wanglab/gogpt-training-data huggingface dataset:
Protein: 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase eta-2 (EC 3.1.4.11) (Phosphoinositide phospholipase C-eta-2) (Phosphoinositide phospholipase C-like 4) (PLC-L4) (Phospholipase C-like protein 4) (Phospholipase C-eta-2) (PLC-eta2) (O75038)
Organism: Homo sapiens (Human)
Function: The production of the second messenger molecules diacylglycerol (DAG) and inositol 1,4,5-trisphosphate (IP3) is mediated by activated phosphatidylinositol-specific phospholipase C enzymes. This phospholipase activity is very sensitive to calcium. May be important for formation and maintenance of the neuronal network in the postnatal brain (By similarity).
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:A2AP18}. Cell membrane {ECO:0000250|UniProtKB:A2AP18}. Note=Localized predominantly at the plasma membrane. {ECO:0000250|UniProtKB:A2AP18}.
Interaction partners:
- Inositol polyphosphate multikinase
- Phosphatidylinositol 3,4,5-trisphosphate 3-phosphatase and dual-specificity protein phosphatase PTEN
- Multiple inositol polyphosphate phosphatase 1
- Phosphatidylinositol 4-phosphate 5-kinase type-1 beta
- Inositol polyphosphate-5-phosphatase A
- Phosphatidylinositol 4-phosphate 5-kinase type-1 gamma
- Phosphatidylinositol 5-phosphate 4-kinase type-2 beta
- Phosphatidylinositol 5-phosphate 4-kinase type-2 gamma
- Phosphatidylinositol 4-phosphate 5-kinase type-1 alpha
- Phosphatidylinositol 5-phosphate 4-kinase type-2 alpha
Sequence:
MSGPWPSPDSRTKGTVAWLAEVLLWVGGSVVLSSEWQLGPLVERCMGAMQEGMQMVKLRGGSKGLVRFYYLDEHRSCIRWRPSRKNEKAKISIDSIQEVSEGRQSEVFQRYPDGSFDPNCCFSIYHGSHRESLDLVSTSSEVARTWVTGLRYLMAGISDEDSLARRQRTRDQWLKQTFDEADKNGDGSLSIGEVLQLLHKLNVNLPRQRVKQMFREADTDDHQGTLGFEEFCAFYKMMSTRRDLYLLMLTYSNHKDHLDAASLQRFLQVEQKMAGVTLESCQDIIEQFEPCPENKSKGLLGIDGFTNYTRSPAGDIFNPEHHHVHQDMTQPLSHYFITSSHNTYLVGDQLMSQSRVDMYAWVLQAGCRCVEVDCWDGPDGEPIVHHGYTLTSKILFKDVIETINKYAFIKNEYPVILSIENHCSVIQQKKMAQYLTDILGDKLDLSSVSSEDATTLPSPQMLKGKILVKGKKLPANISEDAEEGEVSDEDSADEIDDDCKLLNGDASTNRKRVENTAKRKLDSLIKESKIRDCEDPNNFSVSTLSPSGKLGRKSKAEEDVESGEDAGASRRNGRLVVGSFSRRKKKGSKLKKAASVEEGDEGQDSPGGQSRGATRQKKTMKLSRALSDLVKYTKSVATHDIEMEAASSWQVSSFSETKAHQILQQKPAQYLRFNQQQLSRIYPSSYRVDSSNYNPQPFWNAGCQMVALNYQSEGRMLQLNRAKFSANGGCGYVLKPGCMCQGVFNPNSEDPLPGQLKKQLVLRIISGQQLPKPRDSMLGDRGEIIDPFVEVEIIGLPVDCSREQTRVVDDNGFNPTWEETLVFMVHMPEIALVRFLVWDHDPIGRDFIGQRTLAFSSMMPGYRHVYLEGMEEASIFVHVAVSDISGKVKQALGLKGLFLRGPKPGSLDSHAAGRPPARPSVSQRILRRTASAPTKSQKPGRRGFPELVLGTRDTGSKGVADDVVPPGPGPAPEAPAQEGPGSGSPRDTRPLSTQRPLPPLCSLETIAEEPAPGPGPPPPAAVPTSSSQGRPPYPTGPGANVASPLEDTEEPRDSRPRPCNGEGAGGAYERAPGSQTDGRSQPRTLGHLPVIRRVKSEGQVPTEPLGGWRPLAAPFPAPAVYSDATGSDPLWQRLEPCGHRDSVSSSSSMSSSDTVIDLSLPSLGLGRSRENLAGAHMGRLPPRPHSASAARPDLPPVTKSKSNPNLRATGQRPPIPDELQPRSLAPRMAGLPFRPPWGCLSLVGVQDCPVAAKSKSLGDLTADDFAPSFEGGSRRLSHSLGLPGGTRRVSGPGVRRDTLTEQLRWLTVFQQAGDITSPTSLGPAGEGVAGGPGFVRRSSSRSHSRVRAIASRARQAQERQQRLQGLGRQGPPEEERGTPEGACSVGHEGSVDAPAPSKGALGPASAAAENLVLLRL
Protein: Mitochondrial ornithine transporter 2 (Solute carrier family 25 member 2) (Q9BXI2)
Organism: Homo sapiens (Human)
Function: Mitochondrial transporter of the positively charged amino acids ornithine, lysine and arginine, and the neutral amino acid citrulline. In addition, transports the basic amino acids histidine, homoarginine, and asymmetric dimethylarginine (aDMA), but not symmetric DMA, and the D-forms of lysine, arginine, ornithine and histidine. Functions by both counter-exchange and uniport mechanisms.
