wanglab/gogpt-training-data huggingface dataset:
Protein: Serine/threonine-protein phosphatase with EF-hands 1 (PPEF-1) (EC 3.1.3.16) (Protein phosphatase with EF calcium-binding domain) (PPEF) (Serine/threonine-protein phosphatase 7) (PP7) (O14829)
Organism: Homo sapiens (Human)
Function: May have a role in the recovery or adaptation response of photoreceptors. May have a role in development.
Interaction partners:
- Rhodopsin
- Golgi phosphoprotein 3
- Sex comb on midleg-like protein 2
- Cyclin-dependent kinase-like 5
Sequence:
MGCSSSSTKTRRSDTSLRAALIIQNWYRGYKARLKARQHYALTIFQSIEYADEQGQMQLSTFFSFMLENYTHIHKEELELRNQSLESEQDMRDRWDYVDSIDVPDSYNGPRLQFPLTCTDIDLLLEAFKEQQILHAHYVLEVLFETKKVLKQMPNFTHIQTSPSKEVTICGDLHGKLDDLFLIFYKNGLPSERNPYVFNGDFVDRGKNSIEILMILCVSFLVYPNDLHLNRGNHEDFMMNLRYGFTKEILHKYKLHGKRILQILEEFYAWLPIGTIVDNEILVIHGGISETTDLNLLHRVERNKMKSVLIPPTETNRDHDTDSKHNKVGVTFNAHGRIKTNGSPTEHLTEHEWEQIIDILWSDPRGKNGCFPNTCRGGGCYFGPDVTSKILNKYQLKMLIRSHECKPEGYEICHDGKVVTIFSASNYYEEGSNRGAYIKLCSGTTPRFFQYQVTKATCFQPLRQRVDTMENSAIKILRERVISRKSDLTRAFQLQDHRKSGKLSVSQWAFCMENILGLNLPWRSLSSNLVNIDQNGNVEYMSSFQNIRIEKPVQEAHSTLVETLYRYRSDLEIIFNAIDTDHSGLISVEEFRAMWKLFSSHYNVHIDDSQVNKLANIMDLNKDGSIDFNEFLKAFYVVHRYEDLMKPDVTNLG
Protein: BBG-LP12 (Q15K34)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
SESLVVKALTKKRSSLGSLSSLNEKPTELDYERKRNYHKASRSLDLDLDLVSNEAGESPVATTPSTGSVSPPQPASLHDEDAEATIAGIRARRQLSRGDAAKLSTSELLERAAEARNAIAAEIRAQAEDAAASGGGARCVEIVKDSCGLGFSIEGGFDSPLGNRPLIVKKVFMGGAAQKTNQVRNGDEILSINGASTSRMTRVDAWNYMKQLPLGPVKICFA
Protein: Integrin subunit alpha E (A0A0G2JVR6)
Organism: Rattus norvegicus (Rat)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004479, ECO:0000256|RuleBase:RU003762}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004479, ECO:0000256|RuleBase:RU003762}.
Interaction partners:
Sequence:
QLWVRHTRVSLWPAGLKPLGAFNVDVDWSWVTALQPGAPSVLNSLLHQDPSNNQTCLLVARRSSNRNSAVLYRCATSIIPDEIGCQPVEHILMPKGRYQGVTLVRNHNGVLVCIQVQSRKPRSLNSELTGACSLLTPNLDLQAQAYFSDLGKDWSGTSKLRVLVKEELMISVLGAGTEIAIVLDGSGSIEPSDFQKAKDFISTMMRNFYEKCFECNFALVQYGGVIQTEFDLLDSRDINASLAKVQSIVQVKEVTKTASAMQHVLDNIFIPSRGSRKKALKVMVVLTDGDIFRDPLNLTTVISSSKMQGVVRFAIGVGNAFENNNTYRELKLIASDPKAAHTFKVTNYSALDGLLSKLQQRIIHMEGTVGDTLQYQLAQTGFSAQILDKGQVLLGTVGAFNWSGGALLYNTQNGRGRFLNQTAKEDFRAAQYSYLGYSVAALHKAHGVSYVAGAPRHKLRGAVFELQKEDGEETFMRRIEGEQMGSYFGSVLCPVDINMDGITDFLLVAAPFYHIRGEEGRVYVYRVHEQDAPFSLVYTLSGYPGLTSSRFGFAMAAVGDINQDKFTDVAIGAPLEGFGAGDGASYGSVYIYNGHSGGLHASPSQQIRASSVALGLYYFGMSVSGGLDFSGDDLADITVGSQDVAVVLRSRPVVDLTVSMTFTPDALPMAFKDKMDVELCFKVDSSAVPSEPGLRGMSLNFTVDVDVTKQKQRLQCADRSCCQSCLMKWSGGSSLCEHFGLISTEEELCEDDCFSNITIKVSYEFQTSEERRNHPNPILDHYKEPSAIFQLPYEKDCKNKVFCIAEIQLTTAISQQDLVVGITKEVTMNISLTNSGEDSYMTNMALNYPRNLQFKKIQKPLSPDIQCDDPKPVASVLVMNCKIGHPILKRSSVNVSVTWQLEESIFPNRTADITVTISNSNEKSLARETHSLQFRHAFIAVLSRPSVMYMNTSQSSSDHKEFFFNVHGENHFGAVFQLQICVPITLRDLQIIRVKHLTKTQAHTECTQSQEPTCGSDPVQNVEEWHSVICAITSNKENVTVAAEISMGHTKQLLRDISELQILGEISFNKSLYEGLNAENHRTKITVIFLKEEKPHSLPLIIGSSIGGLLVLVVIIAILFKCGFFKRKYKQLNLESVRKAQLKSDSLLED
Protein: Capsid protein (CP) (Coat protein) (P03591)
Organism: Alfalfa mosaic virus (strain 425 / isolate Leiden)
Function: Capsid protein. Binds to the to the 3' end of the nonpolyadenylated viral RNA and is involved in viral RNA translation initiation. Probably binds RNA and plays a role in packaging.
