wanglab/gogpt-training-data huggingface dataset:
Protein: Ferric citrate uptake sigma factor regulator FecR (P23485)
Organism: Escherichia coli (strain K12)
Function: Regulation of iron dicitrate transport. In the absence of citrate FecR inactivates fecI. FecR is probably a sensor that recognizes iron dicitrate in the periplasm.
Subcellular location: Cell inner membrane {ECO:0000269|PubMed:9573190}; Single-pass membrane protein {ECO:0000255}. Note=Contains an internal twin-arginine motif immediately upstream of the transmembrane region which allows it to be translocated across the inner membrane via the Tat system. {ECO:0000269|PubMed:32015149}.
Interaction partners:
- Ferric citrate uptake sigma factor FecI
- Fe
- Fe
- Hydroxamate siderophore receptor FhuE
- Fe
- Fe
- Fe
- Biopolymer transport protein ExbB
- Biopolymer transport protein ExbD
- Ferrichrome outer membrane transporter/phage receptor
Sequence:
MNPLLTDSRRQALRSASHWYAVLSGERVSPQQEARWQQWYEQDQDNQWAWQQVENLRNQLGGVPGDVASRALHDTRLTRRHVMKGLLLLLGAGGGWQLWQSETGEGLRADYRTAKGTVSRQQLEDGSLLTLNTQSAADVRFDAHQRTVRLWYGEIAITTAKDALQRPFRVLTRQGQLTALGTEFTVRQQDNFTQLDVQQHAVEVLLASAPAQKRIVNAGESLQFSASEFGAVKPLDDESTSWTKDILSFSDKPLGEVIATLTRYRNGVLRCDPAVAGLRLSGTFPLKNTDAILNVIAQTLPVKIQSITRYWINISPL
Protein: ER-derived vesicles protein ERV41 (Q04651)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Constituent of COPII-coated endoplasmic reticulum-derived transport vesicles. Required for efficient transport of a subset of secretory proteins to the Golgi. The C-terminal Ile-Leu motif is required for exit from the endoplasmic reticulum. Facilitates retrograde transport from the Golgi to the endoplasmic reticulum.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:11758914, ECO:0000269|PubMed:12426381}; Multi-pass membrane protein {ECO:0000255}. Golgi apparatus membrane {ECO:0000269|PubMed:10713261, ECO:0000269|PubMed:11758914, ECO:0000269|PubMed:12426381, ECO:0000269|PubMed:16107716}; Multi-pass membrane protein. Cytoplasmic vesicle, COPII-coated vesicle membrane {ECO:0000269|PubMed:11157978, ECO:0000269|PubMed:12426381}; Multi-pass membrane protein {ECO:0000255}. Note=Recycles between endoplasmic reticulum and Golgi. Resides in the endoplasmic and Golgi compartments, and then packaged into endoplasmic reticulum derived vesicles. {ECO:0000269|PubMed:12426381}.
Interaction partners:
- ER-derived vesicles protein ERV46
- ERAD-associated E3 ubiquitin-protein ligase component HRD3
- U1 SNP1-associating protein 1
- Degradation in the endoplasmic reticulum protein 1
- tRNA modification GTPase MSS1
- Endoplasmic reticulum vesicle protein 25
- Protein SVP26
- ER-derived vesicles protein ERV29
- Protein ERP1
- Coatomer subunit beta
Sequence:
MAGLKTFDAFPKTEEQYKKKSTKGGLTSLLTYLFLLFIAWTEFGEYFGGYIDQQYVVDSQVRDTVQINMDIYVNTKCDWLQINVRDQTMDRKLVLEELQLEEMPFFIPYDTKVNDINEIITPELDEILGEAIPAEFREKLDTRSFFDESDPNKAHLPEFNGCHVFGSIPVNRVSGELQITAKSLGYVASRKAPLEELKFNHVINEFSFGDFYPYIDNPLDNTAQFNQDEPLTTYVYYTSVVPTLFKKLGAEVDTNQYSVNDYRYLYKDVAAKGDKMPGIFFKYNFEPLSIVVSDVRLSFIQFLVRLVAICSFLVYCASWIFTLLDMALITIMGPKWSLRYQPDDKTKGILDR
