wanglab/gogpt-training-data huggingface dataset:
Protein: Kinetochore protein nuf2 (NMS complex subunit nuf2) (Q10173)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Acts as a component of the NMS (Ndc80-MIND-Spc7) super complex which has a role in kinetochore function during late meiotic prophase and throughout the mitotic cell cycle. Acts as a component of the essential kinetochore-associated NDC80 complex, which is required for chromosome segregation and spindle checkpoint activity.
Subcellular location: Nucleus. Chromosome, centromere, kinetochore. Cytoplasm, cytoskeleton, microtubule organizing center, spindle pole body. Note=Associated with kinetochores.
Interaction partners:
- Kinetochore protein spc25
- Kinetochore protein ndc80
- Kinetochore protein spc24
- Kinetochore protein mis13
- Centromere protein mis12
- Outer kinetochore KNL1 complex subunit spc7
- Kinetochore protein nnf1
- Spindle assembly checkpoint serine/threonine-protein kinase bub1
- Kinetochore protein mis14
- Mitotic spindle checkpoint component mad2
Sequence:
MARKHTFPSLKRAEILECIDGLGIPFTAKELDQPTSKAVIPLYEEFLDLFMGLTRQNLEEKVNSLQDSVENFEIIHESLRFTVFYQILSQFMQNICFHDFTIQDLLKPDRNRLQLILSAVINFAKLREERLQQFDDDIQKRESLLETYTLLDAQRKDLEEKVLLSQDRKLESEAIIKQNEERNEEMFQSLIEDKRLCSQVRTEYDRIRMEASELKIRYHNVDSLMASTLEEIEKLQSSIVHSPEKLKGKIADTSLRIQNDRSQQVELDKKSKILHTKLNSLQLIEGDLNACLKVLEECLVELDKLEHATVLLSTNQELCDQIEINKKKLEFRKEQLLKQLSNAQEKLEHEQHSRNQKLEAAKQRMDNIREEYKVITQERNKKIQETEKKNAMIEMTEQKIAGMREELESQISSITMEFEKLKSHVELYIAELLRNLRSSNS
Protein: NDR1/HIN1-like protein 13 (Q9ZVD2)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Required for plant immunity against the bacterial pathogen Pseudomonas syringae pv. tomato DC3000 (Pst DC3000).
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:Q9FNH6}; Single-pass membrane protein {ECO:0000255}.
Interaction partners:
- Peroxidase 56
- Probable serine/threonine-protein kinase PBL7
Sequence:
MAERVYPADSPPQSGQFSGNFSSGEFPKKPAPPPSTYVIQVPKDQIYRIPPPENAHRFEQLSRKKTNRSNCRCCFCSFLAAVFILIVLAGISFAVLYLIYRPEAPKYSIEGFSVSGINLNSTSPISPSFNVTVRSRNGNGKIGVYYEKESSVDVYYNDVDISNGVMPVFYQPAKNVTVVKLVLSGSKIQLTSGMRKEMRNEVSKKTVPFKLKIKAPVKIKFGSVKTWTMIVNVDCDVTVDKLTAPSRIVSRKCSHDVDLW
Protein: Aminoadipate-semialdehyde synthase (A4D0W4)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MLQVHRTGLGRLGVSLSKGLHHKAVLAVRREDVNAWERRAPLAPKHIKGITNLGYKVLIQPSNRRAIHDKDYVKAGGILQEDISEACLILGVKRPPEEKLMSRKTYAFFSHTIKAQEANMGLLDEILKQEIRLIDYEKMVDHRGVRVVAFGQWAGVAGMINILHGMGLRLLALGHHTPFMHIGMAHNYRNSSQAVQAVRDAGYEISLGLMPKSIGPLTFVFTGTGNVSKGAQAIFNELPCEYVEPHELKEVSQTGDLRKVYGTVLSRHHHLVRKTDAVYDPAEYDKHPERYISRFNTDIAPYTTCLINGIYWEQNTPRLLTRQDAQSLLAPGKFSPAGVEGCPALPHKLVAICDISADTGGSIEFMTECTTIEHPFCMYDADQHIIHDSVEGSGILMCSIDNLPAQLPIEATECFGDMLYPYVEEMILSDATQPLESQNFSPVVRDAVITSNGTLPDKYKYIQTLRESRERAQSLSMGTRRKVLVLGSGYISEPVLEYLSRDGNIEITVGSDMKNQIEQLGKKYNINPVSMDICKQEEKLGFLVAKQDLVISLLPYVLHPLVAKACITNKVNMVTASYITPALKELEKSVEDAGITIIGELGLDPGLDHMLAMETIDKAKEVGATIESYISYCGGLPAPEHSNNPLRYKFSWSPVGVLMNVMQSATYLLDGKVVNVAGGISFLDAVTSMDFFPGLNLEGYPNRDSTKYAEIYGISSAHTLLRGTLRYKGYMKALNGFVKLGLINREALPAFRPEANPLTWKQLLCDLVGISPSSEHDVLKEAVLKKLGGDNTQLEAAEWLGLLGDEQVPQAESILDALSKHLVMKLSYGPEEKDMIVMRDSFGIRHPSGHLEHKTIDLVAYGDINGFSAMAKTVGLPTAMAAKMLLDGEIGAKGLMGPFSKEIYGPILERIKAEGIIYTTQSTIKP
