wanglab/gogpt-training-data huggingface dataset:
Protein: Probable N-succinyldiaminopimelate aminotransferase DapC (DAP-AT) (EC 2.6.1.17) (P9WPZ5)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: Involved in the lysine biosynthetic pathways. It catalyzes the transfer of an amino group from L-glutamate to N-succinyl-2-l-amino-6-oxoheptanedioate (N-succinyl-2-l-amino-6-ketopimelate) in a PLP-dependent reaction, yielding as products N-succinyl-l-2,6-diaminoheptanedioate (N-succinyl-diaminopimelate) and 2-oxoglutarate (Probable).
Subcellular location: Cytoplasm {ECO:0000305}.
Interaction partners:
- Putative succinyl-diaminopimelate desuccinylase DapE
- 2,3,4,5-tetrahydropyridine-2,6-dicarboxylate N-succinyltransferase
- Acetylornithine aminotransferase
- Diaminopimelate epimerase
- Aspartokinase
- Aspartate-semialdehyde dehydrogenase
- Diaminopimelate decarboxylase
- 4-hydroxy-tetrahydrodipicolinate synthase
- Putative acyltransferase Rv0859
- Probable fatty oxidation protein FadB
Sequence:
MTVSRLRPYATTVFAEMSALATRIGAVNLGQGFPDEDGPPKMLQAAQDAIAGGVNQYPPGPGSAPLRRAIAAQRRRHFGVDYDPETEVLVTVGATEAIAAAVLGLVEPGSEVLLIEPFYDSYSPVVAMAGAHRVTVPLVPDGRGFALDADALRRAVTPRTRALIINSPHNPTGAVLSATELAAIAEIAVAANLVVITDEVYEHLVFDHARHLPLAGFDGMAERTITISSAAKMFNCTGWKIGWACGPAELIAGVRAAKQYLSYVGGAPFQPAVALALDTEDAWVAALRNSLRARRDRLAAGLTEIGFAVHDSYGTYFLCADPRPLGYDDSTEFCAALPEKVGVAAIPMSAFCDPAAGQASQQADVWNHLVRFTFCKRDDTLDEAIRRLSVLAERPAT
Protein: Cyclin 1 (Q8IKK0)
Organism: Plasmodium falciparum (isolate 3D7)
Interaction partners:
- CDK-activating kinase assembly factor MAT1
- RNA polymerase II transcription factor B subunit 4, putative
- Cyclin-dependent kinase 2 homolog
- DNA 5'-3' helicase
- DNA 3'-5' helicase
- Transcription initiation factor IIE subunit alpha, putative
- BSD domain-containing protein
- General transcription factor IIH subunit 4
- General transcription factor IIH subunit
- DNA-directed RNA polymerase II subunit RPB3, putative
Sequence:
MNYPEDTTHMKKWFFKSRKEIDNICLKKYNDFKEEFKDYNIKIPKYNDVEKTKVYFCYQLVHFCEIKMLRPHIVECATILYNRFYLKEIILEYDPRILIFTCIVLAIKIEGYGRLYKINEFFNDIDINLDKVLEHENIVCSSLNFELNFLYTKECIFYIKSQFEKYINKYILEADKIDNSMETIINTICFNASKDCIKLIENFYTTFIYTPSQIALYCFTNNIKKNLNIANADMFILEFITNNNQILFQKMKNKIKEMDESYRTYIGLRNTFDDENTTRQIGETLDMCIDIYDILKKKKNSKKSKKKKLDNKEDNVTEPNKKLQVS
Protein: Kinesin (Q583I7)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MEASVGVEVAWSSEIVGSPQVGGYLQLVKQAQPVDVASDAVPSNTSDLVEGMSSSTSLSSVEMITTQHTRRFDGDGWKCVLDNHMVALCDVFVKDAAAACDVPLENVALRELRLGSLYVTFHVTHDADIDEEEIQQRVDLYPFREVMRLYANRDAPPDGVDALLKRNAELEAETKAMIARLKDENDKRIEKLIRDHEKALKDLQEKVDERERELVGINNDLEALLQQMTEQKNSLEEERKKAIEAIKRERARNEKLAHRNSELVAAIIQENKKEMEAKEREFEEQLLEKDVVIENLRAKLRTKNEATNGDVPHAGRSPMSNADPDRAEEFAKLMGRMEEMAIVLEKTQESETEARSEIQKLSEALKLSEEARQSDAVIYENNTLALKQQLQSFWDTKLAEDHQKRQEESRARRGASGVRGEKTNETIVKQYEAALENIIRTLQDRLTILREEHASFIKVSEKETINERDILNENEAESQRVRQTFRTVSLTLQRVFWGTRDDEVPPLITELDNAAACSEKSRASVKMTLALLDSRLQSFVEQKEWMETHQQALEELMTSLRTLNKRAFERQLSLMNEQSARLPSAP
Protein: Spore coat protein W (Q08310)
Organism: Bacillus subtilis (strain 168)
Interaction partners:
- Spore coat protein V
- Spore coat protein X
- Spore coat protein Y
- Spore coat protein Z
- Spore coat protein G
- Spore coat protein T
- Spore protein CgeB
- Sporulation-specific transcription factor SpoVIF
- Spore crust protein CgeA
- Spore coat protein B
Sequence:
MSDNDKFKEELAKLPEVDPMTKMLVQNIFSKHGVTKDKMKKVSDEEKEMLLNLVKDLQAKSQALIENQKKKKEEAAAQEQKNTKPLSRREQLIEQIRQRRKNDNN
Protein: Aldehyde dehydrogenase 5, mitochondrial (EC 1.2.1.-) (EC 1.2.1.4) (P40047)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Minor mitochondrial aldehyde dehydrogenase isoform. Plays a role in regulation or biosynthesis of electron transport chain components. Involved in the biosynthesis of acetate during anaerobic growth on glucose.
