wanglab/gogpt-training-data huggingface dataset:
Protein: 2Fe-2S ferredoxin-like superfamily protein (F4IE99)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Plastid, chloroplast {ECO:0000256|ARBA:ARBA00004229}.
Interaction partners:
Sequence:
MALILPCTFCTSLQKKNFPINRRYITNFRRGATTATCEFRIPVEVSTPSDRGSLVVPSHKVTVHDRQRGVVHEFEDQYILHSAESQNISLPFACRHGCCTSCAVRVKSGELRQPQALGISAELKSQRISSLDLIQCQKTYLTGYALLCVGFPTSDLEVETQDEDEVYWLQFGRYFARGPIERDDYALELAMGDE
Protein: Non-structural protein 1 (NSP1) (NCVP2) (Non-structural RNA-binding protein 53) (NS53) (Q99FX5)
Organism: Rotavirus A (strain RVA/SA11-4F/G3P6[1]) (RV-A) (Simian Agent 11 (strain 4F))
Function: Plays a role in the inhibition of host innate immunity by inducing the degradation of key host factors required to activate interferon production such as IRF3, IRF5 or IRF7. Associates with components of cullin RING ligases (CRLs) including CUL1 or CUL3, which are essential multisubunit ubiquitination complexes, to modulate their activities.
Subcellular location: Host cytoplasm, host cytoskeleton {ECO:0000255|HAMAP-Rule:MF_04088, ECO:0000269|PubMed:8189533}.
Interaction partners:
Sequence:
MATFKDACFHYRRLTALNRRLCNIGANSICMPVPDAKIKGWCLECCQIADLTHCYGCSLPHVCKWCVQNRRCFLDNEPHLLKLRTVKHPITKDKLQCIIDLYNIIFPINDKVIRKFERMIKQRKCRNQYKIEWYNHLLLPITLNAAAFKFDENNLYYVFGLYEKSVSDIYAPYRIVNFINEFDKLLLDDINFTRMSNLPIELRNHYAKKYFQLSRLPSSKLKQIYFSDFTKETVIFNTYTKTPGRSIYRNVTEFNWRDELELYSDLKNDKNKLIAAMMTSKYTRFYAHDNNFGRLKMTIFELGHHCQPNYVASNHPGNASDIQYCKWCNIKYFLSKIDWRIRDMYNLLMEFIKDCYKSNVNVGHCSSVENIYPLIKRLIWSLFTNHMDQTIEEVFNHMSPVSVEGTNVIMLILGLNISLYNEIKRTLNVDSIPMVLNLNEFSSIVKSISSKWYNVDELDKLPMSIKSTEELIEMKNSGTLTEEFELLISNSEDDNE
Protein: Centromere protein W (A0A0R4IXK5)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Chromosome, centromere, kinetochore {ECO:0000256|ARBA:ARBA00004629}. Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MSKKAPRAALKHHMKKNANIRIGKNADLMAQLNLLMVLHRLAEECRVKAFEEKSATIKTHHVRAVAKKLLKSTRG
Protein: Probable cyclic di-GMP phosphodiesterase PdeK (EC 3.1.4.52) (P37649)
Organism: Escherichia coli (strain K12)
Function: Phosphodiesterase (PDE) that catalyzes the hydrolysis of cyclic-di-GMP (c-di-GMP) to 5'-pGpG.
Subcellular location: Cell membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Cyclic di-GMP phosphodiesterase PdeH
- Probable diguanylate cyclase DgcC
- Probable diguanylate cyclase DgcI
- Diguanylate cyclase DgcM
- Probable diguanylate cyclase DgcJ
- Probable diguanylate cyclase CdgI
- Probable diguanylate cyclase DgcQ
- Diguanylate cyclase DgcP
- Probable diguanylate cyclase DgcE
- Cellulose synthase catalytic subunit
Sequence:
MRVSRSLTIKQMAMVAAVVLVFVFIFCTVLLFHLVQQNRYNTATQLESIARSVREPLSSAILKGDIPEAEAILASIKPAGVVSRADVVLPNQFQALRKSFIPERPVPVMVTRLFELPVQISLGVYSLERPANPQPIAYLVLQADSFRMYKFVMSTLSTLVTIYLLLSLILTVAISWCINRLILHPLRNIARELNAIPAKELVGHQLALPRLHQDDEIGMLVRSYNLNQQLLQRHYEEQNENAMRFPVSDLPNKALLMEMLEQVVARKQTTALMIITCETLRDTAGVLKEAQREILLLTLVEKLKSVLSPRMILAQISGYDFAVIANGVQEPWHAITLGQQVLTIMSERLPIERIQLRPHCSIGVAMFYGDLTAEQLYSRAISAAFTARHKGKNQIQFFDPQQMEAAQKRLTEESDILNALENHQFAIWLQPQVEMTSGKLVSAEVLLRIQQPDGSWDLPDGLIDRIECCGLMVTVGHWVLEESCRLLAAWQERGIMLPLSVNLSALQLMHPNMVADMLELLTRYRIQPGTLILEVTESRRIDDPHAAVAILRPLRNAGVRVALDDFGMGYAGLRQLQHMKSLPIDVLKIDKMFVEGLPGDSSMIAAIIMLAQSLNLQMIAEGVETEAQRDWLAKAGVGIAQGFLFARPLPIEIFEESYLEEK
