wanglab/gogpt-training-data huggingface dataset:
Protein: Myelin basic protein (F8W3A0)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Myelin membrane {ECO:0000256|ARBA:ARBA00004392}; Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004392}; Cytoplasmic side {ECO:0000256|ARBA:ARBA00004392}.
Interaction partners:
Sequence:
MATASTSGQNPFGLGRKKKAPGVLDQISRFFGGDKKRKGKRPHHSSTRRRGDVNPVVHFFRSFGESRSRSPPKRWSTIF
Protein: Spectrin alpha chain, erythrocytic 1 (Erythroid alpha-spectrin) (P08032)
Organism: Mus musculus (Mouse)
Function: Spectrin is the major constituent of the cytoskeletal network underlying the erythrocyte plasma membrane. It associates with band 4.1 and actin to form the cytoskeletal superstructure of the erythrocyte plasma membrane.
Subcellular location: Cytoplasm, cytoskeleton. Cytoplasm, cell cortex.
Interaction partners:
- Spectrin beta chain, erythrocytic
- Spectrin beta chain
- Caspase-3
- Spectrin beta chain
- Spectrin alpha chain, non-erythrocytic 1
- Ankyrin-1
- Ammonium transporter Rh type A
- Band 3 anion transport protein
- Spectrin beta, non-erythrocytic 5
- Spectrin beta chain, non-erythrocytic 1
Sequence:
METPKETAVESSGPKVLETAEEIQHRRAEVLNQYQRFKDRVAERGQKLEESYHYQVFRRDADDLEKWIMEKLEIAKDKTYEPTNIQGKYQKHESFVSEVQAKSRVLPELEEIREARFAEDHFAHEATKTHLKQLRLLWDLLLELTQEKSDVLLRALKFYQYSQECEDILEWVKEKEAIVTLVELGDDWERTEVLHKKFEEFQEELTARKGKVDRVNQYANECAQEKHPKLPEIKAKQDEVNAAWDRLWSLALKRRESLSNAADLQRFKRDVNEAIQWMEEKEPQLTSEDYGKDLVSSEALFHNHKRLERNLAVMDDKVKELCAKADKLMISHSADAPQIQQMKLDLVSNWERIRALATNRYAKLKASYGYHRFLSDYDELSGWMKEKTALINADELPTDVASGEALLARHQQHKHEIDSYDDRFQSADATGQELLDGNHEASEEIREKMTILANDWAALLELWDKCQHQYRQCLDFHLFYRDSEQVDSWMSRQEAFLENEDLGNSVGSVEALLQKHDDFEEAFTAQEEKIITLDETATKLIDNDHYDSENIAAIRDGLLARRDALRERAATRRKLLVDSQLLQQLYQDSDDLKTWINKKKKLADDDDYKDVQNLKSRVQKQQDFEEELAVNEIMLNNLEKTGQEMIEDGHYASEAVAARLSEVANLWKELLEATAQKGTQLYEANQLLQFENNAEDLKRWLEEVEWQVTSEDYGKGLADVQNLLRKHGLLESDVTARQNQVDTLTDMAAHFEEIGHPDSGDIRARQESLLSRFEALKEPLAIRKKKLIDLLKLQQICRDSEDEEAWIQETEPSAASTHLGKDLVAAKNLLNRHEVILADIASHEPRIQVITERGNKMVEEGHFAAEDIASRVESLNKNMESLHARAIRRENDLKANVQLQQYLADLHEAEAWIKEKEPIVDNKNYGADEEAAGALLKKHEAFLVDLNAFENSIKALRDQAEVCQQQQAAPVDEAGREARVIALYDFEARSRREVSMKKNDVLTLLSSINKDWWKVEADDHQGFVPAVYVRKLAPDELPGFPQHRQEEPVNIPQLQQQVETLYHSLLDRAEERRRRLLQRYNEFLLAYEAGDMLEWIQEKKTENTGVELDDVWELQKKFDEFQRDLKSNEPRLKDINKVADELLFEELLTPEGAHIRQELNTRWNSLKRLADEQYQLLSSAHAVEMFHREADDVKEQIDKKCRALNAADPGSDLLSVQALQRQHEVFERDIIPLGEKVTTLGETAERLCESHPDATEDLQKQRTELNEAWDTLQGLTSDRKESLNEAHKFFLFLSKASDLENWIKTIGGVISSPELAEDLTGTEILLERHQEHHDDIKREDPTFQALEDFGTELIDSGHRNRREIDNTLQNINSKRDNLEKSWENRKKMLDQCLELQLFRGKCDQVESWMVARENSLRSDDRDHLNSLQALMKKRDDLDKAITAQEGKISDLENVATRLIDNDHYAKEEIAARLQRVLDRWKALKEQLLTELGKLGDYADLKQFYRDLEDLEEWINEMLPIACDESYKDPTNIQRKYLKHQAFENEVNGRAEQVDGVINLGNSLIERRVCDGDEENMQEQLDKLKENWDYLLERTTDKGQKLNEASRQQRFNTSIRDFEFWLSEAEGLLAMKDQARDLTSAGNLLKKHQLLEAEMLAREDPLKDLNDLAQELISSGTFNIDQIEEKMNGVNERFENVQSLAAAHHEKLKETYALFQFFQDLDDEEAWIEEKLLRVSSQDYGRDLQSVQNLLKKHKRLEGELVAHEPAVQNVLDTAESLRDKAAVGKEEIQERLAQFVQHWEKLKELAKTRGVNLEESLEYLQFMENAEEEEAWLGEKCALVSRGDSGDTLAATQSLLKKHEALENDFAVHKNRVQDVCAQGEDILNKEETQNKDKISTKIQVLNEKTASLAKALAAWKSQLDDVHAFQQFNWKADVVESWIGEKEASLKTKSNGADLTAFLTLLAKHDTLDASLQSFQQERLSEIAELKDQLVAGEHSQAKAIEEQHAALLRHWEQLLEASRVHRQKLLEKQLPLQKAEELFMEFAHKASAFNNWCENAEEDLSEPVHCVSLNEIRQLQKEHEAFLASLAGAQEDFNYLLELDKQIKALNVPSSPYTWLTVDVLGRIWNHLPDIIKEREQELQKEEARQIKNFEMCQEFEQNASAFLQWIQETRAYFLDGSLLKETGTLESQLEANKRKQKEIQAMKRHLTKIEDLGDSMEEALILDIKYSTIGLAQQWDQLHQLGMRMQHNLEQQIQAKDTIGVSEETLKEFSTTYKHFDENLTGRLTHKEFRSCLRGLNYYLPMVEEGEPEPKFEKFLNAVDPGRKGYVSLEDYTSFLIDKESENIKTSDDIESAFQALAEGKAYITKEDMKQALTPEQVSFCTIHMQQYMDPRGRSQPAGYDYVGFTNSFFGN