Subcellular location: Virion {ECO:0000305}.
Interaction partners:
Sequence:
MSSSQKKAGGKAGKPTKRSQNYAALRKAQLPKPPALKVPVVKPTNTILPQTGCVWQSLGTPLSLSSFNGLGARFLYSFLKDFVGPRILEEDLIYRMVFSITPSHAGTFCLTDDVTTEDGRAVAHGNPMQEFPHGAFHANEKFGFELVFTAPTHAGMQNQNFKHSYAVALCLDFDAQPEGSKNPSFRFNEVWVERKAFPRAGPLRSLITVGLFDEADDLDRH
Protein: Fgr6-4p (A0A1D8PIQ1)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Interaction partners:
Sequence:
MSEVPNQESPSSSIFKQSNASTSTKIHGAPSSSQIANVDFNTLRKLNTNTSFSSNLTNSTTKTSNALSRLFTRNKSSSNISIHPSSSDDDSSPKTLRESTSPSESSKSVSGNKLRIAKKLKFPKNQSSRKPDLFLDTSSTISEDSSSFRKVITGNSLNEMNKSRKSSMSSPMSTTFHSLFHRSHHNGSNLQRDTNQVATGMTPLSGKFDDFSKASKTTLCLSSNSSNSIISNPELAQIYNFTNPNISIEDGETNLDHSNSSFLDIHKKMLVPADSFIQNKLNKYHQTEVGLGIYESELDHDKDSKIYSNLYHYLKPLFTPSFSISDSGQKGRMRPILGASVEEIANFVKESFCLHQPNHERSFRSKTRSSVSSLGREKVEDFDYRQLSNLFEKLMALLSHNLQTADSSEVSLQALILNAWKYYNAYVRFYLLSIFQPLQLHLNELSMRNHNGSKIIRIDDLLLVSFRKVFITEQGIGSGDRETSQFLGNAESEDLTGNGLLTSTLAVLSSIS
Protein: Pleckstrin homology domain-containing family B member 1 (PH domain-containing family B member 1) (Evectin-1) (Q9WU68)
Organism: Rattus norvegicus (Rat)
Subcellular location: Membrane {ECO:0000269|PubMed:10200314}. Cytoplasm {ECO:0000250|UniProtKB:Q9QYE9}. Note=Localizes to the apical juxta-nuclear Golgi region of the cytoplasm (By similarity). Membrane-associated. Highly expressed in the outer segments of photoreceptor cells, both in rods and cones (By similarity). {ECO:0000250|UniProtKB:Q9QYE9, ECO:0000250|UniProtKB:Q9UF11}.
Interaction partners:
Sequence:
MALVRGGWLWRQSSILRRWKRNWFALWLDGTLGYYHDETAQDEEDRVVIHFNVRDIKVGQECQDVQPPEGRSRDGLLTVNLREGSRLHLCAETRDDAIAWKTALMEANSTPAPAGATVPPRSRRVCPKVRCTSLSWKPCKVERRIWVRVYSPYQDYYEVVPPNAHEATYVRSYYGPPYGPGVTHVIVREDPCYSSGAPLAMGMLAGAATGAALGSLMWSPCWF
Protein: NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 5, mitochondrial (Complex I-SGDH) (CI-SGDH) (NADH-ubiquinone oxidoreductase SGDH subunit) (Q02380)
Organism: Bos taurus (Bovine)
Function: Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed not to be involved in catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone.