Protein: Auxilin-like clathrin uncoating factor SWA2 (Bud site selection protein 24) (DnaJ-related protein SWA2) (J protein SWA2) (Synthetic lethal with ARF1 protein 2) (Q06677)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Cofactor for the uncoating of clathrin-coated vesicles (CCVs) by Hsp70-type chaperones (SSA1/2/3 and SSB1/2). Coat disassembly is important for fusion of vesicles with target membranes and for recycling components of clathrin coats to the cytoplasm for further rounds of vesicle formation. Binds to assembled clathrin and recruits the ATP-activated chaperone to CCVs. Stimulates the ATPase activity of the clathrin-associated Hsp70-type chaperone SSA1, which then disrupts clathrin-clathrin interactions, leading to release of the clathrin coat. In addition, prevents unproductive clathrin assembly in the cell. Also required for cortical endoplasmic reticulum inheritance.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:11084334}. Endoplasmic reticulum membrane {ECO:0000269|PubMed:11084334}; Peripheral membrane protein {ECO:0000269|PubMed:11084334}.
Interaction partners:
- Clathrin heavy chain
- Protein SIS1
- J domain-containing protein APJ1
- Pre-mRNA-splicing factor CWC23
- DnaJ-like protein 1
- Protein CAJ1
- Diphthamide biosynthesis protein 4
- DnaJ protein homolog XDJ1
- J protein JJJ2
- Mitochondrial protein import protein MAS5
Sequence:
MSDPFAHLLTSLKNKDSASASKETTPQSSNSPSITGSAVADVARTDKSPNDSLHSISAPPLIPSPKVDFSAPPLVPTNSTTKSNTANNTPPSALANTDDDFNQLFGMGTVTTTDTIQKPDEDYYGSKEDHLYNGDDALVDEVKDMEIARLMSLGLSIEEATEFYENDVTYERYLEILKSKQKERNDLAIRKKESGIKMEKSGLSNIVGTDSNNLFSMATDFFNKGKKLVDQWTSFPPEANDRLNNYSKTHDKVEDYDLPQVNDSPNRILFEDNEVVENLPPADNPDQDLLTDFETKIDITKRTAPDVSHSSSPTSGILIEENSRRNEPLIEDSLLDFSEGNLTNSKSNEDSTLFNENSNTDSTIPISDIELSGYNEFKAKGTSLFKNGDYINSLQEYEKSLNTLPLNHPLRIIALSNIIASQLKIGEYSKSIENSSMALELFPSSKAKWKNKISNSDPERSFNDIWPKIMIRRAESFEHLESFKKALETYQELIKKNFFDDKIMQGKRRCQDFINPPPVKKSMPVKKKTTTTSPATKKQNLTASSSNSPISVDSTSEIKKRELENAKLALYDKVFEKISSWKDGKDDDIRHLLANLSSLLTWCNWKDVSMQDLVMPKRVKITYMKAVAKTHPDKIPESLSLENKMIAENIFSTLSIAWDKFKLQNDIN
Protein: LRP chaperone MESD (LDLR chaperone MESD) (Mesoderm development candidate 2) (Mesoderm development protein) (Q9ERE7)
Organism: Mus musculus (Mouse)
Function: Chaperone specifically assisting the folding of beta-propeller/EGF modules within the family of low-density lipoprotein receptors (LDLRs). Acts as a modulator of the Wnt pathway through chaperoning the coreceptors of the canonical Wnt pathway, LRP5 and LRP6, to the plasma membrane. Essential for specification of embryonic polarity and mesoderm induction. Plays an essential role in neuromuscular junction (NMJ) formation by promoting cell-surface expression of LRP4. May regulate phagocytosis of apoptotic retinal pigment epithelium (RPE) cells.
Subcellular location: Endoplasmic reticulum {ECO:0000269|PubMed:12581525}. Note=Released from apoptotic cells and shed photoreceptor outer segments (PubMed:27184668). {ECO:0000269|PubMed:27184668}.
