wanglab/gogpt-training-data huggingface dataset:
Protein: 2-oxoadipate dioxygenase/decarboxylase (EC 1.13.11.93) (2-hydroxyglutarate synthase) (O04551)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
Sequence:
MGSLDLPYASSFKGGSETFLQNVFESILKTYLRKNPMAKTIWELVKSVDNEKISYDHFFFRTFKVDGYGIDSLASFFMDYGYKVGGRLDFPKKKVQVLWLSPPDVHFPDNGYGIGNGPLPRLVIAELLVEELSPESQEIIRKYLKPEGGKQAVLSSTLGSLIWEKPTSTDFNQLAKESEFAAWTLVYGYTMNHLAFAVHRLKHRFSDIKCVKEYFEENGFELNKDGGVLKVSEDSLLLQVSAMSEKLVVEFADGVTQIVPASYIEFVERLVLPQFKDMPCDEIKEFHRREGLEQASAYHIMESTRFTA
Protein: UBA domain-containing protein RUP1 (Q12242)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Modulates the activity of the RSP5 HECT ubiquitin-protein ligase through its mediation of the interaction between RSP5 and the deubiquitinase UBP2. Involved in regulation of cell wall homeostasis.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:14562095}. Nucleus {ECO:0000269|PubMed:14562095}.
Interaction partners:
- Ubiquitin carboxyl-terminal hydrolase 2
- E3 ubiquitin-protein ligase RSP5
- Ubiquitin-ribosomal protein eS31 fusion protein
- Proline-rich protein HUA1
Sequence:
MMDNQAVKSLLEMGIPHEVAVDALQRTGGNLEAAVNFIFSNELPEQAEMGEENDGSQPRISENKIVAGTKPCDVPNNGDQDIDMPDVSGVDVDYDDDEDITDERSGSNSTSGCRVTAQNYDRYSISETSIPPPSYSIVQHNEFKSNVGDPTVVLPLPLNSLIESYFGLFALLTAVYFPHVFLKPDFKDLNYRADWFKGSSFTEPKYRLAYCEAEDGSTTSEIVLASGPNEGLQPHLLWQLQKLISVVNTRKCERAFVSAKVFTSSLEPQLRSKLADSEHLYEVLPAFIKSLAVDLEMCPGIRDRETRSLFISSALHTPNKNEPPMETFLSLFHFLPEEYDSNLYKMFNVLLYPEEEEEEEDVIRGGEQEEARYVEPENTLKEVAPVLTILFNELETNTESVSLPNGVDIPLEFYPQLYTKQCKDQLIRHIISKRKQARTRSRCLLQEINELKSYQGKNISTILESTLAYLQTIPDDANNEAAKQIASLKDTLNSARAAKMEEYKDLASKLHGEWNLSHPETHIINTAKQLGLIENPYILTMAALSPYSYFIRSRNGAWSWIQSNTLGTEFKVKKCSSPSVVQEAIKHGTKYASETPLMFIYCEEGKIPTEEVVAEALKSNSGCLKFAEDDQNSLKTLRSQFFDGMGDPEQATNNINNGNDNDNDDDIDSDN
Protein: Terephthalate 1,2-dioxygenase, terminal oxygenase component subunit beta 1 (TPADO terminal oxygenase component) (EC 1.14.12.15) (TER dioxygenase system) (TERDOS) (Terephthalate 1,2-dioxygenase small subunit 1) (Q3C1E2)
Organism: Comamonas sp
Function: Component of the terephthalate 1,2-dioxygenase multicomponent enzyme system which catalyzes the dioxygenation of terephthalate (TER/TPA) to 1,2-dihydroxy-3,5-cyclohexadiene-1,4-dicarboxylic acid (DCD). It can also use 2,5-dicarboxypyridine (PDC) and 1,4-napthalenedicarboxylic acid (NDC) as substrates, and preferentially uses NADPH which is the physiological electron donor.
Interaction partners:
Sequence:
MINEIQIAAFNAAYAKTVDSDAMEQWPTFFTKDCHYRVTNVDNHAEGLAAGIVWADSQDMLTDRISALREANIYERHRYRHILGLPSIQSGDATQASASTPFMVLRIMHTGETEVFASGEYLDKFTTIDGKLRLQERIAVCDSTVTDTLMALPL
Protein: Accessory gland-specific peptide 57Dc (45 kDa cAMP-dependent phosphoprotein) (Male accessory gland secretory protein 57Dc) (Pp45) (Q9V3J3)
Organism: Drosophila melanogaster (Fruit fly)
Function: Transferred from male to female during mating and may affect egglaying and behavior after mating.
Subcellular location: Secreted {ECO:0000269|PubMed:10451922}.