Subcellular location: Mitochondrion matrix {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:14576278, ECO:0000269|PubMed:9473035}.
Interaction partners:
- Acetyl-coenzyme A synthetase 1
- Acetyl-coenzyme A synthetase 2
- Polyamine oxidase FMS1
- Acetyl-CoA hydrolase
- NADP-dependent alcohol dehydrogenase 6
- 4-aminobutyrate aminotransferase
- Alcohol dehydrogenase 4
- NADP-dependent alcohol dehydrogenase 7
- Glutamate decarboxylase
- Probable amidase
Sequence:
MLSRTRAAAPNSRIFTRSLLRLYSQAPLRVPITLPNGFTYEQPTGLFINGEFVASKQKKTFDVINPSNEEKITTVYKAMEDDVDEAVAAAKKAFETKWSIVEPEVRAKALFNLADLVEKHQETLAAIESMDNGKSLFCARGDVALVSKYLRSCGGWADKIYGNVIDTGKNHFTYSIKEPLGVCGQIIPWNFPLLMWSWKIGPALATGNTVVLKPAETTPLSALFASQLCQEAGIPAGVVNILPGSGRVVGERLSAHPDVKKIAFTGSTATGRHIMKVAADTVKKVTLELGGKSPNIVFADADLDKAVKNIAFGIFYNSGEVCCAGSRIYIQDTVYEEVLQKLKDYTESLKVGDPFDEEVFQGAQTSDKQLHKILDYVDVAKSEGARLVTGGARHGSKGYFVKPTVFADVKEDMRIVKEEVFGPIVTVSKFSTVDEVIAMANDSQYGLAAGIHTNDINKAVDVSKRVKAGTVWINTYNNFHQNVPFGGFGQSGIGREMGEAALSNYTQTKSVRIAIDKPIR
Protein: Urease subunit gamma (EC 3.5.1.5) (Urea amidohydrolase subunit gamma) (A0A0H3LA58)
Organism: Mycobacterium tuberculosis (strain ATCC 35801 / TMC 107 / Erdman)
Subcellular location: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00739, ECO:0000256|RuleBase:RU003850}.
Interaction partners:
Sequence:
MRLTPHEQERLLLSYAAELARRRRARGLRLNHPEAIAVIADHILEGARDGRTVAELMASGREVLGRDDVMEGVPEMLAEVQVEATFPDGTKLVTVHQPIA
Protein: Nitric oxide synthase 1 (EC 1.14.13.39) (Constitutive NOS) (NC-NOS) (NOS type I) (Neuronal NOS) (N-NOS) (nNOS) (Nitric oxide synthase, brain) (bNOS) (Peptidyl-cysteine S-nitrosylase NOS1) (Q9Z0J4)
Organism: Mus musculus (Mouse)
Function: Produces nitric oxide (NO) which is a messenger molecule with diverse functions throughout the body. In the brain and peripheral nervous system, NO displays many properties of a neurotransmitter. Probably has nitrosylase activity and mediates cysteine S-nitrosylation of cytoplasmic target proteins such SRR. Isoform NNOS Mu may be an effector enzyme for the dystrophin complex.
Subcellular location: Cell membrane, sarcolemma {ECO:0000269|PubMed:7545544}; Peripheral membrane protein {ECO:0000255}. Cell projection, dendritic spine {ECO:0000250|UniProtKB:P29476}. Note=In skeletal muscle, it is localized beneath the sarcolemma of fast-twitch muscle fiber by associating with the dystrophin glycoprotein complex (PubMed:7545544). In neurons, enriched in dendritic spines (By similarity). {ECO:0000250|UniProtKB:P29476, ECO:0000269|PubMed:7545544}.