Interaction partners:
- Low-density lipoprotein receptor-related protein 6
- Low-density lipoprotein receptor-related protein 5
Sequence:
MAASRWLRAVLLFLCASDLLLLPPPNAYAADTPGEATPPPRKKKDIRDYNDADMARLLEQWEKDDDIEEGDLPEHKRPSAPIDFSKLDPGKPESILKMTKKGKTLMMFVTVSGNPTEKETEEITSLWQGSLFNANYDVQRFIVGSDRAIFMLRDGSYAWEIKDFLVSQDRCAEVTLEGQMYPGKGGGSKEKNKTKPEKAKKKEGDPKPRASKEDNRAGSRREDL
Protein: Heat shock factor protein 3 (HSF 3) (HSF 3C) (HSTF 3C) (Heat shock transcription factor 3) (HSTF 3) (P38531)
Organism: Gallus gallus (Chicken)
Function: DNA-binding protein that specifically binds heat shock promoter elements (HSE) and activates transcription. HSF3 binds DNA constitutively only when the C-terminal region is deleted.
Subcellular location: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}. Note=Cytoplasmic during normal growth and moves to the nucleus upon activation. {ECO:0000250}.
Interaction partners:
- Heat shock protein beta-1
- Uncharacterized protein.
- Outer dense fiber of sperm tails 2 like.
Sequence:
MREGSALPGAPGAAPVPGFLAKLWALVEDPQSDDVICWSRNGENFCILDEQRFAKELLPKYFKHNNISSFIRQLNMYGFRKVVALENGMITAEKNSVIEFQHPFFKQGNAHLLENIKRKVSAVRTEDLKVCAEDLHKVLSEVQEMREQQNNMDIRLANMKRENKALWKEVAVLRQKHSQQQKLLSKILQFILSLMRGNYIVGVKRKRSLTDAAGASPSKYSRQYVRIPVESGQAMAFSEHNSDDEDGNRTGLIIRDITDTLENATNGLLAVAHTSGRDRETQTALDPGLPICQVSQPNELSCAEPIPPVHINDVSKPNEMGNVAVELHTAQANAPEDPVSVIDSILNENNSGNQNDPLLDREEIQDFLNCIDASLEELQAMLSGKQYSFGSEAFSDVFNPELPALDMNLMETSPGMENIANMEDSTEDLGASERETAGSKGGQEGTESCDSSVLFQNCVLKWNFSSL
Protein: Thyroid hormone receptor interactor 11 (H0YJ97)
Organism: Homo sapiens (Human)
Subcellular location: Golgi apparatus {ECO:0000256|ARBA:ARBA00004555}.
Interaction partners:
Sequence:
XELSDYEERIEELENLLQQGGSGVIETDLSKIYEMQKTIQVLQIEKVESTKKMEQLEDKIKDINKKLSSAENDRDILRREQEQLNVEKRQIMEECENLKLECSKLQPSAVKQSDTMTEKERILAQSASVEEVFRLQQALSDAENEIMRLSSLNQEELQMSLLKLNNEYEVIKSTATRDISLDSELHDLRLNLEAKEQELNQSISEKETLIAEIEELDRQNQEATKHMILIKDQLSKQQNEGDSIISKLKQDLNDEKKRVHQLEDDKMDITKELDVQKEKLIQSEVALNDLHLTKQKLEDKVENLVDQLNKSQESNVSIQKENLELKEHIRQNEEELSRIRNELMQSLNQDSNSNFKDTLLKEREAEVRNLKQNLSELEQLNENLKKVAFDVKMENEKLVLACEDVRHQLEECLAGNNQLSLEKNTIVETLKMEKGEIEAELCWAKKRLLEEANKYEKTIEELSNARNLNTSALQLEHEHLIKLNQKKDMEIAELKKNIEQMDTDHKETKDVLSSSLEEQKQLTQLINKKEIFIEKLKERSSKLQEELDKYSQALRKNEILRQTIEEKDRSLGSMKEENNHLQEELERLREEQSRTAPVADPKTLDSVTELASEVSQLNTIKEHLEEEIKHHQKIIEDQNQSKMQLLQSLQEQKKEMDEFRYQHEQMNATHTQLFLEKDEEIKSLQKTIEQIKTQLHEERQDIQTDNSDIFQETKVQSLNIENGSEKHDLSKAETERLVKGIKERELEIKLLNEKNISLTKQIDQLSKDEVGKLTQIIQQKDLEIQALHARISSTSHTQDVVYLQQQLQAYAMEREKVFAVLNEKTRENSHLKTEYHKMMDIVAAKEAALIKLQDENKKLSTRFESSGQDMFRETIQNLSRIIREKDIEIDALSQKCQTLLAVLQTSSTGNEAGGVNSNQFEELLQERDKLKQQVKKMEEWKQQVMTTVQNMQHESAQLQEELHQLQAQVLVDSDNNSKLQVDYTGLIQSYEQNETKLKNFGQELAQVQHSIGQLCNTKDLLLGKLDIISPQLSSASLLTPQSAECLRASKSEVLSESSELLQQELEELRKSLQEKDATIRTLQENNHRLSDSIAATSELERKEHEQTDSEIKQLKEKQDVLQKLLKEKDLLIKAKSDQLLSSNENFTNKVNENELLRQAVTNLKERILILEMDIGKLKGENEKIVETYRGKETEYQALQETNMKFSMMLREKEFECHSMKEKALAFEQLLKEKEQGKTGELNQLLNAVKSMQEKTVVFQQERDQVMLALKQKQMENTALQNEVQRLRDKEFRSNQELERLRNHLLESEDSYTREALAAEDREAKLRKKVTVLEEKLVSSSNAMENASHQASVQVESLQEQLNVVSKQRDETALQLSVSQEQVKQYALSLANLQMVLEHFQQEEKAMYSAELEKQKQLIAEWKKNAENLEGKVISLQECLDEANAALDSASRLTEQLDVKEEQIEELKRQNELRQEMLDDVQKKLMSLANSSEGKVDKVLMRNLFIGHFHTPKNQRHEVLRLMGSILGVRREEMEQLFHDDQGGVTRWMTGWLGGGSKSVPNTPLRPNQQSVVNSSFSELFVKFLETESHPSIPPPKLSVHDMKPLDSPGRRKRDTNAPESFKDTAESRSGRRTDVNPFLAPRSAAVPLINPAGLGPGGPGHLLLKPISDVLPTFTPLPALPDNSAGVVLKDLLKQ
Protein: NUP-1 protein (Q585C9)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MTDFGREAAKLLRATEDALYYRRSTAGSCEWADRDLKFRTSSSATGDMRGNSNFPFEAAWRTDNDGEKCGDSAAYIAELQRQLRVVMSEVAGLRSELAAERDSRSSTLTALGRRWKEEVLVEVRTSEHQSRRAIDELSVAIQQQRKDEETARSLLQHRVEDLLRDSKVRDRTQFDMQEQLREQVDAMRERLESAVSECALLRVECVQHQERENSAIAQRLDAELMRYIDMRAEEQRERQQLKQQLKSDVEAFGTHVQELVDKTWKSHLATTRRELQAPIDTLVKQMAQHTEGMTDLSAKVHDCTTTCRAELRLQTTTLQERVSAAEASAAVMLSRIDRAERKADGAQEAASRADATIAVVRDVAERAVVVSQRAMATAQRAEDAIEDRDARVAQLESHLAAVSTAEKLRADLEGVRRTAQRAESGVDALRHVYERDVQEQQNEKRQLDALMDRVSVYEKQQQHLRTSLESITDNRIPQLQHRIVVLEEARETLAAEASRGENAIMQNQQHALNIEGTVRSLNERLEQLRRDMNVSSQALSTRVEAANDAALRCETSSSTSRGEVERMERRVAQLEVQSTRLVADLTNLRSTADDNAKDTQTLSAQLQQHQRLWQEQRESRRELEATAIATNEAEIAAEQMAGRLEVKFNQHMRRVETNMAERTDKLEARANEASSRLDRLEDKGQSTSSLVTQVGETVQQQQQQFARDLQACRAKIDALNGTLTEIDEASERRFKDCVLQQDLNAIRRAVRTLETELHTIGADVTQHKQWAGSQEDCSLRIKRLEDEHRRQQNLLGEMRETLREVHDELKETQHFTTTLSQSVCTKEVRATEKGDGWPSQVPRVEKALFDSHRMTSSSEGQGNVASTPVIKRSTAGESLVAGLAPNVLAGTSMRRVESDPSQLADSPEPQKPPRLSQSSDSSLISQGKRLLSPALPTKVESTAKEGNLAQTGSTVQGSIDDKKPPSASNTKSIIDRPTQSAVARKVEGSSSDSTVNTLEMSVPIEKRGPIMFAPRESSSSASSAEARQPQQKQHRTQERRGDELVRANVDATALPVSLKPSESNSSSDSITRMKPSVEKTLTPPSSSKDTAVMGPILTVSKADSTREEEEKGDSEAPKTKVTVSQYDDWDDDSEDHPTAPMSEPTRTEAPKVDEKEEETKEVKTAEGKKAEGDGLKSDLSVVTTGRASNVPPETGTDEGLGSIVGSHIGRRGTFQPIEDPGEDISFTVPRHGVSTASSDSSTKSKEAQKQKPPAVKQFTSFDDSSSEEEGA
Protein: Progesterone receptor (PR) (Nuclear receptor subfamily 3 group C member 3) (Q00175)
Organism: Mus musculus (Mouse)
Function: The steroid hormones and their receptors are involved in the regulation of eukaryotic gene expression and affect cellular proliferation and differentiation in target tissues. Depending on the isoform, progesterone receptor functions as transcriptional activator or repressor.
Subcellular location: Nucleus. Cytoplasm. Note=Nucleoplasmic shuttling is both hormone- and cell cycle-dependent. On hormone stimulation, retained in the cytoplasm in the G(1) and G(2)/M phases (By similarity). {ECO:0000250}.