Protein: Manganese transport regulator (I6Y1Q2)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
- Probable transcriptional regulatory protein NarL
- HTH hxlR-type domain-containing protein
- Probable transcriptional regulatory protein
- Probable transcriptional regulatory protein
- ECF RNA polymerase sigma factor SigJ
- Probable transcriptional regulatory protein
- Transcriptional regulatory protein
- Possible transcriptional regulatory protein
- Uncharacterized protein Rv0093c
- Uncharacterized HTH-type transcriptional regulator Rv0377
Sequence:
MRADEEPGDLSAVAQDYLKVIWTAQEWSQDKVSTKMLAERIGVSASTASESIRKLAEQGLVDHEKYGAVTLTDSGRRAALAMVRRHRLLETFLVNELGYRWDEVHDEAEVLEHAVSDRLMARIDAKLGFPQRDPHGDPIPGADGQVPTPPARQLWACRDGDTGTVARISDADPQMLRYFASIGISLDSRLRVLARREFAGMISVAIDSADGATVDLGSPAAQAIWVVS
Protein: 2-methylcitrate dehydratase (2-MC dehydratase) (EC 4.2.1.79) (Aconitate hydratase) (ACN) (Aconitase) (EC 4.2.1.3) (O06582)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: Involved in the catabolism of short chain fatty acids (SCFA) via the tricarboxylic acid (TCA)(acetyl degradation route) and via the 2-methylcitrate cycle I (propionate degradation route). Catalyzes the dehydration of 2-methylcitrate (2-MC) to yield the cis isomer of 2-methyl-aconitate. Could also catalyze the dehydration of citrate and the hydration of cis-aconitate (By similarity).
Interaction partners:
- 2-methylcitrate synthase
- HTH-type transcriptional regulator PrpR
- Uncharacterized protein Rv1998c
- Conserved membrane protein
- Isocitrate lyase
- HTH-type transcriptional regulator RamB
- Citrate synthase 1
Sequence:
MPDQDTKVRFFRVFCWCPVLRMVRIMLMHAVRAWRSADDFPCTEHMAYKIAQVAADPVDVDPEVADMVCNRIIDNAAVSAASMVRRPVTVARHQALAHPVRHGAKVFGVEGSYSADWAAWANGVAARELDFHDTFLAADYSHPADNIPPLVAVAQQLGVCGAELIRGLVTAYEIHIDLTRGICLHEHKIDHVAHLGPAVAAGIGTMLRLDQETIYHAIGQALHLTTSTRQSRKGAISSWKAFAPAHAGKVGIEAVDRAMRGEGSPAPIWEGEDGVIAWLLAGPEHTYRVPLPAPGEPKRAILDSYTKQHSAEYQSQAPIDLACRLRERIGDLDQIASIVLHTSHHTHVVIGTGSGDPQKFDPDASRETLDHSLPYIFAVALQDGCWHHERSYAPERARRSDTVALWHKISTVEDPEWTRRYHCADPAKKAFGARAEVTLHSGEVIVDELAVADAHPLGTRPFERKQYVEKFTELADGVVEPVEQQRFLAVVESLADLESGAVGGLNVLVDPRVLDKAPVIPPGIFR
Protein: NADH-ubiquinone oxidoreductase chain 4 (EC 7.1.1.2) (NADH dehydrogenase subunit 4) (P05508)
Organism: Rattus norvegicus (Rat)
Function: Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) which catalyzes electron transfer from NADH through the respiratory chain, using ubiquinone as an electron acceptor. Essential for the catalytic activity and assembly of complex I.
