wanglab/gogpt-training-data huggingface dataset:
Protein: 5'-nucleotidase, cytosolic IB (Q6AXN7)
Organism: Rattus norvegicus (Rat)
Interaction partners:
Sequence:
MSQTSLKTKKKNEPGMRYSKESLDAEKRKDSDKSGARLSTQGSQEIPVPNTDSRGYVVRNQWSRTSRSPSTRAPSVDENRSRNTVVKQAPNSSANSRTSSASASQHETSTSPPPQVSEKSPVQQPSPQTRTITPLDSQPPTPPETEPDSRRTSKMYTATDPWAHRDNREPRDLQLREYAHSCDSREGIPKTREYPRTPPTEWKSYVQRRLQYGSSVDMDPDCLPDGQHHRQKQQIEEDEVDEAYWSSVSMLYEKIPSCTRPRPPKPKHAITIAVSSRALFNMVDDRKIYEEEGLEKYMEYQLTNENVILTPGPAFRFVKALQHVNSRLRDLYPDEQDLFDIVLMTNNHAQVGVRLINSVNHYGLLIDRFCLTGGKSPIGYLKAYLTNLYLSADSEKVQEAIKEGIASATMFAGAKDMAYCDTQLRVAFDGDAVLFSDESEHIAKDHGLDKFFQHETLFENKPLAQGPLKGFLEDLGKLQKKFYAKDERLLCPIRTYLVTARSAASSGARVLKTLRRWGLEIDEALFLAGAPKGPILVKIRPHIFFDDQMFHIEAAQKFGTITAHVPYGIAQKRN
Protein: Wiskott-aldrich syndrome family protein, putative (DUF1118) (Q9SD79)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- B12D protein
- At2g46540/F11C10.23
- At1g72040
- MICOS complex subunit, putative
- At1g68680
- Mitochondrial import inner membrane translocase subunit TIM22-1
- Mitochondrial import inner membrane translocase subunit TIM22-4
Sequence:
MAAKLICSSLTVHSMANKKPSPSAATRTITSKKSTATPQVKLLTRVEQLKLLTKAEKAGLLSLAEKSGFSLSTIERLGLLTKAEEFGVLSAATNPETPGTLFTLSLGLLLLGPVFAYVVPEDYTWEVVIQVLVALLSVLGGSAAFAASGFVSNLQKSD
Protein: RNA editing complex protein (Q38B91)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- RNA editing complex protein MP46
- MP18 RNA editing complex protein
- RNA-editing ligase 2, mitochondrial
- RNA-editing-associated protein 1
- RNA editing complex protein MP61
- REH2-associated factor 1
- RNA editing 3' exouridylylase MP99
- RNA editing complex protein MP67
- REH2-associated factor 2
- RNA editing complex protein MP63
Sequence:
MRVRSLLLCIRRDPLQRAVDVAYASGMLLGSGSSRGTTHFSETTAFTSSNFAADLRGGRVGLAGDGGTKCDDRNGELVRGRIQFASRCAEGPFVGASPTVTSCAHIEGVVRQVECGYVGGDRVLQFIIEVEEVPASGGTPMRLPLAVRWRPGSEVAQNRMDEWQKEMERLVGRRVLASGRLQVEECFDSGSRRLYKTPSLVLPATSTVEMISLQELEC
Protein: Quick-to-court, isoform K (M9PC20)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MSLQLNGGSDISSSGTSSSSSNNKESSPRTTRTPRTPQTPQTPQTPASGVAASVAETPHSCIRQGNCVKANQVKLSTLHESKISPRTPPVTPDSPSTYLDDDIDSMYSFATTTSGRSTMSCEHPYVARNGTTFSGRKMKYVVHCSNYAGQVGPDYLTPTQRAQRQIRRLKELLCIARQDLEQKDTELLRLTREVVELRLFKASLSSPEERSASSDAVTVREAELKTSQDVSPIVDMVDEGNAKGSPRHLSRQQQQQANHSLQAMQMSAEMQSSYADSGHFEDLTMSSVHSKDSQTQSEACGTATPDGEADVGCGAGGDSASNLENYELQRQELISMYEHRIEELIRSQDSATSDLKRSHNDKVEALLQKLAECNTRYSDMVPDYEQAKQRIRELEKQLEDLQRKLIEHEEKQNKMYLHMYQQGQEAERISRADQALDLAQRQPESKVSINELLHQLQSTQDELENIRASECRMRECGSNHALLTAKEAISLWVLGARKTIYRRLLEAQKNRTHVDPEVTLQFLKSAIFYFLTDKENSQGHLQAIESILEFTDAEKQKISAANRTPKLHAKMSKTMSTILVRAKLHCFQLIGWRH
Protein: Transmembrane GTPase Marf (EC 3.6.5.-) (Mitochondrial assembly regulatory factor) (Mitofusin) (Q7YU24)
Organism: Drosophila melanogaster (Fruit fly)
Function: Mitochondrial outer membrane GTPase that mediates mitochondrial clustering and fusion. Mitochondrial fusion is the physical merging of mitochondria that gives rise to mitochondrial networks, and this process is counterbalanced by mitochondrial fission which fragments networks. Promotes, but is not required for park recruitment to dysfunctional mitochondria.