Subcellular location: Mitochondrion membrane {ECO:0000269|PubMed:12948741}; Multi-pass membrane protein {ECO:0000255}. Mitochondrion inner membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
Sequence:
MKSGPGIQAAIDLTAGAAGGTACVLTGQPFDTIKVKMQTFPDLYKGLTDCFLKTYAQVGLRGFYKGTGPALMAYVAENSVLFMCYGFCQQFVRKVAGMDKQAKLSDLQTAAAGSFASAFAALALCPTELVKCRLQTMYEMEMSGKIAKSHNTIWSVVKGILKKDGPLGFYHGLSSTLLQEVPGYFFFFGGYELSRSFFASGRSKDELGPVHLMLSGGVAGICLWLVVFPVDCIKSRIQVLSMYGKQAGFIGTLLSVVRNEGIVALYSGLKATMIRAIPANGALFVAYEYSRKMMMKQLEAY
Protein: PTTG1 interacting protein (A8MXQ1)
Organism: Homo sapiens (Human)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004479}.
Interaction partners:
Sequence:
MGQAVSCVLGRLQPVKCTGARRVGRRGLRKQTSQECLWCNTNKACLDYPVTSVLPPASLCKLSSARWGVCWVNFEALIITMSVVGGTLLLGIAICCCCCCRRKRSRKPDRSEEKAMREREERRIRQEERRAEMKTRHDEIRKKYGLFKEENPYARFENN
Protein: Late cornified envelope protein 4A (Late envelope protein 8) (Small proline-rich-like epidermal differentiation complex protein 4A) (Q5TA78)
Organism: Homo sapiens (Human)
Function: Precursors of the cornified envelope of the stratum corneum.
Interaction partners:
- Late cornified envelope protein 5A
- Late cornified envelope protein 1A
- Late cornified envelope protein 2B
- Late cornified envelope protein 2C
- Late cornified envelope protein 2D
- Late cornified envelope protein 6A
- Protein KPLCE
- Late cornified envelope protein 2A
- Late cornified envelope protein 1C
- Late cornified envelope protein 1B
Sequence:
MSCQQNQQQCQPPPKCPIPKYPPKCPSKCASSCPPPISSCCGSSSGGCGCCSSEGGGCCLSHHRHHRSHCHRPKSSNCYGSGSGQQSGGSGCCSGGGCC
Protein: Serine/threonine-protein phosphatase 2A activator (EC 5.2.1.8) (Phosphotyrosyl phosphatase activator) (H0Y6E5)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496, ECO:0000256|RuleBase:RU361210}.
Interaction partners:
Sequence:
XKTYRMEPAGSQGVWGLDDFQFLPFIWGSSQLIDHPYLEPRHFVDEKAVNENHKDYMFLECILFITEMKTGPFAEHSNQLWNISAVPSWSKVNQGLIRMYKAEVSGGWPVCPSLLPHLVLGWGQSKRCGTWGSCFLLPHCFALNLRPAPLTLGASESPIWGMGSQRSTSHPSPEKLQSSSVLMSLEAEARTCCMGSGGDGGLPSPLSSGQRLLKARAV
Protein: Proteasome 26S ATPase subunit 1 variant (Q53HB3)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MGQSQSGGHGPGGGKKDDKDKKKKYEPPVPTRVGKKKKRTKGPDAASKLPLVTPHTQCRLKLLKLERIKDYLLMEEEFIRNQEQMKPLEEKQEEERSKVDDLRGTPMSVGTLEEIIDDNHAIVSTSVGSEHYVSILSFVDKDLLEPGCSVLLNHKVHAVIGVLMDDTDPLVTVMKVEKAPQETYADIGGLDNQIQEIKESVELPLTHPEYYEEMGIKPPKGVILYGPPGTGKTLLAKAVANQTSATFLRVVGSELIQKYLGDGPKLVRELFRVAEEHAPSIVFIDEIDAIGTKRYDSNSGGEREIQRTMLELLNQLDGFDSRGDVKVIMATNRIETLDPALIRPGRIDRKIEFPLPDEKTKKRIFQIHTSRMTLADDVTLDDLIMAKDDLSGADIKAICTEAGLMALRERRMKVTNEDFKKSKENVLYKKQEGTPEGLYL
Protein: Cingulin (B9EK46)
Organism: Homo sapiens (Human)
Subcellular location: Cell junction, tight junction {ECO:0000256|ARBA:ARBA00004435}.