Subcellular location: Mitochondrion inner membrane {ECO:0000250|UniProtKB:P03910}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- NADH dehydrogenase iron-sulfur protein 8, mitochondrial
- NADH dehydrogenase 1 alpha subcomplex subunit 5
- NADH-ubiquinone oxidoreductase 75 kDa subunit, mitochondrial
- NADH dehydrogenase 1 beta subcomplex subunit 5, mitochondrial
- NADH:ubiquinone oxidoreductase subunit V3
- NADH dehydrogenase iron-sulfur protein 4, mitochondrial
- NADH dehydrogenase 1 beta subcomplex subunit 8, mitochondrial
- NADH-ubiquinone oxidoreductase chain 6
- NADH dehydrogenase 1 alpha subcomplex subunit 8
- Cytochrome c oxidase subunit 1
Sequence:
MLKIIFPSIMLLPLTWLSANKKIWTNVTSYSFLVSLLSLSLLWQNDENYLNFSVMFSSDPLSTPLIILTTWLLPLMMLASQNHMKKENMMHQKLYISMLISLQILLIMTFSATELILFYILFEATLIPTLIIITRWGNQTERLNAGIYFLFYTLIGSIPLLIALISIQNSMGTLNFLILSLTTHPLPSTWSNTILWLACMMAFMIKMPLYGVHLWLPKAHVEAPIAGSMILAAILLKLGGYGMMRVSIILDPLTKSLAYPFIILSLWGMIMTSSICLRQTDLKSLIAYSSVSHMALVITAIMIQTPWSFMGATMLMIAHGLTSSLLFCLANTNYERIHSRTMIMARGLQMIFPLMATWWLLASLANLALPPLINLMGELFIVMATFSWSNPSIILMATNIVITGIYSMYMIITTQRGKLTSHMNNLQPSHTRELTLMALHIIPLMLLTINPKLITGLTM
Protein: Phosphatidylinositol 4-kinase beta (PI4K-beta) (PI4Kbeta) (PtdIns 4-kinase beta) (EC 2.7.1.67) (O02810)
Organism: Bos taurus (Bovine)
Function: Phosphorylates phosphatidylinositol (PI) in the first committed step in the production of the second messenger inositol-1,4,5,-trisphosphate (PIP). May regulate Golgi disintegration/reorganization during mitosis, possibly via its phosphorylation (By similarity). Involved in Golgi-to-plasma membrane trafficking (By similarity).
Subcellular location: Endomembrane system {ECO:0000250}. Mitochondrion outer membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Rough endoplasmic reticulum membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Golgi apparatus {ECO:0000269|PubMed:11526106}. Golgi apparatus membrane {ECO:0000250|UniProtKB:Q9UBF8}. Note=Found in the outer membrane of mitochondria and membranes of the rough endoplasmic reticulum. Recruited to the Golgi complex by the small GTPase ARF to stimulate the synthesis of phosphatidylinositol 4,5-bisphosphate (PIP2) on the Golgi complex. Recruited to the Golgi apparatus membrane by ACBD3, GGA2 is also involved in the recruitment. {ECO:0000250|UniProtKB:Q9UBF8}.
Interaction partners:
- CDP-diacylglycerol--inositol 3-phosphatidyltransferase
- Phosphatidylinositol 4-kinase type 2
- Phosphatidylinositol 4-kinase type 2
- Phosphatidylinositol-4-phosphate 5-kinase type 1 gamma
- PIP5K1A protein
- Phosphatidylinositol 4-kinase alpha
- Phosphatidylinositol-4-phosphate 5-kinase type 1 beta
- Golgi resident protein GCP60
- Phosphatidylinositol-3-phosphatase SAC1
- 1-phosphatidylinositol 3-phosphate 5-kinase
Sequence:
MGDTIVEPAPLKPTSEPAPGPPGNNGGSLLSVITEGVGELSVIDPEVAQKACQEVLEKVKLLHGGVAISSRGTPLELVNGDGVDSEIRCLDDPPAQIREEEDEMGATVASGTAKGARRRRQNNSAKQSWLLRLFESKLFDISMAISYLYNSKEPGVQAYIGNRLFCFRNEDVDFYLPQLLNMYIHMDEDVGDAIKPYIVHRCRQSINFSLQCALLLGAYSSDMHISTQRHSRGTKLRKLILSDELKPAHRKRELPSLSPAPDTGLSPSKRTHQRSKSDATASISLSSNLKRTASNPKVENEDEELSSSTESIDNSFSSPVRLAPEREFIKSLMAIGKRLATLPTKEQKTQRLISELSLLNHKLPARVWLPTAGFDHHVVRVPHTQAVVLNSKDKAPYLIYVEVLECENFDTTSVPARIPENRIRSTRSVENLPECGITHEQRAGSFSTVPNYDNDDEAWSVDDIGELQVELPEVHTNSCDNISQFSVDSITSQESKEPVFIAAGDIRRRLSEQLAHTPTAFKRDPEDPSAVALKEPWQEKVRRIREGSPYGHLPNWRLLSVIVKCGDDLRQELLAFQVLKQLQSIWEQERVPLWIKPYKILVISADSGMIEPVVNAVSIHQVKKQSQLSLLDYFLQEHGSYTTEAFLSAQRNFVQSCAGYCLGCYLLQVKDRHNGNILLDAEGHIIHIDFGFILSSSPRNLGFETSAFKLTTEFVDVMGGLDGDMFNYYKMLMLQGLIAARKHMDKVVQIVEIMQQGSQLPCFHGSSTIRNLKERFHMSMTEEQLQLLVEQMVDGSMRSITTKLYDGFQYLTNGIM
Protein: CD151 antigen (Platelet-endothelial tetraspan antigen 3) (PETA-3) (CD antigen CD151) (Q9QZA6)
Organism: Rattus norvegicus (Rat)
Function: Essential for the proper assembly of the glomerular and tubular basement membranes in kidney.