Subcellular location: Mitochondrion outer membrane {ECO:0000269|PubMed:26214738}; Multi-pass membrane protein {ECO:0000250}.
Interaction partners:
- E3 ubiquitin-protein ligase parkin
- Serine/threonine-protein kinase Pink1, mitochondrial
- Dynamin-like GTPase OPA1, mitochondrial
- Mitochondrial Rho GTPase
- Mitochondrial fission 1 protein
- Voltage-dependent anion-selective channel
- dynamin GTPase
- Dynamin
- Transmembrane GTPase fzo
- Cell death protein rpr
Sequence:
MAAYLNRTISMVTGQTGPADDDRHASSTDTVDKSGPGSPLSRFNSSLQQSGSTMAANLLPESRLYQSNDKSPLQIFVRAKKKINDIYGEIEEYVHETTTFINALHAEAEIVDKAERELFESYVYKVAAIREVLQRDHMKVAFFGRTSNGKSSVINAMLREKILPSGIGHTTNCFCQVEGSNGGEAYLMTEGSEEKLNVVNIKQLANALCQEKLCESSLVRIFWPRERCSLLRDDVVFVDSPGVDVSANLDDWIDNHCLNADVFVLVLNAESTMTRAEKQFFHTVSQKLSKPNIFILNNRWDASANEPECQESVKSQHTERCIDFLTKELKVSNEKEAAERVFFVSARETLQARIEEAKGNPPHMGAIAEGFQIRYFEFQDFERKFEECISQSAVKTKFQQHSSRGKSVSGDMKSMLDNIYERITIFRNLKQDQKNLLTERIQGTETQMMQVTREMKMKIHNMVEEVEEKVSKALNEEIWRLGVLIDEFNMPFHPERLVLNIYKKELNAHVESGLGSNLRARLSMALAMNVESAQTEMTDRMHALVPNEQLLATSTKMVVRTQPFEMLYSLNCQNLCADFQEDLEFKFSWGIAAMIQRFTGKVRERSKKGQPALVNRQSSIGHSVSTPTTTPVEATPVCLLPAPVVAGITPEQLSLISRFAVSSIGSQGTVGGLVVAGVMLKTIGWRVLVGVGALYGCIYLYERLSWTNSAKERTFKSQYVRHATKKLKMIVDLTSANCSHQVQQELSSTFARLCRTVDTATTDMNDELKTLDSQLNILEANQKQLKLLRNKANYIQNELDIFEHNYISPQ
Protein: Transcription factor bHLH28 (Basic helix-loop-helix protein 28) (AtbHLH28) (bHLH 28) (Transcription factor EN 40) (bHLH transcription factor bHLH028) (Q9LUK7)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00981}.
