wanglab/gogpt-training-data huggingface dataset:
Protein: C3H1-type domain-containing protein (H2KZI6)
Organism: Caenorhabditis elegans
Interaction partners:
- Trafficking protein particle complex subunit 6B
- Trafficking protein particle complex subunit
- Trafficking protein particle complex subunit 9
- Trafficking protein particle complex subunit 3 homolog
- Trafficking protein particle complex subunit 10
- Trafficking protein particle complex subunit 2-like protein
- Trafficking protein particle complex subunit
- Trafficking protein particle complex subunit 8
- Trafficking protein particle complex subunit 5
- Trafficking protein particle complex subunit 11 domain-containing protein
Sequence:
MADVYTPTKTMDGAFLPAVGSPNTSIDSPAVYVPTPLTAPSTSKTTPVKPEDQTTRQKYGGSVSYSPSNPGIRIVKRKPKPEAVAAAAAVPTAIYSGKRHATDDGEDAGLAALKLYFQKPNRGILRGPAISNLNQRGTRRLIFADTRGLPLVHVKEIERIAAIHSNVADYRCSERNEAAAFGQEMEVFEDVEWSLVPVKRSKPARSEMSESGLREERRIEEEGIMRGAMFGMCQLEDNPALNEQAAVDRANYTPTIIPTVSVPSEPTTLATIRDLPLPGRPPRVRPQDLLLQVKPNQGFHTLPLYHSQRPENPRRPMYAQQQQQQSAHQTPTPHIQQVFQETEPVTNYYTATTSVPETPEPAPAAQPASRFELPSNLKEMLNQLKKKGFVSSDETPSPTTSAPPPVDPLAAAMQTAQQMMLQQGNTYASEEVPQDYPMDGYVATFATPEMMAQERRQDSRNSEGWTQSGWKIPEPCVYFISRPGGCNRGDQCRFIHDEEMRRQKMAELPPRGPNHHHDNFRGGRGRGFRGGYNNRNNYNNHHDRDFRDNAGGNRGRFGDTEGFRGARYARGGFAPRNNSRFDQKPAYNDDGGHLGSPNAHGSQYQDPVPTKRARVSRFDRQGEDDAPGQDMDQRPPRRNRFDEQPPRRTFRSRFDQQADHDEMSQA
Protein: Probable NADH dehydrogenase [ubiquinone] iron-sulfur protein 2, mitochondrial (EC 7.1.1.2) (Complex I-49kD) (CI-49kD) (NADH-ubiquinone oxidoreductase 49 kDa subunit) (Q93873)
Organism: Caenorhabditis elegans
Function: Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) that is believed to belong to the minimal assembly required for 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 (By similarity).
Subcellular location: Mitochondrion inner membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Matrix side {ECO:0000250}.
Interaction partners:
- Probable NADH dehydrogenase flavoprotein 2, mitochondrial
- NADH dehydrogenase 1 alpha subcomplex subunit 9, mitochondrial
- Probable NADH dehydrogenase iron-sulfur protein 7, mitochondrial
- NADH dehydrogenase iron-sulfur protein 3
- Probable NADH dehydrogenase iron-sulfur protein 8, mitochondrial
- NADH dehydrogenase 1 alpha subcomplex subunit 13
- Cytochrome b-c1 complex subunit Rieske, mitochondrial
- NADH-ubiquinone oxidoreductase chain 5
- NADH-ubiquinone oxidoreductase 75 kDa subunit
- NADH-ubiquinone oxidoreductase chain 4
Sequence:
MLGRKIAGTCLRANVPSVAATSSTPATQTRNSHTIWYPDAKFERQFKTGGTLGKLWMSERVSDFDEKIGLDKLEKLAYSDPVMSDNYSGKQREKNLENMILNFGPQHPAAHGVLRLVLKLEGEVIIKAIPHIGLLHRATEKLIEHKTYTQALPYFDRLDYVSMMCNEQAWSLAVEKLLGIDIPTRAKYIRTLMGELTRIQNHIMGITTHALDVGAMTPFFWMFEEREKLFEFSERVSGARMHANYVRPGGVAWDLPIGLMDDIYDWAIKFPERIDELEDMLTENRIWKARTIDIGLVSAADALNWGFSGVMVRGSGIKQDVRKTEPYDAYADMEFDVPIGTKGDCYDRYLCRIEEMRQSLNIVHQCLNKMPAGEIKVDDHKVVPPKRAEMKENMESLIHHFKFFTEGFQVPPGATYVPIEAPKGEFGVYLVADGTGKPYRCFIRAPGFAHLAAIHDVCYMSLIADIVAVIGTMDIVFGEVDR
Protein: Casein kinase II subunit beta (CK II beta) (P40232)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Regulatory subunit of casein kinase II/CK2 (By similarity). As part of the kinase complex regulates the basal catalytic activity of the alpha subunit a constitutively active serine/threonine-protein kinase that phosphorylates a large number of substrates containing acidic residues C-terminal to the phosphorylated serine or threonine (By similarity).