Interaction partners:
Sequence:
MEQAPNMAEPRGPVDHGVQIRFITEPVSGAEMGTLRRGGRRPAKDARASTYGVAVRVQGIAGQPFVVLNSGEKGGDSFGVQIKGANDQGASGALSSDLELPENPYSQVKGFPAPSQSSTSDEEPGAYWNGKLLRSHSQASLAGPGPVDPSNRSNSMLELAPKVASPGSTIDTAPLSSVDSLINKFDSQLGGQARGRTCRRTRMLPPEQRKRSKSLDSRLPRDTFEERERQSTNHWTSSTKYDNHVGTSKQPAQSQNLSPLSGFSRSRQTQDWVLQSFEEPRRSAQDPTMLQFKSTPDLLRDQQEAAPPGSVDHMKATIYGILREGSSESETSVRRKVSLVLEKMQPLVMVSSGSTKAVAGQGELTRKVEELQRKLDEEVKKRQKLEPSQVGLERQLEEKTEECSRLQELLERRKGEAQQSNKELQNMKRLLDQGEDLRHGLETQVMELQNKLKHVQGPEPAKEVLLKDLLETRELLEEVLEGKQRVEEQLRLRERELTALKGALKEEVASRDQEVEHVRQQYQRDTEQLRRSMQDATQDHAVLEAERQKMSALVRGLQRELEETSEETGHWQSMFQKNKEDLRATKQELLQLRMEKEEMEEELGEKIEVLQRELEQARASAGDTRQVEVLKKELLRTQEELKELQAERQSQEVAGRHRDRELEKQLAVLRVEADRGRELEEQNLQLQKTLQQLRQDCEEASKAKMVAEAEATVLGQRRAAVETTLRETQEENDEFRRRILGLEQQLKETRGLVDGGEAVEARLRDKLQRLEAEKQQLEEALNASQEEEGSLAAAKRALEARLEEAQRGLARLGQEQQTLNRALEEEGKQREVLRRGKAELEEQKRLLDRTVDRLNKELEKIGEDSKQALQQLQAQLEDYKEKARREVADAQRQAKDWASEAEKTSGGLSRLQDEIQRLRQALQASQAERDTARLDKELLAQRLQGLEQEAENKKRSQDDRARQLKGLEEKVSRLETELDEEKNTVELLTDRVNRGRDQVDQLRTELMQERSARQDLECDKISLERQNKDLKTRLASSEGFQKPSASLSQLESQNQLLQERLQAEEREKTVLQSTNRKLERKVKELSIQIEDERQHVNDQKDQLSLRVKALKRQVDEAEEEIERLDGLRKKAQREVEEQHEVNEQLQARIKSLEKDSWRKASRSAAESALKNEGLSSDEEFDSVYDPSSIASLLTESNLQTSSC
Protein: Immunoglobulin-binding protein 1 (B-cell signal transduction molecule alpha 4) (Protein alpha-4) (CD79a-binding protein 1) (Protein phosphatase 2/4/6 regulatory subunit) (Renal carcinoma antigen NY-REN-16) (P78318)
Organism: Homo sapiens (Human)
Function: Associated to surface IgM-receptor; may be involved in signal transduction. Involved in regulation of the catalytic activity of the phosphatases PP2A, PP4 and PP6 by protecting their partially folded catalytic subunits from degradative polyubiquitination until they associate with regulatory subunits.
Subcellular location: Cytoplasm {ECO:0000305}.
Interaction partners:
- Serine/threonine-protein phosphatase 2A catalytic subunit alpha isoform
- Serine/threonine-protein phosphatase 2A catalytic subunit beta isoform
- Serine/threonine-protein phosphatase 6 catalytic subunit
- Serine/threonine-protein phosphatase 4 catalytic subunit
- E3 ubiquitin-protein ligase Midline-1
- Serine/threonine-protein kinase mTOR
- Regulatory-associated protein of mTOR
- Target of rapamycin complex subunit LST8
- Vascular cell adhesion protein 1
- Proline-rich AKT1 substrate 1
Sequence:
MAAEDELQLPRLPELFETGRQLLDEVEVATEPAGSRIVQEKVFKGLDLLEKAAEMLSQLDLFSRNEDLEEIASTDLKYLLVPAFQGALTMKQVNPSKRLDHLQRAREHFINYLTQCHCYHVAEFELPKTMNNSAENHTANSSMAYPSLVAMASQRQAKIQRYKQKKELEHRLSAMKSAVESGQADDERVREYYLLHLQRWIDISLEEIESIDQEIKILRERDSSREASTSNSSRQERPPVKPFILTRNMAQAKVFGAGYPSLPTMTVSDWYEQHRKYGALPDQGIAKAAPEEFRKAAQQQEEQEEKEEEDDEQTLHRAREWDDWKDTHPRGYGNRQNMG
Protein: NEDD4 family-interacting protein 2 (NEDD4 WW domain-binding protein 5A) (Putative MAPK-activating protein PM04/PM05/PM06/PM07) (Putative NF-kappa-B-activating protein 413) (Q9NV92)
Organism: Homo sapiens (Human)
Function: Activates HECT domain-containing E3 ubiquitin-protein ligases, including ITCH, NEDD4, NEDD4L, SMURF2, WWP1 and WWP2, and consequently modulates the stability of their targets. As a result, may control many cellular processes. Recruits ITCH, NEDD4 and SMURF2 to endosomal membranes. Negatively regulates KCNH2 potassium channel activity by decreasing its cell-surface expression and interfering with channel maturation through recruitment of NEDD4L to the Golgi apparatus and multivesicular body where it mediates KCNH2 degradation. May modulate EGFR signaling. Together with NDFIP1, limits the cytokine signaling and expansion of effector Th2 T-cells by promoting degradation of JAK1, probably by ITCH- and NEDD4L-mediated ubiquitination (By similarity).