Protein: HTH tetR-type domain-containing protein (P71830)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Interaction partners:
- Conserved alanine rich protein
- Uncharacterized protein
- Probable transcriptional regulatory protein
Sequence:
MGVTAAVTPKGERRRYALVSAAAELLGEGGFEAVRHRAVARRAGLPLASTTYYFSSLDDLIARAVEHIGMIEVAQLRARVSALSRRRRGPETTAVVLVDLLVGEMSSPGLAEQLISRYERHIACTRLPDLRESMRRSLRQRAEAVAEAIERSGRSAQIELVCTLICAVDGSVVSALVEGRDPRAAALATVVDLIDVLAPVDQRPVPF
Protein: Monacolin J acid methylbutanoyltransferase (EC 2.3.1.238) (Lovastatin biosynthesis cluster protein D) (Lovastatin hydrolase) (Simvastatin synthase LovD) (SV synthase) (Q9Y7D1)
Organism: Aspergillus terreus
Function: Monacolin J acid methylbutanoyltransferase; part of the gene cluster that mediates the biosynthesis of lovastatin (also known as mevinolin, mevacor or monacolin K), a hypolipidemic inhibitor of (3S)-hydroxymethylglutaryl-coenzyme A (HMG-CoA) reductase (HMGR). The first step in the biosynthesis of lovastatin is the production of dihydromonacolin L acid by the lovastatin nonaketide synthase lovB and the trans-acting enoyl reductase lovC via condensation of one acetyl-CoA unit and 8 malonyl-CoA units. Dihydromonacolin L acid is released from lovB by the thioesterase lovG. Next, dihydromonacolin L acid is oxidized by the dihydromonacolin L monooxygenase lovA twice to form monacolin J acid. The 2-methylbutyrate moiety of lovastatin is synthesized by the lovastatin diketide synthase lovF via condensation of one acetyl-CoA unit and one malonyl-CoA unit. Finally, the covalent attachment of this moiety to monacolin J acid is catalyzed by the transesterase lovD to yield lovastatin. LovD has broad substrate specificity and can also convert monacolin J to simvastatin using alpha-dimethylbutanoyl-S-methyl-3-mercaptopropionate (DMB-S-MMP) as the thioester acyl donor, and can also catalyze the reverse reaction and function as hydrolase in vitro. LovD has much higher activity with LovF-bound 2-methylbutanoate than with free diketide substrates.
Interaction partners:
Sequence:
MGSIIDAAAAADPVVLMETAFRKAVKSRQIPGAVIMARDCSGNLNYTRCFGARTVRRDECNQLPPLQVDTPCRLASATKLLTTIMALQCMERGLVDLDETVDRLLPDLSAMPVLEGFDDAGNARLRERRGKITLRHLLTHTSGLSYVFLHPLLREYMAQGHLQSAEKFGIQSRLAPPAVNDPGAEWIYGANLDWAGKLVERATGLDLEQYLQENICAPLGITDMTFKLQQRPDMLARRADQTHRNSADGRLRYDDSVYFRADGEECFGGQGVFSGPGSYMKVLHSLLKRDGLLLQPQTVDLMFQPALEPRLEEQMNQHMDASPHINYGGPMPMVLRRSFGLGGIIALEDLDGENWRRKGSLTFGGGPNIVWQIDPKAGLCTLAFFQLEPWNDPVCRDLTRTFEHAIYAQYQQG
Protein: Aspartyl aminopeptidase 4 (EC 3.4.11.21) (P38821)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Aspartyl aminopeptidase that contributes to peptide degradation both in the cytosol and the vacuole. Cells may respond to environmental conditions by changing the distributions of the cytosolic enzyme to the vacuole when cells need more active vacuolar degradation.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:21343297}. Vacuole lumen {ECO:0000269|PubMed:17651441, ECO:0000269|PubMed:21343297}. Note=In growing conditions, a small portion localizes in the vacuole, but actively transported to the vacuole under nutrient starvation conditions. {ECO:0000269|PubMed:21343297}.