Interaction partners:
- Casein kinase II subunit alpha
- Casein kinase II subunit beta-2
- Ribosomal RNA-processing protein 7
- U3 small nucleolar RNA-associated protein 22
- rRNA biogenesis protein rrp36
- U3 small nucleolar ribonucleoprotein protein imp3
- U3 small nucleolar RNA-associated protein 6
- U3 small nucleolar RNA-associated protein 21 homolog
- U3 small nucleolar ribonucleoprotein protein imp4
- Uncharacterized protein C1604.06c
Sequence:
MQLYSSESESDDSQYWVDWFLGLKGNEFFCEVDEDFIQDRFNLTGLSHEVPHYSQSLDLILDVLDPDLPEEVQDEVEASARHLYGLIHARYILTAQGLYKMLEKYKKCDFGHCPRVLCNGQPMLPVGLSDIAHTKSVKLYCPRCEDVYTPKSQRHASIDGAYFGTSFPHMLFQVYPELAVPKSQERYIPRIFGFKVHSYSATFKKQDVYKEKQKKRLQGAEAESKNKLAIT
Protein: Homeobox protein Nkx-2.8 (Homeobox protein NK-2 homolog H) (O15522)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- Paired box protein Pax-9
- Histone-lysine N-methyltransferase SMYD3
- Probable helicase with zinc finger domain
Sequence:
MATSGRLSFTVRSLLDLPEQDAQHLPRREPEPRAPQPDPCAAWLDSERGHYPSSDESSLETSPPDSSQRPSARPASPGSDAEKRKKRRVLFSKAQTLELERRFRQQRYLSAPEREQLASLLRLTPTQVKIWFQNHRYKLKRARAPGAAESPDLAASAELHAAPGLLRRVVVPVLVRDGQPCGGGGGGEVGTAAAQEKCGAPPAAACPLPGYPAFGPGSALGLFPAYQHLASPALVSWNW
Protein: T cell receptor associated transmembrane adaptor 1 (C9JF66)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MSDKMYSYSSDHTRVDEYYIEDTPIYGNLDDMISEPMDENCYEQMKARPEKSVNKMQEATPSAQATNETQMCYASLDHSVKGKRRKPRKQNTHFSDKDGDEQLHAIDASVSKTTLVDSFSPESQAVEENIHDDPIRLFGLIRAKREPIN
Protein: Chromobox protein homolog hpl-1 (HP1-like heterochromatin protein 1) (G5EET5)
Organism: Caenorhabditis elegans
Function: Seems to be involved in transcriptional silencing in heterochromatin-like complexes (By similarity). Involved in epigenetic repression (By similarity). Probably does not act as global transcriptional repressor. Plays a role in linking epigenetic regulation with the innate immune response. Acting in concert with chromobox protein homolog hpl-2 and histone H1 protein his-24, involved in reproduction, somatic gonad development, male tail development and vulval cell fate decisions; perhaps as a result of modulating expression of Hox genes mab-5 and egl-5. Role in growth and somatic gonad development is antagonized by histone-lysine N-methyltransferase set-2/SET1. Required for larval development, acting redundantly with hpl-2. Plays a role in the formation of the vulva and in fertility, acting together with a CoREST-like complex, and hpl-2.
Subcellular location: Nucleus {ECO:0000269|PubMed:16905130, ECO:0000269|PubMed:26476455}. Note=Partially co-localizes with histone H3 tails methylated at 'Lys-9' (H3K9me3) and 'Lys-23'(H3K23me2) in chromatin (PubMed:26476455). Localizes to distinct nuclear foci, not overlapping significantly with hpl-2, in embryonic cells (PubMed:16905130, PubMed:26476455). {ECO:0000269|PubMed:16905130, ECO:0000269|PubMed:26476455}.