Subcellular location: Endosome membrane {ECO:0000269|PubMed:18776082}; Multi-pass membrane protein {ECO:0000269|PubMed:18776082}. Golgi apparatus membrane {ECO:0000269|PubMed:12796489, ECO:0000269|PubMed:26363003}. Endosome, multivesicular body membrane {ECO:0000269|PubMed:26363003}.
Interaction partners:
- E3 ubiquitin-protein ligase NEDD4
- E3 ubiquitin-protein ligase NEDD4-like
- NEDD4-like E3 ubiquitin-protein ligase WWP2
- E3 ubiquitin-protein ligase Itchy homolog
- NEDD4-like E3 ubiquitin-protein ligase WWP1
Sequence:
MARRRSQRVCASGPSMLNSARGAPELLRGTATNAEVSAAAAGATGSEELPPGDRGCRNGGGRGPAATTSSTGVAVGAEHGEDSLSRKPDPEPGRMDHHQPGTGRYQVLLNEEDNSESSAIEQPPTSNPAPQIVQAASSAPALETDSSPPPYSSITVEVPTTSDTEVYGEFYPVPPPYSVATSLPTYDEAEKAKAAAMAAAAAETSQRIQEEECPPRDDFSDADQLRVGNDGIFMLAFFMAFIFNWLGFCLSFCITNTIAGRYGAICGFGLSLIKWILIVRFSDYFTGYFNGQYWLWWIFLVLGLLLFFRGFVNYLKVRNMSESMAAAHRTRYFFLL
Protein: Rho GTPase activating protein at 15B, isoform C (Q9VX92)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
- Rho GTPase activating protein at 16F, isoform E
- ARF GTPase-activating protein Git
Sequence:
MEQARPVPAPRRLYPELRPANYENIEIRRPNSPSNNINHNNIKKLNINAENLHGNCAEKKLPSSGQNKLILQENNSDSQQPIYGPDANENVQEPVYATPRPAPRQRLPPAGEPEDSYPDPDDEVPLRILRAAPQIPPKPLNILLDQRSSICSEVSTTSVQTPGKADEDREGSRYASNASLDCSESSHSGKFKSQSPGYVDAVDSSIPQSDHPDPNGHHPQAESSSAEQSSGSQDGDDDNNLLRSLGTTSKLLGEAIGERITFKAKGAKKRLDRNFKSSTEAISNIGADAGRSLKHASKRFGSNFSLGRNKDKADIGIGGRPGGSGEMDLDRRQTMPSTEVFNTIQFSSPLNRNGGLPDLRENDAKLQKEDYLRPDPDQEDDGCYEVPKTQGKPPSYDEALRSRPSPSDSPMSRNLAQEAAQLVQLRNQRQLSSSSSNGDESPRLPMPAFPPPRLSQQPEQFRMDALQPPVRQKRRKNYEHIELRRPPVDSAQLEELNRAAAAAEREESLLISAKNAEAETKTPKPERSDSWEFYGEDENEEEDRDEEQEGSSSPEPLYANQEATYGKLFEMATAGSSRSNVLTPNQVAEQQQLACITEDSELDACEGAVGGVPLPQAVIEEFDPLSSKCSTLARSNKSNELLLLEHLLEEDTYGTVKAEQDDVSMCTSEEEPTTSAATSPKPQQPQIVHQNARLLSDSMENMLDSDQERAKPYLSRMPESANKASGPVDLASASRNRTNWFVPDKASCSDVTPNTSKTTPPIEGDSPPTYLEAIGGSKDAAGNQENRSTIGSRFRQTINAISNVKLKMDAMKRKASFRGANQRQSDVRVALQMVPRPSLSPLLIRYEGPLVRFPSGVVEDILKEMQNRKAILRERQFQTFLDQEMKTPREMIPLDTITTLQCVSNSRVTDTATHFYCFEITTSQPKNGNGAGDAMSSNPNLLMTSSSSGNVKQQRVSHLYGVGKESERGVWMQKILESLTNSLPVKYTCHYYRAGWCYLKNSITSEWSGTWLVLRKSQRRLIFVSEANGNVEKMDLRKARCIVLKESDESIDNLHVESGPMLMIDCPPYAVYMIMSSARETKIWRHIIREVAHNNGFSLGDQQLTRYDVPVIVDKCINFVYIHGSMSEGIYRKSGSENSMHKLMSAFRADAFNVEITRNEYNEHDVANVLKRFMRDLPERLLGKLTDSFVFVTELAVASEKIPIYRELLARLSAIERETLRRIVGHLVFISSQQAKNKMSVQNLTMIWGPTLLAKKSDELIYSQKEADVLSDLVVLYKNLFPCSADEIKREQAMLACLQKYYAAAETLKDAVKQSGDIKIWISLNPNPENKTEEKTQVNATISPTKTAYELCREYSAKMQLPTHQLTLYEVILNDSLERPLHHDTKVFDVILNWSYWPEEDRKHNYLVVRPVEMLREIQRAVKNLATVTPGKELRFADSRTKTFKTLQCELRDGKIVVSKKDKNDKTTIVREIFLQSSTAYLGCERKRDFPWSWAITFVERTQAQIMRSRDAPFIGHVLAGSEWGDRTIWYSSIWYCLYRDNILPPAEIIIK
Protein: Uncharacterized RING finger protein C16G5.03 (O60117)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Mitochondrion {ECO:0000269|PubMed:16823372}. Nucleus {ECO:0000269|PubMed:16823372}.
