSEVKSPAFDKNENISPQAEADEDMGDEVDSMLDKSEVNNPAIGKDENISPQVKGDEDMGHEVGSMLDKSGDDIYKTLHIKRKWMETYVKESFKGSNQKLERFCKTNERERKNINNKFCEQYITTFQKSDMDVQKFNEEKEKSVNSCQKEQQALKLSKCSQNQTLEAVKEMHEKSMEVLMNLGTKN
Protein: Transcription factor 7 (TCF-7) (T-cell-specific transcription factor 1) (T-cell factor 1) (Q00417)
Organism: Mus musculus (Mouse)
Function: Transcriptional activator involved in T-cell lymphocyte differentiation. Necessary for the survival of CD4(+) CD8(+) immature thymocytes. Isoforms lacking the N-terminal CTNNB1 binding domain cannot fulfill this role. Binds to the T-lymphocyte-specific enhancer element (5'-WWCAAAG-3') found in the promoter of the CD3E gene. Represses expression of the T-cell receptor gamma gene in alpha-beta T-cell lineages. Inhibits the developmental program of IL17A effector gamma-delta T-cell subsets via regulating the transcription of T-cell lineage effector proteins. Required for the development of natural killer receptor-positive lymphoid tissue inducer T-cells. TLE1, TLE2, TLE3 and TLE4 repress transactivation mediated by TCF7 and CTNNB1 (By similarity). May also act as feedback transcriptional repressor of CTNNB1 and TCF7L2 target genes.
Subcellular location: Nucleus.
Interaction partners:
- Catenin beta-1
- Axin-2
- Serine/threonine-protein kinase NLK
- Junction plakoglobin
- C-terminal-binding protein 1
- C-terminal-binding protein 2
- Axin-1
- Transcription factor 7-like 1
- Transcription factor 7-like 2
- Adenomatous polyposis coli protein
Sequence:
MPQLDSGGGGAGRGDDLGAPDELLAFQDEGEEQDDKNRDSPVGPERDLAELKSSLVNESEGAAAGAGVPGPGVRVHGEAEGAPEALGREHTSQRLFPDKLPESLEDGLKAPECTSGMYKETVYSAFNLLMPYPPASGAGQHPQPQPPLHNKPGQPPHGVPQLSPLYEHFSSPHPTPAPADISQKQGVHRPLQTPDLSGFYSLTSGSMGQLPHTVSWPSPPLYPLSPSCGYRQHFPAPTAAPGAPYPRFTHPSLMLGSGVPGHPAAIPHPAIVPSSGKQELQPYDRNLKTQAEPKAEKEAKKPVIKKPLNAFMLYMKEMRAKVIAECTLKESAAINQILGRRWHALSREEQAKYYELARKERQLHMQLYPGWSARDNYGKKKRRSREKHQESTTGGKRNAFGTYPEKAAAPAPFLPMTVL
Protein: Heat shock protein DDB_G0280215 (Q54VP4)
Organism: Dictyostelium discoideum (Social amoeba)
Interaction partners:
- Peptidase A1 domain-containing protein
- SrfA-induced gene F protein
- Putative uncharacterized protein DDB_G0284619
Sequence:
MSINWLTHPFEELSNLKHSLDETLKNWTEPAPTAATSMDWGWKPRMDVCENKDYYKIILELPSFNKDEIEVQVNGRFLSIKGQKIEHTTDEWKYHRRERYSGGEFHRAVALPEGIDGSSIQAKFQSGVLLLLIPKTGGKTSQHISLFGREEHGNKRNVIDLEEKERKRRMEESDPMLGRRWGTGRSLFSGSKLNNQNDTMYRKPSASDLRLVKQMETKERERRIRDTKGETEKKKNALKVSRYIKSLGMNPRSTLRRGGREMEKIIHLEERERQARIRDKGRMRQQQALAKKVSNLIKHSGGAARLRHTGFNYSTITKGYNTNKTKFDRFGKENDSFGGFNINKSFTNQFKGFGKNSGGKSINITTGGFKAPSQFNKFTHNLEEKERQRRLNDKKGQNDAKRLAAEISHMIGNAHF
Protein: UDP-glycosyltransferase 708C1 (EC 2.4.1.360) (C-glucosyltransferase a) (FeCGTa) (UDP-glucose:2-hydroxyflavanone C-glucosyltransferase) (A0A0A1HA03)
Organism: Fagopyrum esculentum (Common buckwheat) (Polygonum fagopyrum)
Function: UDP-glucose-dependent glucosyltransferase catalyzing the C-glucosylation of 2-hydroxyflavanones (2-hydroxynaringenin, 2-hydroxyeriodictyol and 2-hydroxypinocembrin) and phloretin. No activity with flavanones, flavones or flavonols. Exhibits C-glycosylation activity toward 2',4',6'-trihydroxyacetophenone and phloretin using UDP-glucose as sugar donor. Can use UDP-galactose as sugar donor, but catalytic efficiency is 14-fold lower toward UDP-galactose than toward UDP-glucose.