Interaction partners:
- Histone-lysine N-methyltransferase set-25
- Protein lin-61
- C2H2-type domain-containing protein
- Histone 24
- Chromo domain-containing protein cec-4
- Histone-lysine N-methyltransferase mes-2
- Lysine-specific histone demethylase
- Chromo domain-containing protein cec-3
Sequence:
MSRQNPVRSTRGNSLRAREAQQAQDAPLFQESSSNVFVVEKVLNKRLTRGGSEYYIKWQGFPESECSWEPIENLQCDRMIQEYEKEAAKRTTRKRRYSPQPSTSSSAELQPSTSDEWAGKTLKTIIGITKAPGELHFLCKFSDDSVHLIPLREANVRFPSQVIKFYETRLVLQGVSPTIPGGMS
Protein: SAM domain-containing protein (H8P173)
Organism: Caenorhabditis elegans
Interaction partners:
Sequence:
MAARRGGRPGYRGAFRGAARGAPSRRPAPAAEVAPETPVAAPMAPAAPAAPATPEAAPAAEVMDTSIATEMPQESAVDLSNVSAATEMDTSKEGEASRPTSEKKKFQKIRTTEMDRLMSMDLGPKDGGRVGELGHMWPESRRRPAAPLPETPAAQPRKSLPRRAAEKKKPEDSDAAEEQEVEMEVDNDASTSTPRNARGGRGGGNRRGSRRGQKRTSGGSGKLVEPKKEPVDEPAEKIPKRSEAAPEVPATATTKEAPPSTSSSPPDAPATPATPASSDSRDSPRKIRAMIFSLTGSPPESETPPVLQQEQVISTAAPTAGRHPNIIQQVPHINRIPPQPLRRLTAPQAPPASQPEEPPVQQTVPVVKVELASAPAPIVRDPQSTEPVPPAMPTLVENNHEATLILPPNKTSDYTRWNAQDLINWVRLLITNNVDSTIAIMVREEFDGETLACLVLDDDFRKEVPIPYGHYKKMKIYGTEVLNHYRTEKYQADLRKFHEELAAWKAQQR
Protein: Palmitoyl-protein thioesterase ABHD10, mitochondrial (EC 3.1.2.22) (Acyl-protein thioesterase ABHD10) (Alpha/beta hydrolase domain-containing protein 10) (Abhydrolase domain-containing protein 10) (Mycophenolic acid acyl-glucuronide esterase, mitochondrial) (EC 3.1.1.93) (Q6PE15)
Organism: Mus musculus (Mouse)
Function: Acts as an acyl-protein thioesterase that hydrolyzes fatty acids from acylated residues in proteins. Regulates the mitochondrial S-depalmitoylation of the nucleophilic active site residue of peroxiredoxin-5/PRDX5, a key antioxidant protein, therefore modulating mitochondrial antioxidant ability. Also catalyzes the deglucuronidation of mycophenolic acid acyl-glucuronide, an active metabolite of the immunosuppressant drug mycophenolate (By similarity).
Subcellular location: Mitochondrion {ECO:0000250|UniProtKB:Q9NUJ1}.
Interaction partners:
- Alpha/beta hydrolase domain-containing protein 17A
Sequence:
MAAWAPCRRWGWAAVSFGRHPGLSASLARKPPRAWWLSACRQKASLSFLNRSELPNLAYKRLKGKTPGIIFIPGYLSNMNGIKAVAVEEFCKSLGHAFIRFDYSGIGSSDGNLAECTVGKWRKDVLSILDDVAEGPQILVGSSLGGWLMLHAAIARPEKVIALIGIATAADGLVTQYHALPVETQKEIEMKGEWTLPSRYNKEGYFRIPYSFIKEAEHHCLLHSPIPVTCPVRLLHGMKDEIVPWQRSLQVADRIVSPDVDVILRKQGDHRMKEKADIHLLICTIDDLIDKLSTVVP
Protein: Fos-related antigen 2 (FRA-2) (P15408)
Organism: Homo sapiens (Human)
Function: Controls osteoclast survival and size (By similarity). As a dimer with JUN, activates LIF transcription (By similarity). Activates CEBPB transcription in PGE2-activated osteoblasts (By similarity).
Subcellular location: Nucleus {ECO:0000250|UniProtKB:P51145}.