Interaction partners:
- Autophagy-related protein 19
- Alpha-mannosidase
- Intermediate cleaving peptidase 55
- Autophagy-related protein 34
- Autophagy-related protein 8
- Autophagy-related protein 11
Sequence:
MFRIQLRTMSSKTCKSDYPKEFVSFLNSSHSPYHTVHNIKKHLVSNGFKELSERDSWAGHVAQKGKYFVTRNGSSIIAFAVGGKWEPGNPIAITGAHTDSPALRIKPISKRVSEKYLQVGVETYGGAIWHSWFDKDLGVAGRVFVKDAKTGKSIARLVDLNRPLLKIPTLAIHLDRDVNQKFEFNRETQLLPIGGLQEDKTEAKTEKEINNGEFTSIKTIVQRHHAELLGLIAKELAIDTIEDIEDFELILYDHNASTLGGFNDEFVFSGRLDNLTSCFTSMHGLTLAADTEIDRESGIRLMACFDHEEIGSSSAQGADSNFLPNILERLSILKGDGSDQTKPLFHSAILETSAKSFFLSSDVAHAVHPNYANKYESQHKPLLGGGPVIKINANQRYMTNSPGLVLVKRLAEAAKVPLQLFVVANDSPCGSTIGPILASKTGIRTLDLGNPVLSMHSIRETGGSADLEFQIKLFKEFFERYTSIESEIVV
Protein: Large ribosomal subunit protein uL23 (50S ribosomal protein L23) (P0ADZ0)
Organism: Escherichia coli (strain K12)
Function: One of the early assembly proteins, it binds 23S rRNA; is essential for growth. One of the proteins that surround the polypeptide exit tunnel on the outside of the subunit. Acts as the docking site for trigger factor for Ffh binding to the ribosome (SRP54) and to nascent polypeptide chains.
Interaction partners:
- Large ribosomal subunit protein uL18
- Elongation factor Tu 1
- Small ribosomal subunit protein uS13
- Large ribosomal subunit protein uL4
- Large ribosomal subunit protein bL21
- Large ribosomal subunit protein uL6
- GTP pyrophosphokinase
- Large ribosomal subunit protein uL30
- Large ribosomal subunit protein bL33
- Large ribosomal subunit protein uL14
Sequence:
MIREERLLKVLRAPHVSEKASTAMEKSNTIVLKVAKDATKAEIKAAVQKLFEVEVEVVNTLVVKGKVKRHGQRIGRRSDWKKAYVTLKEGQNLDFVGGAE
Protein: Solute carrier family 16 member 6a (H6WYF6)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
Sequence:
MAQWIFRLRSCFGSKVYSEVPDGGWGWIVAVALFLVEVFTYGVIKSFGIFLKDLMSDFNETNSRVSWIISICVFVMTFTAPLSTMLSNRFGFQPVVMFGGFLISLGTISTAFTSSINQMYLTIGIATGLGYCLTFLPTATILSQYFSRRRSVVMAMASTGESFATFAFAPAFTALKNYIGRRYTLVVIGTLQGITIICGALLRPIVIKPTSLTETEQKITYTLPVEQVQGFGSSGDSVVQSLEQEQGLKSGIELEEVEPVQINLKQQDNTSKNRLLDLTVLKEGSFLCYSAFGLFATLGFFAPQLYVVELSASLGTERDKAAYMLSIMAISEIIGRLSIGWVMNCGCIRKIFVLLICVSLMCLVLVLFTIVNGFWGLVVCCVLYGFLLGNITSTHIPMLAEDDVVGIQRMPLAVGVYVCIQSFAGLAGPPLGGVLVDITQNYSAAFYSCAAGMGLGAIFLGLVRPAKTGHLCRRRNNGENNSAVEQVSKASQRNC
Protein: Ribosome biogenesis protein nsa1 (O94698)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Involved in the biogenesis of the 60S ribosomal subunit.
Subcellular location: Nucleus, nucleolus {ECO:0000250}.