Protein: N-acetyltransferase eso1 (EC 2.3.1.-) (ECO1 homolog) (Sister chromatid cohesion protein eso1) (O42917)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Probable acetyltransferase required for the establishment of sister chromatid cohesion and couple the processes of cohesion and DNA replication to ensure that only sister chromatids become paired together. In contrast to the structural cohesins, the deposition and establishment factors are required only during S phase. The relevance of acetyltransferase function remains unclear (By similarity).
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- Proliferating cell nuclear antigen
- Inheritance of peroxisomes protein 2
- Structural maintenance of chromosomes protein 3
- DNA repair protein rev1
- DNA polymerase zeta catalytic subunit
- Sister chromatid cohesion protein pds5
- DNA polymerase zeta processivity subunit
- Wings apart-like protein homolog 1
- Postreplication repair E3 ubiquitin-protein ligase rad18
- Structural maintenance of chromosomes protein 6
Sequence:
MELGKSKFSWKDLQYCDKAGTQNSPLRVVAHIDQDAFYAQVESVRLGLDHSVPLAVQQWQGLIAVNYAARAANISRHETVTEAKKKCPELCTAHVKTWKAGESEAKYHENPNPNYYKTCLDPYRHESVKILNIIKKHAPVVKKASIDECFIELTSDVKRIVLEEYPYLKIPSEDSNVALPQAPVLLWPAEFGMVIEEEVVDRTKEDYERDWDDVFLFYAAKIVKEIRDDIYLQLKYTCSAGVSFNPMLSKLVSSRNKPNKQTILTKNAIQDYLVSLKITDIRMLGGKFGEEIINLLGTDSIKDVWNMSMDFLIDKLGQTNGPLVWNLCHGIDNTEITTQVQIKSMLSAKNFSQQKVKSEEDAINWFQVFASDLRSRFLELEGMRRPKTICLTVVSRFLRKSRSSQIPMNVDISTQFIVEATSKLLRQLQQEFDVYPISNLSISFQNIIEVDRNSRGIEGFLKKSNDEIYMSTSVSPSIEGRAKLLNENMRENNSFELSSEKDIKSPKRLKRGKGKGIFDMLQQTAVSKPTENSADETYTCEECEQKITLSERNEHEDYHIALSISRKERYNNLVPPSHDKPKQVKPKTYGRKTGSKHYAPLSDETNNKRAFLDAFLGNGGNLTPNWKKQTPKAISNSSDNMTQLHLDLANSTVTCSECSMEYNSTSEEDILLHSRFHSRVLGGVTVSFQCSPIYRVNYGLSSDCIYSINSESSLIDQRKAEEALSFVNNELSSEPIETIGVDKYTTFLFISDKKCVGLLLAERISSAYIVDELELNNNNSTSSAVYIKNENLRKGFVLGISRIWVSASRRKQGIASLLLDNALKKFIYGYVISPAEVAFSQPSESGKQFIISWHRSRNNGSSKSLRYAVYES
Protein: Antagonist of mitotic exit network protein 1 (Chromosome stability protein 13) (Increased copper-sensitivity protein 4) (P38285)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Negative regulator of the mitotic exit network (MEN), required for multiple cell cycle checkpoints. Acts in the daughter cell to inhibit the mitotic exit pathway once MEN has executed its function. Through its binding ability to TEM1, interferes with the TEM1-CDC5 association, required for CDC5 kinase activation and MEN activation. Required for daughter cell separation and chromosome stability. Involved in copper sensitivity.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:12628189}. Nucleus {ECO:0000269|PubMed:12628189, ECO:0000269|PubMed:14562095}.