Interaction partners:
- Transmembrane protein
- Protein TIFY 3A
- TRF-like 8
- Uncharacterized protein
- At3g12470
- Putative F-box/LRR-repeat protein At3g59230
- CASP-like protein
- Gb|AAD55616.1
- B3 domain-containing protein At5g60130
- Probable inactive purple acid phosphatase 14
Sequence:
MINTDDNLLMIEALLTSDPSPPLLPANLSLETTLPKRLHAVLNGTHEPWSYAIFWKPSYDDFSGEAVLKWGDGVYTGGNEEKTRGRLRRKKTILSSPEEKERRSNVIRELNLMISGEAFPVVEDDVSDDDDVEVTDMEWFFLVSMTWSFGNGSGLAGKAFASYNPVLVTGSDLIYGSGCDRAKQGGDVGLQTILCIPSHNGVLELASTEEIRPNSDLFNRIRFLFGGSKYFSGAPNSNSELFPFQLESSCSSTVTGNPNPSPVYLQNRYNLNFSTSSSTLARAPCGDVLSFGENVKQSFENRNPNTYSDQIQNVVPHATVMLEKKKGKKRGRKPAHGRDKPLNHVEAERMRREKLNHRFYALRAVVPNVSKMDKTSLLEDAVCYINELKSKAENVELEKHAIEIQFNELKEIAGQRNAIPSVCKYEEKASEMMKIEVKIMESDDAMVRVESRKDHHPGARLMNALMDLELEVNHASISVMNDLMIQQANVKMGLRIYKQEELRDLLMSKIS
Protein: Pectate disaccharide-lyase (EC 4.2.2.9) (Exopolygalacturonate lyase) (ExoPL) (Q05526)
Organism: Dickeya dadantii (strain 3937) (Erwinia chrysanthemi (strain 3937))
Function: Catalyzes the formation of unsaturated digalacturonates from polygalacturonate or short oligogalacturonates.
Subcellular location: Cytoplasm.
Interaction partners:
- Oligogalacturonate lyase
- Exopolygalacturonate lyase PelX
- Pectinesterase A
- Pectate lyase C
- Pectate lyase B
- Pectinesterase B
- Pectate lyase A
- Pectate lyase E
- Pectate lyase D
- Oligogalacturonide ABC transporter, permease component
Sequence:
MSIFTDLNTSRKWQIDQWLSAVNSHIEKIQQYGHSVVNPTPLLADGFEIKTQSPVVWQFPDGHDAPISNFASQQNWLRLLISMSVITETEKYRHLAFCQSEYFLNRFVDENSGLFYWGGHRFINLDTLASEGPESKSMVHELKHHLPYYEFLHQVNPEKTRHFIQGFWNAHVEDWSCLDLGRHGDYARQRDPDVFLHSRHDVVTPANWPELPLTKGLTFVNAGTDLIYAAFVYARHTGDAHAAAWGKHLYRQYVLARNPETGMPVYQFSSPLQRQPVPADDNQTQSWFGDRAQRQFGPEFGAIAREANVLFRDMRPLLIDNPLAMLDILRHQPDAEILTWVIAGLKNYYQYAYDVNSNSLRPMWNNGQDMTDYCFKRDGYYGKAGTVLKPFPLEGDYLLPLVRAWLLSDDDDLHTLIVTMLSRLEKQGIHQSASPFLLLAITELAHAKQSAQWAEYAWQMAEILFKRYFHHGLFVRSEHHRYVRLDDPFPAILLTLIAACRNKWSEVPAVLTQGGYIHGDYRINGESRVIYDTEFIYPEKLIH
Protein: NADPH-dependent diflavin oxidoreductase 1 (EC 1.18.1.-) (NADPH-dependent FMN and FAD-containing oxidoreductase) (G5EGH9)
Organism: Caenorhabditis elegans
Subcellular location: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03178}.