Interaction partners:
- Calmodulin-like protein 3
- Calmodulin-like protein 4
- Calmodulin-1
- Calmodulin 5
- Calmodulin-4
- Carboxyl-terminal PDZ ligand of neuronal nitric oxide synthase protein
- Disks large homolog 4
- Glutamate receptor ionotropic, NMDA 1
- Glutamate receptor ionotropic, NMDA 2B
- Alpha-1-syntrophin
Sequence:
MEEHTFGVQQIQPNVISVRLFKRKVGGLGFLVKERVSKPPVIISDLIRGGAAEQSGLIQAGDIILAVNDRPLVDLSYDSALEVLRGIASETHVVLILRGPEGFTTHLETTFTGDGTPKTIRVTQPLGTPTKAVDLSRQPSASKDQPLAVDRVPGPSNGPQHAQGRGQGAGSVSQANGVAIDPTMKNTKANLQDSGEQDELLKEIEPVLSILTGGGKAVNRGGPAKAEMKDTGIQVDRDLDGKLHKAPPLGGENDRVFNDLWGKGNVPVVLNNPYSENEQSPASGKQSPTKNGSPSRCPRFLKVKNWETDVVLTDTLHLKSTLETGCTEQICMGSIMLPSHHIRKSEDVRTKDQLFPLAKEFLDQYYSSIKRFGSKAHMDRLEEVNKEIESTSTYQLKDTELIYGAKHAWRNASRCVGRIQWSKLQVFDARDCTTAHGMFNYICNHVKYATNKGNLRSAITIFPQRTDGKHDFRVWNSQLIRYAGYKQPDGSTLGDPANVEFTEICIQQGWKPPRGRFDVLPLLLQANGNDPELFQIPPELVLEVPIRHPKFDWFKDLGLKWYGLPAVSNMLLEIGGLEFSACPFSGWYMGTEIGVRDYCDNSRYNILEEVAKKMDLDMRKTSSLWKDQALVEINIAVLYSFQSDKVTIVDHHSATESFIKHMENEYRCRGGCPADWVWIVPPMSGSITPVFHQEMLNYRLTPSFEYQPDPWNTHVWKGTNGTPTKRRAIGFKKLAEAVKFSAKLMGQAMAKRVKATILYATETGKSQAYAKTLCEIFKHAFDAKAMSMEEYDIVHLEHEALVLVVTSTFGNGDPPENGEKFGCALMEMRHPNSVQEERKSYKVRFNSVSSYSDSRKSSGDGPDLRDNFESTGPLANVRFSVFGLGSRAYPHFCAFGHAVDTLLEELGGERILKMREGDELCGQEEAFRTWAKKVFKAACDVFCVGDDVNIEKANNSLISNDRSWKRNKFRLTYVAEAPELTQGLSNVHKKRVSAARLLSRQNLQSPKSSRSTIFVRLHTNGNQELQYQPGDHLGVFPGNHEDLVNALIERLEDAPPANHVVKVEMLEERNTALGVISNWKDESRLPPCTIFQAFKYYLDITTPPTPLQLQQFASLATNEKEKQRLLVLSKGLQEYEEWKWGKNPTMVEVLEEFPSIQMPATLLLTQLSLLQPRYYSISSSPDMYPDEVHLTVAIVSYHTRDGEGPVHHGVCSSWLNRIQADDVVPCFVRGAPSFHLPRNPQVPCILVGPGTGIAPFRSFWQQRQFDIQHKGMNPCPMVLVFGCRQSKIDHIYREETLQAKNKGVFRELYTAYSREPDRPKKYVQDVLQEQLAESVYRALKEQGGHIYVCGDVTMAADVLKAIQRIMTQQGKLSEEDAGVFISRLRDDNRYHEDIFGVTLRTYEVTNRLRSESIAFIEESKKDTDEVFSS
Protein: WH2 domain-containing protein (Q87GE5)
Organism: Vibrio parahaemolyticus serotype O3:K6 (strain RIMD 2210633)
Interaction partners:
Sequence:
MLKIKLPQQTSLAPSSETTQRLPVKISIKSICNKSICKTLHSLADKCHRFSKEIKQRSANHTPSSSHENLTTINLKSQNSAATFESTVELSIKHGSSIPPAPPLPGAIPPAPPLNLSKGAPKSSSNSLDSVNEDHSKLMEQIRQGVKLKSATKSLSADKSSADAHSKLMEELLTGGRKLKKVATSDIPAPPPLPSASTSKSPDSRNALLSEIAGFSKDRLRKTGSLETLNSSQSKDKESFEPTTHERLLSEDLFKQSPKLSEQELDELANNLADYLFQAADIDWHQVISEKTRGLTTEEMAKSEHRYVQAFCREILKYPDCYKSADVASPESPKSGGGSVIDVALKRLQTGRERLFTTTDEKGNRELKKGDAILESAINAARMAISTEEKNTILSNNVKSATFEVFCELPCMDGFAEQNGKTAFYALRAGFYSAFKNTDTAKQDITKFMKDNLQAGFSGYSYQGLTNRVAQLEAQLAALSAKLS
Protein: Trehalose-phosphate phosphatase A (AtTPPA) (EC 3.1.3.12) (Trehalose 6-phosphate phosphatase) (O64896)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Removes the phosphate from trehalose 6-phosphate to produce free trehalose. Trehalose accumulation in plant may improve abiotic stress tolerance.