Interaction partners:
- Cell cycle serine/threonine-protein kinase CDC5/MSD2
- Protein phosphatase PP2A regulatory subunit A
- Mitotic check point protein BFA1
- Serine/threonine-protein phosphatase PP2A-1 catalytic subunit
- Serine/threonine-protein phosphatase PP2A-2 catalytic subunit
- Protein phosphatase PP2A regulatory subunit B
- Mitotic check point protein BUB2
- Suppressor of kinetochore protein 1
- Protein TEM1
- Protein DSE1
Sequence:
MKLERVSSNGSFKRGRDIQSLESPCTRPLKKMSPSPSFTSLKMEKPFKDIVRKYGGHLHQSSYNPGSSKVELVRPDLSLKTDQSFLQSSVQTTPNKKSCNEYLSTPEATPLKNTATENAWATSRVVSASSLSIVTPTEIKNILVDEFSELKLGQPLTAQHQRSHAVFEIPEIVENIIKMIVSLESANIPKERPCLRRNPQSYEHSLLMYKDEERAKKAWSAAQQLRDPPLVGHKEKKQGALFSCMMVNRLWLNVTRPFLFKSLHFKSVHNFKEFLRTSQETTQVMRPSHFILHKLHQVTQPDIERLSRMECQNLKWLEFYVCPRITPPLSWFDNLHKLEKLIIPGNKNIDDNFLLRLSQSIPNLKHLVLRACDNVSDSGVVCIALNCPKLKTFNIGRHRRGNLITSVSLVALGKYTQVETVGFAGCDVDDAGIWEFARLNGKNVERLSLNSCRLLTDYSLPILFALNSFPNLAVLEIRNLDKITDVRHFVKYNLWKKSLDAPILIEACERITKLIDQEENRVKRINSLVALKDMTAWVNADDEIENNVD
Protein: DNA topoisomerase 3-beta-1 (EC 5.6.2.1) (DNA topoisomerase III beta-1) (O95985)
Organism: Homo sapiens (Human)
Function: Releases the supercoiling and torsional tension of DNA introduced during the DNA replication and transcription by transiently cleaving and rejoining one strand of the DNA duplex. Introduces a single-strand break via transesterification at a target site in duplex DNA. The scissile phosphodiester is attacked by the catalytic tyrosine of the enzyme, resulting in the formation of a DNA-(5'-phosphotyrosyl)-enzyme intermediate and the expulsion of a 3'-OH DNA strand. The free DNA strand than undergoes passage around the unbroken strand thus removing DNA supercoils. Finally, in the religation step, the DNA 3'-OH attacks the covalent intermediate to expel the active-site tyrosine and restore the DNA phosphodiester backbone (By similarity). Possesses negatively supercoiled DNA relaxing activity.