Interaction partners:
- Transcription factor JunD
- Transcription factor JunB
- Transcription factor Jun
- Protein c-Fos
- Protein FosB
- Fos-related antigen 1
- Mitogen-activated protein kinase 8
- Mitogen-activated protein kinase 9
- Cyclic AMP-dependent transcription factor ATF-7
- Cyclic AMP-responsive element-binding protein 5
Sequence:
MYQDYPGNFDTSSRGSSGSPAHAESYSSGGGGQQKFRVDMPGSGSAFIPTINAITTSQDLQWMVQPTVITSMSNPYPRSHPYSPLPGLASVPGHMALPRPGVIKTIGTTVGRRRRDEQLSPEEEEKRRIRRERNKLAAAKCRNRRRELTEKLQAETEELEEEKSGLQKEIAELQKEKEKLEFMLVAHGPVCKISPEERRSPPAPGLQPMRSGGGSVGAVVVKQEPLEEDSPSSSSAGLDKAQRSVIKPISIAGGFYGEEPLHTPIVVTSTPAVTPGTSNLVFTYPSVLEQESPASPSESCSKAHRRSSSSGDQSSDSLNSPTLLAL
Protein: RNA-binding protein 3 (RNA-binding motif protein 3) (W8E7I1)
Organism: Capra hircus (Goat)
Function: Cold-inducible mRNA binding protein that enhances global protein synthesis at both physiological and mild hypothermic temperatures. Reduces the relative abundance of microRNAs, when overexpressed. Enhances phosphorylation of translation initiation factors and active polysome formation.
Subcellular location: Nucleus {ECO:0000250|UniProtKB:Q925G0}. Cytoplasm {ECO:0000250|UniProtKB:Q925G0}. Cell projection, dendrite {ECO:0000250|UniProtKB:Q925G0}. Note=Localizes in mRNA granules in dentrites. {ECO:0000250|UniProtKB:Q925G0}.
Interaction partners:
Sequence:
MSSEEGKLFVGGLNFNTDERALEDHFSSFGPISEVVVVKDRETQRSRGFGFITFTNPEHASNAMRAMNGESLDGRQIRVDHAGKSARGSRGGAFGSYERGRGYPRGGGDQGYGSGRYDNRPGAYGFGYGYGYGRSRDYGGRSQGGYDRYSGGNYRDNYDN
Protein: Ribonucleoside-diphosphate reductase subunit M2 (EC 1.17.4.1) (Ribonucleotide reductase small chain) (Ribonucleotide reductase small subunit) (P11157)
Organism: Mus musculus (Mouse)
Function: Provides the precursors necessary for DNA synthesis. Catalyzes the biosynthesis of deoxyribonucleotides from the corresponding ribonucleotides. Inhibits Wnt signaling (By similarity).
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:P31350}. Nucleus {ECO:0000250|UniProtKB:P31350}. Note=Localized to the cytoplasm in S phase cells. May localize to the nucleus in G2 phase cells. {ECO:0000250|UniProtKB:P31350}.
Interaction partners:
- Ribonucleoside-diphosphate reductase large subunit
- Ribonucleoside-diphosphate reductase subunit M2 B
- Thymidylate kinase
- Lymphokine-activated killer T-cell-originated protein kinase
- Cyclin-dependent kinase 1
- dCTP pyrophosphatase 1
- DNA replication licensing factor MCM5
- Cyclin-A2
- Pyruvate kinase PKM
- Nucleoside diphosphate kinase, mitochondrial
Sequence:
MLSVRTPLATIADQQQLQLSPLKRLTLADKENTPPTLSSTRVLASKAARRIFQDSAELESKAPTNPSVEDEPLLRENPRRFVVFPIEYHDIWQMYKKAEASFWTAEEVDLSKDIQHWEALKPDERHFISHVLAFFAASDGIVNENLVERFSQEVQVTEARCFYGFQIAMENIHSEMYSLLIDTYIKDPKEREYLFNAIETMPCVKKKADWALRWIGDKEATYGERVVAFAAVEGIFFSGSFASIFWLKKRGLMPGLTFSNELISRDEGLHCDFACLMFKHLVHKPAEQRVREIITNAVRIEQEFLTEALPVKLIGMNCTLMKQYIEFVADRLMLELGFNKIFRVENPFDFMENISLEGKTNFFEKRVGEYQRMGVMSNSTENSFTLDADF
Protein: Thiol-disulfide oxidoreductase LTO1 (EC 1.17.4.-) (Protein LUMEN THIOL OXIDOREDUCTASE 1) (Vitamin K reductase) (Q8L540)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Thiol-disulfide oxidoreductase catalyzing disulfide bond formation of chloroplast proteins and involved in redox regulation and photosynthetic electron transport. Required for the assembly of photosystem II (PSII) through the formation of disulfide bond in PSBO, a subunit of the PSII oxygen-evolving complex in the thylakoid lumen. Involved in the formation of disulfide bonds in the lumenal protein FKBP13. In vitro, reduces phylloquinone (vitamin K1) and menaquinone (vitamin K2) to their respective quinol. Cannot reduce phylloquinone epoxide to phylloquinone. Plays an important role in regulating the thylakoid lumen redox.