Interaction partners:
- Ribosome biogenesis protein erb1
- Brix domain-containing protein C4F8.04
- Ribosome biogenesis protein ytm1
- Ribosome biogenesis protein nsa2
- Pescadillo homolog
- Protein mak16
- Probable rRNA-processing protein ebp2
- Probable nucleolar GTP-binding protein 1
- Ribosomal RNA-processing protein 1 homolog
- Ribosome biogenesis protein rlp24
Sequence:
MKLLLGDEIGQLKFIEIKKGTDTSNPESEAPVIQKFGELDREKGVLFMLKHEMNVFVARKNGTIECWNVNQEPPILSSLWQLDSSLLETASIVSMKYSNGWLMLALSDGNLLFRHIESSKLRKLQLHGPLSAVELHPRIPGIIAAGGKENDVCLYSCNPTCKSNIDELELWRTENVVKVFQGKNVKNDSLNLRVRVWITGIVFTEDIINVIDGKSEDDESLCFHFATITHYGQLRFYDTKHGRRPVSTFDVSTSPLSHVGLLPSIKLLYFADKRAQISIFDHSKKKVIGRFQGVKGAPSSIHCLGNVVAITGLDRNVRIFDADRKPLANAYIKALPTSIIVINERDAEIIKKEEELEAAKEEEEEIWRNMEQLEDTEDKKPSKRIKL
Protein: Siderophore iron transporter mirA (Enterobactin permease) (Major facilitator iron-regulated transporter A) (Q8X1Z7)
Organism: Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Function: Involved in the transport of siderophore enterobactin and so has a role in iron homeostasis.
Subcellular location: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
Sequence:
MALDDISAVPKGALDTDPAVERPPPLLDADRSDSERLQPGVKRAEMLRKGWTRQGLIIAFTGLFLATLSINFGDYSTQVYVPYATSAFKQHSAMSAARVVGNITRIAAYPIIAKLGDVFGRAEMFILSIVFQAVGYAIYAGCKNVGQYIAGGIFEAIGSTGFGLTQQVFVADVTNLINRAVWSTLPDSLTVIPALYLGTEIAEAVLEKNEWRWGFGMWAIIEPVCSVLLVGTMLYYQKRARKDPSPAEFASEPTERNVDDGWWKRIYNLVWVQLDAFGAILLLLGLSLFLVPLSLTGSGNSDDWHRGSFIAMLVLGVVIFVAFLAWDTWCAKKPFIPYRMIKNRTVAAACLLGILDFFHYSVFSVFFTSYLQVAAHHGAGPATRIDNSLRVAFQVAGIFAAYFMKFTKRSQVWVFTGVPLCVLGMGVLLYLVDMGEGRVGNEAAFVTAKSLIGIGRGFYQTASQVSVQAKVSRGEVSVVTAVFFAAMSIGGAIGTSVAGAIWRSTLPPKLAQHLPAELKDQAQAIFGSIVVAQKYEVGTPARDAIDMCYRQSQRMLAIAALAALAPMLIIMFFLENVPLTDETTLIELHGNREAVKKNHSGGEGKEARS
Protein: Interleukin-6 (IL-6) (P26893)
Organism: Sus scrofa (Pig)
Function: Cytokine with a wide variety of biological functions in immunity, tissue regeneration, and metabolism. Binds to IL6R, then the complex associates to the signaling subunit IL6ST/gp130 to trigger the intracellular IL6-signaling pathway. The interaction with the membrane-bound IL6R and IL6ST stimulates 'classic signaling', whereas the binding of IL6 and soluble IL6R to IL6ST stimulates 'trans-signaling'. Alternatively, 'cluster signaling' occurs when membrane-bound IL6:IL6R complexes on transmitter cells activate IL6ST receptors on neighboring receiver cells.
Subcellular location: Secreted {ECO:0000250|UniProtKB:P05231}.
Interaction partners:
- Interleukin-6 receptor subunit alpha
- Interleukin-10
- Toll-like receptor 4
- Signal transducer and activator of transcription 3
- Interleukin 6 signal transducer.
- Tyrosine-protein kinase JAK2
- Tyrosine-protein kinase
- Interleukin-5
- C-C motif chemokine 2
- Interleukin-1 beta
Sequence:
MNSLSTSAFSPVAFSLGLLLVMATAFPTPERLEEDAKGDATSDKMLFTSPDKTEELIKYILGKISAMRKEMCEKYEKCENSKEVLAENNLNLPKMAEKDGCFQSGFNQETCLMRITTGLVEFQIYLDYLQKEYESNKGNVEAVQISTKALIQTLRQKGKNPDKATTPNPTTNAGLLDKLQSQNEWMKNTKIILILRSLEDFLQFSLRAIRIM
Protein: LD27370p (Q9VUK9)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Nucleus {ECO:0000256|PROSITE-ProRule:PRU00371}.