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:P48509}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P48509}. Note=Relocalizes to the immune synapse in T-cells upon activation. {ECO:0000250|UniProtKB:P48509}.
Interaction partners:
- Integrin subunit alpha 3
- Plectin
- Collagen alpha-1
- Dystonin
- CD63 antigen
- Integrin beta-4
- Integrin alpha-6
- Integrin beta-1
- CD81 antigen
- Prostaglandin F2 receptor negative regulator
Sequence:
MGEFNEKKATCGTVCLKYLLFTYNCCFWLAGLAVMAVGIWTLALKSDYISLLASSTYLATAYILVVAGVVVMVTGVLGCCATFKERRNLLRLYFILLLIIFLLEIIAGILAYVYYQQLNTELKENLKDTMIKRYHQSGHEGVTNAVDKLQQEFHCCGSNNSRDWRDSEWIRSGEADSRVVPDSCCKTVVTGCGKREHASNIYKVEGGCITKLESFIQEHLRVIGAVGIGIACVQVFGMIFTCCLYRSLKLEHY
Protein: Glycogen [starch] synthase isoform 2 (EC 2.4.1.11) (P27472)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Transfers the glycosyl residue from UDP-Glc to the non-reducing end of alpha-1,4-glucan. Is believed to regulate the synthesis of glycogen.
Subcellular location: Cytoplasm, cytosol {ECO:0000269|PubMed:38832010}. Note=Localizes to glycogen granules in the cytosol. {ECO:0000269|PubMed:38832010}.
Interaction partners:
- Glycogenin-2
- Glycogenin-1
- Glycogen [starch] synthase isoform 1
- 1,4-alpha-glucan-branching enzyme
- GLC7-interacting protein 2
- UTP--glucose-1-phosphate uridylyltransferase
- Glycogen phosphorylase
- Trehalose-phosphatase
- Serine/threonine-protein phosphatase 1 regulatory subunit GAC1
- Phosphoglucomutase 2
Sequence:
MSRDLQNHLLFETATEVANRVGGIYSVLKSKAPITVAQYKDHYHLIGPLNKATYQNEVDILDWKKPEAFSDEMRPVQHALQTMESRGVHFVYGRWLIEGAPKVILFDLDSVRGYSNEWKGDLWSLVGIPSPENDFETNDAILLGYTVAWFLGEVAHLDSQHAIVAHFHEWLAGVALPLCRKRRIDVVTIFTTHATLLGRYLCASGSFDFYNCLESVDVDHEAGRFGIYHRYCIERAAAHSADVFTTVSQITAFEAEHLLKRKPDGILPNGLNVIKFQAFHEFQNLHALKKEKINDFVRGHFHGCFDFDLDNTLYFFIAGRYEYKNKGADMFIEALARLNYRLKVSGSKKTVVAFIVMPAKNNSFTVEALKGQAEVRALENTVHEVTTSIGKRIFDHAIRYPHNGLTTELPTDLGELLKSSDKVMLKRRILALRRPEGQLPPIVTHNMVDDANDLILNKIRQVQLFNSPSDRVKMIFHPEFLNANNPILGLDYDEFVRGCHLGVFPSYYEPWGYTPAECTVMGVPSITTNVSGFGAYMEDLIETNQAKDYGIYIVDRRFKAPDESVEQLVDYMEEFVKKTRRQRINQRNRTERLSDLLDWKRMGLEYVKARQLALRRGYPDQFRELVGEELNDSNMDALAGGKKLKVARPLSVPGSPRDLRSNSTVYMTPGDLGTLQEVNNADDYFSLGVNPAADDDDDGPYADDS
Protein: NAD(+) hydrolase TcpF (EC 3.2.2.6) (TIR domain-containing protein in E.faecalis) (tcpF) (Q833J1)
Organism: Enterococcus faecalis (strain ATCC 700802 / V583)
Function: Virulence factor that suppresses host Toll-like receptor (TLR)-mediated cytokine production upon infection. Acts as a NAD(+) hydrolase (NADase) by catalyzing cleavage of NAD(+) into ADP-D-ribose (ADPR) and nicotinamide. Interacts with various phosphatidylinositol phosphates, such as phosphatidylinositol 3-phosphate (PtdIns(3)P), phosphatidylinositol 4-phosphate (PtdIns(4)P), phosphatidylinositol 3,4-bisphosphate (PtdIns(3,4)P), phosphatidylinositol 3,5-bisphosphate (PtdIns(3,5)P), phosphatidylinositol 4,5- bisphosphate (PtdIns(4,5)P), and phosphatidylinositol 3,4,5-trisphosphate (PtdIns(3,4,5)P).