Subcellular location: Mitochondrion inner membrane {ECO:0000305|PubMed:10852722, ECO:0000305|PubMed:18721790}; Single-pass membrane protein {ECO:0000255}; Matrix side {ECO:0000305}.
Interaction partners:
- NADH dehydrogenase 1 beta subcomplex subunit 1
- NADH dehydrogenase iron-sulfur protein 2, mitochondrial
- NADH dehydrogenase 1 beta subcomplex subunit 4
- NADH dehydrogenase 1 alpha subcomplex subunit 9, mitochondrial
- NADH dehydrogenase 1 alpha subcomplex subunit 5
- NADH dehydrogenase 1 alpha subcomplex subunit 2
- NADH dehydrogenase iron-sulfur protein 4, mitochondrial
- NADH dehydrogenase 1 alpha subcomplex subunit 12
- NADH dehydrogenase 1 alpha subcomplex subunit 7
- Acyl carrier protein, mitochondrial
Sequence:
MAAMSLLHRASVSAVAALSGRRLGTRLGFGGFLTRDFPKTVAPVRHSGDHGKRLFIIKPSGFYDKRFLKLLRFYILLTGIPVAIGITLINVFIGEAELAEIPEGYVPEHWEYFKHPISRWIARTFFDGPEKNYERTMAILQIEAEKAELRLKELEVRRLMRARGDGPWFHYPTIDKELIDHSPKATPDN
Protein: SLAM family member 5 (Cell surface antigen MAX.3) (Hly9-beta) (Leukocyte differentiation antigen CD84) (Signaling lymphocytic activation molecule 5) (CD antigen CD84) (Q9UIB8)
Organism: Homo sapiens (Human)
Function: Self-ligand receptor of the signaling lymphocytic activation molecule (SLAM) family. SLAM receptors triggered by homo- or heterotypic cell-cell interactions are modulating the activation and differentiation of a wide variety of immune cells and thus are involved in the regulation and interconnection of both innate and adaptive immune response. Activities are controlled by presence or absence of small cytoplasmic adapter proteins, SH2D1A/SAP and/or SH2D1B/EAT-2. Can mediate natural killer (NK) cell cytotoxicity dependent on SH2D1A and SH2D1B (By similarity). Increases proliferative responses of activated T-cells and SH2D1A/SAP does not seem be required for this process. Homophilic interactions enhance interferon gamma/IFNG secretion in lymphocytes and induce platelet stimulation via a SH2D1A-dependent pathway. May serve as a marker for hematopoietic progenitor cells Required for a prolonged T-cell:B-cell contact, optimal T follicular helper function, and germinal center formation. In germinal centers involved in maintaining B-cell tolerance and in preventing autoimmunity (By similarity). In mast cells negatively regulates high affinity immunoglobulin epsilon receptor signaling; independent of SH2D1A and SH2D1B but implicating FES and PTPN6/SHP-1. In macrophages enhances LPS-induced MAPK phosphorylation and NF-kappaB activation and modulates LPS-induced cytokine secretion; involving ITSM 2 (By similarity). Positively regulates macroautophagy in primary dendritic cells via stabilization of IRF8; inhibits TRIM21-mediated proteasomal degradation of IRF8.
Subcellular location: Cell membrane {ECO:0000269|PubMed:11389028, ECO:0000269|PubMed:12962726}; Single-pass type I membrane protein {ECO:0000269|PubMed:11389028, ECO:0000269|PubMed:12962726}.
Interaction partners:
- SH2 domain-containing protein 1A
- SH2 domain-containing protein 1B
- CD48 antigen
- Cytotoxic T-lymphocyte protein 4
- T-cell surface antigen CD2
Sequence:
MAQHHLWILLLCLQTWPEAAGKDSEIFTVNGILGESVTFPVNIQEPRQVKIIAWTSKTSVAYVTPGDSETAPVVTVTHRNYYERIHALGPNYNLVISDLRMEDAGDYKADINTQADPYTTTKRYNLQIYRRLGKPKITQSLMASVNSTCNVTLTCSVEKEEKNVTYNWSPLGEEGNVLQIFQTPEDQELTYTCTAQNPVSNNSDSISARQLCADIAMGFRTHHTGLLSVLAMFFLLVLILSSVFLFRLFKRRQGRIFPEGSCLNTFTKNPYAASKKTIYTYIMASRNTQPAESRIYDEILQSKVLPSKEEPVNTVYSEVQFADKMGKASTQDSKPPGTSSYEIVI
Protein: FtsZ-like protein (EC 3.6.1.-) (Q3BK72)
Organism: Magnetospirillum gryphiswaldense (strain DSM 6361 / JCM 21280 / NBRC 15271 / MSR-1)
Function: Required for synthesis of single-domain magnetite particles and magnetosomes, especially in the absence of nitrate. Forms filaments, which form bundles in the presence of GTP. Has both GTPase and ATPase activity; GTPase is 2.5 time more efficient. Has no activity on CTP or TTP. May be involved in redox control for magnetite crystallization (Probable). Mild overexpression causes cell elongation. May recruit other proteins (MamX, MamY and MamZ and possibly Mms6) to a complex required for biomineralization (Probable).