Interaction partners:
- MOB kinase activator-like 4
- Homeobox protein goosecoid
- CTP synthase
Sequence:
MAPKKSTIVLNVEQFIHDIEERPAIWNRNFHCNKAFLEQMWDELSGAHKLPKIVLKAKWKGLRDNFRVEYKRIPRADNGDFMVDPATFESKWLHYYALLFLTDHMRHRLPKNEQDQSFYFSQQSEDCEKTVVEPDLTNGLIRRLQDSDEDYDEEEMEADGEASEATMEETMPTPPAAHQMNQVSTTPLATGALRAQEEAHQHALIKAGLLRAQLMELEKEAEDLSRKPPPPQQMTSPVAPSLQVLVEPPAAHCSPPPMVTTTSAQVQQPGSAAVLAPATTTSASSVSSNGAPMGGKRSVSPPPLYNKAHHPLATLAAAHLAAKDRNEDFGPTSAVGGNGDHLSFTQHSYANGLIPALKLKRPRLSEDSNFNGSSTMDTPLVPEDDDYHYLLSLHPYMKQLTAAQKLRIRTKIQKLIFKELYKEDLEESK
Protein: C-C chemokine receptor type 8 (C-C CKR-8) (CC-CKR-8) (CCR-8) (CC chemokine receptor CHEMR1) (CMKBRL2) (Chemokine receptor-like 1) (CKR-L1) (GPR-CY6) (GPRCY6) (TER1) (CD antigen CDw198) (P51685)
Organism: Homo sapiens (Human)
Function: Receptor for the chemokine CCL1/SCYA1/I-309. May regulate monocyte chemotaxis and thymic cell line apoptosis. Alternative coreceptor with CD4 for HIV-1 infection.
Subcellular location: Cell membrane; Multi-pass membrane protein.
Interaction partners:
- C-C motif chemokine 1
- C-C motif chemokine 17
- C-C motif chemokine 18
- C-C motif chemokine 22
- C-C motif chemokine 4
- C-C motif chemokine 8
- C-C motif chemokine 16
- C-C motif chemokine 20
- C-C motif chemokine 5
- C-C motif chemokine 2
Sequence:
MDYTLDLSVTTVTDYYYPDIFSSPCDAELIQTNGKLLLAVFYCLLFVFSLLGNSLVILVLVVCKKLRSITDVYLLNLALSDLLFVFSFPFQTYYLLDQWVFGTVMCKVVSGFYYIGFYSSMFFITLMSVDRYLAVVHAVYALKVRTIRMGTTLCLAVWLTAIMATIPLLVFYQVASEDGVLQCYSFYNQQTLKWKIFTNFKMNILGLLIPFTIFMFCYIKILHQLKRCQNHNKTKAIRLVLIVVIASLLFWVPFNVVLFLTSLHSMHILDGCSISQQLTYATHVTEIISFTHCCVNPVIYAFVGEKFKKHLSEIFQKSCSQIFNYLGRQMPRESCEKSSSCQQHSSRSSSVDYIL
Protein: Small ribosomal subunit protein eS10 (EC 3.6.1.52) (40S ribosomal protein S10) (A0A1W2PQS6)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}. Nucleus, nucleolus {ECO:0000256|ARBA:ARBA00004604}.