Interaction partners:
Sequence:
MMGDLTTSFPATTLTTNDQPHVVVCSGAGMGHLTPFLNLASALSSAPYNCKVTLLIVIPLITDAESHHISSFFSSHPTIHRLDFHVNLPAPKPNVDPFFLRYKSISDSAHRLPVHLSALSPPISAVFSDFLFTQGLNTTLPHLPNYTFTTTSARFFTLMSYVPHLAKSSSSSPVEIPGLEPFPTDNIPPPFFNPEHIFTSFTISNAKYFSLSKGILVNTFDSFEPETLSALNSGDTLSDLPPVIPIGPLNELEHNKQEELLPWLDQQPEKSVLYVSFGNRTAMSSDQILELGMGLERSDCRFIWVVKTSKIDKDDKSELRKLFGEELYLKLSEKGKLVKWVNQTEILGHTAVGGFLSHCGWNSVMEAARRGVPILAWPQHGDQRENAWVVEKAGLGVWEREWASGIQAAIVEKVKMIMGNNDLRKSAMKVGEEAKRACDVGGSSATALMNIIGSLKR
Protein: Putative synaptobrevin homolog YKT6 (EC 2.3.1.-) (Putative prenylated SNARE protein ykt6) (Q54ES8)
Organism: Dictyostelium discoideum (Social amoeba)
Function: Vesicular soluble NSF attachment protein receptor (v-SNARE) mediating vesicle docking and fusion to a specific acceptor cellular compartment. Functions in endoplasmic reticulum to Golgi transport and in early/recycling endosome to TGN transport as part of a SNARE complex. Has a S-palmitoyl transferase activity (By similarity).
Subcellular location: Cytoplasm, cytosol {ECO:0000250}. Cytoplasmic vesicle membrane {ECO:0000250}; Lipid-anchor {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Golgi apparatus membrane {ECO:0000250}; Lipid-anchor {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Cytoplasmic vesicle, phagosome membrane {ECO:0000250}; Lipid-anchor {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Endosome membrane {ECO:0000250}; Lipid-anchor {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Note=Probably cycles through vesicles between Golgi and endosomes. {ECO:0000250}.
Interaction partners:
- Vesicle transport through interaction with t-SNAREs homolog 1A
- V-SNARE family protein
- Probable syntaxin-8B
- t-SNARE family protein
- Synaptobrevin domain-containing protein
- V-SNARE family protein
- Golgi SNAP receptor complex member 1
- t-SNARE coiled-coil homology domain-containing protein
- Vesicle-trafficking protein SEC22b
- Sec1 family domain-containing protein 1 homolog
Sequence:
MKVYSIGLFKVVPGNKPVLLNIVYELSSFGFFQRGSVKEVSLFVSRETVGRTNVGERVSMEHTQTQKVCHTTVDSKGLGCSVLTDSEYPGRVAHTLIRICLEEFYKVHPESEWRGLQSDVELQTPALDQLLLKYQNPETADPMMNLQKNLDETITIVKKTVEQLGQRGEKLDDLAAKSDDLSFQSKAFMNNAERMNKCCGYV
Protein: Heme/hemoglobin uptake outer membrane receptor PhuR (Q9HV88)
Organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Subcellular location: Cell outer membrane {ECO:0000256|ARBA:ARBA00004571, ECO:0000256|PROSITE-ProRule:PRU01360}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004571, ECO:0000256|PROSITE-ProRule:PRU01360}.