Interaction partners:
- Nuclear receptor coactivator 1
- Nuclear receptor corepressor 2
- Nuclear receptor corepressor 1
- Nuclear receptor coactivator 3
- Phosphatidylinositol 4,5-bisphosphate 3-kinase catalytic subunit alpha isoform
- Estrogen receptor
- Heat shock protein HSP 90-beta
- cAMP-dependent protein kinase catalytic subunit beta
- cAMP-dependent protein kinase catalytic subunit alpha
- Mitogen-activated protein kinase 14
Sequence:
MTELQAKDPQVLHTSGASPSPPHIGSPLLARLDSGPFQGSQHSDVSSVVSPIPISLDGLLFPRSCRGPELPDGKTGDQQSLSDVEGAFSGVEATHREGGRNSRAPEKDSRLLDSVLDSLLTPSGTEQSHASPPACEAITSWCLFGPELPEDPRSVPATKGLLSPLMSRPEIKAGDSSGTGAGQKVLPKGLSPPRQLLLPTSGSAHWPGAGVKPSPQPAAGEVEEDSGLETEGSAAPLLKSKPRALEGTGSGGGVAANAASAAPGGVTLVPKEDSRFSAPRVSLEQDSPIAPGRSPLATTVVDFIHVPILPLNHALLAARTRQLLEGDSYDGGATAQGPFAPPRGSPSAPSPPVPCGDFPDCTYPLEGDPKEDVFPLYGDFQTPGLKIKEEEEGADAAVRSPRPYLSAGASSSTFPDFPLAPAPQRAPSSRPGEAAVAGGPSSAAVSPASSSGSALECILYKAEGAPPTQGSFAPLPCKPPAAGSCLLPRDSLPAAPATAAAPAIYQPLGLNGLPQLGYQAAVLKDSLPQVYPPYLNYLRPDSEASQSPQYGFDSLPQKICLICGDEASGCHYGVLTCGSCKVFFKRAMEGQHNYLCAGRNDCIVDKIRRKNCPACRLRKCCQAGMVLGGRKFKKFNKVRVMRTLDGVALPQSVGLPNESQALGQRITFSPNQEIQLVPPLINLLMSIEPDVVYAGHDNTKPDTSSSLLTSLNQLGERQLLSVVKWSKSLPGFRNLHIDDQITLIQYSWMSLMVFGLGWRSYKHVSGQMLYFAPDLILNEQRMKELSFYSLCLTMWQIPQEFVKLQVTHEEFLCMKVLLLLNTIPLEGLRSQSQFEEMRSSYIRELIKAIGLRQKGVVPSSQRFYQLTKLLDSLHDLVKQLHLYCLNTFIQSRTLAVEFPEMMSEVIAAQLPKILAGMVKPLLFHKK
Protein: Peptidoglycan D,D-transpeptidase FtsI (EC 3.4.16.4) (Essential cell division protein FtsI) (Murein transpeptidase) (Penicillin-binding protein 3) (PBP-3) (Peptidoglycan synthase FtsI) (P0AD68)
Organism: Escherichia coli (strain K12)
Function: Essential cell division protein that catalyzes cross-linking of the peptidoglycan cell wall at the division septum. Required for localization of FtsN.
Subcellular location: Cell inner membrane {ECO:0000255|HAMAP-Rule:MF_02080, ECO:0000269|PubMed:2677607, ECO:0000269|PubMed:9614966}; Single-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_02080, ECO:0000269|PubMed:2677607, ECO:0000269|PubMed:9614966}; Periplasmic side {ECO:0000269|PubMed:2677607, ECO:0000269|PubMed:9614966}. Note=The bulk of the molecule, except for the N-terminal membrane anchor region, protrudes into the periplasmic space (PubMed:2677607, PubMed:9614966). Localizes to the division septum during the later stages of cell growth and throughout septation (PubMed:15601716, PubMed:9379897, PubMed:9603865, PubMed:9882665). Localization is dependent on FtsZ, FtsA, FtsK, FtsQ, FtsL and FtsW, but not on FtsN (PubMed:11703663, PubMed:11807049, PubMed:9603865, PubMed:9882665). {ECO:0000269|PubMed:11703663, ECO:0000269|PubMed:11807049, ECO:0000269|PubMed:15601716, ECO:0000269|PubMed:2677607, ECO:0000269|PubMed:9379897, ECO:0000269|PubMed:9603865, ECO:0000269|PubMed:9614966, ECO:0000269|PubMed:9882665}.