Interaction partners:
- Alpha,alpha-trehalose-phosphate synthase 1
- Trehalase
- Probable alpha,alpha-trehalose-phosphate synthase 10
- Alpha,alpha-trehalose-phosphate synthase 5
- Probable alpha,alpha-trehalose-phosphate synthase 2
- Probable alpha,alpha-trehalose-phosphate synthase 4
- Alpha,alpha-trehalose-phosphate synthase 6
- Probable alpha,alpha-trehalose-phosphate synthase 9
- Probable alpha,alpha-trehalose-phosphate synthase 7
- Probable alpha,alpha-trehalose-phosphate synthase 3
Sequence:
MDMKSGHSSPVMTDSPPISNSRLTIRQNRLPYSSAAATAISQNNNLLLTVPRKKTGILDDVKSNGWLDAMKSSSPPPTILNKDNLSNDATDMTYREWMQLKYPSALTSFEKIMSFAKGKRIALFLDYDGTLSPIVEEPDCAYMSSAMRSAVQNVAKYFPTAIISGRSRDKVYEFVNLSELYYAGSHGMDIMSPAGESLNHEHSRTVSVYEQGKDVNLFQPASEFLPMIDKVLCSLIESTKDIKGVKVEDNKFCISVHYRNVEEKNWTLVAQCVDDVIRTYPKLRLTHGRKVLEIRPVIDWDKGKAVTFLLESLGLNNCEDVLPIYVGDDRTDEDAFKVLRDGPNHGYGILVSAVPKDSNAFYSLRDPSEVMEFLKSLVTWKRSMG
Protein: Probable membrane glycine and proline rich protein (O53445)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Interaction partners:
- Fumarate hydratase class II
- Fructose-1,6-bisphosphatase class 2
Sequence:
MTVPPAGPYGNYPYGPNTYGQDPYWGGQPQGGSYPPAYPPQQYPPGWPAGPYPPGPPPPGPGSKTPWLILAGLAVLGVILLVVILVIGLRGDNKSTTATSPATSAPTSQPFSQQTATGCTPNVSGGVQPIGDSISAGKLSFPTSAAPGWSAFSDDQNPNLIDAVGVGHEVAGADQWMMQAEVAITNFVTTMDVAAQASKLMQCVADGPGYAGSSPTLGPTKTSSITVDGVRAARVDADITIADSSRNVKGDSVTIIAVDTKPVTVFLGATPIGDATSRATVERVIEALKVNKS
Protein: Phosphatidylinositol N-acetylglucosaminyltransferase subunit A (EC 2.4.1.198) (GlcNAc-PI synthesis protein) (Phosphatidylinositol-glycan biosynthesis class A protein) (Q94BX4)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Necessary for the synthesis of N-acetylglucosaminyl-phosphatidylinositol, the very early intermediate in GPI-anchor biosynthesis (Probable). Required for pollen germination and pollen tube growth.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000255}.
Interaction partners:
- Phosphatidylinositol N-acetylglucosaminyltransferase subunit C
- N-acetylglucosaminyl transferase component family protein / Gpi1 family protein
- Phosphatidylinositolglycan-like protein
- Dolichol-phosphate mannose synthase subunit 2
- Phosphatidylinositol N-acetylglucosaminyltransferase subunit P
- Phosphatidylinositol N-acetylglucosaminyltransferase, GPI19/PIG-P subunit
- N-acetylglucosaminylphosphatidylinositol deacetylase
- N-acetylglucosaminylphosphatidylinositol deacetylase
- Mannosyltransferase APTG1
- GPI mannosyltransferase 1
Sequence:
MAEPPKLRVLMVSDFFFPNFGGVENHIYYLSQCLLKLGHKVVVMTHAYGNRSGVRYMTGGLKVYYVPWRPFVMQTTFPTVYGTLPIVRTILRREKITVVHGHQAFSTLCHEALMHARTMGYKVVFTDHSLYGFADVGSIHMNKVLQFSLADIDQAICVSHTSKENTVLRSGLSPAKVFMIPNAVDTAMFKPASVRPSTDIITIVVISRLVYRKGADLLVEVIPEVCRLYPNVRFVVGGDGPKHVRLEEMREKHSLQDRVEMLGAVPHSRVRSVLVTGHIFLNSSLTEAFCIAILEAASCGLLTVSTRVGGVPEVLPDDMVVLAEPDPDDMVRAIEKAISILPTINPEEMHNRMKKLYSWQDVAKRTEIVYDRALKCSNRSLLERLMRFLSCGAWAGKLFCMVMILDYLLWRLLQLLQPDEDIEEAPDICLCHHRGVEVSEGLRKKIK
Protein: Cytochrome c oxidase subunit Vb (Os01g0612200 protein) (cDNA clone:J023089B16, full insert sequence) (P92683)
Organism: Oryza sativa subsp. japonica (Rice)
Interaction partners:
- Cytochrome c oxidase
- Cytochrome c oxidase subunit
- Complex III subunit 9
- Cytochrome c oxidase subunit
- Cytochrome c oxidase subunit 6b
- Cytochrome c oxidase subunit 3
- Cytochrome b-c1 complex subunit 6
- Complex III subunit VII
- Cytochrome b-c1 complex subunit 7
- Cytochrome b-c1 complex subunit 7
Sequence:
MWRRLQTLAPALRRAASASASAAASGAAGPASLARAAPLSTAAAAAFRRTSPLLSGDKPATVEDVMPIATGLEREELAAELKGEKRFDMDPPVGPFGTKEAPAVIESYYNKRIVGCPGGEGEDEHDVVWFWLKKDEPHECPVCSQYFVLKVIGDGGDPDGHDDDDEHHH
Protein: HFE protein (Homeostatic iron regulator) (Q6B0J5)
Organism: Homo sapiens (Human)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004251}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004251}.