Interaction partners:
- Small ribosomal subunit protein uS3
- Small ribosomal subunit protein eS24
- Small ribosomal subunit protein uS14
- Small ribosomal subunit protein uS12
- Small ribosomal subunit protein eS1
- Small ribosomal subunit protein eS8
- Large ribosomal subunit protein eL31
- Small ribosomal subunit protein uS17
- Large ribosomal subunit protein eL34
- Large ribosomal subunit protein eL15
Sequence:
MLMPKKNRIAIYELLFKEGVMVAKKDVHMPKHPELADKNVPNLHVMKAMQSLKSRGYVKEQFAWRHFYWYLTNEGIQYLRDYLHLPPEIVPATLRRSRPETGRPRPKGLEGERPARLTRGEADRDTYRRSAVPPGADKKAEAGAGSATEFQFVLLVSSSRHPDRWIVPGGGMEPEEEPSVAAVREVCEEAGVKGTLGRLVGIFENQERKHRTYVYVLIVTEVLEDWEDSVNIGRKREWFKIEDAIKVLQYHKPVQASYFETLRQGYSANNGTPVVATTYSVSAQSSMSGIR
Protein: Lipoprotein LpqH (19 kDa lipoprotein) (Putative transporter LpqH) (A5U990)
Organism: Mycobacterium tuberculosis (strain ATCC 25177 / H37Ra)
Function: Might be involved in ligand transport (By similarity). A host TLR2 agonist (toll-like receptor), shown experimentally for human and mouse. Acts in host macrophages to modify the expression of different subsets of interferon-gamma-induced (IFN-g) genes, possibly by chromatin remodeling. Represses IFN-g induction of mouse macrophage MHC class II transactivator (Ciita), greatly enhances IFN-g induction of mouse macrophage inducible nitric oxide synthase (iNOS, Nos2). At least for Ciita repression, acts via mouse TLR2 and MAPK to inhibit IFN-g-induced enrichment of acetylated histones H3 and H4 at the host Ciita but not at Nos2 loci. Host Ciita regulates the expression of MHC-II and other genes involved in Ag processing and presentation, thus its repression contributes to immune envasion by M.tuberculosis. Requires both host TLR1 and TLR2 as coreceptors to elicit host response in mouse, although TLR6 may play a redundant role, and a partial requirement for CD14 as an accessory receptor.
Subcellular location: Cell membrane {ECO:0000255|PROSITE-ProRule:PRU00303}; Lipid-anchor {ECO:0000255|PROSITE-ProRule:PRU00303}. Extracellular vesicle, bacterial extracellular vesicle {ECO:0000269|PubMed:26109643}. Note=Found in bacterial extracytoplasmic vesicles both in culture supernatant and isolated from infected mouse macrophages: there is almost no co-localization of mouse and M.tuberculosis markers in the vesicles, suggesting they do not mix (PubMed:26109643). {ECO:0000269|PubMed:26109643}.
Interaction partners:
Sequence:
MKRGLTVAVAGAAILVAGLSGCSSNKSTTGSGETTTAAGTTASPGAASGPKVVIDGKDQNVTGSVVCTTAAGNVNIAIGGAATGIAAVLTDGNPPEVKSVGLGNVNGVTLGYTSGTGQGNASATKDGSHYKITGTATGVDMANPMSPVNKSFEIEVTCS
Protein: Anillin-like protein 2 (Q09994)
Organism: Caenorhabditis elegans
Function: Required to maintain the structure of the rachis, the central cytoplasmic core of the syncytial adult gonad. Failure to maintain the rachis leads to premature dissociation of oocytes and thereby impedes oogenesis.
Interaction partners:
- Kinesin-like protein
- Rac GTPase-activating protein 1
- Ras-like GTP-binding protein rhoA
- F-box domain-containing protein
- Myosin-11
- WAPL domain-containing protein