Interaction partners:
- Cell division protein FtsQ
- Cell division protein FtsN
- Probable peptidoglycan glycosyltransferase FtsW
- Cell division protein FtsL
- Cell division protein FtsA
- Penicillin-binding protein 1B
- UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--2,6-diaminopimelate ligase
- DNA translocase FtsK
- UDP-N-acetylmuramoylalanine--D-glutamate ligase
- Cell division protein FtsZ
Sequence:
MKAAAKTQKPKRQEEHANFISWRFALLCGCILLALAFLLGRVAWLQVISPDMLVKEGDMRSLRVQQVSTSRGMITDRSGRPLAVSVPVKAIWADPKEVHDAGGISVGDRWKALANALNIPLDQLSARINANPKGRFIYLARQVNPDMADYIKKLKLPGIHLREESRRYYPSGEVTAHLIGFTNVDSQGIEGVEKSFDKWLTGQPGERIVRKDRYGRVIEDISSTDSQAAHNLALSIDERLQALVYRELNNAVAFNKAESGSAVLVDVNTGEVLAMANSPSYNPNNLSGTPKEAMRNRTITDVFEPGSTVKPMVVMTALQRGVVRENSVLNTIPYRINGHEIKDVARYSELTLTGVLQKSSNVGVSKLALAMPSSALVDTYSRFGLGKATNLGLVGERSGLYPQKQRWSDIERATFSFGYGLMVTPLQLARVYATIGSYGIYRPLSITKVDPPVPGERVFPESIVRTVVHMMESVALPGGGGVKAAIKGYRIAIKTGTAKKVGPDGRYINKYIAYTAGVAPASQPRFALVVVINDPQAGKYYGGAVSAPVFGAIMGGVLRTMNIEPDALTTGDKNEFVINQGEGTGGRS
Protein: Maf1 regulator (Q584J2)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- DNA-directed RNA polymerase subunit
- DNA-directed RNA polymerase subunit beta
- DNA-directed RNA polymerase III subunit RPC3
Sequence:
MEFVPLESFEFLNSLLQGVEAQGCLMTVRLEAFTCRCTRKKKLLAASIAEYANKTTPPLRPLCSANAPVPPLLNLSDDSAHVVPTEPVEPSDIDDRLVFLVAALNSIYGEDGYDFSVLTEEDFVPCDEAHVRAEVNNTLRSFPSSCGPAVGQFWVRVTEHASDASQGCEYFRFASPSCDPMASRALFSQHYFLYNKRARLLVSLLIFAEGNLYRGDDGAMVENSLYYETDDNSTHSRLWFSSPDGASEDDEHVLVGKNVHYYCRA
Protein: DNA topoisomerase 4 subunit B (EC 5.6.2.2) (Topoisomerase IV subunit B) (Q92QA5)
Organism: Rhizobium meliloti (strain 1021) (Ensifer meliloti) (Sinorhizobium meliloti)
Interaction partners:
Sequence:
MDDSSDLFSAMPQQPKPADAAPRKPAAPAAGNEASRPAPKTSDGSDYDASAIEVLEGLEPVRRRPGMYIGGTDEKALHHLFAEVIDNSMDEAVAGHANFIDVNLDADGYLTVTDNGRGIPVENHPKFPGKSTLEVVMTVLHAGGKFDGKAYETSGGLHGVGVSVVNALSDDLEVEVARNRRLYRQRFSRGIAQGGLEDLGDVHNRRGTRVRFHPDPQIFGPHARFEPARLFRMARSKAYLFGGVEIRWSCDPALLPEGSEIPDRAVFHFPGGLKDYLAATLGKEFTVTREIFAGKSEKSGGHGSLEWAVTWYGGDQQIHSYCNTIPTPEGGTHEAGLRIALTKGLKNYAELTQNKRAAIVTTDDVMISAAGMLSVFIREPEFVGQTKDKLATVEAQRIVENALRDPFDHYLADNPAEAAKLLDWVVERAEERVRRRKEKEVSRKTAVRKLRLPGKLADCAQNTAEGAELFIVEGDSAGGSAKQARNRANQAILPLRGKILNVASAGREKLGANQQIGDLVQALGCGTRSKYREEDLRYERIIIMTDADVDGAHIASLLITFFYQEMPELIRGGHLYLAVPPLYRLSQGSKTLYARDDAHREELMRTEFNGRGKVELGRFKGLGEMLPAQLKETTMDPAKRTLLKVEIDDVDFEGTRDAVDSLMGTKAEARFRFIQERAVFADNLDI
Protein: Protein-L-isoaspartate(D-aspartate) O-methyltransferase (PIMT) (EC 2.1.1.77) (L-isoaspartyl protein carboxyl methyltransferase) (Protein L-isoaspartyl/D-aspartyl methyltransferase) (Protein-beta-aspartate methyltransferase) (P22061)
Organism: Homo sapiens (Human)
Function: Initiates the repair of damaged proteins by catalyzing methyl esterification of L-isoaspartyl and D-aspartyl residues produced by spontaneous isomerization and racemization of L-aspartyl and L-asparaginyl residues in aging peptides and proteins. Acts on EIF4EBP2, microtubule-associated protein 2, calreticulin, clathrin light chains a and b, Ubiquitin C-terminal hydrolase isozyme L1, phosphatidylethanolamine-binding protein 1, stathmin, beta-synuclein and alpha-synuclein (By similarity).