Interaction partners:
Sequence:
MSIAILYGSETGTAQDIAESLRREAQQRHLQARVHELDEYDVSQLPMEKVVLFVVSTTGQGEMPPNMRKTWKLLLRKSLGADFLKNVNIGVLGLGDSSYQKYNFAGKKLYRRLVQLGAKMMCGVHLADDQHEIGIDGAFIPWKTECWKKIKEIAENLSIYREMTAEIDTSVQITTKYRFLELGGESGNDDDDSDEDLEPQIEIPDYFPLKVLKNRRLTSAEHFQDTRLVDFEISDRNRSKMGFQPGDVLMVRPYNPEETVKIAIEALGLTEEQLKKPLKIVKNDRFSKNPPNFLVGTKTTLLTCLQRYFDLQQVPKRSFFEMLGYYSTNPPEKERLQELASPEGLDDYLDYANRSRRTTAEALRDFVATSKNLKPDYLFEILTTIRPRAFSIASAPSPFHLELLVAKVEYKSRMADKRRGLCSTFISRLKPGDEVFCKIRPGTFKFPSPEAPVICIGPGTGVAPFRSLFGHRSLFSAHFPGILFFGCRSEHHDYYFSDEWPELSGVAVIPAFSRDTDGRKVYVQHKMGENAGKIKRMLDLGAQVFIAGSSGDMPKAVSAVLAQIQGDEWTRRAEETGKIQYETWS
Protein: Cruzioseptin-9 (CZS-9) (A0A193H327)
Organism: Cruziohyla calcarifer (Splendid leaf frog) (Agalychnis calcarifer)
Function: Has antimicrobial activity.
Subcellular location: Secreted {ECO:0000269|PubMed:27321580}.
Interaction partners:
Sequence:
KRGFLDVITHVGKAVGKAALNAVNEMVNQGEQ
Protein: Ras-related protein Ral-A (EC 3.6.5.2) (P11233)
Organism: Homo sapiens (Human)
Function: Multifunctional GTPase involved in a variety of cellular processes including gene expression, cell migration, cell proliferation, oncogenic transformation and membrane trafficking. Accomplishes its multiple functions by interacting with distinct downstream effectors. Acts as a GTP sensor for GTP-dependent exocytosis of dense core vesicles. The RALA-exocyst complex regulates integrin-dependent membrane raft exocytosis and growth signaling. Key regulator of LPAR1 signaling and competes with GRK2 for binding to LPAR1 thus affecting the signaling properties of the receptor. Required for anchorage-independent proliferation of transformed cells. During mitosis, supports the stabilization and elongation of the intracellular bridge between dividing cells. Cooperates with EXOC2 to recruit other components of the exocyst to the early midbody. During mitosis, also controls mitochondrial fission by recruiting to the mitochondrion RALBP1, which mediates the phosphorylation and activation of DNM1L by the mitotic kinase cyclin B-CDK1.
Subcellular location: Cell membrane {ECO:0000269|PubMed:17875936, ECO:0000269|PubMed:18756269, ECO:0000269|PubMed:19306925}; Lipid-anchor {ECO:0000269|PubMed:17875936}; Cytoplasmic side. Cleavage furrow {ECO:0000269|PubMed:18756269}. Midbody, Midbody ring {ECO:0000269|PubMed:16213214}. Mitochondrion {ECO:0000269|PubMed:21822277}. Note=Predominantly at the cell surface in the absence of LPA. In the presence of LPA, colocalizes with LPAR1 and LPAR2 in endocytic vesicles (PubMed:19306925). May colocalize with CNTRL/centriolin at the midbody ring (PubMed:16213214). However, localization at the midbody at late cytokinesis was not confirmed (PubMed:18756269). Relocalizes to the mitochondrion during mitosis where it regulates mitochondrial fission (PubMed:21822277). {ECO:0000269|PubMed:16213214, ECO:0000269|PubMed:18756269, ECO:0000269|PubMed:19306925, ECO:0000269|PubMed:21822277}.
Interaction partners:
- Exocyst complex component 8
- RalA-binding protein 1
- Ral guanine nucleotide dissociation stimulator
- Exocyst complex component 2
- Ral guanine nucleotide dissociation stimulator-like 1
- Ras GTPase-activating protein 1
- Exocyst complex component 4
- Phospholipase D1
- Ral guanine nucleotide dissociation stimulator-like 2
- Phospholipase D2
Sequence:
MAANKPKGQNSLALHKVIMVGSGGVGKSALTLQFMYDEFVEDYEPTKADSYRKKVVLDGEEVQIDILDTAGQEDYAAIRDNYFRSGEGFLCVFSITEMESFAATADFREQILRVKEDENVPFLLVGNKSDLEDKRQVSVEEAKNRAEQWNVNYVETSAKTRANVDKVFFDLMREIRARKMEDSKEKNGKKKRKSLAKRIRERCCIL
Protein: ADP-ribosylation factor (Q803D1)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Golgi apparatus {ECO:0000256|ARBA:ARBA00004555, ECO:0000256|RuleBase:RU369003}.