Interaction partners:
- Tudor domain-containing protein 3
- Fanconi anemia group M protein
- RecQ-mediated genome instability protein 1
- RecQ-like DNA helicase BLM
- Bifunctional 3'-5' exonuclease/ATP-dependent helicase WRN
- DNA topoisomerase 3-alpha
- RecQ-mediated genome instability protein 2
- E3 ubiquitin-protein ligase TRIM41
- ATP-dependent DNA helicase Q5
- Single-stranded DNA-binding protein, mitochondrial
Sequence:
MKTVLMVAEKPSLAQSIAKILSRGSLSSHKGLNGACSVHEYTGTFAGQPVRFKMTSVCGHVMTLDFLGKYNKWDKVDPAELFSQAPTEKKEANPKLNMVKFLQVEGRGCDYIVLWLDCDKEGENICFEVLDAVLPVMNKAHGGEKTVFRARFSSITDTDICNAMACLGEPDHNEALSVDARQELDLRIGCAFTRFQTKYFQGKYGDLDSSLISFGPCQTPTLGFCVERHDKIQSFKPETYWVLQAKVNTDKDRSLLLDWDRVRVFDREIAQMFLNMTKLEKEAQVEATSRKEKAKQRPLALNTVEMLRVASSSLGMGPQHAMQTAERLYTQGYISYPRTETTHYPENFDLKGSLRQQANHPYWADTVKRLLAEGINRPRKGHDAGDHPPITPMKSATEAELGGDAWRLYEYITRHFIATVSHDCKYLQSTISFRIGPELFTCSGKTVLSPGFTEVMPWQSVPLEESLPTCQRGDAFPVGEVKMLEKQTNPPDYLTEAELITLMEKHGIGTDASIPVHINNICQRNYVTVESGRRLKPTNLGIVLVHGYYKIDAELVLPTIRSAVEKQLNLIAQGKADYRQVLGHTLDVFKRKFHYFVDSIAGMDELMEVSFSPLAATGKPLSRCGKCHRFMKYIQAKPSRLHCSHCDETYTLPQNGTIKLYKELRCPLDDFELVLWSSGSRGKSYPLCPYCYNHPPFRDMKKGMGCNECTHPSCQHSLSMLGIGQCVECESGVLVLDPTSGPKWKVACNKCNVVAHCFENAHRVRVSADTCSVCEAALLDVDFNKAKSPLPGDETQHMGCVFCDPVFQELVELKHAASCHPMHRGGPGRRQGRGRGRARRPPGKPNPRRPKDKMSALAAYFV
Protein: LIM homeobox transcription factor 1-alpha (LIM/homeobox protein 1.1) (LMX-1.1) (LIM/homeobox protein LMX1A) (Q8TE12)
Organism: Homo sapiens (Human)
Function: Acts as a transcriptional activator by binding to an A/T-rich sequence, the FLAT element, in the insulin gene promoter. Required for development of the roof plate and, in turn, for specification of dorsal cell fates in the CNS and developing vertebrae (By similarity).
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00108}.
Interaction partners:
- Neurogenin-2
- Nuclear receptor subfamily 4 group A member 2
- Homeobox protein MSX-1
- Hepatocyte nuclear factor 3-beta
- Achaete-scute homolog 1
- Proto-oncogene Wnt-1
- Homeobox protein OTX2
- Homeobox protein Nkx-2.2
- Paired box protein Pax-2
Sequence:
MLDGLKMEENFQSAIDTSASFSSLLGRAVSPKSVCEGCQRVILDRFLLRLNDSFWHEQCVQCASCKEPLETTCFYRDKKLYCKYDYEKLFAVKCGGCFEAIAPNEFVMRAQKSVYHLSCFCCCVCERQLQKGDEFVLKEGQLLCKGDYEKERELLSLVSPAASDSGKSDDEESLCKSAHGAGKGTAEEGKDHKRPKRPRTILTTQQRRAFKASFEVSSKPCRKVRETLAAETGLSVRVVQVWFQNQRAKMKKLARRQQQQQQDQQNTQRLSSAQTNGGGSAGMEGIMNPYTALPTPQQLLAIEQSVYSSDPFRQGLTPPQMPGDHMHPYGAEPLFHDLDSDDTSLSNLGDCFLATSEAGPLQSRVGNPIDHLYSMQNSYFTS
Protein: Coniferin beta-glucosidase (EC 3.2.1.126) (Q9ZT64)
Organism: Pinus contorta (Shore pine) (Lodgepole pine)
Function: Involved in the release of monolignols for lignin biosynthesis. Unable to hydrolyze 4-nitrophenyl beta-cellobioside or alpha-linked methylumbelliferyl glucoside.