Interaction partners:
Sequence:
MGPRARPALLLLMLLQTAVLQGRLLRSHSLHYLFMGASEQDLGLSLFEALGYVDDQLFVFYDHESRRVEPRTPWVSSRISSQMWLQLSQSLKGWDHMFTVDFWTIMENHNHSKESHTLQVILGCEMQEDNSTEGYWKYGYDGQDHLEFCPDTLDWRAAEPRAWPTKLEWERHKIRARQNRAYLERDCPAQLQQLLELGRGVLDQQEGSESSSLPGKVTTLRCRALNYYPQNITMKWLKDKQPMDAKEFEPKDVLPNGDGTYQGWITLAVPPGEEQRYTCQVEHPGLDQPLIVIWEPSPSGTLVIGVISGIAVFVVILFIGILFIILRKRQGSRGAMGHYVLAERE
Protein: Uncharacterized protein (Q57X15)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MVEKKQAKKQRIRMTNKAVEGLRFSTVRMPAKSEVQKQQTDISRLISDHEDKRSGDSTRENGEEGARGRSSGNGRTRQVGSAAFDPIPNDPMFFIVEKSKYWPPPSLEDLHKSVGVEMSGDGFDPYDRREDDEQARQARTKIVRGELNHPRGKPRKNTLVKLESSSGSDTDSDK
Protein: Cyclin dependent kinase 16 (E5RIU4)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MDRMKKIKRQLSMTLRGGRGIDKTNGAPEQIGLDESGGGGGSDPGEAPTRAAPGELRSARGPLSSAPEIVHEDLKMGSDGESDQASATSSDEVQSPVRVRMRNHPPRKISTEDINKRLSLPADIRLPEGYLEKLTLNSPIFDKPLSRRLRRVS
Protein: Alpha-actinin-1 (Alpha-actinin cytoskeletal isoform) (F-actin cross-linking protein) (Non-muscle alpha-actinin-1) (Q9Z1P2)
Organism: Rattus norvegicus (Rat)
Function: F-actin cross-linking protein which is thought to anchor actin to a variety of intracellular structures. This is a bundling protein (By similarity).
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000269|PubMed:21210813}. Cytoplasm, myofibril, sarcomere, Z line {ECO:0000250|UniProtKB:P12814}. Cell membrane {ECO:0000269|PubMed:21210813}. Cell junction {ECO:0000269|PubMed:21210813}. Cell projection, ruffle {ECO:0000250|UniProtKB:Q7TPR4}. Note=Colocalizes with MYOZ2 and PPP3CA at the Z-line of heart and skeletal muscle. Colocalizes with PSD in membrane ruffles and central reticular structures. {ECO:0000250|UniProtKB:Q7TPR4}.