- Kinesin-like protein
- Actin
- Protein ECT2
- Cytokinesis defective protein 7
Sequence:
MYRRENINFSHPPQLKSPPPMSSPLDSNRSYRWTSLTAANNSKFADTPVKETPQKPDMSWWSPSRGDTWRLNAPRGRTLDLVAAFDQCSRQDQLDSPRYANLGRYRRNSEPMQDNEKEVVTTNFIDDSMIEDHEEYEEHDIELGTDFYDPHMIRHHRSSERFEQSLGTGQQIETIHISTRLVPQLKRVPNSDYANDGRGDMKEYGSISKKNETPILDGTPKRPSPLTTRNIHKVDINRMDHLMKTENTVAGFITLTPQVSKVTHKSDFSKHFGQEESVRASPMSRRNRRGTQTIVLPSFDSPASVRKSIPSPGLPTKTDIRSPSSLVKSIANDFEKADFGFHRKIDAAEEIAQLRKRADNSTFDENQNMVSDSAEDNVSNDFVPRISHLEMHPSVHMGISGYAKKNHVPYGESNEEVLYSLPIKKQSRNVDREGMDQTDEILLTPRAITMRQSLPFSDIPEERTCDKIDEMFDFVEVPTGDYDDKTTLERTVDGYAEVKSQKSPNKMIRNRLDLSTNTYQEIEFEKDTTPYMQEFEEDGTGYSASSSGPQFTRSPTLVTPHAGQSVAEYRVSDKEGCAKTEKVVVQKMSQPSALATSTPKGTFAWRNKNQSNAADDSFVSSISNFSAADKINDSKRQISKLIETIEKTRKHIQLAEISLIDAKRAQMVVQELASQRVLLICRERLKLQLDEVRRLQALSVVRHPPPPINRHFKSAMVISNIAIHLNKNFNCRGSFAFIVALKCRTEIEATGVVTLLAHYQTRMHVIHFGEHMHFSNLPVDFVIAMEVYMMRVPEYKAPEKTCAAVLAAKFRNLLVPNSAHRRARNNSVLSNRTVLSMPGYQAPDCDFRFCGKLTLDRDSAGDRQFYLDDVTYPLEGTVKLQSHCSSLPEAIDVEYRGFLYLFDERSPNGEAAWDRYWAMLHRGIIFFWKNPIDEKNQKVPLSQIDLTKCTNQSVEETRNGRDHEFHIELLIDQTPSLLEKRRVVLAAESSDHLASWLNAINDTLFVLRS
Protein: Cilia- and flagella-associated protein 69 (A5D8W1)
Organism: Homo sapiens (Human)
Function: Cilium- and flagellum-associated protein. In the olfactory epithelium, regulates the speed of activation and termination of the odor response and thus contributes to the robustness of olfactory transduction pathways (By similarity). Required for sperm flagellum assembly and stability.
Subcellular location: Cell projection, cilium {ECO:0000250|UniProtKB:Q8BH53}. Cell projection, cilium, flagellum {ECO:0000269|PubMed:29606301}. Note=Localizes to the midpiece of the sperm flagellum. {ECO:0000269|PubMed:29606301}.
Interaction partners:
- Cilia- and flagella-associated protein 43
- Cilia- and flagella-associated protein 44
- Cilia- and flagella-associated protein 251
- Glutamine-rich protein 2
- Dynein axonemal heavy chain 1
Sequence:
MWTEEAGATAEAQESGIRNKSSSSSQIPVVGVVTEDDEAQDVFKPMDLNRVIKLLEETDKDGLEEKQLKFVKKLVQCYQNGLPLRDLAQIFKILNLCSGKIKNQPRFIESAYDIIKLCGLPFLKKKVSDEITYAEDTANSIALLGDLMKIPSSELRIQICKCIVDFYHAEPPKKHIPGYQQASSSYKIQMAEVGGLAKTMVQSMTLLENQLVEKLWVLKVLQHLSTSEVNCTIMMKAQAASGICTHLNDPDPSGQLLFRSSEILWNLLEKSSKEEVIQQLSNLECLLALKEVFKNLFMRGFSHYDRQLRNDILVITTIIAQNPEAPMIECGFTKDLILFATFNEVKSQNLLVKGLKLSNSYEDFELKKLLFNVIVILCKDLPTVQLLIDGKVILALFTYVKKPEKQKIIDWSAAQHEELQLHAIATLSSVAPLLIEEYMSCQGNARVLAFLEWCESEDPFFSHGNSFHGTGGRGNKFAQMRYSLRLLRAVVYLEDETVNKDLCEKGTIQQMIGIFKNIISKPNEKEEAIVLEIQSDILLILSGLCENHIQRKEIFGTEGVDIVLHVMKTDPRKLQSGLGYNVLLFSTLDSIWCCILGCYPSEDYFLEKEGIFLLLDLLALNQKKFCNLILGIMVEFCDNPKTAAHVNAWQGKKDQTAASLLIKLWRKEEKELGVKRDKNGKIIDTKKPLFTSFQEEQKIIPLPANCPSIAVMDVSENIRAKIYAILGKLDFENLPGLSAEDFVTLCIIHRYLDFKIGEIWNEIYEEIKLEKLRPVTTDKKALEAITTASENIGKMVASLQSDIIESQACQDMQNEQKVYAKIQATHKQRELANKSWEDFLARTSNAKTLKKAKSLQEKAIEASRYHKRPQNAIFHQTHIKGLNTTVPSGGVVTVESTPARLVGGPLVDTDIALKKLPIRGGALQRVKAVKIVDAPKKSIPT
Protein: Spore morphogenesis and germination protein YwcE (P39603)
Organism: Bacillus subtilis (strain 168)
Function: Required for proper spore morphogenesis. Important for spore germination.