Interaction partners:
- Phosphatidylinositol 4-kinase beta
- Coatomer subunit gamma-2
- ADP-ribosylation factor 2a
- ADP-ribosylation factor 6
- ADP-ribosylation factor
- Coatomer subunit beta
- Golgi-specific brefeldin A-resistance guanine nucleotide exchange factor 1
- ADP-ribosylation factor GTPase-activating protein 3.
- Neuronal calcium sensor 1
- Clathrin heavy chain
Sequence:
MGNIFANLFKVFGKKEMRILMVGLDAAGKTTILYKLKLGEIVTTIPTIGFNVETVEYKNISFTVWDVGGQDKIRPLWRHYFQNTQGLIFVVDSNDRERVNEAREELMRMLAEDELREAVLLVFANKQDLPNAMNAAEITDKLGLHSLRHRNWYIQATCATSGDGLYEGLDWLSNQLKNQK
Protein: Calcium uniporter protein, mitochondrial (Mitochondrial calcium uniporter) (Q8IQ70)
Organism: Drosophila melanogaster (Fruit fly)
Function: Mitochondrial inner membrane calcium uniporter that mediates calcium uptake into mitochondria. Constitutes a pore-forming and calcium-conducting subunit. Mitochondrial calcium homeostasis plays key roles in cellular physiology and regulates cell bioenergetics, cytoplasmic calcium signals and activation of cell death pathways. Together with Itpr, has a role in oxidative stress-induced ER-mitochondria calcium transfer. During pupation, required for memory function in mushroom body neurons.
Subcellular location: Mitochondrion inner membrane {ECO:0000269|PubMed:27568554}; Multi-pass membrane protein {ECO:0000269|PubMed:27568554}.
Interaction partners:
- Calcium uptake protein 1 homolog, mitochondrial
- Essential MCU regulator
- Mitochondrial calcium uptake 3, isoform D
- Uncharacterized protein, isoform A
- Essential MCU regulator, mitochondrial
- Inositol 1,4,5-trisphosphate receptor
- Mitochondrial proton/calcium exchanger protein
- Calcium-transporting ATPase sarcoplasmic/endoplasmic reticulum type
- AFG3 like matrix AAA peptidase subunit 2, isoform A
- Paraplegin, isoform A
Sequence:
MSRNRAAMVSAFRLFLRPATTTTHRSLALRLAPGTTFALHLRPCHELQQHRSFASTAEDGETDKHKKPTTGEDIYVEYVNGMPHMTVRLPSRNELCQFALKPISHNVGDLLAMLRAEDRGIDRAAVINKHGVRIASSCTIESLLDDSFSIQINNRTLDVNPPKRDKVTLESMDKVGDVRKVIAQLYEAFNVGEYQLEKSNQLAKELETLRYELEPLEEKKLELSKKAARRTNFMTWMGLGLMSVQFGILARLTWWEYSWDIMEPVTYFVTYGTTMAMYAYYCVTKREYMMEDVKNREFSLSLYRNAKKVQFDVEHYNELKRKSAELEYNLRRINDPLNMQLPSHLVRTQENTPPTLTEEKAERKYT
Protein: BRAP2 RING ZnF UBP domain-containing protein 1 (EC 2.3.2.27) (E5KGE0)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: RING-type ubiquitin E3 ligase required for seed germination and post-germination growth.