Interaction partners:
- Alpha-actinin-4
- Actin, cytoplasmic 2
- Zyxin
- Actin, cytoplasmic 1
- Catenin alpha-1
- Catenin alpha-2
- Vinculin
- Parvin, beta
- Membrane-associated guanylate kinase, WW and PDZ domain-containing protein 1
- Catenin alpha 3
Sequence:
MDHYDSQQTNDYMQPEEDWDRDLLLDPAWEKQQRKTFTAWCNSHLRKAGTQIENIEEDFRDGLKLMLLLEVISGERLAKPERGKMRVHKISNVNKALDFIASKGVKLVSIGAEEIVDGNVKMTLGMIWTIILRFAIQDISVEETSAKEGLLLWCQRKTAPYKNVNIQNFHISWKDGLGFCALIHRHRPELIDYGKLRKDDPLTNLNTAFDVAERYLDIPKMLDAEDIVGTARPDEKAIMTYVSSFYHAFSGAQKAETAANRICKVLAVNQENEQLMEDYEKLASDLLEWIRRTIPWLENRVPENTMQAMQQKLEDFRDYRRLHKPPKVQEKCQLEINFNTLQTKLRLSNRPAFMPSEGRMVSDINNAWGCLEQAEKGYEEWLLNEIRRLERLDHLAEKFRQKASIHEAWTDGKEAMLRQKDYETATLSEIKALLKKHEAFESDLAAHQDRVEQIAAIAQELNELDYYDSPSVNARCQKICDQWDNLGALTQKRREALERTEKLLETIDQLYLEYAKRAAPFNNWMEGAMEDLQDTFIVHTIEEIQGLTTAHEQFKATLPDADKERLAILGIHNEVSKIVQTYHVNMAGTNPYTTITPQEINGKWDHVRQLVPRRDQALTEEHSRQQHNERLRKQFGAQANVIGPWIQTKMEEIGRISIEMHGTLEDQLSHLRQYEKSIVNYKPKIDQLEGDHQLIQEALIFDNKHTNYTMEHIRVGWEQLLTTIARTINEVENQILTRDAKGISQEQMNEFRASFNHFDRDHSGTLGPEEFKACLISLGYDIGNDPQGEAEFARIMSIVDPNRLGVVTFQAFIDFMSRETADTDTADQVMASFKILAGDKNYITGDELRRELPPDQAEYCIARMAPYAGPDSVPGALDYMSFSTALYGESDL
Protein: Tafazzin family protein (A0A8I6ACA3)
Organism: Rattus norvegicus (Rat)
Subcellular location: Mitochondrion inner membrane {ECO:0000256|ARBA:ARBA00004137}; Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004137}; Intermembrane side {ECO:0000256|ARBA:ARBA00004137}. Mitochondrion outer membrane {ECO:0000256|ARBA:ARBA00024323}; Peripheral membrane protein {ECO:0000256|ARBA:ARBA00024323}; Intermembrane side {ECO:0000256|ARBA:ARBA00024323}.
Interaction partners:
Sequence:
MPLHVKWPFPAVPRLTWTLASSVVMGLVGTYSCFWTKYMNHLTVYNKEVLYELIENRGPATPLITVSNHQSCMDDPHLWGILKLRHIWNLKLMRWTPAAADICFTKELHSHFFSLGKCVPVCRGDGVYQKGMDFILEKLNHGDWVHIFPEGKVNMSSEFLRFKWGIGRLIAECHLNPIILPLWHVENHRADWEALQYTPCA
Protein: DDB1- and CUL4-associated factor 5 (Breakpoint cluster region protein 2) (BCRP2) (WD repeat-containing protein 22) (Q96JK2)
Organism: Homo sapiens (Human)
Function: Is a substrate receptor for the CUL4-DDB1 E3 ubiquitin-protein ligase complex (CRL4). The complex CRL4-DCAF5 is involved in the ubiquitination of a set of methylated non-histone proteins, including SOX2, DNMT1 and E2F1.
Interaction partners:
- DNA damage-binding protein 1
- Cullin-4A
- DDB1- and CUL4-associated factor 4
- Cullin-4B
- DDB1- and CUL4-associated factor 12
- DDB1- and CUL4-associated factor 10
- DNA damage-binding protein 2
- DDB1- and CUL4-associated factor 6
- DDB1- and CUL4-associated factor 16
- Short transient receptor potential channel 4-associated protein
Sequence:
MKRRAGLGGSMRSVVGFLSQRGLHGDPLLTQDFQRRRLRGCRNLYKKDLLGHFGCVNAIEFSNNGGQWLVSGGDDRRVLLWHMEQAIHSRVKPIQLKGEHHSNIFCLAFNSGNTKVFSGGNDEQVILHDVESSETLDVFAHEDAVYGLSVSPVNDNIFASSSDDGRVLIWDIRESPHGEPFCLANYPSAFHSVMFNPVEPRLLATANSKEGVGLWDIRKPQSSLLRYGGNLSLQSAMSVRFNSNGTQLLALRRRLPPVLYDIHSRLPVFQFDNQGYFNSCTMKSCCFAGDRDQYILSGSDDFNLYMWRIPADPEAGGIGRVVNGAFMVLKGHRSIVNQVRFNPHTYMICSSGVEKIIKIWSPYKQPGCTGDLDGRIEDDSRCLYTHEEYISLVLNSGSGLSHDYANQSVQEDPRMMAFFDSLVRREIEGWSSDSDSDLSESTILQLHAGVSERSGYTDSESSASLPRSPPPTVDESADNAFHLGPLRVTTTNTVASTPPTPTCEDAASRQQRLSALRRYQDKRLLALSNESDSEENVCEVELDTDLFPRPRSPSPEDESSSSSSSSSSEDEEELNERRASTWQRNAMRRRQKTTREDKPSAPIKPTNTYIGEDNYDYPQIKVDDLSSSPTSSPERSTSTLEIQPSRASPTSDIESVERKIYKAYKWLRYSYISYSNNKDGETSLVTGEADEGRAGTSHKDNPAPSSSKEACLNIAMAQRNQDLPPEGCSKDTFKEETPRTPSNGPGHEHSSHAWAEVPEGTSQDTGNSGSVEHPFETKKLNGKALSSRAEEPPSPPVPKASGSTLNSGSGNCPRTQSDDSEERSLETICANHNNGRLHPRPPHPHNNGQNLGELEVVAYSSPGHSDTDRDNSSLTGTLLHKDCCGSEMACETPNAGTREDPTDTPATDSSRAVHGHSGLKRQRIELEDTDSENSSSEKKLKT
Protein: Sperm mitochondrial-associated cysteine-rich protein (P49901)
Organism: Homo sapiens (Human)
Function: Involved in sperm motility. Its absence is associated with genetic background dependent male infertility. Infertility may be due to reduced sperm motility in the female reproductive tract and inability to penetrate the oocyte zona pellucida (By similarity).