Interaction partners:
- Putative pyridoxal kinase C6F6.11c
Sequence:
MKKQFLVRKNSSNSRYLRRDCVICLQKDGLRAQLSPCGHDQFDYSCICRWMDQSLTCPICKRHVDCVFYGFHGSSLYKKWYTQSLGSNQYSISRQLLRQPSFSSSENTDRLADLLRVRRFIYQKAWKSYENPSLSSHRQYQIPTPIQLASSASLLKKVESFIAKELLLFEYLDGHQINFIQIFLMGLLRVQNIQHPQTIDELAEFIGHEESSILLHELQRYLQFRPLSISSYLYSKRYLYGPEGLTMVQLLSQIENIQHESGPETENS
Protein: Negative aliphatic amidase regulator (P74390)
Organism: Synechocystis sp. (strain ATCC 27184 / PCC 6803 / Kazusa)
Interaction partners:
- High-affinity branched-chain amino acid transport protein
- Slr1201 protein
- High-affinity branched-chain amino acid transport ATP-binding protein
- High-affinity branched-chain amino acid transport ATP-binding protein
- High-affinity branched-chain amino acid transport permease protein
Sequence:
MTNPFGRRKFLLYGSATLGASLLLKACGGGTEPTTEPTAEPTESPTTGTAPTGEPIKVGLLHSLSGTMAISETTVVEAAELAIEEINAAGGVLGRPIEAIKEDGASDWPTFAEKAAKLIDQDKVPVVFGCWTSASRKAVLPVFEAKNHMLWYPVQYEGQECSKNIFYTGAAPNQQIEPAVDWLLENKGNKFFLVGSDYVFPRTANTIIKEQLKAKGGETLGEDYLPLGNTEVTPIITKIREALPDGGVIFNTLNGDSNVAFFKQIQAAGLTPDKYPVMSVSVAEEEVRQIGKEYLLGQFASWNYFQSVDTPANQKFVAAFKAKYGEDRVTNDPMEAAYISVYLWKAAVEAAGDVGETPEGLEKVRAAAIGKTFDAPEGMVTMQPNHHISKTVRIGEVNDEGQFTIVWSSDGPVDPIPWNQFVPETKGFTCDWTRTDVENPGKFKAS
Protein: Oxygen-dependent coproporphyrinogen-III oxidase (CPO) (Coprogen oxidase) (Coproporphyrinogenase) (EC 1.3.3.3) (P36553)
Organism: Escherichia coli (strain K12)
Function: Involved in the heme biosynthesis. Catalyzes the aerobic oxidative decarboxylation of propionate groups of rings A and B of coproporphyrinogen-III to yield the vinyl groups in protoporphyrinogen-IX.
Subcellular location: Cytoplasm.