Interaction partners:
- Polyubiquitin 12
- Transmembrane Fragile-X-F-associated protein
- Transmembrane Fragile-X-F-associated protein
- ARM repeat superfamily protein
- ARM repeat superfamily protein
- Protein BYPASS1-LIKE
- Phosphatidylglycerophosphate phosphatase 1, chloroplastic/mitochondrial
- E3 ubiquitin-protein ligase AIRP1
- Ubiquitin 13
- Small ribosomal subunit protein eS25z
Sequence:
MFILRVHSVDSERPISVEEEESGFTYASKRAQPPLKLIQPSLKLTDRKGLIHLYRKSSHSSLPNPSSRSTTLFIVAVPNYLSSLDFIRFCDSRISQVSDILFIRNDGMEDRYSVLITFSDQSEADGFYNNLNGKKFAPSEAEVCHILYVMSVEHTEFDEVAAEAPTGFTELPTCPICLERLDPDTSGIVSTLCDHSFQCSCTSKWTYLSCQVCRLCQQQDEILNCSICGKTENVWACLVCGFVGCGRYKEGHSIRHWKETHHCYSLDLRTQQIWDYVGDSYVHRLNHSKIDGKSVEMSTSCLSHQGDCGLCECSEDTGISGAIFNSKVDSIVIEYNDLLASQLKGQRQYYESLIVEARSKQESSIAEAVEQIVVNTMQELQNKIEKCEEEKSGITEVNTKLIKEQDTWRKKAKEIEEREAALLGSKDEMITDLQEQIRDITVFIEAKKTLKKMSSDTDGIREGTVLPVPISPEPVSSVRRQKKSNRRK
Protein: Capsid protein (CP) (Coat protein) (P03602)
Organism: Brome mosaic virus (BMV)
Function: Capsid protein. Binds specifically to the subgenomic RNA4 to ensure selective packaging.
Subcellular location: Virion {ECO:0000305}.
Interaction partners:
Sequence:
MSTSGTGKMTRAQRRAAARRNRWTARVQPVIVEPLAAGQGKAIKAIAGYSISKWEASSDAITAKATNAMSITLPHELSSEKNKELKVGRVLLWLGLLPSVAGRIKACVAEKQAQAEAAFQVALAVADSSKEVVAAMYTDAFRGATLGDLLNLQIYLYASEAVPAKAVVVHLEVEHVRPTFDDFFTPVYR
Protein: Platelet factor 4 (PF-4) (C-X-C motif chemokine 4) (P06765)
Organism: Rattus norvegicus (Rat)
Function: Released during platelet aggregation. Neutralizes the anticoagulant effect of heparin because it binds more strongly to heparin than to the chondroitin-4-sulfate chains of the carrier molecule. Chemotactic for neutrophils and monocytes. Inhibits endothelial cell proliferation.
Subcellular location: Secreted.
Interaction partners:
- C-X-C chemokine receptor type 3
- C-C motif chemokine 5
- C-X-C motif chemokine
- C-X-C motif chemokine 10
- C-X-C motif chemokine ligand 13
- C-X-C motif chemokine
- Stromal cell-derived factor 1
- Chemokine
- C-C motif chemokine 2
- Macrophage inflammatory protein-1 alpha receptor
Sequence:
MSAAAVFRGLRPSPELLLLGLLLLPAVVAVTRASPEESDGDLSCVCVKTSSSRIHLKRITSLEVIKAGPHCAVPQLIATLKNGSKICLDRQVPLYKKIIKKLLES
Protein: ATP synthase F(1) complex subunit epsilon, mitochondrial (ATPase subunit epsilon) (ATP synthase F1 subunit epsilon) (P29418)
Organism: Rattus norvegicus (Rat)
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. Part of the complex F(1) domain and of the central stalk which is part of the complex rotary element. 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. Mitochondrion inner membrane.
Interaction partners:
- ATP synthase subunit ATP5MPL, mitochondrial
- ATP synthase F
- ATP synthase F
- ATP synthase F
- ATP synthase F
- ATP synthase F
- ATP synthase peripheral stalk subunit OSCP, mitochondrial
- ATP synthase peripheral stalk subunit d, mitochondrial
- ATP synthase peripheral stalk subunit b, mitochondrial
- ATP synthase F
Sequence:
MVAYWRQAGLSYIRFSQICAKAVRDALKTEFKANAEKTSGTSIKTVKIKKE
Protein: Elongator complex protein 4 (A0A1W2PRJ0)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}. Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MAAVATCGSVAASTGSAVATASKSNVTSFQRRGPRASVTNDSGPRLVSIAGTRPSVRNGQLLVSTGLPALDQLLGGGLAVGTVLLIEEDKYNIYSPLLFKYFLAEGIVNGHTLLVASAKEDPANILQELPAPLLDDKCKKEFDEDVYNHKTPESNIKMKIAWRYQLLPKMEQIGPVSSSRFGHYYDASKRMPQELIEASNWHGFFLPEKISSTLKVEPCSLTPGYTKLLQFIQNIIYEEGFDGSNPQKKQRNILRIGIQNLGSPLWGDDICCAENGGNSHSLTKFLYVLRGLLRTSLSACIITMPTHLIQNKAIIARVTTLSDVVVGLESFIGSERETNPLYKDYHGLIHIRQIPRLNNLICDESDVKDLAFKLKRKLFTIEDWRKSLWSFPNLKI
Protein: Mitochondrial intermembrane space import and assembly protein 40 (Mitochondrial import inner membrane translocase TIM40) (P36046)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Required for the import and folding of small cysteine-containing proteins (small Tim) in the mitochondrial intermembrane space (IMS). Forms a redox cycle with ERV1 that involves a disulfide relay system. Precursor proteins to be imported into the IMS are translocated in their reduced form into the mitochondria. The oxidized form of MIA40 forms a transient intermolecular disulfide bridge with the reduced precursor protein, resulting in oxidation of the precursor protein that now contains an intramolecular disulfide bond and is able to undergo folding in the IMS. Reduced MIA40 is reoxidized by FAD-linked sulfhydryl oxidase ERV1.