Interaction partners:
- Heme-transport protein, PhuT
- Hemin import ATP-binding protein HmuV
- Heme oxygenase PigA
- Probable hemin degrading factor
- Probable permease of ABC transporter
- Heme acquisition protein HasAp
- Sigma factor PvdS
- Second ferric pyoverdine receptor FpvB
- Haem-binding uptake Tiki superfamily ChaN domain-containing protein
- Protein TonB
Sequence:
MPLSPPFALRPCLALLLLSPSLALAGNAVPLTPTTITATRTEQAVDSVPSTVSVQTREQLDRQNVNNIKELVRYEPGVSVGGAGQRAGITGYNIRGIDGNRILTQIDGVELPNDFFSGPYAQTHRNYVDPDIVKRVEILRGPASALYGSNAIGGAVSYFTLDPSDIIKDGKDVGARLKAGYESASHSWLTSATVAGRADDFDGLLHYGYRQGHETESNGGHGGTGLSRSEANPEDADSYSLLGKLGWNYAEGSRFGLVFEKYKSDVDTDQKSAYGGPYDKGKPAIPPSMLPGGMYQWRKGNDTLTRERYGLEHHFLLDSQVADRIQWSLNYQLAKTDQATREFYYPITRKVLRTRDTTYKERLWVFDSQLDKSFAIGETEHLLSYGINLKHQKVTGMRSGTGTNLDTGADSPRDALERSSDFPDPTVKTYALFAQDSISWNDWTFTPGLRYDYTRMEPHITDEFLRTMKQSQNTAVDESDKKWHRVSPKFGVTYDFAQHYTWYGQYAQGFRTPTAKALYGRFENLQAGYHIEPNPNLKPEKSQSFETGLRGKFDEGSFGVAVFYNKYRDFIDEDALNTDSTGGNGQTFQSNNIERAVIKGVELKGRLELGAFGAPQGLYTQGSVAYAYGRNKDNGEPINSVNPLTGVFGLGYDEADGNYGGLLSWTLVKRKDRVDDSTFHTPDGTASQFKTPGFGVLDLSAYYRLSKDLTLNAGLYNLTDKKYWLWDDVRGYDSVGEASALAPANIDRLSQPGRNFAVNLVWDI
Protein: Cold shock-like protein CspI (CPS-I) (P0A986)
Organism: Escherichia coli (strain K12)
Subcellular location: Cytoplasm {ECO:0000250}.
Interaction partners:
- Uncharacterized protein YnfN
- Cold shock-like protein CspB
- Uncharacterized protein YnaE
- 30S ribosome-binding factor
Sequence:
MSNKMTGLVKWFNPEKGFGFITPKDGSKDVFVHFSAIQSNDFKTLTENQEVEFGIENGPKGPAAVHVVAL
Protein: Replication factor C subunit 5 (AtRFC5) (Activator 1 subunit 5) (Protein EMBRYO DEFECTIVE 2810) (Q9CAQ8)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Functions in cell replication and proliferation. May be involved in chromatin assembly and remodeling. Plays a role in the negative control of pathogenesis-related gene expression and systemic acquired resistance (SAR).
Subcellular location: Nucleus {ECO:0000269|PubMed:19482917}.