Interaction partners:
- Deoxyguanosinetriphosphate triphosphohydrolase, putative
- Uncharacterized protein
Sequence:
MSNGKKIFISHSSKDQEYVDAFIQLLKKFGFRTQDIFYSSTIETGVQPGELIFDTIKRELTNQPVMLYFLSDHYYQSIPCLNEMGASWMLSDKHYPIALNNFSMKDMKGVISSERLAIAFNDKTSTNEINCLLKKLSHDTDVQAEPDFELNVEKNIQPFQNKLTQLIRQASYLKPDEKGYFETILSTHRPVYGTAKGVYDCFKLPSLIEPKSLGLDTLSEDESHWLFFFLTWGTFQEGEKVRFKLKKDKAYNNREFSDIGKCKNIYVSYLEKVE
Protein: Fizzy-related, isoform A (Fizzy-related, isoform B) (GH07620p) (RE20929p) (Q9W4H9)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Cell division cycle protein 27 homolog
- G2/mitotic-specific cyclin-B
- Shattered
- G2/mitotic-specific cyclin-A
- Anaphase-promoting complex subunit 2
- Anaphase-promoting complex subunit 5
- Cyclin-dependent kinase 1
- Cell division cycle 16
- Anaphase-promoting complex subunit 10
- Cyclosome subunit 8
Sequence:
MFSPEYEKRILKHYSPVARNLFNNFESSTTPTSLDRFIPCRAYNNWQTNFASINKSNDNSPQTSKKQRDCGETARDSLAYSCLLKNELLGSAIDDVKTAGEERNENAYTPAAKRSLFKYQSPTKQDYNGECPYSLSPVSAKSQKLLRSPRKATRKISRIPFKVLDAPELQDDFYLNLVDWSSQNVLAVGLGSCVYLWSACTSQVTRLCDLSPDANTVTSVSWNERGNTVAVGTHHGYVTVWDVAANKQINKLNGHSARVGALAWNSDILSSGSRDRWIIQRDTRTPQLQSERRLAGHRQEVCGLKWSPDNQYLASGGNDNRLYVWNQHSVNPVQSYTEHMAAVKAIAWSPHHHGLLASGGGTADRCIRFWNTLTGQPMQCVDTGSQVCNLAWSKHSSELVSTHGYSQNQILVWKYPSLTQVAKLTGHSYRVLYLALSPDGEAIVTGAGDETLRFWNVFSKARSQKENKSVLNLFANIR
Protein: NAD(P)H-quinone oxidoreductase subunit 6, chloroplastic (EC 7.1.1.-) (NAD(P)H dehydrogenase subunit 6) (NADH-plastoquinone oxidoreductase subunit 6) (Q6ENA4)
Organism: Oryza nivara (Indian wild rice) (Oryza sativa f. spontanea)
Function: NDH shuttles electrons from NAD(P)H:plastoquinone, via FMN and iron-sulfur (Fe-S) centers, to quinones in the photosynthetic chain and possibly in a chloroplast respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be plastoquinone. Couples the redox reaction to proton translocation, and thus conserves the redox energy in a proton gradient (By similarity).
Subcellular location: Plastid, chloroplast thylakoid membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}.
Interaction partners:
- NAD
- NAD
- NAD
- NAD
- Uncharacterized protein
- NAD
- NAD
- NAD
- NAD
- NAD
Sequence:
MDLPGPIHEILVLFGGFVLLLGGLGVVLLTNPTFSAFSLGLVLVCISLFYILLNSYFVAVAQLLIYVGAINVLIIFAVMFVNGSEWSKDKNFWTIGDGFTSLVCITIPFSLMTTIPDTSWYGILWTTRSNQIVEQGLINNVQQIGIHLATDFYLPFELISIILLVSLIGAITMARQ
Protein: Lupeol synthase 1 (AtLUP1) (EC 5.4.99.41) ((S)-2,3-epoxysqualene synthase) (EC 4.2.1.128) (Beta-amyrin synthase) (EC 5.4.99.39) (Germanicol synthase) (EC 5.4.99.34) (Lupan-3-beta,20-diol synthase) (Q9C5M3)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Multifunctional enzyme that converts oxidosqualene to lupeol and 3,20-dihydroxylupane. Minor production of beta-amyrin, germanicol, taraxasterol and psi-taraxasterol.