Subcellular location: Plastid, chloroplast thylakoid membrane {ECO:0000305|PubMed:20626653, ECO:0000305|PubMed:21781282}; Multi-pass membrane protein {ECO:0000305|PubMed:20626653, ECO:0000305|PubMed:21781282}.
Interaction partners:
- Peptidyl-prolyl cis-trans isomerase FKBP13, chloroplastic
- Cytochrome c-type biogenesis ccda-like chloroplastic protein
- Thioredoxin-like protein HCF164, chloroplastic
- Oxygen-evolving enhancer protein 1-1, chloroplastic
- Oxygen-evolving enhancer protein 1-2, chloroplastic
- Protein SUPPRESSOR OF QUENCHING 1, chloroplastic
- Protein disulfide-isomerase LQY1, chloroplastic
- Peptidyl-prolyl cis-trans isomerase CYP38, chloroplastic
- Violaxanthin de-epoxidase, chloroplastic
- AT4g31560
Sequence:
MMARFVSVSSCQFHFGFREVSPPSVTSYPRRFEVSDRRFPAIPIKCSSSEPENGEDSAPSLSSSSSSSTSEVSTSNSSTYNWYTGIGGIGMLDTAYLTYLKVTGSDAFCPIGGGTCGDVLNSDYAVVFGVPLPVIGFVMYGVVTALSAELGEGNLPFGISKSNGRFALFGITTAMASASAYFLYILSTKLSGSSCLYCLVSAFLSFSLFFLSVKDVKLQEIQQVVGLQICLAIIVVASLTASYSTAQPIPSRSGDIELPYFRTEISSSSSPYAIALAKHLNSIGAKMYGAFWCSHCLEQKEMFGREAAKELNYVECFPDGYKKGTKILKACADAAIEGFPTWIINDKVLSGEIELAELAEMTGFSLDQANETNQLQ
Protein: Uncharacterized protein ycf76 (ORF72) (Q6EN94)
Organism: Oryza nivara (Indian wild rice) (Oryza sativa f. spontanea)
Subcellular location: Plastid, chloroplast.
Interaction partners:
Sequence:
MKKILFSMFYSILVGEEPDSVFLKKEGKQNQVKMIWVAPSSCAKDLTISEGTGATFLFNFHSRVSICFHALF
Protein: Dorsal interacting protein 2 (Q9VN42)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- RE25177p
Sequence:
MATRSCAYKDCEYYYVGHENALTKGRTLFAFPKQPQRARIWHENGQVHPKIPHSQLFMCSLHFDRKFISSSKNRTLLVGEAVPFPYEESSSKPEEEPQQVASTSHESYYINLSDDELSINNVDTTSVTTIDAVHDSPPQKRPKESSIVIALKEAVKMEPNPNAGRVRAEPDNIDTTEVSVFNFKGQEYVQMSMEYYLQEKRKMAKLLQDYKNALRSIKKHISHLDL
Protein: Kinesin family member 1B (Kinesin-like protein KIF1B (EC 5.6.1.3)) (F1QBV5)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000256|ARBA:ARBA00004245}.