Subcellular location: Mitochondrion inner membrane {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:14576278, ECO:0000269|PubMed:15359280, ECO:0000269|PubMed:15364952, ECO:0000269|PubMed:15620710, ECO:0000269|PubMed:16407407}; Single-pass type II membrane protein {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:14576278, ECO:0000269|PubMed:15359280, ECO:0000269|PubMed:15364952, ECO:0000269|PubMed:15620710, ECO:0000269|PubMed:16407407}; Intermembrane side {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:14576278, ECO:0000269|PubMed:15359280, ECO:0000269|PubMed:15364952, ECO:0000269|PubMed:15620710, ECO:0000269|PubMed:16407407}.
Interaction partners:
- Cytochrome c oxidase copper chaperone
- Mitochondrial FAD-linked sulfhydryl oxidase ERV1
- Mitochondrial import inner membrane translocase subunit TIM9
- Mitochondrial import inner membrane translocase subunit TIM10
- Mitochondrial inner membrane protease ATP23
- Mitochondrial import inner membrane translocase subunit TIM13
- Mitochondrial import inner membrane translocase subunit TIM8
- Mitochondrial import inner membrane translocase subunit TIM12
- Mitochondrial import receptor subunit TOM40
- Cytochrome c oxidase assembly protein COX19
Sequence:
MLRNLVVRNACRNRPSIQVARGLCRHQTRRLMASSPQFGRNSNQEKTAGFIMGILSMAGALYFIAPNRKPLFASRKVESDKTAEEELSSGGEQSPENEDDNNSKSDENGDDNDSKNDETEAGPQLGGDKIGASKVAEDGELVVLAEEDNKSSEDKDTDESKVSTKDDEQSNEDNATANNQKDENISSENSEENTSDKTLDNNAGSSEKKDPEHSDDEKSQQGQSDDKTTTEDNNGEEESSKKTVSDSENSAKQSESSDEEKEELRKQEEKQMGPTEEEVQHEGAYNPDTGEINWDCPCLGGMAHGPCGEEFKSAFSCFVYSEAEPKGIDCVEKFQHMQDCFRKYPEHYAEQLKETSDDEEPQDKVKVNTIESAPNVSSAKENAAKKAEQSDVKKEPLNEESKP
Protein: Uncharacterized protein (Q38A87)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MSSLAERLVQQLLKFHQRGAELEQEQKTLAEEEKCNQTLQERLKQMQEQVQKVREIRAVLNEHNRAAEEKYEQAIKDDEAKRALMSEELQATLSEVNSYAEEIAHMEAKAAQENKLLKEQLEIYTRFHLDGQDKYNEIMRSREQEYAKLEAKKEADAARKPQLLAELSEENERFLQTRKEEKELEVLMDGWVARVTELQERFLKARRFFESFKEEKERHVKRIRSLESEKTVLLARVERCRAERDKEQAKAKAFEEKVITQKKQIEKLSAVAHMLESGSLAESTDAAT
Protein: Homeobox-leucine zipper protein HDG8 (HD-ZIP protein HDG8) (Homeodomain GLABRA 2-like protein 8) (Homeodomain transcription factor HDG8) (Protein HOMEODOMAIN GLABROUS 8) (Q9M9P4)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Probable transcription factor.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- Homeodomain-like superfamily protein
- At4g14500
- Pleckstrin homology
- Maternally expressed PAB C-terminal protein
- Polyketide cyclase/dehydrase and lipid transport superfamily protein