Interaction partners:
- Squalene epoxidase 1
- Squalene epoxidase 2, mitochondrial
- Squalene epoxidase 6
- Squalene epoxidase 5
- Squalene epoxidase 3
- Squalene epoxidase 4
- Arabidiol synthase
- Tirucalladienol synthase
- Baruol synthase
- Thalianol synthase 1
Sequence:
MWKLKIGKGNGEDPHLFSSNNFVGRQTWKFDHKAGSPEERAAVEEARRGFLDNRFRVKGCSDLLWRMQFLREKKFEQGIPQLKATNIEEITYETTTNALRRGVRYFTALQASDGHWPGEITGPLFFLPPLIFCLYITGHLEEVFDAEHRKEMLRHIYCHQNEDGGWGLHIESKSVMFCTVLNYICLRMLGENPEQDACKRARQWILDRGGVIFIPSWGKFWLSILGVYDWSGTNPTPPELLMLPSFLPIHPGKILCYSRMVSIPMSYLYGKRFVGPITPLILLLREELYLEPYEEINWKKSRRLYAKEDMYYAHPLVQDLLSDTLQNFVEPLLTRWPLNKLVREKALQLTMKHIHYEDENSHYITIGCVEKVLCMLACWVENPNGDYFKKHLARIPDYMWVAEDGMKMQSFGCQLWDTGFAIQALLASNLPDETDDALKRGHNYIKASQVRENPSGDFRSMYRHISKGAWTFSDRDHGWQVSDCTAEALKCCLLLSMMSADIVGQKIDDEQLYDSVNLLLSLQSGNGGVNAWEPSRAYKWLELLNPTEFMANTMVEREFVECTSSVIQALDLFRKLYPDHRKKEINRSIEKAVQFIQDNQTPDGSWYGNWGVCFIYATWFALGGLAAAGETYNDCLAMRNGVHFLLTTQRDDGGWGESYLSCSEQRYIPSEGERSNLVQTSWAMMALIHTGQAERDLIPLHRAAKLIINSQLENGDFPQQEIVGAFMNTCMLHYATYRNTFPLWALAEYRKVVFIVN
Protein: GEO10356p1 (MIP01406p) (MIP10950p) (Seminal fluid protein 24Ba) (B9EQU3)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Seminal fluid protein 24Bb
Sequence:
METKFVVITFLISYVLAQSNADCGNKPIVDGNCDQIIKGFTFATEENRCKKFRAKGCTVGGNYFRAKDECELKCKGYINWGIESFGNGDWEESEIEDYWNNGSEESEVESISNRGSKKRTL
Protein: At1g76380 (DNA-binding bromodomain-containing protein) (A4FVS4)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- SWI/SNF complex subunit SWI3C
- Histone acetyltransferase subunit NuA4-domain protein
- Histone acetyltransferase of the MYST family 2
- Histone acetyltransferase of the MYST family 1
- SWI/SNF complex subunit SWI3A
- DNA-binding bromodomain-containing protein
- SWI/SNF complex subunit SWI3B
- Protein PHOTOPERIOD-INDEPENDENT EARLY FLOWERING 1
- At1g20670
- Mediator of RNA polymerase II transcription subunit-like protein
Sequence:
MGEVADNNTLMKRKKKGRPSLLDLQKRALKQQQLLQRRNPNEENEEELRSSSRNPNFSNRSNRRRNSNSEDDDDERRDKKHRLLHGLNSHEGRDSSNSKSGGGDLDSDARNRRKIDGSDNTGEKASKATDILLQRGSLVESTPLPDKKLLFFILDRVQKKDTYGVYSDPADPEELPDYYEIIKNPMDFTTLRKKLESGAYTTLEQFEQDVFLICTNAMEYNSADTVYYRQARAMLELAKKDFGNLRQESDGEEPVSLSQQPKVVKRGRPPGSGLKKQLEQSLIDRTTSDISADAAAFTYAGDSSRLSGSYNLRKNPPSYGFRHAETSVRINHNSENQSGLLIDWEKEFPPSVVKAVNKYGMKNVDENRRDTYNQNSASLQDSSIFTLLDDNLKQLTPVGLKAEYGYARSLARYAANIGPVAWTFANVRIEKLLPTGTEFGPGWVGENPENPPQQQNLMSGKQKCSNDYASDDHHQSSRIMSPSTSVSSSIIGNIHSSHESKESVQVLNQETEINGLVRGSSGFNHKPNQMLETAGSQQGNIKQEFQRLPPDLNARLSSPNSPGSNHQAGSSQHPDLALQL
Protein: Serine/threonine-protein phosphatase 1 regulatory subunit 10 (MHC class I region proline-rich protein CAT53) (Phosphatase 1 nuclear targeting subunit) (Protein PNUTS) (O55000)
Organism: Rattus norvegicus (Rat)