Interaction partners:
- KIF-binding protein
- RNA-binding motif protein 4.2
- Kinesin family member 15
- Kinesin-like protein
Sequence:
MSGASVKVAVRVRPFNSRETGKESKCIIQMQGNSTTILNPKNPKEPKTFSFDYSYWSHTSPDDPSFASQNQVYNDIGKEMLQHAFEGYNVCIFAYGQTGAGKSYTMMGKQEEGQEGIIPQLCEELFEKINDNNNEEISYSVEVAYMEIYCERVRDLLNPKNKGNLRVREHPLLGPYVEDLSKLAVTSYTDIADLMDAGNKARTVAATNMNETSSRSHAVFTIVFTQRKYDSETDLSTEKVSKISLVDLAGSERADSTGAKGTRLKEGANINKSLTTLGKVISALAEVSKKKKKTDFIPYRDSVLTWLLRENLGGNSRTAMVAALSPADINFDETLSTLRYADRAKQIKCNAVINEDPNAKLVRELKDEVSRLKELLRAQGLGDILDTPMGCLTASPSSGSLCSQAGLQSVSSIQERIMSTPGGEEAIERLKESEKIIAELNETWEEKLRKTEAIRMEREALLAEMGVAIREDGGTLGVFSPKKTPHLVNLNEDPLMSECLLYYIKDGITRVGQADAERRQDIVLSGAHIKEEHCIFRSERNANGHVIVTLEPCEGSETYVNGKRVNSAVQLRSGNRIIMGKNHVFRFNHPEQARAEREKTPSAETPVEPVDWTFAQRELLEKQGIDMKQEMEKRLTEMEILYKKEKEEADQLLEQQRLVYESKLQELQKQVETRSLAAETPDEEEEEEEEDEVPWTQHKYELAQWAFRKWRYHQFTSLRDQLWGNAVYLKEANAISVELKKKVQFQFVLLTDTLYSPLPPELLPPEPEKERDARPFPRTVVAVEVQDLKNGATHYWSLEKLKQRLDQMREMYDRAGEMASSNQGDDGEGALTGSDPFYDRFHWFKLVGSSPIFHGCVNERLADRTPSPTFSTTDSEITELADERQSEMEDFMDDEAFVDDTSSDAGTEEGSDIFSDGQDPFYDRSPWFILVGRAFVYLSNLLYPVPLVHRVAVVTEKGDVRGFLRVGVQAIAADEEAPDYGSGVRQSGTAKISFDNEYFKKNDFTSVAMTRSGLSLEELRIVEGQGQSSEVITPSEEMNRINEMDLKLGNVDTKLGDGLAEHLEVGSIFTFRVTVLQASGIPAEYADIFCQFNFLHRHDEAFSTEPLKNTGRGAPLGFYHVQNISVEVTESFIEYIKTKPIVFEVFGHYQQHPLHIHGQDVVSPSQPSRKYYPPPMPLSKPVPATKLNTITKSNLGQCVSKYDLLAWFEISELEPTGEYIPAVVDHTGGLPCHGTYLLHQGIQRRITVTLIHEKGSELHWKDVRELVVGRIRNKPEVDDSAADAVLSLNIISAKNLKSSHNSSRTFYRFEAVWDSSLHNSLLLNRVTPYGEKIYMTLSAYLELDHCIQPAIITKDICMVFYSRDAKISPPRSLRNLFGSGYSKTPDCNKVTGVYELSLCKIADTGSPGMQRRRRKVLDTSVAYVRGEENLAGWRPRGDSLILEHQWELDKMEQLHEVEKTRHLLLLREKLGETPPPKSLSESLSPSLSSGTLSTSTSISSQISSTTFESAITPSESSGYDSTDIESLVDREKELATKCLRLLTHTFNSEYNQMCNSISDCKFSDISPMGRDPSVSSFSSATLTPSSTCPSLSDSRYTLHTQKTPEANSRATSPSGSDYENFPMVPILETSYLARAGKHEFLNLVPNIEEMRPGSVVSKKGILNFMEPRSNTWVKHFVVVRRPYVFIYNNDKDPVERGVLNLSTAQVEYSEDQQAMLKTPHTFAMCTKHRGILLQANNDKDMNDWLYAFNPLLAGTIRSKLARRRSGVMKN
Protein: RE29005p (Q8MZ04)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MPEVLSGTPTNSHNKANIAMMNNVRLSNISPTLSMNGSSNEASNLHPLSMYGGSISPQSNDSGMSDSLGKYVPGSGYGDGMMAQSPSQGGNGPQSALTAAQKELFSQRKQREFTPDNKKDESYWDRRRRNNEAAKRSREKRRYNDMVLEQRVIELTKENHVLKAQLDAIRDKFNISGENLVSVEKILASLPTSEQVLSNTKRAKMSGSGGSSSGSSPSGSGSGEGSPQGGHNGYPVGPPLSPLIYGPNGNARPEATVKSVHHIHHAGVAPPPTHLQQLVVPQSQTQHLYQPQPQQHQPHQQQQISQPPQQQQQQQEPSPSAGSSSPVISDPHNRPPSTTIANLQVQLQQALNRNVRPEDLDSLRKVVAAGALYNAAAVVGAPPPPPSAGLYVPAPSAYKDHLEAAAAWSHNVEAAVSSSAVDAVSSSSVSGSAASVLNLSRRACSPSYEHMLSSTTSSTLSSASSSGAVSGDDEQEHEPAHMAPLQLQRSSPQQGSDANNCLPLKLRHKSHLGDKDAAATALLSLQHIKQEPNCSRASPPAWNDGGDNSSDERDSGISIASAEWTAQLQRKLLAPKEANVVTSAERDQCSSRSWSA
Protein: 65-kDa microtubule-associated protein 8 (AtMAP65-8) (Q9C7G0)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Nucleus {ECO:0000269|PubMed:15469496}. Cytoplasm {ECO:0000269|PubMed:15469496}. Cytoplasm, cytoskeleton, spindle pole {ECO:0000269|PubMed:15469496}. Note=Present in MT cortical arrays. Concentrated in dots surrounding the nuclei.