Interaction partners:
Sequence:
MEVSVLMWVLLFYSLLGFQVTTARLDRNNFPSDFMFGTASSAYQYEGAVREDGKGPSTWDALTHMPGRIKDSSNGDVAVDQYHRYMEDIELMASLGLDAYRFSISWSRILPEGRGEINMAGIEYYNNLIDALLQNGIQPFVTLFHFDLPKALEDSYGGWLSPQIINDFEAYAEICFRAFGDRVKYWATVNEPNLFVPLGYTVGIFPPTRCAAPHANPLCMTGNCSSAEPYLAAHHVLLAHASAVEKYREKYQKIQGGSIGLVISAPWYEPLENSPEERSAVDRILSFNLRWFLDPIVFGDYPQEMRERLGSRLPSISSELSAKLRGSFDYMGINHYTTLYATSTPPLSPDHTQYLYPDSRVYLTGERHGVSIGERTGMDGLFVVPHGIQKIVEYVKEFYDNPTIIIAENGYPESEESSSTLQENLNDVRRIRFHGDCLSYLSAAIKNGSDVRGYFVWSLLDNFEWAFGYTIRFGLYHVDFISDQKRYPKLSAQWFRQFLQHDDQGSIRSSSSI
Protein: Erythrocyte membrane protein band 4.1 like 2 (E9PHY5)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MTTEVGSVSEVKKDSSQLGTDATKEKPKEVAENQQNQSSDPEEEKGSQPPPAAESQSSLRRQKREKETSESRGISRFIPPWLKKQKSYTLVVAKDGGDKKEPTQAVVEEQVLDKEEPLPEEQRQAKGDAEEMAQKKQEIKVEVKEEKPSVSKEEKPSVSKVEMQPTELVSKEREEKVKETQEDKLEGGAAKRETKEVQTNELKAEKASQKVTKKTKTVQCKVTLLDGTEYSCDLEKHAKGQVLFDKVCEHLNLLEKDYFGLLFQESPEQKNWLDPAKEIKRQLRNLPWLFTFNVKFYPPDPSQLTEDITRYFLCLQLRQDIASGRLPCSFVTHALLGSYTLQAELGDYDPEEHGSIDLSEFQFAPTQTKELEEKVAELHKTHRGLSPAQADSQFLENAKRLSMYGVDLHHAKDSEGVDIKLGVCANGLLIYKDRLRINRFAWPKILKISYKRSNFYIKVRPAELEQFESTIGFKLPNHRAAKRLWKVCVEHHTFYRLVSPEQPPKAKFLTLGSKFRYSGRTQAQTRQASTLIDRPAPHFERTSSKRVSRSLDGAPIGVMDQSLMKDFPGAAGEISAYGPGLVSIAVVQDGDGRREVRSPTKAPHLQLIEGKSSHETLNIVEEKKRAEVGKDERVITEEMNGKEISPGSGPGEIRKVEPVTQKDSTSLSSESSSSSSESEEEDVGEYRPHHRVTEGTIREEQEYEEEVEEEPRPAAKVVEREEAVPEASPVTQAGASVITVETVIQENVGAQKIPGEKSVHEGALKQDMGEEAEEEPQKVNGEVSHVDIDVLPQIICCSEPPVVKTEMVTISDASQRTEISTKEVPIVQTETKTITYESPQIDGGAGGDSGTLLTAQTITSESVSTTTTTHITKTVKGGISETRIEKRIVITGDGDIDHDQALAQAIREAREQHPDMSVTRVVVHKETELAEEGED
Protein: TEL2-interacting protein 2 (P47168)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Component of the ASTRA complex probably in chromatin remodeling.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:14562095}. Nucleus {ECO:0000305|PubMed:14562095}.
Interaction partners:
- TEL2-interacting protein 1
- Telomere length regulation protein TEL2
- ASTRA-associated protein 1
- SAGA complex/NuA4 acetyltransferase complex subunit TRA1
- RuvB-like protein 1
- RuvB-like protein 2
Sequence:
MTAVTDIIDELNDSSLSSTRLRELCLQLRKKTDTGCAITVSDEVNLIESLSYHSISPGVDIQINTDVLQTIDYYFQRNKSEHDEIMCVLISKLQPLLLKRKSNFELKEQRNLGLKPTLGMSLKEDNLMQAWVSQGGLKGIPLFYVILLHLKRRDISTNLSWIIPGILNILDDTTDIRRIKLRGVLLLQTLLNHTFMNETNDSKWIQFSSTGLFPLFEKTLINMCYFLPPSYNADETIAIWRVVFPTIQSLYKVEFLDNYTKYQYHLEKFMSEIILQNIIPRASLAYENLTLYALECTMNILRLQREGSVVHLQRLIFVLGEYIVRNPFYTTFPKLISKTLSVVSTLIKVCPNERIVAHRFDILSLILVTYDKCSQEDALNESILQQCKETISWLLNCDCAMGEQLSTLSKQPRFQLLFEFS
Protein: 5-methyltetrahydropteroyltriglutamate--homocysteine methyltransferase 3, chloroplastic (EC 2.1.1.14) (Cobalamin-independent methionine synthase 3) (AtMS3) (Q0WNZ5)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Catalyzes the transfer of a methyl group from 5-methyltetrahydrofolate to homocysteine resulting in methionine formation.
Subcellular location: Plastid, chloroplast {ECO:0000269|PubMed:15024005}.