Subcellular location: Cell membrane {ECO:0000269|PubMed:16159778}. Spore membrane {ECO:0000269|PubMed:16159778}; Multi-pass membrane protein {ECO:0000269|PubMed:16159778}. Spore outer membrane {ECO:0000269|PubMed:16159778}; Multi-pass membrane protein {ECO:0000269|PubMed:16159778}. Note=Inner and outer prespore membrane. Mother cell membrane.
Interaction partners:
- Phage-like element PBSX protein XkdA
Sequence:
MMDMFFAYLLVASATPLFIWLDNKKVALSAIPPIILMWVFFFFYATESLSPLGHTLMIILFAVNVIVAHIAAFIIYGLPYLRRKRSS
Protein: Mitochondrial ubiquitin ligase activator of NFKB 1 (EC 2.3.2.27) (E3 ubiquitin-protein ligase MUL1) (Growth inhibition and death E3 ligase) (Protein Hades) (RING-type E3 ubiquitin transferase NFKB 1) (Q8VCM5)
Organism: Mus musculus (Mouse)
Function: Exhibits weak E3 ubiquitin-protein ligase activity (By similarity). E3 ubiquitin ligases accept ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and then directly transfer the ubiquitin to targeted substrates (By similarity). Can ubiquitinate AKT1 preferentially at 'Lys-284' involving 'Lys-48'-linked polyubiquitination and seems to be involved in regulation of Akt signaling by targeting phosphorylated Akt to proteosomal degradation (By similarity). Mediates polyubiquitination of cytoplasmic TP53 at 'Lys-27' which targets TP53 for proteasomal degradation, thus reducing TP53 levels in the cytoplasm and mitochondrion (By similarity). Proposed to preferentially act as a SUMO E3 ligase at physiological concentrations (By similarity). Plays a role in the control of mitochondrial morphology by promoting mitochondrial fragmentation, and influences mitochondrial localization (By similarity). Likely to promote mitochondrial fission through negatively regulating the mitochondrial fusion proteins MFN1 and MFN2, acting in a pathway that is parallel to the PRKN/PINK1 regulatory pathway. May also be involved in the sumoylation of the membrane fission protein DNM1L (By similarity). Inhibits cell growth (By similarity). When overexpressed, activates JNK through MAP3K7/TAK1 and induces caspase-dependent apoptosis (By similarity). Involved in the modulation of innate immune defense against viruses by inhibiting RIGI-dependent antiviral response (By similarity). Can mediate RIGI sumoylation and disrupt its polyubiquitination (By similarity).
Subcellular location: Mitochondrion outer membrane {ECO:0000250|UniProtKB:Q969V5}; Multi-pass membrane protein {ECO:0000255}. Peroxisome {ECO:0000250|UniProtKB:Q969V5}. Note=Transported in mitochondrion-derived vesicles from the mitochondrion to the peroxisome. {ECO:0000250|UniProtKB:Q969V5}.
Interaction partners:
- Ubiquitin carboxyl-terminal hydrolase 30
- Serine/threonine-protein kinase PINK1, mitochondrial
Sequence:
MESGSRPSLGQVILLGTSSMVTAVLYSIYRQKAQVAQELKGAKKIHLGEDLKGILSEAPGKCVPYAVIEGAVRSVKETLNSQFVENCKGVIQRLSLQEHKMVWNRTTHLWNDYSKIIHQRTNTVPFDLVPHEDGVAVSVRVLKPLDSVDLGLETVYEKFHPSVQSFTDAIGHYISGERPKGIQETEEMLKVGATLTGIGELVLDNNAVRLQPPKQGMQYYLSSQDFDSLLHRQESSVRLWKILVLVFGFATCATLFFILRKQYLHRQERLRQQQLQEEFLEHEAQLLSQASPEDRESLKSACVVCLSNFKSCVFLECGHVCSCRQCYLALPEPKRCPICRREITRVIPLYNS