Interaction partners:
- Accessory gland-specific peptide 57Da
- Accessory gland-specific peptide 57Db
- ACP53C14A
- Accessory gland-specific peptide 70A
- ACP53C14B
- Accessory gland-specific peptide 26Aa
- Seminal fluid protein 24Bb
- Accessory gland-specific peptide 26Ab
- GEO08953p1
- GEO13347p1
Sequence:
MHGTHFLILLLLCGVLGSNGVTPDIKNVAKAERNMHNMLRCLKKNEPIVKSRILTLPPNCNQYVSAVVETWKPEGV
Protein: Dehydrin Xero 1 (P25863)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Dehydrin family protein
- At4g38410
- 1,4-dihydroxy-2-naphthoyl-CoA synthase, peroxisomal
- Dehydrin HIRD11
- Late embryogenis abundant protein 41
- RING-H2 finger protein ATL18
- Late embryogenesis abundant protein M17
- Probable desiccation-related protein LEA14
- Late embryogenesis abundant domain-containing protein / LEA domain-containing protein
- Esterase/lipase/thioesterase family protein
Sequence:
MESYQNQSGAQQTHQQLDQFGNPFPATTGAYGTAGGAPAVAEGGGLSGMLHRSGSSSSSSSEDDGLGGRRRKKKGITEKIKEKLPGHHDSNKTSSLGSTTTAYDTGTVHHEKKGMMEKIKEKLPGGHH
Protein: Endo-1,4-beta-xylanase A (Xylanase A) (EC 3.2.1.8) (B4XVN1)
Organism: Streptomyces sp
Function: Contributes to hydrolysis of hemicellulose, the major component of plant cell-walls. Hydrolyzes xylan to xylose and xylobiose.
Interaction partners:
Sequence:
MFRHHPTRGRRTAGLLAAALATLSAGLTAVAPAHPARADTATLGELAEAKGRYFGSATDNPELPDTQYTQILGSEFSQITVGNTMKWQYTEPSRGRFDYTAAEEIVDLAESNGQSVRGHTLVWHNQLPSWVDDVPAGELLGVMRDHITHEVDHFKGRLIHWDVVNEAFEEDGSRRQSVFQQKIGDSYIAEAFKAARAADPDVKLYYNDYNIEGIGPKSDAVYEMVKSFKAQGIPIDGVGMQAHLIAGQVPASLQENIRRFADLGVDVALTELDIRMTLPRTAAKDAQQATDYGAVVEACLVVSRCVGITVWDYTDKYSWVPSVFPGQGAALPWDEDFAKKPAYHAIAAALNGGSPAPGGNCTATYRVTSQWQGGFTAEITVGNDHTAPITGWTVTWTLSSGQSISHMWNGNLTVNGQDVTVRDVGYNGTLGGNGSTTFGFQGEGVADTPADVTCTPGRPSGTSA
Protein: ATP synthase-coupling factor 6, mitochondrial (ATPase subunit F6) (Q24407)
Organism: Drosophila melanogaster (Fruit fly)
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(0) domain and the peripheric stalk, which acts as a stator to hold the catalytic alpha(3)beta(3) subcomplex and subunit a/ATP6 static relative to the rotary elements.
Subcellular location: Mitochondrion. Mitochondrion inner membrane.
Interaction partners:
- ATP synthase subunit d, mitochondrial
- ATP synthase subunit beta, mitochondrial
- Putative ATP synthase subunit f
- ATP synthase subunit alpha, mitochondrial
- Protein stunted
- ATP synthase F
- ATP synthase subunit O, mitochondrial
- ATP synthase F
- ATP synthase subunit g
- ATP synthase subunit b, mitochondrial
Sequence:
MLSQSLLSGMRVLRTEARRNFGIVAPALNKASDPIQQLFLDKVREYKQKSAGGKLVDSNPDIERELKTELDRVAKQFGSDGKTDMLKFPEFQFPDVKVDPITQAPQ
Protein: Kinesin-like protein (F4HU83)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000256|ARBA:ARBA00004245}.