Interaction partners:
- Replication factor C subunit 3
- Cell cycle checkpoint protein RAD17
- Replication factor C subunit 2
- Chromosome transmission fidelity protein 18 homolog
- Checkpoint protein
- Replication factor C subunit 4
- Proliferating cell nuclear antigen 2
- Replication factor C subunit 1
- Proliferating cellular nuclear antigen 1
- Protein STICHEL
Sequence:
MTELTSAMDIDVDEIQPRKPINKGKDVVGFGPPPQSKATPWVEKYRPQSLDDVAAHRDIIDTIDRLTNENKLPHLLLYGPPGTGKTSTILAVARKLYGPKYRNMILELNASDDRGIDVVRQQIQDFASTQSFSLGKSSVKLVLLDEADAMTKDAQFALRRVIEKYTKSTRFALIGNHVNKIIPALQSRCTRFRFAPLDGVHMSQRLKHVIEAERLVVSDCGLAALVRLSNGDMRKALNILQSTHMASKEITEEESKQITEEDVYLCTGNPLPKDIEQISHWLLNKPFDECYKDVSEIKTRKGLAIVDIVKEITLFIFKIKMPSAVRVQLINDLADIEYRLSFGCNDKLQLGAIISTFTHARSIIVGAAK
Protein: BICD family-like cargo adapter 1 (Bicaudal D-related protein 1) (BICD-related protein 1) (BICDR-1) (Coiled-coil domain-containing protein 64A) (A0JNT9)
Organism: Mus musculus (Mouse)
Function: Acts as an adapter protein linking the dynein motor complex to various cargos and converts dynein from a non-processive to a highly processive motor in the presence of dynactin. Facilitates the interaction between dynein and dynactin and activates dynein processivity (the ability to move along a microtubule for a long distance without falling off the track). Predominantly recruits 2 dyneins, which increases both the force and speed of the microtubule motor. Component of secretory vesicle machinery in developing neurons that acts as a regulator of neurite outgrowth. Regulates the secretory vesicle transport by controlling the accumulation of Rab6-containing secretory vesicles in the pericentrosomal region restricting anterograde secretory transport during the early phase of neuronal differentiation, thereby inhibiting neuritogenesis.
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000305|PubMed:36071160}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000269|PubMed:20360680}. Note=Localizes around the centrosome.
Interaction partners:
- Ras-related protein Rab-6A
- Dynactin subunit 5
- Dynactin subunit 4
- Alpha-centractin
- Actin-related protein 10
- Dynactin subunit 6
- Dynactin subunit 2
- Cytoplasmic dynein 1 light intermediate chain 2
- Actin, cytoplasmic 1
- Cytoplasmic dynein 1 heavy chain 1
Sequence:
MSAFCLGLAGRASAPAEPDSACCMELPAGAGDAVRSPATAAALVSFPGGPGELELALEEELALLAAGERSSEPGEHPQAEPESPVEGHGPPLPPPPTQDPELLSVIRQKEKDLVLAARLGKALLERNQDMSRQYEQMHKELTDKLEHLEQEKHELRRRFENREGEWEGRVSELETDVKQLQDELERQQLHLREADREKTRAVQELSEQNQRLLDQLSRASEVERQLSMQVHALKEDFREKNSSTNQHIIRLESLQAEIKMLSDRKRELEHRLSATLEENDLLQGTVEELQDRVLILERQGHDKDLQLHQSQLELQEVRLSYRQLQGKVEELTEERSLQSSAATSTSLLSEIEQSMEAEELEQEREQLRLQLWEAYCQVRYLCSHLRGNDSADSAVSTDSSMDESSETSSAKDVPAGSLRTALNDLKRLIQSIVDGVEPTVTLLSVEMTALKEERDRLRVTSEDKEPKEQLQKAIRDRDEAIAKKNAVELELAKCKMDMMSLNSQLLDAIQQKLNLSQQLEAWQDDMHRVIDRQLMDTHLKEQSRPAAAAFPRGHGVGRGQEPSTADGKRLFSFFRKI
Protein: L-amino acid N-acetyltransferase AaaT (L-methionine N-acetyltransferase) (EC 2.3.1.-) (L-phenylalanine N-acetyltransferase) (EC 2.3.1.53) (P46854)
Organism: Escherichia coli (strain K12)
Function: Catalyzes the N-acetylation of L-phenylalanine and L-methionine using acetyl-CoA as acetyl donor in vitro. Cannot accept L-tyrosine as substrate and propionyl-CoA, succinyl-CoA or (S)-methylmalonyl-CoA as acyl donors. Is also able to acetylate and thus detoxify several nonhydrolyzable aminoacyl adenylates, but not the processed form of the peptide-nucleotide antibiotic microcin C (McC). When overproduced, provides complete resistance to leucyl sulfamoyl adenylate (LSA) and partial resistance to alanyl sulfamoyl adenylate (ASA) and phenylalanyl sulfamoyl adenylate (FSA). Therefore, may protect bacteria from various toxic aminoacyl nucleotides, either exogenous or those generated inside the cell during normal metabolism.