Subcellular location: Cytoplasm. Mitochondrion membrane {ECO:0000305}; Peripheral membrane protein {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Note=Becomes associated with the spermatid mitochondrion capsule at step 16 of spermatogenesis. {ECO:0000250}.
Interaction partners:
- Selenoprotein P
Sequence:
MCDQTKHSKCCPAKGNQCCPPQQNQCCQSKGNQCCPPKQNQCCQPKGSQCCPPKHNHCCQPKPPCCIQARCCGLETKPEVSPLNMESEPNSPQTQDKGCQTQQQPHSPQNESRPSK
Protein: Protein RhsC (P16918)
Organism: Escherichia coli (strain K12)
Function: Rhs elements have a nonessential function. They may play an important role in the natural ecology of the cell.
Interaction partners:
- Uncharacterized protein YbfB
Sequence:
MSGKPAARQGDMTQYGGSIVQGSAGVRIGAPTGVACSVCPGGVTSGHPVNPLLGAKVLPGETDIALPGPLPFILSRTYSSYRTKTPAPVGSLGPGWKMPADIRLQLRDNTLILSDNGGRSLYFEHLFPGEDGYSRSESLWLVRGGVAKLDEGHRLAALWQALPEELRLSPHRYLATNSPQGPWWLLGWCERVPEADEVLPAPLPPYRVLTGLVDRFGRTQTFHREAAGEFSGEITGVTDGAGRHFRLVLTTQAQRAEEARQQAISGGTEPSAFPDTLPGYTEYGRDNGIRLSAVWLTHDPEYPENLPAAPLVRYGWTPRGELAAVYDRSNTQVRSFTYDDKYRGRMVAHRHTGRPEICYRYDSDGRVTEQLNPAGLSYTYQYEKDRITITDSLNRREVLHTQGEGGLKRVVKKEHADGSVTQSQFDAVGRLRAQTDAAGRTTEYSPDVVTGLITRITTPDGRASAFYYNHHSQLTSATGPDGLEIRREYDEWGRLIQETAPDGDITRYRYDNPHSDLPCATEDATGSRKTMTWSRYGQLLSFTDCSGYVTRYDHDRFGQVTAVHREEGLSQYRAYDSRGQLIAVKDTQGHETRYEYNAAGDLTTVIAPDGSRNGTQYDAWGKAICTTQGGLTRSMEYDAAGRVIRLTSENGSHTTFRYDVLDRLIQETGFDGRTQRYHHDLTGKLIRSEDEGLVTHWHYDEADRLTHRTVNGETAERWQYDERGWLTDISHISEGHRVTVHYGYDSKGRLASEHLTVHHPQTNELLWQHETRHAYNAQGLANRCIPDSLPAVEWLTYGSGWLSGMKLGDTPLVEYTRDRLHRETLRSFGRYELTTAYTPAGQLQSQHLNSLLSDRDYTWNDNGELIRISSPRQTRSYSYSTTGRLTGVHTTAANLDIRIPYTTDPAGNRLPDPELHPDSALSMWPDNRIARDAHYLYRYDRHGRLTEKTDLIPEGVIRTDDERTHRYHYDSQHRLVHYTRTQYAEPLVESRYLYDPLGRRVAKRVWRRERDLTGWMSLSRKPQVTWYGWDGDRLTTIQNDRTRIQTIYQPGSFTPLIRVETATGELAKTQRRSLADTLQQSGGEDGGSVVFPPVLVQMLDRLESEILADRVSEESRRWLASCGLTVAQMQSQMDPVYTPARKIHLYHCDHRGLPLALISTEGTTAWYAEYDEWGNLLNEENPHQLQQLIRLPGQQYDEESGLYYNRHRYYDPLQGRYITQDPIGLKGGWNFYQYPLNPISNIDPLGLETLKCIKPLHSMGGTGERSGPDIWGNPFYHQYLCVPDGKGDYTCGGQDQRGESKGDGLWGPGKASNDTKEAAGRCDLVETDNSCVENCLKGKFKEVRPRYSVLPDIFTPINLGLFKNCQDWSNDSLETCKMKCSGNNIGRFIRFVFTGVM
Protein: Multidrug transporter AQR1 (Drug:H(+) antiporter AQR1) (DHA AQR1) (Flucytosine exporter AQR1) (Q6FNQ2)
Organism: Candida glabrata (strain ATCC 2001 / BCRC 20586 / JCM 3761 / NBRC 0622 / NRRL Y-65 / CBS 138) (Yeast) (Nakaseomyces glabratus)
Function: Multidrug transporter acts as a determinant of resistance to acetic acid, flucytosine and clotrimazole, these 3 compounds acting synergistically against the pathogen. Reduces the intracellular accumulation of the antifungal agents flucytosine and, to a moderate extent, of clotrimazole. Its role in acetic acid resistance may be indirect, presumably through the transport of a still unidentified physiological substrate.