Interaction partners:
Sequence:
MAMASSRNGAVRGSMRPVSGANSSNLRSSSFKSRIPSSAPAPRRSSSASIGAADNGVPGRVRVAVRLRPRNADESVADADFADCVELQPELKRLKLRKNNWDTETYEFDEVLTEAASQKRVYEVVAKPVVESVLEGYNGTVMAYGQTGTGKTFTLGRLGDEDTAARGIMVRSMEDIIGGTSLDTDSISVSYLQLYMETIQDLLDPTNDNIAIVEDPRTGDVSLPGATHVEIRNQQNFLELLQLGETHRVAANTKLNTESSRSHAILMVHVKRSVVENEFPVSNEMESSSHFVRPSKPLVRRSKLVLVDLAGSERVHKSGSEGHMLEEAKSINLSLSALGKCINAIAENSPHVPLRDSKLTRLLRDSFGGTARTSLIVTIGPSPRHRGETTSTILFGQRAMKVENMLKIKEEFDYKSLSKKLEVQLDKVIAENERQLKAFDDDVERINRQAQNRISEVEKNFAEALEKEKLKCQMEYMESVKKLEEKLISNQRNHENGKRNGEVNGVVTASEFTRLKESLENEMKLRKSAEEEVSKVKSQSTLKTRSGEGEDAGITRLQKLLEDEALQKKKLEEEVTILRSQLVQLTFEADQISLHCMPSLKILLNTHVLFFQMRRCLDRGAPGNSYSGTDSLPSRHSQARESVNGQKAPFATLCEQVGLQKILQLLESDDANIRIHAVKVVANLAAEEANQEKIVEAGGLTSLLMLLRSYEDETVRRVAAGAIANLAMNEVSQQLIVDQGGISLLSLTAADAEDPQTLRMVAGAIANLCGNDKLQARLWSDGGIKALLGMVRCGHPDVLAQVARGIANFAKCESRATTQGVKSGRSLLIEDGALPWIVQHANDEAAPIRRHIELALCHLAQHEVNAKEMISGGALWELVRISKECSREDIRSLAHRTLSSSPVFRSEIRRLGIQF
Protein: Importin beta SMX1 (Suppressor of mRNA export mutant protein 1) (karyopherin-108) (Q04175)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Nuclear transport factor (karyopherin) involved in protein transport between the cytoplasm and nucleoplasm. Required for the nuclear import of ribosomal proteins (RPL11, RPL16, RPL25, RPL31A), the poly(A)-binding protein PAB1, the HO endonuclease or the tRNA and snRNA chaperone LHP1. Indirectly involved in nuclear mRNA export through its PAB1 nuclear import activity.
Subcellular location: Cytoplasm. Nucleus, nuclear pore complex.
Interaction partners:
- Importin subunit beta-1
- Importin subunit beta-2
- Importin subunit beta-4
- Importin subunit beta-3
- La protein homolog
- Importin subunit beta-5
- mRNA transport regulator MTR10
- Importin subunit alpha
- Shuttling pre-60S factor ECM1
- Exportin-T
Sequence:
MVQEQAILSCIEQTMVADAKIIKEAEQQLFEFQKQPGFTSFLLNIVSDDNFALNVRLSSAIYLKNKIHRSWDTKREDGIKADEKLSIKERLIETLVKNCENNHIRPILTETINGILVGQEDWDLAPIIKNLLSSGDASYIYPGLLLLFQLCKAHRWDMVGSRDYIDSVIEELFPIVEGIASNIGSQTDYRSNEILYLILKSFKYACLNNLPQYFSQPERIMSWVQLHLYLCSKPLPVEVMELDPADRSLDKRVKVNKWGFGNLNRFLQRYNKITKAITKEFIDYIFNTIVPIILREFFKDIEAWGNNSLWLSDSSLYFLISFLEKCVTIDQLYPLIEPHLQIIFENVIFPCLCANEQSIELLEDDQEEYTRRYFDINREGSTPDAASADFIFLIGSKRPEKLNNILPFINDIFTRFDANSSDINMAFKEEGALRTLSNLFSFIDEPSVLENIFGHFIVPLLSQDKYMFLVARSLETIALYSEEFKDMNILSQLFELTYTNFLNSNVLPVQIEAADAIKCLIVSNPQIHPAVSAHVPGMMEKLLKLSKIFEIDILSEVMEALVERFSDELSPFAKDLASNLVEQFLRIAQALVENPSETYSASDQEQEIQASGLLQTMTTMVMSMNKVPLIESLAPVVKFVVLHAQISFITEAVDLLDALTISSHLLYNQIAPPIWELLHDILDSFQTYAMDYFEAYSIFFETIVMTGFPQDQTYVQPLLEILSAKLESEVDYDIEHVMQILMYFALSMRDIPLFSKAIKVSTNDELGLDSKCIVKLGLANLFAKPIETLQIMENEGFTINFFTNWFNEKFYSVFAIKLQVLVILTLLKMPEVPNSVSPLLNNLTNKLVELTLSLPKAIRNRDAVTEGKSLEGDLTPEEEEEYFIECDDDMKETVLDQINVFQEVHTFFKNLQNEDAGKYEKIINYLDESKRDSLQVILEFVSQH
Protein: Aminomethyltransferase, mitochondrial (EC 2.1.2.10) (Glycine cleavage system T protein) (GCVT) (Q8CFA2)
Organism: Mus musculus (Mouse)
Function: The glycine cleavage system catalyzes the degradation of glycine.
Subcellular location: Mitochondrion {ECO:0000250|UniProtKB:P48728}.