Subcellular location: Cytoplasm {ECO:0000269|PubMed:30367002, ECO:0000305|PubMed:24272781}. Note=Upon mild overexpression assembles into foci at midcell and at cell poles, foci colocalize with FtsZ but not with MamK filaments. Subcellular location is independent of other magnetosome locus encoded proteins, but may depend on FtsZ (PubMed:24272781). A similar construct shows a dispersed location at 6 hours post-induction and a dot-like distribution at 18 hours post-induction (PubMed:30367002). {ECO:0000269|PubMed:24272781, ECO:0000269|PubMed:30367002}.
Interaction partners:
- Cell division protein FtsA
- Magnetosome protein MamX
- Magnetosome protein MamZ
- Actin-like protein MamK
- Liposome tubulation protein MamY
- Magnetosome formation protease MamE
- Magnetite biomineralization protein Mms6
- Magnetosome-associated protein MamJ
- Magnetosome protein MamC
- Multi-heme protein MamP
Sequence:
MFGVEPISFCEDMTMIRPRIIVIGVGGAGGNAVNNMILSKIEGVEFIAANTDAQALGLSLADRRIPLGGYVTKGLGAGSRPELGRSAAQESIDDILTAIDDANMVFITAGMGGGTGSGAAPVIAQAARERGILTIGVVTKPFHFEGGHRMGTAEAAIEELQHVVDTLIIIPNQNLFRIASERTTFIDAFKMADNVLNSGVRSVTDLVVKPGLINLDFADIRIVMSEMGKAIMGTGEAEGEPRAVKAAEAAISNPLLGDTSIAGAKGVLINITGGMDMTLFEVDEAANRIRTEVAPDANIIFGSTFDEKLDGKMRVSVVATGIA
Protein: Pseudocleavage protein nop-1 (Q09314)
Organism: Caenorhabditis elegans
Function: Required for formation of the pseudocleavage furrow during the first cleavage of the embryo and also mediates aster-induced furrowing during cytokinesis. Promotes cortical recruitment of ani-1 and nmy-2 during pseudocleavage and cytokinesis and promotes the accumulation of actin at furrowing regions. Regulates establishment of embryonic cell polarity.
Subcellular location: Nucleus {ECO:0000269|PubMed:22918944}. Cytoplasm {ECO:0000269|PubMed:22918944}. Cytoplasm, cell cortex {ECO:0000269|PubMed:22918944}. Cleavage furrow {ECO:0000269|PubMed:22918944}. Note=Highly concentrated in interphase nuclei. As well as a significant cytoplasmic pool, a distinct cortical localization is also detected, particularly at ingressing pseudocleavage and cleavage furrows.
Interaction partners:
- Anillin-like protein 1
- Rac GTPase-activating protein 1
- Myosin-11
- Protein ECT2
- Kinesin-like protein
- Rho-GAP domain-containing protein
Sequence:
MSAPKKRKSDIHSDDRDHADHQTKKEKHWFEEKSEQNGENRRSSIFKGFLKKVKSSTTLKSTNKSASSSKMDTIANETHLSITSESSITSVESCHSAQFPNVAKNAMLRTLVNRDSFTPVPPPDGESVTFILPEIGSSKLEFTSKMDDAISIESRMSIGSCHTIDEDSASIGSTSVFCTPSRNPLMRNGLRMSTRSVPENQDDMPPALFRSLCNSAVRRVPTSKSEGGGTPMRRSMRMSIQKRNLSSKNMEDVPEEEALTVSNSSIRVDAPIAEEDEEVFGAAKEYFDNNVTSHNDSADEGTCSMSRLSTTSERASGVGGSSIFQGRRSSIFRKIFPGKSESKDRRMSDNNQASEQYMDKKSRRASVVSFNEFTSVSGLSVNDSASKNPKDLTESPQQPKLRKKTASSSNLSQRISSVFRMGSNSTVKLNEYVPSPIVSQSSRRNTLTGNSSISSGVGSIASGTSDQGYGTIGSRSGQSISRCGSRRDDEGKKERTRRLLDRIIISDVPAGELLKLKIEQVKKQKQLEMDELFETQLTESSSSDTSQSENLQFDVVAVDIKADGSPFSTTAATFMDSELSKRVKEEIVSNYRPDRCGSITEYEPELVFVMPEQPQASLKSLNDSVSSNADINLDHLRNVRSGLCKSIEEWKRITKMRESSTMLIYPMFCQSEEEWDSKGTIDAIFLMLDGILMNTKRWMPNGKCILAGVTPNNVILLRNKFDELKLSVAISESDGPASSNDDFDTQSTASTSTVFGAKI
Protein: WD repeat-containing protein 91 (A4D1P6)
Organism: Homo sapiens (Human)
Function: Functions as a negative regulator of the PI3 kinase/PI3K activity associated with endosomal membranes via BECN1, a core subunit of the PI3K complex. By modifying the phosphatidylinositol 3-phosphate/PtdInsP3 content of endosomal membranes may regulate endosome fusion, recycling, sorting and early to late endosome transport. It is for instance, required for the delivery of cargos like BST2/tetherin from early to late endosome and thereby participates indirectly to their degradation by the lysosome. May play a role in meiosis (By similarity).