Interaction partners:
- Microtubule-associated protein 70-5
- Kinesin-like protein KIN-14I
- Kinesin-like protein KIN-14L
- At5g19870)
- Transmembrane E3 ubiquitin-protein ligase FLY2
- Kinesin-like protein KIN-14K
- Kinesin-like protein KIN-14H
- Filament-like plant protein 3
- Microtubule-associated protein 70-1
- Endo-1,4-beta-xylanase 3
Sequence:
MGSLQTPIEMRSSSLLDTSCGYLLRELQMIWDEVGEDKFEREKVLLDIEQECVEAYRRKVDHANVSRSRLHQELAESEAELTHFLLCLGERSVPGRPEKKGGTLREQLDSIAPALREMRLRKDERVKQFRSVKGEIQKISAEIAGRSTYEDSTRKITIDDNDLSNKKLEEYQNELHRLHDEKNERLQKVDIYICAIRDLSATLGTEASMIITKIHPSLNDLYGISKNISDDILKKLNGTVVSLEEEKHKRLEKLHHLGRALSNLWNLMDASYEDRQKFFHVIDLLSSAPSDVCAPGSITLDIIQQAEAEVKRLDQLKASRIKELFIKKQKELEDTCNMSHMETPSTEMGNITNLVDSGEVDHVDLLAAMDEKIARAKEEAASRKGIIEKVDRWMLASDEERWLEEYDQDENRYSVSRNAHRNLRRAERARITVSKISGLVESILVKAKSWEVERQKVFLYNEVPLVAMLQEYNKLRQEKEMEKQRLREMKKMSIPQPVAEGDNFYMARPASSNRRISNRSMNGGFGSGSPINRKYSGGFNNTNNNYTALGTSIRRESRKSEA
Protein: Prohibitin-2 (P50085)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Prohibitin probably acts as a holdase/unfoldase for the stabilization of newly synthesized mitochondrial proteins.
Subcellular location: Mitochondrion inner membrane {ECO:0000269|PubMed:10207067, ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:14576278, ECO:0000269|PubMed:15525670, ECO:0000269|PubMed:38964378}; Single-pass type II membrane protein {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:14576278, ECO:0000269|PubMed:15525670}; Intermembrane side {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:14576278, ECO:0000269|PubMed:15525670}.
Interaction partners:
- Prohibitin-1
- Mitochondrial inner membrane m-AAA protease component YTA10
- Mitochondrial inner membrane m-AAA protease component YTA12
- Mitochondrial inner membrane i-AAA protease supercomplex subunit YME1
- Elongation factor Tu, mitochondrial
- Non-selective voltage-gated ion channel 2
- Mitochondrial Rho GTPase 1
- Mitochondrial fission 1 protein
- Rhomboid protein 1, mitochondrial
- Mitochondrial import inner membrane translocase subunit TIM50
Sequence:
MNRSPGEFQRYAKAFQKQLSKVQQTGGRGQVPSPRGAFAGLGGLLLLGGGALFINNALFNVDGGHRAIVYSRIHGVSSRIFNEGTHFIFPWLDTPIIYDVRAKPRNVASLTGTKDLQMVNITCRVLSRPDVVQLPTIYRTLGQDYDERVLPSIVNEVLKAVVAQFNASQLITQREKVSRLIRENLVRRASKFNILLDDVSITYMTFSPEFTNAVEAKQIAQQDAQRAAFVVDKARQEKQGMVVRAQGEAKSAELIGEAIKKSRDYVELKRLDTARDIAKILASSPNRVILDNEALLLNTVVDARIDGRGK
Protein: Hyaluronidase PH-20 (Hyal-PH20) (EC 3.2.1.35) (Hyaluronoglucosaminidase PH-20) (Sperm adhesion molecule 1) (Sperm surface antigen 2B1) (Sperm surface protein PH-20) (Q62803)
Organism: Rattus norvegicus (Rat)
Function: Involved in sperm-egg adhesion. Upon fertilization sperm must first penetrate a layer of cumulus cells that surrounds the egg before reaching the zona pellucida. The cumulus cells are embedded in a matrix containing hyaluronic acid which is formed prior to ovulation. This protein aids in penetrating the layer of cumulus cells by digesting hyaluronic acid (By similarity).