Interaction partners:
- Glycine dehydrogenase
- Glycine cleavage system H protein, mitochondrial
- Dihydrolipoyl dehydrogenase, mitochondrial
- Bifunctional methylenetetrahydrofolate dehydrogenase/cyclohydrolase 2, mitochondrial
- Bifunctional methylenetetrahydrofolate dehydrogenase/cyclohydrolase
- Serine hydroxymethyltransferase, mitochondrial
- Serine hydroxymethyltransferase, cytosolic
- Bifunctional purine biosynthesis protein ATIC
- Monofunctional C1-tetrahydrofolate synthase, mitochondrial
- Trifunctional purine biosynthetic protein adenosine-3
Sequence:
MHRIVSVVAPLGFRLQAQPLVQSRPLSSVQDVLRRTPLYDFHLAHGGKMVAFAGWSLPVQYRDSHVDSHLHTRRHCSLFDVSHMLQTKIFGCDRVKLLESVVVGDIAELRPNQGTLSLFTNEAGGILDDLIVSNTSEGHLYVVSNAGCRDKDLALMQDKVKEFQNRGLDVGLEVVENALLALQGPTATQVLQAGVTDDMKKLPFMTSAVMEVFGVSGCRVTRCGYTGEDGVEISVPATGAVHLATTLLKNPEVKLAGLAARDSLRLEAGLCLYGNDIDEHTTPVEGSLSWTLGKRRRIAMDFPGAKIIVPQLKGEVQRRRVGLICEGAPVRAHSPILNTEGTVIGTVTSGCPSPSLKKNVAMGYVPFKYSRPGTQLLVEVRRKQQMTVVSKMPFVPTNYYTLK
Protein: V-type proton ATPase catalytic subunit A (V-ATPase subunit A) (EC 7.1.2.2) (V-ATPase 69 kDa subunit) (Vacuolar proton pump subunit alpha) (P31404)
Organism: Bos taurus (Bovine)
Function: Catalytic subunit of the V1 complex of vacuolar(H+)-ATPase (V-ATPase), a multisubunit enzyme composed of a peripheral complex (V1) that hydrolyzes ATP and a membrane integral complex (V0) that translocates protons. V-ATPase is responsible for acidifying and maintaining the pH of intracellular compartments and in some cell types, is targeted to the plasma membrane, where it is responsible for acidifying the extracellular environment. In aerobic conditions, involved in intracellular iron homeostasis, thus triggering the activity of Fe(2+) prolyl hydroxylase (PHD) enzymes, and leading to HIF1A hydroxylation and subsequent proteasomal degradation (By similarity). May play a role in neurite development and synaptic connectivity (By similarity).
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:P38606}. Cytoplasm, cytosol {ECO:0000250|UniProtKB:P50516}. Cytoplasmic vesicle, secretory vesicle {ECO:0000250|UniProtKB:P38606}. Cytoplasmic vesicle, clathrin-coated vesicle membrane {ECO:0000269|PubMed:32764564}; Peripheral membrane protein {ECO:0000305}. Lysosome {ECO:0000250|UniProtKB:P50516}. Note=Co-localizes with WFS1 in the secretory granules in neuroblastoma cell lines. {ECO:0000250|UniProtKB:P38606}.
Interaction partners:
- V-type proton ATPase 21 kDa proteolipid subunit c''
- V-type proton ATPase subunit E 1
- Renin receptor
- V-type proton ATPase subunit H
- V-type proton ATPase subunit d 1
- V-type proton ATPase subunit D
- V-type proton ATPase subunit F
- V-type proton ATPase subunit C 1
- V-type proton ATPase 16 kDa proteolipid subunit c
- V-type proton ATPase 116 kDa subunit a 1
Sequence:
MDFSKLPKIRDEDKESTFGYVHGVSGPVVTACDMAGAAMYELVRVGHSELVGEIIRLEGDMATIQVYEETSGVSVGDPVLRTGKPLSVELGPGIMGAIFDGIQRPLSDISSQTQSIYIPRGVNVSALSRDVKWDFTPCKNLRVGSHITGGDIYGIVNENSLIKHKIMLPPRNRGTVTYIAPPGNYDTSDVVLELEFEGIKEKFSMVQVWPVRQVRPVTEKLPANHPLLTGQRVLDALFPCVQGGTTAIPGAFGCGKTVISQSLSKYSNSDVIIYVGCGERGNEMSEVLRDFPELTMEVDGKVESIMKRTALVANTSNMPVAAREASIYTGITLSEYFRDMGYHVSMMADSTSRWAEALREISGRLAEMPADSGYPAYLGARLASFYERAGRVKCLGNPEREGSVSIVGAVSPPGGDFSDPVTSATLGIVQVFWGLDKKLAQRKHFPSVNWLISYSKYMRALDEYYDKHFTEFVPLRTKAKEILQEEEDLAEIVQLVGKASLAETDKITLEVAKLIKDDFLQQNGYTPYDRFCPFYKTVGMLSNMIAFYDMARRAVETTAQSDNKITWSIIREHMGEILYKLSSMKFKDPVKDGEAKIKADYAQLLEDMQNAFRSLED
Protein: Adenine/guanine permease AZG2 (AzgA-homolog protein) (Protein AZAGUANINE RESISTANT 2) (AtAzg2) (Q84MA8)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Transports natural purines (adenine and guanine) as well as purine analogs. Confers sensitivity to 8-azaadenine and 8-azaguanine (8-azg).