Interaction partners:
- Histidinol-phosphate aminotransferase
- Acetyltransferase YpeA
- Catalase-peroxidase
- Aromatic-amino-acid aminotransferase
- Aspartate aminotransferase
- Ribosomal-protein-serine acetyltransferase
- Bifunctional chorismate mutase/prephenate dehydratase
- Uncharacterized N-acetyltransferase YhbS
- [Ribosomal protein uS5]-alanine N-acetyltransferase
Sequence:
MSEIVIRHAETRDYEAIRQIHAQPEVYCNTLQVPHPSDHMWQERLADRPGIKQLVACIDGDVVGHLTIDVQQRPRRSHVADFGICVDSRWKNRGVASALMREMIEMCDNWLRVDRIELTVFVDNAPAIKVYKKYGFEIEGTGKKYALRNGEYVDAYYMARVK
Protein: At1g50450/F11F12_20 (Saccharopine dehydrogenase) (Q94BZ0)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Electron transfer flavoprotein subunit alpha, mitochondrial
- Electron transfer flavoprotein subunit beta, mitochondrial
- Geranylgeranyl diphosphate reductase, chloroplastic
- peptidylprolyl isomerase
- Plasma membrane fusion protein
- MAR-binding filament-like protein 1
- Large ribosomal subunit protein uL13c
- Threonine--tRNA ligase, chloroplastic/mitochondrial 2
- AT3g07470/F21O3_18
Sequence:
MTRALLLQPYRATVRAASSRETQYDGVPEVKFSDPSRNYRVLVLGGTGRVGGSTATALSKLCPELKIVVGGRNREKGEAMVAKLGENSEFSQVDINDAKMLETSLRDVDLVVHAAGPFQQAPRCTVLEAAIKTKTAYLDVCDDTSYAFRAKSLEAEAIAANIPALTTAGIYPGVSNVMAAEMVAAARSEDKGKPEKLRFSYYTAGTGGAGPTILATSFLLLGEEVTAYKQGEKVKLRPYSGMITVDFGKGIRKRDVYLLNLPEVRSTHEVLGVPTVVARFGTAPFFWNWGMEIMTKLLPSEVLRDRTKVQQMVELFDPVVRAMDGFAGERVSMRVDLECSDGRTTVGLFSHKKLSVSVGVSTAAFVAAMLEGSTQPGVWFPEEPQGIAVEAREVLLKRASQGTFNFILNKPPWMVETEPKEVVLGIYV
Protein: ManO (A0A0H2UNI9)
Organism: Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4)
Interaction partners:
Sequence:
MAQSLNKTVLLSTTGTSYLSIAGKVGKFLVGDQALEFYPDVNVEQFIQIPWSHINQIGANVTGRKISRHFEVFTDKGKFLFASKDSGAILKIAREKLGNDKVVKLPTLIQTISQKFKNLFAKK
Protein: N6-succino-2-amino-2'-deoxyadenylate synthase (EC 6.3.4.25) (2-amino-2'-deoxyadenylo-succinate synthase) (PurZ) (G3FFN6)
Organism: Vibrio phage phiVC8
Function: Involved in the synthesis of the atypical nucleotide dZTP (2-amino-2'-deoxyadenosine-5'-triphosphate). Catalyzes the condensation of aspartate with deoxyguanylate into dSMP (N6-succino-2-amino-2'-deoxyadenylate), which undergoes defumarylation and phosphorylation respectively by host PurB and guanylate/nucleoside diphosphate kinases to give dZTP. dZTP is integrated into the viral genome instead of adenine by the viral DNA polymerase. This Z-base probably completely replaces adenosine and forms a triple bond to the opposite T-base. The resulting non-standard viral DNA is called Z-genome. The chemically modified DNA is probably harder for the host bacteria to digest with nucleases or restriction enzymes (Probable).