Function: Scaffold protein which mediates the formation of the PTW/PP1 phosphatase complex by providing a binding platform to each component of the complex. The PTW/PP1 phosphatase complex plays a role in the control of chromatin structure and cell cycle progression during the transition from mitosis into interphase. Mediates interaction of WDR82 and PPP1CA. Inhibitor of PPP1CA and PPP1CC phosphatase activities. Has inhibitory activity on PPP1CA only when phosphorylated. Binds to mRNA, single-stranded DNA (ssDNA), poly(A) and poly(G) homopolymers.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00649}. Note=Found in discrete nucleoplasmic bodies and within nucleoli. Associates with chromatin during interphase, excluded from condensed chromosomes during early mitosis and is reloaded onto chromosomes at the late telophase (By similarity). {ECO:0000250}.
Interaction partners:
- Serine/threonine-protein phosphatase PP1-alpha catalytic subunit
- Serine/threonine-protein phosphatase PP1-beta catalytic subunit
- TOX high mobility group box family member 4
- WD repeat-containing protein 82
- Serine/threonine-protein phosphatase PP1-gamma catalytic subunit
- Protein phosphatase 1 regulatory subunit 12A
Sequence:
MGSGPIDPKELLKGLDSFLTRDGEVKSVDGIAKIFSLMKEARKMVSRCTYLNIILQTRAPEVLVKFIDVGGYKLLNSWLTYSKTTNNIPLLQQILLTLQHLPLTVDHLKQNNTAKLVKQLSKSSEDEELRKLASVLVSDWMAVIRSQSSTQPAEKDKKKRKEEGKSRTTLPERPLTEVKAETRAEEAPEKKKEKPKSLRTTAPSHAKFRSTGLELDTPSLVPVKKNSSTVVVSDKYNLKPIPLKRQSATAAPGDAAPPAEKKYKPLNTTPNTTKEIKVKIIPPQPMEGLGFLDALNSAPVPGIKIKKKKKVLSPTAAKPSPFEGKTSTEPSTAKPSSPEPAAPAEPMDTDRPGTPVPAVEVPELMDAASSEPGALDAKPVESPGDPNQLTRKGRKRKTVTWPEEGKLREYFYFELDETERVNVNKIKDFGEAAKREILSDRHAFETARRLSHDNMEEKVPWVCPRPLVLPSPLVIPGSNSQERYIQAEREKGILQELFLNKESPHEPDPEPYEPIPPKLIPLDEECAMDETPYVETLEPGGSGGSPDGAGGSKLPPVLANLMGSMGAGKSPQGPGGGGINVQEILTSIMGSPNNHPSEELLKQPDYSDKLKQMLVPHGLLGPGPVANGFPPGGPGGPKGMQHFPPGPGGPMPGPHGGPGGPVGPRLLGPPPPSRGGDPFWDGPGDPMRGGPMRGGPGPGPGPYHRGRGGRGGNEPPPPPPFRGARGGRSGGGPPNGRGGPGGGGMVGGGGHRPHEGPGGSMGSGHRSHEGPGGSMGSGHRSHEGPGHGGPHGHRPHDVPSHRGHDHRGPPPHEHRGHDGHGGGGHRGHDGGHSHGGDMSNRPVCRHFMMKGNCRYENNCAFYHPGVNGPPLP
Protein: Cytochrome c biogenesis CcmF N-terminal-like mitochondrial protein 1 (Cytochrome c biogenesis orf382) (Q9T6H8)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Forms a complex with CCMFC, CCMFN2 and CCMH that performs the assembly of heme with c-type apocytochromes in mitochondria.
Subcellular location: Mitochondrion inner membrane {ECO:0000269|PubMed:18644794}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Cytochrome c biogenesis CcmF N-terminal-like mitochondrial protein 2
- Cytochrome c biogenesis FC.
- Cytochrome c biogenesis FN2.