Subcellular location: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
- Purine permease 14
- Nucleobase-ascorbate transporter 12
- Nucleobase-ascorbate transporter 3
- Cysteine/Histidine-rich C1 domain family protein
- Putative nucleobase-ascorbate transporter 9
- Equilibrative nucleotide transporter 8
- Nucleobase-ascorbate transporter 5
- Cytoplasmic tRNA 2-thiolation protein 2
- Purine-uracil permease NCS1
- Nucleobase-ascorbate transporter 1
Sequence:
MGREKTLCKSWSDMKKHLNDTVSKSFIGRFFKLEARKTTFTTELRAATATFLTMAYIITVNANILADSGATCSINDCSTVASSSPPGPECVLGSNPGYEQCISRVKKDLVVATSLSAMVGSLAMGLLANLPFGLAPGMGANAYIAYNVVGFRGSGSISYHTAMAIVLLEGCAFLAVSALGLRGKLARLIPQTVRLACAVGIGMFIAFVGLQMNQGIGLVGPDKSTLVTLTACAETDPVTGACLGGKMKSPTFWLAVVGFLITSFGLMKNVKGSMIYGIVFVTAISWIRGTQVTIFPHTPLGDSNYNYFTKIVDFHKIQSTLGAISFTEFRKSEVWVAFATLFYVDLLGTTGVLYTMAEIGGFVEDGKFEGEYAAYLVDAGSSVVGSALGVTTTATFVESSAGLKEGGKTGLTAVIVGLYFLASMFFTPLVTNVPRWAVGPSLVMVGVMMMGVVKDIRWGETKEAVTAFVTILLMPLTYSIANGIIAGIGIYLALSMYDVVLGVAKWLNGVRKRVMREHNQVSSVATVEIV
Protein: C2H2 and C2HC zinc fingers superfamily protein (C2H2-type zinc finger protein-like) (Q9FJV4)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Protein indeterminate-domain 11
- Zinc finger
- Protein indeterminate-domain 7
- Protein indeterminate-domain 12
- At4g35700
- Zinc finger protein WIP6
- Zinc finger protein WIP2
- Protein SENSITIVE TO PROTON RHIZOTOXICITY 2
- Zinc finger protein BALDIBIS
- Polyadenylation and cleavage factor homolog 4
Sequence:
MSSIPNRFNIYGGDTTNHRESLPIEMNHNSRMVRSMFITSDRMNHRDLFSSPPSFSSYQNSHISSSSVGFNNSHMTYHMLKRNYDSVSRADYFSTKDHSHFTQVSFTQTITNKYTTIVPSNIFDTVHYDIGRVKRAIDFRNIWNPKSHLPKKFNRQCEILNPTPLNIVFPHQDSADRQHLDIIFSSSKHNHVFQDGRSLKKISEPTNLFEKSNSYDSQEDEKIDAYQYDGRTHSLPYTKYGPYTCPRCNGVFDTSQKFAAHMLSHYNNETDKERDQRFRARNKKRYRKFMDSLKISKQKI
Protein: Transcription factor A, mitochondrial (mtTFA) (Testis-specific high mobility group protein) (TS-HMG) (P40630)
Organism: Mus musculus (Mouse)
Function: Binds to the mitochondrial light strand promoter and functions in mitochondrial transcription regulation (By similarity). Component of the mitochondrial transcription initiation complex, composed at least of TFB2M, TFAM and POLRMT that is required for basal transcription of mitochondrial DNA (By similarity). In this complex, TFAM recruits POLRMT to a specific promoter whereas TFB2M induces structural changes in POLRMT to enable promoter opening and trapping of the DNA non-template strand (By similarity). Required for accurate and efficient promoter recognition by the mitochondrial RNA polymerase (By similarity). Promotes transcription initiation from the HSP1 and the light strand promoter by binding immediately upstream of transcriptional start sites (By similarity). Is able to unwind DNA (By similarity). Bends the mitochondrial light strand promoter DNA into a U-turn shape via its HMG boxes (By similarity). Required for maintenance of normal levels of mitochondrial DNA. May play a role in organizing and compacting mitochondrial DNA.