Subcellular location: Cytoplasm, cytosol {ECO:0000269|PubMed:3167043}.
Interaction partners:
- Aldehyde dehydrogenase family 16 member A1
Sequence:
MAWKSGGASHSELIHNLRKNGIIKTDKVFEVMLATDRSHYAKCNPYMDSPQSIGFQATISAPHMHAYALELLFDQLHEGAKALDVGSGSGILTACFARMVGCTGKVIGIDHIKELVDDSVNNVRKDDPTLLSSGRVQLVVGDGRMGYAEEAPYDAIHVGAAAPVVPQALIDQLKPGGRLILPVGPAGGNQMLEQYDKLQDGSIKMKPLMGVIYVPLTDKEKQWSRWK
Protein: Tubulin alpha chain (C9JEV8)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000256|ARBA:ARBA00004245}.
Interaction partners:
Sequence:
MGNACWELYCLEHGIQPDGQMPSDKTIGGGDDSFTTFFCETGAGKHVPRAVFVDLEPTVIDEIRNGPYRQLFHPEQLITGKEDAANNYARGHYTIGKEIIDPVLDRIRKLSDQCTGLQGFLVFHSFGGGTGSGFTSLLMERLSVDYGKKSKLE
Protein: Inner kinetochore subunit OKP1 (CENP-Q homolog) (Constitutive centromere-associated network protein OKP1) (Outer kinetochore protein 1) (P53298)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Component of the kinetochore, a multiprotein complex that assembles on centromeric DNA and attaches chromosomes to spindle microtubules, mediating chromosome segregation and sister chromatid segregation during meiosis and mitosis. Component of the inner kinetochore COMA complex, which connects centromere-associated proteins and the outer kinetochore. COMA interacts with other inner kinetochore proteins to form the inner kinetochore constitutive centromere-associated network (CCAN), which serves as a structural platform for outer kinetochore assembly.
Subcellular location: Nucleus {ECO:0000269|PubMed:14562095}. Chromosome, centromere, kinetochore {ECO:0000269|PubMed:10323865}.
Interaction partners:
- Inner kinetochore subunit AME1
- Inner kinetochore subunit NKP1
- Inner kinetochore subunit MCM21
- Inner kinetochore subunit MCM22
- Inner kinetochore subunit IML3
- Inner kinetochore subunit CTF19
- Inner kinetochore subunit CHL4
- Inner kinetochore subunit MCM16
- Inner kinetochore subunit NKP2
- Inner kinetochore subunit CTF3
Sequence:
MAADRDNFLQNIENDSINNGQAMDLSPNRSSSESDSSILMNVNDIKTLRLDVAPEAKSTQSKKSLFYENSDDAEEGEIEERTNKEEGQYHHKGSKQLRFEVGKESTGKLQSHLSDGSATSGEGNVRPWEFRKVIQAEYRERLPRNYELKHWKKPSKIMIGSILRLLETNTVSALDSVFEKYEKEMNQMTHGDNNEVKRIYSKKERLLEIILTKIKKKLRQAKFPSRISERDLDIEYIYSKRQFIQNRYSQELQNNERLEAILSREQNLLEETRKLCMNLKTNNKKRLTEKLIQKDLHPVLNKAMEYTYGLESTNGFMHPDGPVTFRNDSHELNLMLNDPIKSTADVRLDKEEVLSLLPSLKEYTKKSKELKETMGQMISDSHEEEIKEVFVPHHESHQDKTEEDIH
Protein: Conserved regulator of innate immunity protein 3 (Q21018)
Organism: Caenorhabditis elegans
Subcellular location: Mitochondrion matrix {ECO:0000305}.
Interaction partners:
- Protein clpf-1
- Mitochondrial prohibitin complex protein 2
- 3'
- Pre-mRNA-processing factor 19
- Transmembrane protein 208
- Mitochondrial prohibitin complex protein 1
Sequence:
MNTASLVRSLSRVALRSSQVVRMAAPRHFSQSAKVLSVTPELQQALNREIEAEQQLSSDNLQGAVAPTFAGFQVTNKDAEVRLTKKNGSEDILVVFNVNHSVDMDEGFDDEPSQAVAPVPVAMPPFTVEITKGDQRLCFHLELVPVDDQPDEYDFRVEEFYVAPSAKNGNEDVPSEVYASSGKYIDPDLHDLLFVRYLEERGLDARFCKTLVAYATHYEHSQYVGLLDKIKKFISK
Protein: LP11958p (Q8IGZ3)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
CSLAMKTFHSLLFALILALVSLDPSSGYSRRKDERIIREYKREQELNHAKIARDLVHRANWAAVGSLSTNERVKGYPMVNIISIDDSDANNRSTGRIRFLLTDLDFTGPDWQKDNKVTLLFSDEQTLRCKEGGKDPMEPTCARSMISGQVKKLTISTFANWKLAISLFWTSMEVLIK
Protein: 2-dehydropantoate 2-reductase (EC 1.1.1.169) (Ketopantoate reductase) (KPR) (Q5JGC2)
Organism: Thermococcus kodakarensis (strain ATCC BAA-918 / JCM 12380 / KOD1) (Pyrococcus kodakaraensis (strain KOD1))
Function: Catalyzes the NAD(P)H-dependent reduction of ketopantoate into pantoic acid. Prefers NADH rather than NADPH as the electron donor.