Interaction partners:
- Homocysteine S-methyltransferase 1
- Adenosylhomocysteinase 2
- Homocysteine S-methyltransferase 2
- Homocysteine S-methyltransferase 3
- Adenosylhomocysteinase 1
- Cystathionine beta-lyase, chloroplastic
- S-adenosylmethionine synthase 2
- Probable cystathionine gamma-synthase 2
- Cystathionine gamma-synthase 1, chloroplastic
- S-adenosylmethionine synthase 3
Sequence:
MGQLALQRLQPLASLPRRPPSLPPPSSATPSLPCATASRRPRFYVARAMSSHIVGYPRIGPKRELKFALESFWDGKTNVDDLQNVAANLRKSIWKHMAHAGIKYIPSNTFSYYDQMLDTTAMLGAVPSRYGWESGEIGFDVYFSMARGNASAHAMEMTKWFDTNYHYIVPELGPDVNFSYASHKAVVEFKEAKALGIDTVPVLIGPMTYLLLSKPAKGVEKSFCLLSLIDKILPVYKEVLADLKSAGARWIQFDEPILVMDLDTSQLQAFSDAYSHMESSLAGLNVLIATYFADVPAEAYKTLMSLKCVTGFGFDLVRGLETLDLIKMNFPRGKLLFAGVVDGRNIWANDLSASLKTLQTLEDIVGKEKVVVSTSCSLLHTAVDLVNEMKLDKELKSWLAFAAQKVVEVNALAKSFSGAKDEALFSSNSMRQASRRSSPRVTNAAVQQDVDAVKKSDHHRSTEVSVRLQAQQKKLNLPALPTTTIGSFPQTTDLRRIRREFKAKKISEVDYVQTIKEEYEKVIKLQEELGIDVLVHGEAERNDMVEFFGEQLSGFAFTSNGWVQSYGSRCVKPPIIYGDITRPKAMTVFWSSMAQKMTQRPMKGMLTGPVTILNWSFVRNDQPRHETCFQIALAIKDEVEDLEKAGVTVIQIDEAALREGLPLRKSEQKFYLDWAVHAFRITNSGVQDSTQIHTHMCYSNFNDIIHSIIDMDADVITIENSRSDEKLLSVFHEGVKYGAGIGPGVYDIHSPRIPSTEEIAERINKMLAVLDSKVLWVNPDCGLKTRNYSEVKSALSNMVAAAKLIRSQLNKS
Protein: FI19908p1 (Wurstfest, isoform A) (A1ZBJ8)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Uncharacterized protein, isoform A
- Cytosol aminopeptidase
- Male-specific sperm protein Mst84Dc
- Cytosol aminopeptidase
- 10 kDa heat shock protein, mitochondrial
- AT11401p
- Cytosol aminopeptidase
- Protein dpy-30 homolog
- GH09231p
- Uncharacterized protein, isoform C
Sequence:
MVTDAQDTVAPKTSSTKEVQCQHSGALDEPHVEELALPGPAPLATPKSGRVGIFNAEDFLSRAQLNDKINNILRSPTKAPNGVRQRSVFTNNNPSPQATMRFVSSMNSPLAPRMSSLSLTGGVKRGLERGNSSSSMGNSASVGTSTSVLAKECSSQTNSCGRSYMNMGMHASSHSGFGVLPQSGAGYETMGWNMDAGNITRSGKSLTGRFNSGYGYEVDGAYCMPQAHHTQQFPSPMPPPPFAMDRVSSRTFEFENNTPPPCPGSGPIAMSNGTIQLRLREGVRIDMTLDKAVRVLNQRSMVAAALSRNCSNSALIHPNGRILQSGSKVEIVTYDGMKANNFVRYAKMWYKGVSFTSESCALIYLVDTAGTRTTTDTFTDLTKDYTLAVFYDDSRHGPSFVSDAHDVIANSTYNCAEDGTEVYDINGFRITQAADGLVKVSRQHSKCLIRTSPGNGSATLTTTGIHCTASLGKTSHLFVRRNEKRMHFDGSCFIVRNAGHSAGFNENNLLIVY
Protein: Killin (B2CW77)
Organism: Homo sapiens (Human)
Function: DNA-binding protein involved in S phase checkpoint control-coupled apoptosis by mediating p53/TP53-induced apoptosis. Has the ability to inhibit DNA synthesis and S phase arrest coupled to apoptosis. Has affinity to both double- and single-stranded DNA.
Subcellular location: Nucleus {ECO:0000269|PubMed:18385383}.
Interaction partners:
Sequence:
MDRPGPGSARPGRTVHVWGYRVEWKVRNGRKLQPSEWAGRGDLGGFKRRWKDTRATVGTTFRRRSRVSLVGELSKFPLPSDSSGGKSSSSFARGALAWCRQRNPNPSCAAAETGARTSLPKERCRGWRLGNWLHKHPHPNTCPRLPACWLPPILTERGERVPKLVPLLACYPKSKPKD
Protein: Transcription regulator, AsnC family (Q92LT2)
Organism: Rhizobium meliloti (strain 1021) (Ensifer meliloti) (Sinorhizobium meliloti)
Interaction partners:
Sequence:
MELLDGFDLKILSELQRDGHLTNNELSERVALSPSQCSRRRTRLEAEGFITGYQAQIDRQKLGLDLMVVISVTLATHNRDNAKRFANLVSALPEVLEAYALTGEMDYHLRVVTPDLAGLSRFVNEVLLPHDSVQHVKTSIVLETLKSFEGLPIPARMKG
Protein: Large ribosomal subunit protein uL3m (54S ribosomal protein L9, mitochondrial) (YmL9) (P31334)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Component of the mitochondrial ribosome (mitoribosome), a dedicated translation machinery responsible for the synthesis of mitochondrial genome-encoded proteins, including at least some of the essential transmembrane subunits of the mitochondrial respiratory chain. The mitoribosomes are attached to the mitochondrial inner membrane and translation products are cotranslationally integrated into the membrane.