Subcellular location: Cell membrane; Lipid-anchor, GPI-anchor.
Interaction partners:
- Alpha-L-iduronidase
- Arylsulfatase B
- Beta-glucuronidase
- Disintegrin and metalloproteinase domain-containing protein 2
- Protamine-2
- Cysteine-rich secretory protein 2
Sequence:
MGELQFKWLFWRSFAESGGTFQTVLIFLFIPYSLTVDYRATPVLSDTTFVWVWNVPTEACVENVTEPIDLSFFSLIGSPRKTAIGQPVTLFYVDRLGNYPHIDAQQTEHHGGIPQKGDLTTHLVKAKEDVERYIPTDKLGLAIIDWEEWRPTWMRNWTPKDIYRNKSIELVQAADPAINITEATVRAKAQFEGAAKEFMEGTLKLGKHIRPKHLWGFYLFPDCYNNKFQVDNYDGQCPDVEKKRNDDLDWLWKESTGLYPSVYLKKDLKSSRKATLYVRYRVLESIRVSKVSDESNPVPIFVYIRLVFTDHVSEYLLEDDLVNTIGEIVAQGTSGIIIWDAMSLAQRSAGCPILRQYMKTTLNPYIVNVTLAAKMCSQTLCKEKGMCSRKTESSDAYLHLDPSSFSINVTEAGKYEVLGKPEVKDLEYFSEHFKCSCFSKMTCEETSDMRSIQDVNVCMGDNVCIKATLGPNSAFHLLPGKGLLLMTTLAHILHHLPHDIFVFPWKMLVSTP
Protein: Neuromusculin, isoform B (Q0E8B8)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004167}; Single-pass membrane protein {ECO:0000256|ARBA:ARBA00004167}.
Interaction partners:
Sequence:
MGNMALRQSAKDVAKSNCVAVRSSISLSLVLVLCLALVDSSTAQVDTTISQQESQSVVLPCPVDAEKCGKLHSLNWFKGDDRIAAMLLGDSNVTSVNKEFDERVTVEQNPYRLVIKDLKIADEDIYLCDTTFFIPEETCDNFNGYRIELRVLVPPTEVVILDAKGDRIKNGSVVGPMQERQSLKATCTVRNTRPQPEVSWFRGTKRLTTYSPTHDLVDGLYTSTLELDWTLSREDLAQDIECRVKSAAIQNVTVTKFSVDLQVRPTSIDINGVKHHTVQGSKVVLTCDIHGARPAVNLTWYNTTTIISSGENEITEVRSKSLEKSDGTFHTQSELIFNATRFENDRVFRCEAENIVLQINREKPISSALTLEVLYPPVVKVSPSAITANTSEIVLLNCEYFANPASLTQVEWYRNDILVNVNDTTHYKGGNSENVALVIKSTEKEDIGNYSCQLSNNIGKGTSDQKINLDVQYAPTVEILMIPEGPVKESDESNVTLFCNVLDANPSVLTKVRWYANSTLLKELPDCEETREDLCHIDPSKLLLESIGRGFFYNYSCEGFNAAGWGPRSEDKELLVHYEPGPAALSHFPLVAVKKKSVTFSCSVDDPGFPESNRFRWLRGGRGPLQDIVTKDWTVEPVGLDSRTNYSCYAYNEGGKGVMATVNLEVHAPPFFIKNLPPYTGILHSSPNATLTCRIECVPRCDISWQKDGVPIERNDSRYFIKEKYMDASPATGDFESMLSVLHFNMPNWPDSKFNIEADNANYSCVSTGNIVGGSIRSRTYFGIEYAPENTTVSENIVYVQEDTIPGRVICKSRANPEPSYKWIFKNETIANGNALIINTAMNRNDDGTYTCLAYNKHGSSIAKTVIKVQFKPRCEIERQEIDDQDTLICTAYGNPIEADFSWSIKTENETDENLGSGKKENSVEKSFYILQTDYAISRTYRCVANNTVGYGPFCEIEVAEQLAWWQLWEKNTLIILVAAILGLLLTVIVICCIIICICRRRRRQDKYLTEVPINSIQSTRQVVFTKGTVDGTWRV