Subcellular location: Early endosome membrane {ECO:0000269|PubMed:26783301}; Peripheral membrane protein {ECO:0000269|PubMed:26783301}. Late endosome membrane {ECO:0000269|PubMed:26783301, ECO:0000269|PubMed:28404643}.
Interaction partners:
- WD repeat-containing protein 81
- Beclin-1
Sequence:
MAEAVERTDELVREYLLFRGFTHTLRQLDAEIKADKEKGFRVDKIVDQLQQLMQVYDLAALRDYWSYLERRLFSRLEDIYRPTIHKLKTSLFRFYLVYTIQTNRNDKAQEFFAKQATELQNQAEWKDWFVLPFLPSPDTNPTFATYFSRQWADTFIVSLHNFLSVLFQCMPVPVILNFDAECQRTNQVQEENEVLRQKLFALQAEIHRLKKEEQQPEEEEALVQHKLPPYVSNMDRLGDSELAMVCSQRNASLSQSPRVGFLSSLLPQSKKSPSRLSPAQGPPQPQSSAKKESFGGQGTKGKDPTSGAKDGKSLLSGLATGESGWSQHRQRRLQDHGKERKELFSTTTSQCAEKKPEASGPEAEPCPELHTEPVEPLTRASSAGPEGGGVRPEQPFIVLGQEEYGEHHSSIMHCRVDCSGRRVASLDVDGVIKVWSFNPIMQTKASSISKSPLLSLEWATKRDRLLLLGSGVGTVRLYDTEAKKNLCEININDNMPRILSLACSPNGASFVCSAAAPSLTSQVDFSAPDIGSKGMNQVPGRLLLWDTKTMKQQLQFSLDPEPIAINCTAFNHNGNLLVTGAADGVIRLFDMQQHECAMSWRAHYGEVYSVEFSYDENTVYSIGEDGKFIQWNIHKSGLKVSEYSLPSDATGPFVLSGYSGYKQVQVPRGRLFAFDSEGNYMLTCSATGGVIYKLGGDEKVLESCLSLGGHRAPVVTVDWSTAMDCGTCLTASMDGKIKLTTLLAHKA
Protein: Haloacid dehalogenase-like hydrolase domain-containing protein 2 (Q9H0R4)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MAACRALKAVLVDLSGTLHIEDAAVPGAQEALKRLRGASVIIRFVTNTTKESKQDLLERLRKLEFDISEDEIFTSLTAARSLLERKQVRPMLLVDDRALPDFKGIQTSDPNAVVMGLAPEHFHYQILNQAFRLLLDGAPLIAIHKARYYKRKDGLALGPGPFVTALEYATDTKATVVGKPEKTFFLEALRGTGCEPEEAVMIGDDCRDDVGGAQDVGMLGILVKTGKYRASDEEKINPPPYLTCESFPHAVDHILQHLL
Protein: Pre-rRNA-processing protein RIX1 N-terminal domain-containing protein (Q38C13)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MNRNAAQSMTNVVHATDVLGSALTAIDAIVADAQQHQRKKEQREGTGPALAGIKRQRGGEVFAVMAEPHFRALQTIVLLYGVQLMPSLDAIMRRVLICVTSPVLVSSDCWELAAMLGTYFRAGAARLLEEVLALLLAERSPFLLGSPCVVVDVVASQGLPANTNGSTDISGKDRNAVDQEKVYDGSSTQRNLRAFDDLLVALGPFLPSSTMQQVALRYAEEVVVNGMLNAQASAGCSTGQLASYQERQQQQVEPQQTSVEAVLRPQCVSLLTTLLTLCRPLPSNTAACAVRAVKELPMRSFSLYGGVEHHQLLRSVMRLSVTLTALRHPYAIPFYVPPRDVVERPTRRVTMEEGSDGHKVESAQVYPNNEKMPAVGLPIPISGGIKGNDGHSKRREEEGNIKAAYQSTTPMESKTVATPQRQPQQFEGTAEKYCESSVSPAVSQKQKPQAEPTASQAPLTLTVSADDDDDDVEIPEIDMED
Protein: Eukaryotic translation initiation factor 4 gamma 2 (Q5KTT7)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