Interaction partners:
Sequence:
MKNVDLVIDLQFGSTGKGLIAGYLAEKNGYDTVINANMPNAGHTYINAEGRKWMHKVLPNGIVSPNLKRVMLGAGSVFSINRLMEEIEMSKDLLHDKVAILIHPMATVLDEEAHKKAEVGIATSIGSTGQGSMAAMVEKLQRDPTNNTIVARDVAQYDGRIAQYVCTVEEWDMALMASERILAEGAQGFSLSLNQEFYPYCTSRDCTPARFLADMGIPLPMLNKVIGTARCHPIRVGGTSGGHYPDQEELTWEQLGQVPELTTVTKKVRRVFSFSFIQMQKAMWTCQPDEVFLNFCNYLSPMGWQDIVHQIEVAAQSRYCDAEVKYLGFGPTFNDVELREDVM
Protein: Coiled-coil domain containing 92 (F5H285)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MTSPHFSSYDEGPLDVSMAATNLENQLHSAQKNLLFLQREHASTLKGLHSEIRRLQQHCTDLTYELTVKSSEQTGDGTSKSSELKKRCEELEAQLKVKENENAELLKELEQKNAMITVLENT
Protein: AP complex subunit sigma (H0YN38)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasmic vesicle membrane {ECO:0000256|ARBA:ARBA00004180}; Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004180}; Cytoplasmic side {ECO:0000256|ARBA:ARBA00004180}. Golgi apparatus {ECO:0000256|ARBA:ARBA00004555}.
Interaction partners:
Sequence:
MIQAILVFNNHGKPRLVRFYQRFPEEIQQQIVRETFHLVLKRDDNICNFLEGGSLIGGSDYKLIYRHYATLYFVFCVDSSESELGILDLIQVFVETLDKCFENVCELDLIFHMDKVHYILQEVVMGGMVLETNMNEIVAQIEAQNRLEKSEDQVLA
Protein: Interleukin-10 (IL-10) (Cytokine synthesis inhibitory factor) (CSIF) (P29456)
Organism: Rattus norvegicus (Rat)
Function: Major immune regulatory cytokine that acts on many cells of the immune system where it has profound anti-inflammatory functions, limiting excessive tissue disruption caused by inflammation. Mechanistically, IL10 binds to its heterotetrameric receptor comprising IL10RA and IL10RB leading to JAK1 and STAT2-mediated phosphorylation of STAT3. In turn, STAT3 translocates to the nucleus where it drives expression of anti-inflammatory mediators. Targets antigen-presenting cells (APCs) such as macrophages and monocytes and inhibits their release of pro-inflammatory cytokines including granulocyte-macrophage colony-stimulating factor /GM-CSF, granulocyte colony-stimulating factor/G-CSF, IL-1 alpha, IL-1 beta, IL-6, IL-8 and TNF-alpha. Interferes also with antigen presentation by reducing the expression of MHC-class II and co-stimulatory molecules, thereby inhibiting their ability to induce T cell activation (By similarity). In addition, controls the inflammatory response of macrophages by reprogramming essential metabolic pathways including mTOR signaling (By similarity).
Subcellular location: Secreted {ECO:0000250|UniProtKB:P22301}.