Subcellular location: [Isoform Mitochondrial]: Mitochondrion {ECO:0000250|UniProtKB:Q00059}. Mitochondrion matrix, mitochondrion nucleoid {ECO:0000250|UniProtKB:Q00059}.; SUBCELLULAR LOCATION: [Isoform Nuclear]: Nucleus {ECO:0000269|PubMed:8673128}.
Interaction partners:
- Dimethyladenosine transferase 2, mitochondrial
- DNA-directed RNA polymerase, mitochondrial
- Peroxisome proliferator-activated receptor gamma coactivator 1-alpha
- Dimethyladenosine transferase 1, mitochondrial
- Cellular tumor antigen p53
- DNA polymerase subunit gamma-1
- Nuclear respiratory factor 1
- Single-stranded DNA-binding protein, mitochondrial
- NAD-dependent protein deacetylase sirtuin-1
- Twinkle mtDNA helicase
Sequence:
MALFRGMWSVLKALGRTGVEMCAGCGGRIPSSISLVCIPKCFSSMGSYPKKPMSSYLRFSTEQLPKFKAKHPDAKLSELVRKIAALWRELPEAEKKVYEADFKAEWKAYKEAVSKYKEQLTPSQLMGMEKEARQRRLKKKALVKRRELILLGKPKRPRSAYNIYVSESFQEAKDDSAQGKLKLVNEAWKNLSPEEKQAYIQLAKDDRIRYDNEMKSWEEQMAEVGRSDLIRRSVKRSGDISEH
Protein: Cytochrome cd1 nitrite reductase (Q44012)
Organism: Cupriavidus necator (Alcaligenes eutrophus) (Ralstonia eutropha)
Interaction partners:
Sequence:
MKAKNWLYPAIAALPLSLWLGLPHAATKAEPKAEPKAAIPTLTAAEFDHARQIYFERCAGCHGVLRKGATGKSLTPDITRARGTEYLKTFIKYGSPAGMPNWGTSGDLTDPEVDLMARYIQLDPPTPPEYSLADIEKSRKDILPVAQRPTKKMNQYNLDNLFSVTLRDAGEVALIDGDSKQIINIVKTGYAVHISRMSASGRYLYVIGRDARLDLIDLWLPKPDIVAEVKVGMEARSVETSKYKGYEDKYAVAGSYWPPQYVIMEGDTLKPLKVVSTRGMTVDNEYHPEPRVAAIVASHFHPEFVINAKETGKILMVNYSDLSNLKTTTIDSAKFLHDGGFDATGRYFLVAANASDKIAVVDTKEDKLAALIDVGKTPHPGRGANFMHPKLGPVWATSHLGDETISLIGTDPAGHPAQAWKVVQTIKGQGGGSLFIKTHPKSSNLWVDTPLNPDAKLNQSVAVFDTRNLEAGYKVLPIADWAGLKGAGARRVVQAEYNKAGDEVWFSVWGTKDGESALVVVDDKTRTLKTVIKDKRLITPTGKFNAYNTQHDVY
Protein: Cathepsin Z (EC 3.4.18.1) (Cathepsin Y) (Q9R1T3)
Organism: Rattus norvegicus (Rat)
Function: Exhibits carboxy-monopeptidase as well as carboxy-dipeptidase activity. Capable of producing kinin potentiating peptides.
Subcellular location: Secreted.
Interaction partners:
- Apoptosis regulator Bcl-2
- BH3-interacting domain death agonist
- Bcl-2-like protein 1
- Angiotensinogen
- Legumain
- Cathepsin D
- Baculoviral IAP repeat-containing protein 5
Sequence:
MASSGSVQQLRLVLLMLLLAGAARASLYFRPGQTCYRPLHRDHLALLGRRTYPRPHEYLSPADLPKNWDWRNVNGVNYASVTRNQHIPQYCGSCWAHGSTSALADRINIKRKGAWPSTLLSVQNVIDCGNAGSCEGGNDLPVWEYAHKHGIPDETCNNYQAKDQECDKFNQCGTCTEFKECHTIQNYTLWRVGDYGSLSGREKMMAEIYANGPISCGIMATERMSNYTGGIYTEYQNQAIINHIISVAGWGVSNDGIEYWIVRNSWGEPWGERGWMRIVTSTYKGGTGSSYNLAIEEACTFGDPIV
Protein: SPerm CHromatin enriched (Q17626)
Organism: Caenorhabditis elegans
Interaction partners:
- SPerm CHromatin enriched
- Nematode Specific Peptide family
- PDZ domain-containing protein
- SPerm CHromatin enriched
- Sperm-Specific family, class Q
- Sperm-specific class P protein 34
- Sperm-specific class P protein 16
- non-specific serine/threonine protein kinase
- Histone H2A
- PDZ domain-containing protein
Sequence:
MPKSKSQKNKLRPRDSKGRFTPLAKTKRTVVSRSRSRSASRARRSRSVGRPASRRISVRSVSTHTAKSPSLVVVISPSPRRRRSSTSRSSRRSVVRSASRGSVSRRSSSRGSVYGRTGRSRSSKRSRSRSRSRSRSRSRSYSRSRSGSRRSSRRRSRRRSSLKARGRRASTAKKTPAKRRSRSRSQQKVKRSMSRKG
Protein: Serine/threonine-protein kinase 10 (EC 2.7.11.1) (F1NBT0)
Organism: Gallus gallus (Chicken)
Function: May act as a polo kinase kinase by mediating phosphorylation of PLK1.