Sequence:
MESVIAEGGASRFSASSGGGGGRGATQHYPKSVGNSEFLGKTPGPSVQRWVPSRSTRRDVNSSNEKERHDAIFRKVRGILNKLTPEKFDKLCLELLNVGVDSKLVLKGIILLIVDKALEEPKYSSLYAQLCLRLAEDAPNFDGPSTEIQSSQKQSTTFRRLLISKLQDEFENRTRNVDIYDKNDSPLTSEEEEQRAIAKIKMLGNIKFIGELGKLDLIHESILHKCIKTLLEKKKRVQLKDMGEDLECLCQIMRTVGPRLDHEKAKSLMDQYFGRMRSLMNNKDLPARIRFLLQDTVELRENNWVPRKAFIDNGPKTINQIRQDAVKDLGVFIPPMTQGIRTDFFQENSFMPTRIKPDRETLGGLADMFGQMPGSGIGTGPGVIQDRYSPTMGRRTNPLFNGHSGHMAPAPQPFIKSNQGQNLLFQNQTHSSQQQAQSKDMPPRFTKKGQLNADEISLRPAQSFILNKNQMPKLQPQIPTMIPPSAQPPRTSTPPLGQPPQLGLKTNPPPIQEKPQKTIKKPPPAKEELLKMTETVVTSYLSSKNMNDAVNGVREMKAPKHFLPEMLSKMIICSLENPDEDREHVSTLINKLRVEGLVSGENFLQAFLNVLDQCSKIELDVPLVKSYLAQFAARAVIAELVSMAELAHPLENGTHFPLFLLCLQQMAKLKDREWLTDLFQQSKVNMQKMLPEIDQNKDRMLEILEGKGLSFLFPLMKLEKELLKQIKADPAPQTIYKWIKDNISPKLHTDRGFVNILMTSFLQYIFHEMYATDDEEQLSAPTKEQLDQEKQLLLAFKPVMQKFLHDHVELQVSALYALQVHCNAHAFPKGMLLRYFVNFYDMEIIEEEAFLAWKEDITQEFPGKGKALFQVNQWLMWLETAEEEESEEEAD
Protein: Carnitinyl-CoA dehydratase (EC 4.2.1.149) (Crotonobetainyl-CoA hydratase) (P31551)
Organism: Escherichia coli (strain K12)
Function: Catalyzes the reversible dehydration of L-carnitinyl-CoA to crotonobetainyl-CoA. Can also hydrate crotonyl-CoA to hydroxybutyryl-CoA.
Interaction partners:
- Crotonobetainyl-CoA reductase
- Crotonobetaine/carnitine--CoA ligase
- Carnitine operon protein CaiE
- L-carnitine CoA-transferase
- 3-hydroxyadipyl-CoA dehydrogenase
- L-carnitine/gamma-butyrobetaine antiporter
- Protein FixB
- Probable acyl-CoA dehydrogenase YdiO
- Uncharacterized protein YkgL
- Protein FixA
Sequence:
MSESLHLTRNGSILEITLDRPKANAIDAKTSFEMGEVFLNFRDDPQLRVAIITGAGEKFFSAGWDLKAAAEGEAPDADFGPGGFAGLTEIFNLDKPVIAAVNGYAFGGGFELALAADFIVCADNASFALPEAKLGIVPDSGGVLRLPKILPPAIVNEMVMTGRRMGAEEALRWGIVNRVVSQAELMDNARELAQQLVNSAPLAIAALKEIYRTTSEMPVEEAYRYIRSGVLKHYPSVLHSEDAIEGPLAFAEKRDPVWKGR
Protein: Kynurenine formamidase (KFA) (KFase) (EC 3.5.1.9) (Arylformamidase) (N-formylkynurenine formamidase) (FKF) (Q9I234)
Organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Function: Catalyzes the hydrolysis of N-formyl-L-kynurenine to L-kynurenine, the second step in the kynurenine pathway of tryptophan degradation.