Interaction partners:
- Uroporphyrinogen decarboxylase
- Oxygen-independent coproporphyrinogen III oxidase
- Protoporphyrinogen IX dehydrogenase [quinone]
- Ferrochelatase
- N-acetylmuramoyl-L-alanine amidase AmiA
- Delta-aminolevulinic acid dehydratase
- Glutamyl-tRNA reductase
- Uroporphyrinogen-III synthase
- Protein HemY
- Glutamate-1-semialdehyde 2,1-aminomutase
Sequence:
MKPDAHQVKQFLLNLQDTICQQLTAVDGAEFVEDSWQREAGGGGRSRVLRNGGVFEQAGVNFSHVHGEAMPASATAHRPELAGRSFEAMGVSLVVHPHNPYVPTSHANVRFFIAEKPGADPVWWFGGGFDLTPFYGFEEDAIHWHRTARDLCLPFGEDVYPRYKKWCDEYFYLKHRNEQRGIGGLFFDDLNTPDFDRCFAFMQAVGKGYTDAYLPIVERRKAMAYGERERNFQLYRRGRYVEFNLVWDRGTLFGLQTGGRTESILMSMPPLVRWEYDYQPKDGSPEAALSEFIKVRDWV
Protein: Mitochondrial inner membrane protein MPV17 (MpV17 mitochondrial inner membrane protein isoform 2) (B5MC10)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MALWRAYQRALAAHPWKVQVLTAAAGGEAGSAGTPERPDSDHGVPGLWLCGPCGRRLVQGFGSVHPWHHQSGCTEEDVVGSGGLCPVFSRLLSPTGRGT
Protein: Thiosulfate sulfurtransferase 16, chloroplastic (EC 2.8.1.1) (Rhodanese) (Senescence-associated protein) (Sulfurtransferase 16) (AtStr16) (Q39129)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Thought to act during the early stages of leaf senescence. Catalyzes the transfer of a sulfur ion from a donor to cyanide or to other thiol compounds. Substrate preference is thiosulfate > 3-mercaptopyruvate.
Subcellular location: Plastid, chloroplast {ECO:0000269|PubMed:15181206}.
Interaction partners:
- Small ribosomal subunit protein mS29
- Rhodanese-like domain-containing protein 4, chloroplastic
- Large ribosomal subunit protein mL46
- Adenylyltransferase and sulfurtransferase MOCS3
- GDSL esterase/lipase At4g18970
- Molybdopterin synthase catalytic subunit
- Large ribosomal subunit protein uL24c
- Thiosulfate/3-mercaptopyruvate sulfurtransferase 1, mitochondrial
- 2-succinylbenzoate--CoA ligase, chloroplastic/peroxisomal
- Large ribosomal subunit protein mL43
Sequence:
MAEESRVPSSVSVTVAHDLLLAGHRYLDVRTPEEFSQGHACGAINVPYMNRGASGMSKNPDFLEQVSSHFGQSDNIIVGCQSGGRSIKATTDLLHAGFTGVKDIVGGYSAWAKNGLPTKA
Protein: Cell shape-determining protein MreC (Cell shape protein MreC) (Rod shape-determining protein MreC) (Q01466)
Organism: Bacillus subtilis (strain 168)
Function: Involved in formation and maintenance of cell shape. Required for the formation of proper helical filaments of MreB and for cell wall synthesis in the cylindrical part of the cell leading to cell elongation.
Subcellular location: Cell membrane {ECO:0000269|PubMed:22882210}. Cell septum. Membrane raft {ECO:0000269|PubMed:22882210}. Note=Localizes in helical patterns when associated with the cell membrane (PubMed:15745453). Present in detergent-resistant membrane (DRM) fractions that may be equivalent to eukaryotic membrane rafts; these rafts include proteins involved in signaling, molecule trafficking and protein secretion (PubMed:22882210). {ECO:0000269|PubMed:15745453, ECO:0000269|PubMed:22882210}.
Interaction partners:
- Cell shape-determining protein MreB
- Rod shape-determining protein MreD
- Peptidoglycan glycosyltransferase RodA
- Cell shape-determining protein Mbl
- Cell shape-determining protein MreBH
- Septum site-determining protein MinC
- Penicillin-binding protein H
- UDP-N-acetylglucosamine--N-acetylmuramyl-
- UPF0758 protein YsxA
- Cell division protein FtsZ
Sequence:
MPNKRLMLLLLCIIILVAMIGFSLKGGRNTTWPEKVIGDTTGVFQNIFHTPAEFFAGIFENINDLKNTYKENERLREKLDGQTQYEAKLQELEEENKSLRDELGHVKSIKDYKPILATVIARSPDNWAKQVTINKGTQQNVAKDMAVTNEKGALIGKIKSSGLNNFTSAVQLLSDTDRNNRVATKISGKKGSKGYGLIEGYDKEKKRLKMTIIERKDKQDVKKGDLIETSGTGGVFPEGLTIGEVTDIESDSYGLTKVAYVKPAADLTDLNNVIVVNRDVPTVDTEEEGS
Protein: 2-octaprenyl-6-methoxyphenol hydroxylase (EC 1.14.13.-) (P25534)
Organism: Escherichia coli (strain K12)
Function: Is likely an oxygenase that introduces the hydroxyl group at carbon four of 2-octaprenyl-6-methoxyphenol resulting in the formation of 2-octaprenyl-6-methoxy-1,4-benzoquinol.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:30686758}.