Interaction partners:
- Interleukin-10 receptor subunit alpha
- Interleukin 10 receptor subunit beta
- Interferon gamma
- Interleukin-7
- T-cell surface glycoprotein CD4
- Interleukin-1 beta
- Interleukin-5
- Tumor necrosis factor
- Interleukin-6
- Interleukin-1 alpha
Sequence:
MPGSALLCCLLLLAGVKTSKGHSIRGDNNCTHFPVSQTHMLRELRAAFSQVKTFFQKKDQLDNILLTDSLLQDFKGYLGCQALSEMIKFYLVEVMPQAENHGPEIKEHLNSLGEKLKTLWIQLRRCHRFLPCENKSKAVEQVKNDFNKLQDKGVYKAMNEFDIFINCIEAYVTLKMKN
Protein: DCN1-like protein 5 (DCUN1 domain-containing protein 5) (Defective in cullin neddylation protein 1-like protein 5) (Squamous cell carcinoma-related oncogene 5) (Q5PPL2)
Organism: Rattus norvegicus (Rat)
Function: Contributes to the neddylation of all cullins by transferring NEDD8 from N-terminally acetylated NEDD8-conjugating E2s enzyme to different cullin C-terminal domain-RBX complexes which is necessary for the activation of cullin-RING E3 ubiquitin ligases (CRLs). May play a role in DNA damage response and may participate in cell proliferation and anchorage-independent cell growth.
Subcellular location: Nucleus {ECO:0000250|UniProtKB:Q9BTE7}. Cytoplasm, cytoskeleton, spindle {ECO:0000250|UniProtKB:Q9BTE7}. Note=Subcellular localization is independent of the interaction with cullins. {ECO:0000250|UniProtKB:Q9BTE7}.
Interaction partners:
- Ubiquitin-like protein NEDD8
- NEDD8-conjugating enzyme UBE2F
- NEDD8-conjugating enzyme UBC12
- Cullin-3
- Cullin-associated NEDD8-dissociated protein 1
- NEDD8-activating enzyme E1 catalytic subunit
- Cullin 2
- E3 ubiquitin-protein ligase RBX1
Sequence:
MPVKKKRKAPGVAAAVAEDAGLKKCKISSYCRSQPPARLISGEEDFSRKKCLAWFYEYAGPDEVVGPEGMEKFCEDIGVEPENIIMLVLAWKLEAESMGFFTKEEWLKGMTSLQCDCTEKLQSRFDFLRSQLNDISSFKNIYRYAFDFARDKDQRSLDIDTAKSMLALLLGRTWPLFSVFYQYLEQSKYRVMNKDQWYNVLEFSRTVHADLSNYDEDGAWPVLLDEFVEWQKIRQTS
Protein: ABC-type glutathione-S-conjugate transporter (EC 7.6.2.3) (Q9VK56)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004651}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}. Vacuole membrane {ECO:0000256|ARBA:ARBA00004128}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004128}.
Interaction partners:
- GH23453p
Sequence:
MADDTSSPMDRFCGSTFWNATETWYTNDPDFTPCFEQTALVWTPCAFYWAFVIFDFYYLKASLDRNIPWNKLNVSKALVNLGLLVITALDLIMALVKKGGDSELPLYDLDVWGPIIKFATFLLLFIFIPLNRKYGVQTTGCQFIFWFLLTVLSIPRCRTEVRLDAERQKILNSQQPSEQDFSWEEYQFVSFFIFFTFTSIMLILNCFADGMPRQTKYQRGENEIPELSASFLSRITYQWFDKMALKGYRNPLEEKDLWDLRPQDSCSEVMPIFAHHWNQNVRKNYKNKARVEPKAQFSNGNVTFENPHGEKNGRKKGMASIMPPIYKSFGGVFLFGALMKLFTDTLTFAQPQVLSLIISFVEAQDAEPEWKGILYAVLLFVLAAAQTFILGQYFHRMFIVGLRIRTALINAIYRKALRISNSTKKESTVGEIVNLMAVDAQRFMELTTYLNMIWSAPLQIGLALYFLWQQLGPSVLAGLAVMIILIPVNGVIASRIKTYQIRQMKYKDERVKLMNEVLSGIKVLKLYAWEPSFEKQVLDIRDKEIATLRSTAYLNAGTSFLWSCAPFLVSLVTFATYVLTSEANQLSVEKVLVSIALFDLMKLPLTILPMLSVDIAETQVSVNRINKFLNSEELDPNSVLHDSSKPHPMSIENGEFSWGDEITLRNINIEVKKGSLVALVGTVGSGKSSVVQAFLGEMEKLAGVVNTVGKLAYVPQQAWIQNATVRDNILFGQTYDRKRYNKVIDACALRADIDILSAGDLTEIGEKGINLSGGQKQRISLARAVYSDADLYLLDDPLSAVDAHVGKHIFEEVIGPKGILARKSRVLVTHGVTFLPQVDSIYVIKMGEISESGTFDQLVKNKGAFADFIIQHLQEGNEEEEELNQIKRQISSTADVPELLGTVEKAIKLARTESLSDSISVTSADSLMGGGGSLRRRTKRQDSHDSVASAASLKKKQEVEGKLIETEKSQTGGVEFAVYKHYIKSVGIFLSVATLVLNFVFQAFQIGSNLWLTQWANDQNVANDTGLRDMYLGVYGAFGFGQGVLAYFAVVIVYLGGFQAAKTIHNELLAVIIRGSVCRFFDITPIGRLLNSFSGDMDVVDEELPATMDSFMTFIFMVLATIVVISLSTPIFLAVIVPIAFLYYFAQRFYVATSRQLMRLESVSRSPIYSHFSETVTGASTIRAYNVGDRFIEESDAKVDKNQVCKYPSVIANRWLAIRLEMVGNLIILFASLFAVLGGQTNPGLVGLSVSYALQVTQTLNWLVRMSSDIETNIVSVERIKEYGETKQEAPWELEQDKNKPKNWPQEGRVEFQNFQVRYREGLDLVLRGVSFNIQGGEKVGIVGRTGAGKSSLTLALFRIIEAAGGRISIDGVDIASMGLHMLRSRLTIIPQDPVLFSGSLRINLDPFEIKTDDEIWKALELSHLKSFVKSLAAGLNHEIAEGGENLSVGQRQLVCLARALLRKTKVLVLDEATAAVDLETDDLIQKTIRTEFKECTVLTIAHRLNTILDSDKVIVLDKGQIIEFASPTELLDNPKSAFYSMAKDANLV
Protein: Putrescine N-methyltransferase 3 (NtPMT3) (EC 2.1.1.53) (Q9SEH5)
Organism: Nicotiana tabacum (Common tobacco)
Function: Involved in the biosynthesis of pyridine alkaloid natural products, leading mainly to the production of anabasine, anatabine, nicotine and nornicotine, effective deterrents against herbivores with antiparasitic and pesticide properties (neurotoxins); nornicotine serves as the precursor in the synthesis of the carcinogen compound N'-nitrosonornicotine (NNN). Methyltransferase that mediates the conversion of putrescine to N-methylputrescine. Promotes leaves ripening.
Interaction partners:
- arginase
- Arginase 1, mitochondrial-like
- Arginase 1
Sequence:
MEVISTNTNGSTIFKNGAIPMNGYQNGTSKHQNGHQNGTSEHRNGHQNGISEHQNGHQNGTSEHQNGHQNGTISHDNGNELQLLGSSNSIKPGWFSEFSALWPGEAFSLKVEKLLFQGKSDYQDVMLFESATYGKVLTLDGAIQHTENGGFPYTEMIVHLPLGSIPNPKKVLIIGGGIGFTLFEMLRYPTIEKIDIVEIDDVVVDVSRKFFPYLAANFSDPRVTLVLGDGAAFVKAAQAGYYDAIIVDSSDPIGPAKDLFERPFFEAVAKALRPGGVVCTQAESIWLHMHIIKQIIANCRQVFKGSVNYAWTTVPTYPTGVIGYMLCSTEGPEVDFKNPVNPIDKETTQVKSKLAPLKFYNSDIHKAAFILPSFARSMIES