Interaction partners:
- Kynureninase
- Tryptophan 2,3-dioxygenase
- Formate dehydrogenase-O, major subunit
- Nitrate-inducible formate dehydrogenase, gamma subunit
- Formate dehydrogenase iron-sulfur subunit
- Probable amino acid permease
- Malate synthase G
- Fumarate hydratase class I
- Probable transcarboxylase subunit
- Biotin carboxylase
Sequence:
MTSLRYWDISPALDPNTPTWPGDTPFQQEWAARLDEQCPVNVGRITLSPHTGAHVDGPLHYRADGLPIGQVPLDIYMGPCRVIHCIGANPLVTPEHLAGQLDDLPSRVLLRTFERVPANWPEGFCAIAPATIECLAERGVRLVGIDTPSLDPQHSKTLDAHHAVGRHGMAILEGVVLDDVPAGDYELLALPLKFTHLDASPVRAVLRALPTAE
Protein: Cyclopropane mycolic acid synthase 3 (CMAS) (EC 2.1.1.79) (Cyclopropane-fatty-acyl-phospholipid synthase) (CFA synthase) (Cyclopropane fatty acid synthase) (Mycolic acid methyltransferase) (MA-MT) (S-adenosylmethionine-dependent methyltransferase) (AdoMet-MT) (SAM-MT) (P9WPB3)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: Involved in the phagosome maturation block (PMB). Catalyzes the conversion of a double bond to a cyclopropane ring at the proximal position of an alpha mycolic acid via the transfer of a methylene group from S-adenosyl-L-methionine. It can use cis, cis 11,14-eicosadienoic acid and linoelaidic acid as substrate. Cyclopropanated mycolic acids are key factors participating in cell envelope permeability, host immunomodulation and persistence.
Subcellular location: Cytoplasm {ECO:0000250}.
Interaction partners:
- Uncharacterized HTH-type transcriptional regulator Rv0472c
Sequence:
MSVQLTPHFGNVQAHYDLSDDFFRLFLDPTQTYSCAYFERDDMTLQEAQIAKIDLALGKLNLEPGMTLLDIGCGWGATMRRAIEKYDVNVVGLTLSENQAGHVQKMFDQMDTPRSRRVLLEGWEKFDEPVDRIVSIGAFEHFGHQRYHHFFEVTHRTLPADGKMLLHTIVRPTFKEGREKGLTLTHELVHFTKFILAEIFPGGWLPSIPTVHEYAEKVGFRVTAVQSLQLHYARTLDMWATALEANKDQAIAIQSQTVYDRYMKYLTGCAKLFRQGYTDVDQFTLEK
Protein: FAD-linked sulfhydryl oxidase ERV1 (AtErv1) (EC 1.8.3.2) (Mitochondrial sulfhydryl oxidase ERV1) (Q8GXX0)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: FAD-dependent sulfhydryl oxidase that catalyzes disulfide bond formation. Oxidizes thioredoxin in vitro. Required for the import and folding of small cysteine-containing proteins in the mitochondrial intermembrane space. Forms a redox cycle with MIA40 that involves a disulfide relay system. Important for maintaining the cysteine residues in MIA40 in an oxidized state (By similarity).
Subcellular location: Mitochondrion {ECO:0000269|PubMed:14996837}.
Interaction partners:
- Mitochondrial intermembrane space import and assembly protein 40 homolog
- Mitochondrial import inner membrane translocase subunit TIM9
- Mitochondrial import inner membrane translocase subunit TIM10
- Mitochondrial import inner membrane translocase subunit TIM50
- Mitochondrial import inner membrane translocase subunit TIM13
- Cytochrome c oxidase copper chaperone 1
- Mitochondrial import inner membrane translocase subunit TIM8
- Cytochrome C oxidase assembly factor
- Mitochondrial import receptor subunit TOM40-1
- Endoplasmic reticulum oxidoreductin-1
Sequence:
MGEKPWQPLLQSFEKLSNCVQTHLSNFIGIKNTPPSSQSTIQNPIISLDSSPPIATNSSSLQKLPLKDKSTGPVTKEDLGRATWTFLHTLAAQYPEKPTRQQKKDVKELMTILSRMYPCRECADHFKEILRSNPAQAGSQEEFSQWLCHVHNTVNRSLGKLVFPCERVDARWGKLECEQKSCDLHGTSMDF
Protein: Centrosomal protein 112 (A0A8I5ZS92)
Organism: Rattus norvegicus (Rat)
Interaction partners:
Sequence:
MRPLRDIGPSIPKENMANSRLKQIEKEYTQKLAKSSQIIAELQTTISSLKEESSRQQLAAERRLQDVIQKFEDEKQQLIRDNDQAIKALQDELETRSNQVRSAEKKLQHKELEAQEQMMYIRQEYETKFKGLMPASLRQELEDTISSLKSQVNFLQKRASILQEELTTYQSRR
Protein: Anoctamin (A0A8I5ZRU7)
Organism: Rattus norvegicus (Rat)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004651}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}. Membrane {ECO:0000256|RuleBase:RU280814}; Multi-pass membrane protein {ECO:0000256|RuleBase:RU280814}.