Interaction partners:
- Ubiquinone biosynthesis O-methyltransferase
- 2-octaprenylphenol hydroxylase
- Ubiquinone/menaquinone biosynthesis C-methyltransferase UbiE
- Ubiquinone biosynthesis accessory factor UbiJ
- Ubiquinone biosynthesis accessory factor UbiK
- 3-demethoxyubiquinol 3-hydroxylase
- Xaa-Pro aminopeptidase
- UPF0149 protein YgfB
- 4-hydroxybenzoate octaprenyltransferase
- Flavin prenyltransferase UbiX
Sequence:
MSVIIVGGGMAGATLALAISRLSHGALPVHLIEATAPESHAHPGFDGRAIALAAGTCQQLARIGVWQSLADCATAITTVHVSDRGHAGFVTLAAEDYQLAALGQVVELHNVGQRLFALLRKAPGVTLHCPDRVANVARTQSHVEVTLESGETLTGRVLVAADGTHSALATACGVDWQQEPYEQLAVIANVATSVAHEGRAFERFTQHGPLAMLPMSDGRCSLVWCHPLERREEVLSWSDEKFCRELQSAFGWRLGKITHAGKRSAYPLALTHAARSITHRTVLVGNAAQTLHPIAGQGFNLGMRDVMSLAETLTQAQERGEDMGDYGVLCRYQQRRQSDREATIGVTDSLVHLFANRWAPLVVGRNIGLMTMELFTPARDVLAQRTLGWVAR
Protein: Mitogen-activated protein kinase kinase 1a (EC 2.7.12.2) (MAP kinase kinase 1a) (PpMKK1a) (A9RWC9)
Organism: Physcomitrium patens (Spreading-leaved earth moss) (Physcomitrella patens)
Function: The CERK1, MEKK1a/b, MKK1a/b/c and MPK4a/b proteins are involved in pathogen defense. The pathway induces rapid growth inhibition, cell wall depositions and accumulation of defense-related transcripts. This protein is required for full defense response to fungal pathogen chitin.
Interaction partners:
Sequence:
MRRARGKFKGGNSALRVNVPKENAISDYVTASGTFQDGDIMLNKEGIRVVSQTQTSTPAANGNISLSDLETVKVLGKGSGGVVQLVRHKWTNETYALKVIHMNIEETTRKQIVQELKINHASQCPYVVICYHAFYNNGLISIVLEYMDGGSLADIMKELEPKCIKEPNLGVVCKQVLLGLMYLHQTRHIIHRDIKPSNLLVNHKGEVKISDFGVSAVLANSMAVRDTFVGTCTYMSPERVLGGTYGFDSDIWSLGLTLLECALGKYPYQPPGSEEGWMNFYELLQTIVDQPPPVAPADQFSPEFCSFISACLQKDPKCRPTAAELLNHPFVNKYDEEEYGLAKLLPPLVPLA
Protein: MBL associated serine protease 1 (F8W876)
Organism: Homo sapiens (Human)
Interaction partners:
- Ficolin-1
- Ficolin-2
- Ficolin-3
- Mannose-binding protein C
- Plasma protease C1 inhibitor
- Mannan-binding lectin serine protease 2
- Collectin-11
- Collectin-10
- Complement C4-A
- Complement C3
Sequence:
MFGQIQSPGYPDSYPSDSEVTWNITVPDGFRIKLYFMHFNLESSYLCEYDYVKVETEDQVLATFCGRETTDTEQTPGQEVVLSPGSFMSITFRSDFSNEERFTGFDAHYMAVDVDECKEREDEELSCDHYCHNYIGGYYCSCRFGYILHTDNRTCRVECSDNLFTQRTGVITSPDFPNPYPKSSECLYTIELEEGFMVNLQFEDIFDIEDHPEVPCPYDYIKIKVGPKVLGPFCGEKAPEPISTQSHSVLILFHSDNSGENRGWRLSYRAAGNECPELQPPVHGKIEPSQAKYFFKDQVLVSCDTGYKVLKDNVEMDTFQIECLKDGTWSNKIPTCKKNEIDLESELKSEQVTE
Protein: Succinate dehydrogenase [ubiquinone] flavoprotein subunit, mitochondrial (EC 1.3.5.1) (Flavoprotein subunit of complex II) (Fp) (Malate dehydrogenase [quinone] flavoprotein subunit) (EC 1.1.5.-) (Q8K2B3)
Organism: Mus musculus (Mouse)
Function: Flavoprotein (FP) subunit of succinate dehydrogenase (SDH) that is involved in complex II of the mitochondrial electron transport chain and is responsible for transferring electrons from succinate to ubiquinone (coenzyme Q). Can act as a tumor suppressor.
Subcellular location: Mitochondrion inner membrane {ECO:0000250|UniProtKB:Q0QF01}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q0QF01}; Matrix side {ECO:0000250|UniProtKB:Q0QF01}.