- Cytochrome c-type biogenesis CcmH-like mitochondrial protein
- Cytochrome c biogenesis CcmF C-terminal-like mitochondrial protein
- Putative cytochrome c biogenesis ccmB-like mitochondrial protein
- Cytochrome c biogenesis B.
- Maturase
- Putative cytochrome c biosynthesis ccmC-like mitochondrial protein
- Small ribosomal subunit protein uS7m
Sequence:
MSISIYEFFHYSLFLGLFVAFTYNKKQPPAFGAALAFWCILLSFLGLLFCHISNNLSNYNVLTANALFFYQISGTWSNHEGSILLWCWILNFYGFFFCYRGRPQSHNVLKQGGYRESLFFFFVLNFVKNSILSLLRYEQESGLKNQLYTPFVLRTLVDSELCSRRNRTFDGPALFYAPLYPERKIKNPLDAWRFRGSREGKRTHPLLHLARDDKERASSIDEQRIDGALGIALFFSFFLLASSDPFVRNFFVCTEPLAELNPVLQDPILAIHPPCIYAGDVASAEGFGLCRSKMMNGIVALHSPPMRKDAAEKNGTLLCSAGCVGSRITSELFTLKFKHVGAKCYPALLLRSNRSPLMLLRRRFFAFSSFWAGARSHSTKRY
Protein: Actin-like 6A (Q4KM87)
Organism: Rattus norvegicus (Rat)
Interaction partners:
- SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily A member 4
- PHD finger protein 10
- AT-rich interaction domain 1A
- SWI/SNF related, matrix associated, actin dependent regulator of chromatin, subfamily d, member 1
- SWI/SNF related, matrix associated, actin dependent regulator of chromatin, subfamily c, member 2
- SWI/SNF related, matrix associated, actin dependent regulator of chromatin, subfamily c, member 1
- SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily B member 1
- Bromodomain containing 7
- Protein polybromo-1
- RuvB-like helicase
Sequence:
MSGGVYGGDEVGALVFDIGSYTVRAGYAGEDCPKVDFPTAIGVVLERDDGSTMMEIDGDKGKQGGPTYYIDTNALRVPRESMEAISPLKNGMVEDWDSFQAILDHTYKMHVKSEASLHPVLMSEAPWNTRAKREKLTELMFEHYSIPAFFLCKTAVLTAFANGRSTGLILDSGATHTTAIPVHDGYVLQQGIVKSPLAGDFITMQCRELFQEMNIELIPPYMIASKEAVREGSPANWKRKEKLPQVTRSWHNYMCNCVIQDFQASVLQVSDSTYDEQVAAQMPTVHYEFPNGYNCDFGAERLKIPEGLFDPSNVKGLSGNTMLGVSHVVTTSVGMCDIDIRPGLYGSVIVAGGNTLIQSFTDRLNRELSQKTPPSMRLKLIANNTTVERRFSSWIGGSILASLGTFQQMWISKQEYEEGGKQCVERKCP
Protein: Coiled-coil domain containing protein 151 (Q9VTQ3)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Dynein, axonemal, intermediate chain 2, isoform C
- GH13165p
- Outer dynein arm-docking complex subunit 4
- IP19827p
- Ras-like GTP-binding protein Rho1
- Spag1 axonemal dynein assembly factor
- Coiled-coil domain containing protein 114
- AT19426p
Sequence:
MESDKLNELNRQINEIKKRILLAEGQKTANAAEWQKQNRINCDTISSLKKDIKEQTIRASRLRNPLQRPVVIKESTGESRRAQSCTPTLIVGKATYPVGAKNADDAIFLTDLKITESRKQMDLLRHRFKSRQQYFSKLVEKYRGLLANKEAQNQNMGEKPPETLEEDANRKLVCQLENEIHRTNVQWMEAEHIRKKYRSIEASLMTDAERFERSLRELEASLSDQKAEIERLQQVHNEAVEMRDAAKVILQRQEQQANVSQKTRERQALDFRKQVEARKLELERIGRKLFAETKTLVHQDSVGSSSGDQHTAKTENGEEEPVSQLESVTSDMESLFKQLMEASGATSPFEVFERFSAQKESAARLNYLRKAAEAEKANLEAEREALSSELEASKFSDVKESEVNQEVIEQIKNSIAAKEQDRKLDTDEAGKSMGVLKYLKERICEMIFKVQEVDESNIEIPERKLHVSVAELPNFLAHTAEDEDMIEILKVKIKRCQELSKSEDVPPFEIPKLDIVDEEEEEMYKAEQPKSPSIQEGEKPQPMPVCYYNLFAGRAQRAAGTSSSSPEQAPAAVATADDDNEVPSRNFLKRQSVLIVDSKSRRKPFRPTPGGRRK