Interaction partners:
Sequence:
MQMMTRNVLLNMELEEDDDEDGDIVLENFDQTIVCSTFGSLESQEDFRTPEFEEFNGKPDSLFFTDGQRRIDFVLVYEDESKKENNKKGTNEKQKRKRQAYESNLISHGLQLEATRSVSDDKLVFVKVHAPWEVLCTYAEIMHIKLPLKPNDLKTRSTFDTFNWFTKVLRVNESVIKPEQEFFTAPFEKSRMNDFYILDRDSFFNPATRSRIVYFILSRVKYQVMNNVNKFGINRLVSSGIYKAAFPLHDCKFNYKSEDPNCPSERYLLYREWAHPRSIYKKQPLDLIRKYYGEKIGIYFAWLGYYTQMLLLAAVVGVACFLYGYLNQDNCTWSKEVCDPDIGGQILMCPQCDRLCPFWRLNITCESSKKLCIFDSFGTLIFAVFMGVWVTLFLEFWKRRQAELEYEWDTVELQQEEQPRPEYEAQCNHVVINEITQEEERIPFTTCGKCIRITLCASAVFFWILLIIASVIGIIVYRLSVFIVFSTTLPKNPNGTDPIQKYLTPQMATSITASIISFIIIMILNTIYEKVAIMITNFELPRTQTDYENSLTMKMFLFQFVNYYSSCFYIAFFKGKFVGYPGDPVYWLGKYRNEECDPGGCLLELTTQLTIIMGGKAIWNNIQEVLLPWVMNLIGRYKRVSGSEKITPRWEQDYHLQPMGRLGLFYEYLEMIIQFGFVTLFVASFPLAPLLALVNNILEIRVDAWKLTTQFRRMVPEKAQDIGAWQPIMQGIAILAVVTNAMIIAFTSDMIPRLVYYWSFSIPPYGDHTYYTMDGYINNTLSVFNITDFKNTDKENPYIGLGNYTLCRYRDFRNPPGHPQEYKHNIYYWHVIAAKLAFIIVMEHVIYSVKFFISYAIPDVSKITKSKIKREKYLTQKLLHESHLKDLTKNMGLIAERIGGVADSSVRPKLE
Protein: Large ribosomal subunit protein uL6 (60S ribosomal protein L9) (P50882)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Small ribosomal subunit protein uS5
- Large ribosomal subunit protein P1
- Small ribosomal subunit protein uS3
- Small ribosomal subunit protein eS1
- Small ribosomal subunit protein eS12
- Large ribosomal subunit protein eL18
- Large ribosomal subunit protein uL1
- Large ribosomal subunit protein eL22
- Ribosomal protein S30, isoform A
- Large ribosomal subunit protein uL16
Sequence:
MRTINSNQCVKIPKDIKASVKARVVTITGTRGTLKRSFKHLALDMYMPDKRTLKVEKWFGTKKELAAVRTVCSHIENMIKGVTFGFQYKMRAVYAHFPINCVTSENNTVIEIRNFLGEKYIRRVEMAPGVTVVNSTAQKDELIVEGNDIESVSGSAALIQQSTTVKNKDIRKFLDGLYVSEKTTVVKLES
Protein: Atypical response regulator protein ChxR (Transcriptional regulatory protein) (A0A0H3MDW1)
Organism: Chlamydia trachomatis serovar L2 (strain ATCC VR-902B / DSM 19102 / 434/Bu)
Function: May be a global positive regulator of transcription. Binds a cis-acting element of its own promoter DNA sequence and is hence probably also involved in its own transcription activation. The recognition sequence is 5'-WHGAWNH-N(3-5)-WHGAWNH-3', where W is A/T, H is C/A/T, N is G/C/A/T and the linker length in the middle is 3 to 5 nucleotides.
Interaction partners:
Sequence:
MAGPKHVLLVSEHWDLFFQTKELLNPEEYRCTIGQQYKQELSADLVVCEYSLLPREIRSPKSLEGSFVLVLLDFFDEETSVDLLDRGFWYLIRPITPRILKSAISLFLSQHSLHSVPESIRFGPNVFYVLKLTVETPEGSVHLTPSESGILKRLLINKGQLCLRKHLLEEIKNHAKAIVARNVDVHIASLRKKLGAYGSRIVTLRGVGYLFSDDGDKKFSQQDTKLS