- ENHANCED DISEASE RESISTANCE protein
- At3g13062
- Protein trichome birefringence-like 41
- Protein ENHANCED DISEASE RESISTANCE 2-like
- Polycomb group protein FERTILIZATION-INDEPENDENT SEED 2
Sequence:
MDNNGGGSSGNEQYTSGDAKQNGKRTCHRHTPQQIQRLEAYFKECPHPDERQRNQLCRELKLEPDQIKFWFQNKRTQSKTQEDRSTNVLLRGENETLQSDNEAMLDALKSVLCPACGGPPFGREERGHNLQKLRFENARLKDHRDRISNFVDQHKPNEPTVEDSLAYVPSLDRISYGINGGNMYEPSSSYGPPNFQIIQPRPLAETDMSLLSEIAASAVEELKRLFLAEEQFWVKSCIDETYVIDTESYERFSHAVKHFSSTTAHVESSKAVTVVHVEAINLIQMFLDPEKWKELFPTIVNKANTIHVLGSGLPIRGNCNVLQVMWEQLHILSPLVPAREFMVVRCCQEIEKGIWIIADVSHRANFDFGNAACYKRPSGCLIQALPDAHSKVMWIEHVEVDHKLDTHKIYRDLLSGGSGYGAKRWIVTLERMCERMALSSIQTLPPSDRSEVITTGEARRSVMKLGERMVKNFNEMLTMSGKIDFPQQSKNGVRVSIRMNIEAGQPPGIVVSASSSLAIPLTPLQVFAFLQNLDTRQQWDILSYGTVVNEIARIVTGSSETNCVTILRVHPTHEENNDKMVVQDSCKDDMLMLQDCYMDALGGMIVYAPMDMATMHFAVSGEVDPSHIPILPSGFVISSDGRRSTVEDGGTLLTVAFQILVSGKANRSREVNEKSVDTVSALISSTIQRIKGLLNCPEC
Protein: Cytochrome c oxidase subunit 6, mitochondrial (Cytochrome c oxidase polypeptide VI) (Q9UTF6)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Component of the cytochrome c oxidase, the last enzyme in the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over the inner membrane that drives transmembrane transport and the ATP synthase. Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Electrons originating from reduced cytochrome c in the intermembrane space (IMS) are transferred via the dinuclear copper A center (CU(A)) of subunit 2 and heme A of subunit 1 to the active site in subunit 1, a binuclear center (BNC) formed by heme A3 and copper B (CU(B)). The BNC reduces molecular oxygen to 2 water molecules using 4 electrons from cytochrome c in the IMS and 4 protons from the mitochondrial matrix.
Subcellular location: Mitochondrion inner membrane {ECO:0000250|UniProtKB:P00427}; Peripheral membrane protein {ECO:0000250|UniProtKB:P00427}; Matrix side {ECO:0000250|UniProtKB:P00427}.
Interaction partners:
- Cytochrome c oxidase subunit 2
- Cytochrome c oxidase polypeptide 5, mitochondrial
- Cytochrome b-c1 complex subunit 7
- Cytochrome b-c1 complex subunit 2, mitochondrial
- Cytochrome c oxidase subunit 12, mitochondrial
- Cytochrome c oxidase subunit 1
- Cytochrome c1, heme protein, mitochondrial
- Cytochrome b-c1 complex subunit 8
- Cytochrome c oxidase subunit 4, mitochondrial
- Cytochrome c oxidase subunit 13, mitochondrial
Sequence:
MKAVQRIFQTGRFSVAAGPSVRFQAGFLAANRQVRFSSNHGVSLEEINTKYNDFFSNVQDQFELQRGLNNCFAYDIVPSSDVIEQALRAARRVNDFPTAVRIFEGIKVKLPTKEQYQAYVKELKPVCNELGIVLKEDLFK