Subcellular location: Cell membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}.
Interaction partners:
Sequence:
MAFANFRRILRLSTFEKRRSKEYEHVRRDLDPGEVWEVVGELGDGAFGKVYKAKNKETGALAAAKVIETKNEDELEDYMVEIEILATCDHPHIVKLLGAFYWEGKLWIMIEFCPGGAVDATMLELDRGLTEPQIQVICRQMLEALHYLHSKKIIHRDLKAGNVLLTQDGDIKLADFGVSAKNVKTLQKRDSFIGTPYWMAPEVVMCETMKDTPYDYKADIWSLGITLIEMAQIEPPHHELNPMRVLLKIAKSDPPTLSCPSKWSLEFRDFLKTALDKNPETRPSAAQLLEHPFVSKVTSNRALRELVAEAKAEVLEEIEDSRDEAEDDDSSESASLPGKHKRDPSEVSQLSFDGDKPPDSSSLKTTNGPVATEKEMVNGQSDKVLDERISSDSDKLVNSHSTKTLASSGPDEGKATPGKPDIISLSGRRGSSAEGDKQPMPGSKERRSMVDRPESSHLENFPEEKLANGSLDSSAVFPGSRSKGDSDSGSTSASESMDLTISLSADLSLNRESGSISLKDSRMHNKTLKRTRKFVVDGVEVSVTTSKIISEDEKKDEEMRFLRRQELRELRLLQKEEHRNQAQLNSKHQLQLDQMLRRFEQEMTAKKKFYDTELENLERQQKQQIEKMEQDHSLRRREEAKRIRLEQERDHVKFMEQLKQKKKEVKNEVEKLPRQQRKENMKVKMDDFAQRKQTMEQDFLAKQKEDLELAMKNITAQNKKEICDKERECLNKKQQLMRDREACIWDLEERQQQEKHQLIKQQLKDQYFLQRHELLRKHEKEREQMQRYNQRMIEQLKIRQQQEKARLPKIQRSEGKTRMAMYKKSLHIHSSGSAAEQREKIKQFSQQEEKRQKAERLHQQQKHETQMKDMLAQCESNTNELQQLQNEKCHLLIEHETQKLKSLDENHNLHMKEWRDKLRPRKKALEDELNQKKREQEMFFKLSVEADEQTPASPVKHTKFIPFSSTESS
Protein: DNA endonuclease RBBP8 (EC 3.1.-.-) (CtBP-interacting protein) (CtIP) (Q6GNV6)
Organism: Xenopus laevis (African clawed frog)
Function: Endonuclease that cooperates with the MRE11-RAD50-NBN (MRN) complex in DNA-end resection, the first step of double-strand break (DSB) repair through the homologous recombination (HR) pathway. Functions downstream of the MRN complex and ATM, promotes ATR activation and its recruitment to DSBs in the S/G2 phase facilitating the generation of ssDNA.
Subcellular location: Nucleus {ECO:0000269|PubMed:20064462}. Chromosome {ECO:0000250|UniProtKB:Q99708}. Note=Associates with sites of DNA damage in S/G2 phase. Recruited to DSBs by the MRE11-RAD50-NBN (MRN) complex following phosphorylation. {ECO:0000250|UniProtKB:Q99708}.