Subcellular location: Mitochondrion {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:14576278}. Note=Mitoribosomes are tethered to the mitochondrial inner membrane and spatially aligned with the membrane insertion machinery through two distinct membrane contact sites, formed by the 21S rRNA expansion segment 96-ES1 and the inner membrane protein MBA1. {ECO:0000269|PubMed:25609543}.
Interaction partners:
- Large ribosomal subunit protein uL13m
- Large ribosomal subunit protein bL36m
- Small ribosomal subunit protein uS15m
- Large ribosomal subunit protein bL27m
- Large ribosomal subunit protein uL4m
- Large ribosomal subunit protein uL6m
- Large ribosomal subunit protein bL19m
- Large ribosomal subunit protein uL5m
- Large ribosomal subunit protein bL33m
- Small ribosomal subunit protein bS6m
Sequence:
MSKFLQGSIFSISKLHVRYSSTRPFLVAPSIANSITTEAPAINHSPELANARKWLPKRCGLITRKKGMMPYFDKSTGERSAATILEVNNVEVIMHRTSEVNGYFACQVGYGSRHLSKVSRQMLGHFASKVVNPKEHVAEFRVKDEKGLIPPGTLLKPSFFKEGQYVDVRSVSKGKGFTGVMKRYGFKGLRASHGTSIMHRHGGSYGQNQDPGRVLPGRKMPGHMGNEHVTIQNVKVLKVDDENNVIWVKGSVAGPKNSFVKIQDAIKKT
Protein: ATP-dependent 6-phosphofructokinase 7 (ATP-PFK 7) (Phosphofructokinase 7) (EC 2.7.1.11) (Phosphohexokinase 7) (Q9C5J7)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Catalyzes the phosphorylation of D-fructose 6-phosphate to fructose 1,6-bisphosphate by ATP, the first committing step of glycolysis.
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03186, ECO:0000269|PubMed:17485088}.
Interaction partners:
- Glucose-6-phosphate isomerase, cytosolic
- Glucose-6-phosphate isomerase 1, chloroplastic
- Aldolase-type TIM barrel family protein
- transaldolase
- Transketolase-2, chloroplastic
- Transketolase-1, chloroplastic
- 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase
- Mannose-6-phosphate isomerase 1
- Mannose-6-phosphate isomerase 2
- Hexokinase-4
Sequence:
MSSPRSNKPKIVNGPGGYILQDVPHLIDYLPDLPTYPNPLQDNPAYSVVKQYFVHADDSVPEKVVVHKDGPRGVHFRRAGPRQKVYFESDEVHACIVTCGGLCPGLNTVIREVVSSLSYMYGVKRILGIDGGYRGFYAKNTIPLNSKVVNDIHKRGGTIIGTSRGGHDTNKIVDSIQDRGINQVYIIGGDGTQRGASVIFEEIRRRRLKVAVVGIPKTIDNDIPVIDKSFGFDTAVEEAQRAINAAHVEAESNENGIGFVKLMGRYSGYIAMYATLASRDVDCCLIPESPFYLEGEGGLFEFIERRLKDHGHMVIVLAEGAGQDLMCKSMESTPMDASGNKLLKDVGLWLSQSIKDHFKKNKMVMNLKYIDPTYMIRAVPSNASDNVYCTLLAQSAVHGAMAGYTGYTSGLVNGRQTYIPFYRITETQNNVVITDRMWARLLSSTNQPSFLGPKDTSEEKKELPETPLLDDGAVDIPPVTKEVTK
Protein: Hevamine-A [Includes: Chitinase (EC 3.2.1.14); Lysozyme (EC 3.2.1.17)] (P23472)
Organism: Hevea brasiliensis (Para rubber tree) (Siphonia brasiliensis)
Function: Bifunctional enzyme with lysozyme / chitinase activity. May have a role in plugging the latex vessel and cessation of latex flow.
Subcellular location: Vacuole. Note=In the lutoids (vacuoles) from rubber latex.