Subcellular location: Cytoplasm {ECO:0000305|PubMed:23941541}.
Interaction partners:
- 3-methyl-2-oxobutanoate hydroxymethyltransferase
- Pantoate kinase
- Coenzyme A biosynthesis bifunctional protein CoaBC
- D-3-phosphoglycerate dehydrogenase
- Hypothetical membrane protein
- Distant homolog of phosphate transport system regulator PhoU
- 4-phosphopantoate--beta-alanine ligase
- UPF0200 protein TK1334
- Dephospho-CoA kinase
Sequence:
MRIYVLGAGSIGSLFGALLARAGNDVTLIGRREQVDAINKNGLHVFGAEEFTVKPKATIYAPEEPPDLLILAVKSYSTKTALECARQCIGRNTWVLSIQNGLGNEELALKYTPNVMGGVTTNGAMLVEWGKVLWAGKGITVIGRYPTGRDDFVDEVASVFNEAGIDTSVTENAIGWKWAKAIVNSVINGLGTVLEVKNGHLKDDPHLEGISVDIAREGCMVAQQLGIEFEIHPLELLWDTIERTRENYNSTLQDIWRGRETEVDYIHGKIVEYARSVGMEAPRNELLWVLVKAKERINRGKTRNISEGC
Protein: DEK domain-containing chromatin-associated protein 3 (At-DEK3) (AtDEK-3) (Protein DEK 3) (Q9SUA1)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Chromatin-associated protein which contributes to the modulation of chromatin structure (such as super-helical structure of DNA) and function. Binds to chromatin of protein-coding genes throughout the genome to regulate nucleosome occupancy and chromatin accessibility, and to modulate the expression of target genes. Negative regulator of stress tolerance (e.g. high salt).
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00768, ECO:0000269|PubMed:25387881}. Nucleus, nucleolus {ECO:0000269|PubMed:15496452}. Note=Associates with chromatin (PubMed:25387881). Enriched in regions where chromatin is decondensed or sparse in the interphase nuclei (By similarity). {ECO:0000250|UniProtKB:P35659, ECO:0000269|PubMed:25387881}.
Interaction partners:
- Probable polyamine transporter At3g19553
- Large ribosomal subunit protein eL20x
- Gb|AAF32471.1
- F16B3.27 protein
- At1g64490
- Mediator-associated protein 3
- At5g19340
- RING-type E3 ubiquitin transferase
- Shaggy-related protein kinase beta
- Large ribosomal subunit protein eL20w
Sequence:
MGEDTKATIEPTANKTTSLEKPSEAMAGKENAGGKETQELAKDEDMAEPDNMEIDAQIKKDDEKAETEDKESEVKKNEDNAETQKMEEKVEVTKDEGQAEATNMDEDADGKKEQTDDGVSVEDTVMKENVESKDNNYAKDDEKETKETDITEADHKKAGKEDIQHEADKANGTKDGNTGDIKEEGTLVDEDKGTDMDEKVENGDENKQVENVEGKEKEDKEENKTKEVEAAKAEVDESKVEDEKEGSEDENDNEKVESKDAKEDEKEETNDDKEDEKEESKGSKKRGKGTSSGGKVREKNKTEEVKKDAEPRTPFSDRPVRERKSVERLVALIDKDSSKEFRVEKGRGAYLKDIPNVANKVMRKRSDETLKLLHPILFGGRRGKAAQIKTNILGFSGFVWHGDEKKAKEKVKEKLEKCTKEKLWEFCDVLDIHITKATTKKEDIITKLFEFLEKPHVTGDVTGDTTVSEKEKSSKGAKRKRTPKKTSPTAGSSSSKRSAKSQKKSEEATKVVKKSLAHSDDESEEEKEEEEKQEEEKAEEKEEKKEEENENGIPDKSEDEAPQPSESEEKDESEEHSEEETTKKKRGSRLSAGKKESAGRARNKKAVVAAKSSPPEKITQKRSSAKRKKTDDDSDTSPKASSKRKKSENPIKASPAPSKSASKEKPVKRAGKGKDKPSDKVLKNAIVEILKRVDFSTATFTDILKELAKEFTEDLTPRKSSIKMIIQEELTKLADEEEEEEKKEEDSEKEEAGGSGGGEEVKA