Subcellular location: Cell membrane {ECO:0000269|PubMed:23805133}; Multi-pass membrane protein {ECO:0000255}. Note=Also localizes to membrane vesicles (PubMed:23805133). {ECO:0000269|PubMed:23805133}.
Interaction partners:
Sequence:
MVESGPHSINDDLSTNEYIEQPKFYHDDHASDSNSLSDIDDDNKKHGGLYGTVSRTTTRELPEDLESEISSTHSQDAKEDLEIQHNAAPYSLLNYRDKWCMVALLTACGFWSSLGSPIYYPALKQLEKQFDIDENMVNITVVVYLLFQGLAPTCSGGLADKFGRRPVLLIGMLIYVVASIGLACAPSYGVIVFLRCVQSIGISPSIAISSGVVGDFTVKSERGTFVGATSGFVLLGQAFGSLIGAALAAAWDWRAIFWFLTIGCGASFAICFALLPETKRSIVGNLSIRPKNPLNIAPVTLLPAARRKLKYDNPDYETLDKTKPVFDLTSAFKICALPEIFLSLLPPGLAFAMWTLMLSAISSELSAAPYNYKLTIIGVCYLPAGIGGLIGSFATGKIIDFQYKKKLKVFEEKKAAGIIPEDEKFNIMGARLQSVLPQNFLCVVTYILFGWSCDKGWKIPSILITSCVSSFCAMSTLSAMSTLLVDLYPGKSSTASSCFNFMRCSLSAILMGCFAKMKHSLTVGGTFTLLAGLVFVGNFLMFIPMKHGMRWREEREQRAALKAKSMDQANENGYKLFSKIKFSSPFKSEEKV
Protein: ATP synthase F(1) complex catalytic subunit beta, mitochondrial (EC 7.1.2.2) (ATP synthase F1 subunit beta) (Q5ZLC5)
Organism: Gallus gallus (Chicken)
Function: Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core, and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Subunits alpha and beta form the catalytic core in F(1). Rotation of the central stalk against the surrounding alpha(3)beta(3) subunits leads to hydrolysis of ATP in three separate catalytic sites on the beta subunits.
Subcellular location: Mitochondrion inner membrane {ECO:0000250|UniProtKB:P00829}; Peripheral membrane protein {ECO:0000250|UniProtKB:P00829}; Matrix side {ECO:0000250|UniProtKB:P00829}.
Interaction partners:
- ATP synthase subunit gamma
- ATP synthase subunit d
- ATP synthase F1 subunit delta.
- ATP synthase peripheral stalk-membrane subunit b.
- Uncharacterized protein.
- ATP synthase subunit g
- ATP synthase subunit alpha
- ATP synthase subunit alpha
- ATP synthase-coupling factor 6
- Uncharacterized protein
Sequence:
MLGLAGRCSAAAASAARPALRRAAGPSHGFLPLLLSRGAGPAAAVGARRDHAAQAAPAAKAGSATGRIVAVIGAVVDVQFDEGLPPILNALEVQGRETRLVLEVAQHLGENTVRTIAMDGTEGLVRGQKVLDSGAPIRIPVGPETLGRIMNVIGEPIDERGPITTKQFAAIHAEAPEFVEMSVEQKILVTGIKVVDLLAPYAKGGKIGLFGGAGVGKTVLIMELINNVAKAHGGYSVFAGVGERTREGNDLYHEMIESGVINLKDATSKVALVYGQMNEPPGARARVALTGLTVAEYFRDQEGQDVLLFIDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATDMGTMQERITTTRKGSITSVQAIYVPADDLTDPAPATTFAHLDATTVLSRAIAELGIYPAVDPLDSTSRIMDPNIVGPEHYDVARGVQKILQDYKSLQDIIAILGMDELSEEDKLTVARARKIQRFLSQPFQVAEVFTGHMGKLVPLKETIKGFKQILAGEYDHLPEQAFYMVGPIEEAVAKAEKLAEEHA