Interaction partners:
- Succinate dehydrogenase cytochrome b560 subunit, mitochondrial
- Succinate dehydrogenase cytochrome b small subunit, mitochondrial
- Succinate dehydrogenase iron-sulfur subunit, mitochondrial
- Fumarate hydratase, mitochondrial
- Succinate--CoA ligase subunit alpha, mitochondrial
- Succinate dehydrogenase assembly factor 2, mitochondrial
- Succinate--CoA ligase subunit beta, mitochondrial
- NADH dehydrogenase 1 alpha subcomplex subunit 9, mitochondrial
- Cytochrome b-c1 complex subunit Rieske, mitochondrial
- Cytochrome b-c1 complex subunit 2, mitochondrial
Sequence:
MAGVGAVSRLLRGRRLALTGAWPGTLQKQTCGFHFSVGENKKASAKVSDAISTQYPVVDHEFDAVVVGAGGAGLRAAFGLSEAGFNTACLTKLFPTRSHTVAAQGGINAALGNMEEDNWRWHFYDTVKGSDWLGDQDAIHYMTEQAPASVVELENYGMPFSRTEDGKIYQRAFGGQSLKFGKGGQAHRCCCVADRTGHSLLHTLYGRSLRYDTSYFVEYFALDLLMENGECRGVIALCIEDGSIHRIRAKNTVIATGGYGRTYFSCTSAHTSTGDGTAMVTRAGLPCQDLEFVQFHPTGIYGAGCLITEGCRGEGGILINSQGERFMERYAPVAKDLASRDVVSRSMTLEIREGRGCGPEKDHVYLQLHHLPPEQLATRLPGISETAMIFAGVDVTKEPIPVLPTVHYNMGGIPTNYKGQVLKHVNGQDQIVPGLYACGEAACASVHGANRLGANSLLDLVVFGRACALSIAESCRPGDKVPSIKANAGEESVMNLDKLRFADGSIRTSELRLNMQKSMQNHAAVFRVGSVLQEGCEKISQLYGDLKHLKTFDRGMVWNTDLVETLELQNLMLCALQTIYGAEARKESRGAHAREDYKVRVDEYDYSKPIQGQQKKPFGEHWRKHTLSYVDIKTGKVTLEYRPVIDKTLNEADCATVPPAIRSY
Protein: LP01489p (Q5U112)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
Sequence:
MSRCDNHKSRRQQLPVPAPLSSSHSNSSSSRSQGHHHHHHHQLHSSNSDLGGSESFLQYCSDSEKRPPPIVVVVGDGRSRVRRVVRTATRHVTVVSLSTRHKETQTHTSHHVTAVSFPQKSLERSGSTQYELAGAQQPGSANASTCTDSGSVGGYVYLQNHYAPGAHSSSAAINYPAQQHPQMVYQIQQYPTCHQQQQQQHLQQQQHLHQTGAGHYMQVTATGGGQYHHHHMLHGHGHHAHHHGGAVVIAGSGVGTGLGSGATSVIMQHQQQQQQQQNMHKKNSIRNGGDVLKRTRAQSAYELSQDLLEKQIELLERKYGGVRARNAAVTIQRAFRHYMMVKKFASITAMAKAEKRLSRRMVVTASSLGLAEEGASSSSAYGSATESQLTEQQQQQQAQQQQQPRVTIMAGPAGAASPGLSRTPPTRSLSMRERRQLDCSPIPRSQSGASPASISSSTVSTSALASHPHVNLLHAAEPHYYNAQALPQGAAYYTSYHGSPHDLSYASSADTSLNASWVNTSGHSPHTPYYSAAQIYMRPKGGSTTPTPSCIGSTGSGSGGSGSGSSKKVPPEVPKRTSSITAQQQTQLLLLQRQTPPPPSLLRTNGLCKTAENGSLTSVQSSGSDSSVTSAERNLNSDLGSDRSNSPHTWKRGTALNSSQQFSTHSADSAGAVSGGGVGVAGGAGVYAAQMQAAVAAATAAGGMPPADDHAISSHTSAAQYEQHEQQQHEQQQLQAAAAAAGVAQNYKMSETIRKRQYRVGLNLFNKKPEKGITYLIRRGFLENTPQGVARFLITRKGLSRQMIGEYLGNLQNQFNMAVLSCFAMELDLSGRQVDVALRKFQAYFRMPGEAQKIERLMEIFSQRYCECNADIVGRLRSSDTIFVLAFAIIMLNTDLHTPNLKPERRMRVEDFIKNLRGIDDCHDIDKDMLMGIYDRVKSDEFKPGSDHVTQVMKVQATIVGKKPNLALPHRRLVCYCRLYEIPDVNKKERPGVHQREVFLFNDLLVITKIFSKKKTSVTYTFRNSFPLCGTVVTLLDMPNYPFCIQLSQKVDGKILITFNARNEHDRCKFAEDLKESISEMDEMESLRIEAELERQKSARNRAPGNAENRDSGVADVEVCPCPYQQGSQASGEQAPNSADNSQQLKRSALSNSLLDMHEQFGNEKPQRRGSVGSLDSGMSISFQSTTTSSASRENAAAIAAAANAAAAAKMRFNMPPTAAIATPSNVYAAPGMQAYTHANFVQQSQAAYMLQQQQMLQQQAQMQAQAQAQAQAQAQAQAQAQAQAQAQPLTGRIPGRERKASRTDENGRSTEV