Interaction partners:
Sequence:
MSITASTCGSPSSSESLPNGDLFKELWSKLKECHDKDLQELLMKIGKLKKERCLDAQRLEEFYTKNQHLREQQKTLHDTIKVLEDRLRAGLCDRCTVTEEHMRKKQQEFENIRQQNLKLITELMNDKNALQDENKRLSEQLHDMQKNRHRRKSDEENPADTGDGEDGVIPDSPLSTFSLSMVSRMRRKKENKHVRYTEQTQEDALTFDRKISSGTRPQISTQVNMRKGEDVLVAETLELAPLPNKYEVCTEKPVFNLATVVAETLGLDAMEESQSQSVFNQPGITCAPLFHKSEDSSPRQVKVEFTEGSMEGFQTNDDDTEWNRREASPVFGEPVRNIRRGTDMDCSSPPLPVGLSSKLKSHCSRNAPDFSVHAKAEDGALLTRLSHCIETDSVISQCSSNRQDVLRPSPNKSDAQMGKYIFDSEQHKQTGNRYGKRKNAEAEQEESCESSFDKENNIPLKDISGARHSMLDKPLDLSDRFSVLRPQDRSHESSSRTKLTISLVPEKPDTKTILHIDLKENLHQQTRQKKVFVSGLVEHSAFNLHEDNEVTEEDNKPFHDSETEIMCHVPKRKPRAVHRGVQPTSVLQPNLHMVHACLESQGRPPIDNMQWSIDPGADLSQYEMDMTMEDSKSGSPAKPELEDMDYTYVNESCLLKLKMGDPDDSEAESKDQDSFGEMFDKTEYGEYASYIKDKSPSQSISCKERSDIPSIENKKITSEKEHESKGEPYQKQKAFVEPYFQRPERKKPAIDFPHIEVVRNKEERRKMLGHTCKECELYYADLPEEERAKKLASCSRHRFRYIPPSTPENFWEVGFPSTQTCKDRGYIKEELSPCQRPRRRQPYNAIFTSKIKEQKT
Protein: Cysteine protease (EC 3.4.22.-) (Q4Q7T2)
Organism: Leishmania major
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496, ECO:0000256|RuleBase:RU363115}.
Interaction partners:
- Autophagy-related protein
- Protein kinase domain-containing protein
- Protein kinase domain-containing protein
Sequence:
MLRYVQDLWSAFFPTEAVFPLQVVGRSGAAVESREELEKALTDTFLIFTYRDGFEAIPAVTRLIETDQGWGCLLRTSQMLLAHFLWVHGRPADRKLSLFFDHSAETAPFSIHNMIRSVWNRRVFKAEYWSPSQGCEAIKRTVQGAVKTEQLQTRVMVVTSTNGCIYADEVQHTFKQGADVVLVLASVRVSAAAQLTQESYLQIEKLMEQPQCLGVVGGVPGRSYYFFAHNQTQLFYLDPHQRTAAALLCEGLSAAASVTPSVADVRCVHWSRVDTSLFLAFAVTTRDEWAALEVHLSNRFMHVESQQTQRDCDHLGGARPGHADSTFVSPLQMGHSCAMGGASISETAPLVHRRTLRLPRKRFKEGGVGTATAAAAERDDGEDELDTDSWEYLD
Protein: Prostasin (EC 3.4.21.-) (Channel-activating protease 1) (CAP1) (Serine protease 8) [Cleaved into: Prostasin light chain; Prostasin heavy chain] (Q9ES87)
Organism: Rattus norvegicus (Rat)
Function: Possesses a trypsin-like cleavage specificity with a preference for poly-basic substrates. Stimulates epithelial sodium channel (ENaC) activity through activating cleavage of the gamma subunits (SCNN1G) (By similarity).
Subcellular location: Cell membrane {ECO:0000250}; Single-pass membrane protein {ECO:0000250}.; SUBCELLULAR LOCATION: [Prostasin]: Secreted, extracellular space {ECO:0000250}.; SUBCELLULAR LOCATION: [Prostasin light chain]: Secreted, extracellular space {ECO:0000250}. Note=Found in the seminal fluid. Secreted after cleavage of its C-terminus. {ECO:0000250}.; SUBCELLULAR LOCATION: [Prostasin heavy chain]: Secreted, extracellular space {ECO:0000250}. Note=Found in the seminal fluid. Secreted after cleavage of its C-terminus. {ECO:0000250}.
Interaction partners:
- Kunitz-type protease inhibitor 1
- Epithelial sodium channel subunit gamma
- Epithelial sodium channel subunit beta
- Kunitz-type protease inhibitor 2
- Furin
- Epithelial sodium channel subunit alpha
Sequence:
MALRVGLGLGQLEALFVLLLIGLLQSRIGADGTEASCGAVIQPRITGGGSAKPGQWPWQVSITYNGVHVCGGSLVSNQWVVSAAHCFPREHSKEEYEVKLGAHQLDSFSNDIVVHTVAQIISHSSYREEGSQGDIALIRLSSPVTFSRYIRPICLPAANASFPNGLHCTVTGWGHVAPSVSLQTPRPLQQLEVPLISRETCSCLYNINAVPEEPHTIQQDMLCAGYVKGGKDACQGDSGGPLSCPIDGLWYLAGIVSWGDACGAPNRPGVYTLTSTYASWIHHHVAELQPRVVPQTQESQPDGHLCNHHPVFNLAAAQKLSRPILFLPLSLTLGLFSLWLEH