Interaction partners:
Sequence:
MAKRTQAILLLLLAISLIMSSSHVDGGGIAIYWGQNGNEGTLTQTCSTRKYSYVNIAFLNKFGNGQTPQINLAGHCNPAAGGCTIVSNGIRSCQIQGIKVMLSLGGGIGSYTLASQADAKNVADYLWNNFLGGKSSSRPLGDAVLDGIDFDIEHGSTLYWDDLARYLSAYSKQGKKVYLTAAPQCPFPDRYLGTALNTGLFDYVWVQFYNNPPCQYSSGNINNIINSWNRWTTSINAGKIFLGLPAAPEAAGSGYVPPDVLISRILPEIKKSPKYGGVMLWSKFYDDKNGYSSSILDSVLFLHSEECMTVL
Protein: Cytidine deaminase (EC 3.5.4.5) (Cytidine aminohydrolase) (P56389)
Organism: Mus musculus (Mouse)
Function: This enzyme scavenges exogenous and endogenous cytidine and 2'-deoxycytidine for UMP synthesis.
Interaction partners:
- Thymidine phosphorylase
- Uridine phosphorylase 1
- Deoxycytidine kinase
- Thymidine kinase, cytosolic
- Uridine-cytidine kinase-like 1
- Uridine-cytidine kinase 2
- Uridine-cytidine kinase 1
- Thymidine kinase 2, mitochondrial
- Purine nucleoside phosphorylase
- Purine nucleoside phosphorylase
Sequence:
MAQERPSCAVEPEHVQRLLLSSREAKKSAYCPYSRFPVGAALLTGDGRIFSGCNIENACYPLGVCAERTAIQKAISEGYKDFRAIAISSDLQEEFISPCGACRQVMREFGTDWAVYMTKPDGTFVVRTVQELLPASFGPEDLQKIQ
Protein: Chronophin (EC 3.1.3.16) (EC 3.1.3.74) (Pyridoxal phosphate phosphatase) (PLP phosphatase) (Q96GD0)
Organism: Homo sapiens (Human)
Function: Functions as a pyridoxal phosphate (PLP) phosphatase, which also catalyzes the dephosphorylation of pyridoxine 5'-phosphate (PNP) and pyridoxamine 5'-phosphate (PMP), with order of substrate preference PLP > PNP > PMP and therefore plays a role in vitamin B6 metabolism. Also functions as a protein serine phosphatase that specifically dephosphorylates 'Ser-3' in proteins of the actin-depolymerizing factor (ADF)/cofilin family like CFL1 and DSTN. Thereby, regulates cofilin-dependent actin cytoskeleton reorganization, being required for normal progress through mitosis and normal cytokinesis. Does not dephosphorylate phosphothreonines in LIMK1. Does not dephosphorylate peptides containing phosphotyrosine.
Subcellular location: Cytoplasm, cytosol {ECO:0000269|PubMed:15580268}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:15580268}. Cell projection, ruffle membrane {ECO:0000269|PubMed:15580268}; Peripheral membrane protein {ECO:0000269|PubMed:15580268}; Cytoplasmic side {ECO:0000269|PubMed:15580268}. Cell projection, lamellipodium membrane {ECO:0000269|PubMed:15580268}; Peripheral membrane protein {ECO:0000269|PubMed:15580268}; Cytoplasmic side {ECO:0000269|PubMed:15580268}. Cell membrane {ECO:0000269|PubMed:15580268}; Peripheral membrane protein {ECO:0000269|PubMed:15580268}; Cytoplasmic side {ECO:0000269|PubMed:15580268}. Note=Colocalizes with the actin cytoskeleton in membrane ruffles and lamellipodia. Diffusely distributed throughout the cytosol during pro-metaphase and metaphase. Detected at the dynamic cell poles during telophase. Detected at the cleavage furrow and contractile ring during cytokinesis. Transiently detected at the plasma membrane in late stages of cytokinesis. Detected at the midbody. {ECO:0000269|PubMed:15580268}.
Interaction partners:
- Pyridoxal kinase
- Pyridoxine-5'-phosphate oxidase
- Aldehyde oxidase
- Pyridoxal phosphate phosphatase PHOSPHO2
- Cofilin-2
- Cofilin-1
- LIM domain kinase 1
Sequence:
MARCERLRGAALRDVLGRAQGVLFDCDGVLWNGERAVPGAPELLERLARAGKAALFVSNNSRRARPELALRFARLGFGGLRAEQLFSSALCAARLLRQRLPGPPDAPGAVFVLGGEGLRAELRAAGLRLAGDPSAGDGAAPRVRAVLVGYDEHFSFAKLREACAHLRDPECLLVATDRDPWHPLSDGSRTPGTGSLAAAVETASGRQALVVGKPSPYMFECITENFSIDPARTLMVGDRLETDILFGHRCGMTTVLTLTGVSRLEEAQAYLAAGQHDLVPHYYVESIADLTEGLED