wanglab/gogpt-training-data huggingface dataset:
Protein: Zinc finger FYVE domain-containing protein 26 (F6NK88)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
- SPG11 vesicle-trafficking-associated, spatacsin.
- AP-5 complex subunit zeta-1
- Spastin
- Tectonin beta-propeller repeat-containing 2
- WASH complex subunit 5
- Atlastin-1
- Receptor expression-enhancing protein.
- Maspardin
- E3 ubiquitin-protein ligase TRIP12
Sequence:
MHPFGREEETSRRELFGFFRRCLQRGEWELAAACVSQLGEARAEDPHSPRDIVKAIVTHPYPLRWETVGSPHRLAWYWLQVLERPTEIKVSVSVKRELEFLLLLEELEDIPQSVLKELHEAFLYSEEVKGKAPGDSASPLSAALLSCLRSLLTRQQPRLCHSLISFLSNGDPSRDHTLQDAFIQHLTEQVKVPAKDRNREWVEQVCSVLALAPWGSDRSGAQLEPLWEGLWAAREGLMTEERILGCLLRPQSQALLMAYSSTALRLLKDKLLAEAPHTQVDLPDLERVMLGLCCHKDKRLAWKAIYFECLSSGKHFLEQVLLTGLDLIKREEFSKLETLLHSEFQPLSRLLLLLGWMHCQSLESAKTLLTVLHHRQPQSNDSALSDLACTLSCQLGVLEWCTQNNPGISHDALLSHLHMLDHHSALYVLHCLTPLAKFEEHKVLELLQRTGDPSQVDSPSSSVQRNITLFRGFCAMKYALYAISVNARTHAHTGSLDCEPLHELQTEAAQEDETAEGCSNLFQHYLSECQLYLEAVPALFRLELLENIFSLLFLSDSDFTQQTSTATETQPYTNTETSKPKSTKEVNTAEHFLKAENEGERMDELNQINPQLGHLTSGCRGFLVDLNVMEGILRLVREGLEGVCGVGQEDGRALGADVELAESLGCSVTAETFSARLQRLSKYTAEAQWRLQIVTSNHGNGNDGLYLPSPLPSPALPLKRQGSGSSGTSSRRRRKHHRHRSERHVSSERQNGEVSTSTSDGGVCVSVVCRGTETCPCGGSHSWLVPAMLSPPESLLIACIRRGNYIEAQQVIAMYGLENSECAGELVFMDRYREVLIELAQVEQKIESQSLSTSSSSSEGLGTLGATPAGRTRMGSSSRLTLKSIGSAAAAGMAFYSISDVADRLMSTPSRPIPCLEDSYWLSQCTIDSPDFVRPLVEELSPAAMAAFDLSCCQCQLWKTSRQLLETAERRLSSFLEARGVRVDPKVPHANGIRGFPSVLQQISKILNKTSTNKGMSKTDCNGEENAVCSPFGCSAQEVLLSCHSTLTEESITIQQNLNQRLEVTLQTLSSATNTSVDSLVGSNLLTALAEQAALKQSELDCHPVRTAMKQLLQYLDQLCPLVPDGAPDRPDYIRSFFDYVNVLASVLVRSLGSEDQSTVVKLGNPLLLLLQSPAQLLSHLLFDRQVSPDRVLSLLQQERLRLSVQQVVVQRCCETLPLWDSRAVNFSQRVSGLNGGAFCPASIASILQQYAQDCSPSLDLSDPTTTSDPSSESEVSVEDVSAASTSLSTSPPSPSSSSPSSSFLLTPSALSFLKSRSPLVAALACLSASRGGVTRVTSSGWSGLPSYFRGSGRKEAVLDGEQISREGEALLKNFPILRMYLRTMAEPVLGVSLEADEGLGVALCGKPVVGMLFSGLQGNAAQAMAAEAFQQALNNGDLNRALDLLELYAQPCSQEGALRDKLLAFTALQESSSAEQLFRVRDWELRGRVVLQGLDRWPLQQCLDLLHFCLSDQNTKDPLREQLQQRKQELDMYQRMLRLQPSLPWETWQELREESTKNPESVFSQMLEAREFELCAQWVQLYSVSDQSGMQLQTEHLLYLLEHNHTEEAFQLLEALSDSMGLEVSERALDRRPGLAACHFLSDYLTLHFQSQMTPARRRHIHALHLGSKVLLTLPEASRQDYFSLLSDPLLMLEQMLMNLKVDWAAVAITTLRSLLLAQDAGITTQHIDTLLADYARKALDFPYAPREWSRSDSVISLQDAFLQCPAQESCPSSPSHTPPPSTGGTPMQTPSSERRPSGKKIRPLATPFTPPEKTPDRKDWIPDHKQHICMVCQRERFTMFNRRHHCRRCGRLVCHSCSSKKMAVAGFDEPVRVCDQCYNFFHTDSDEELEQGEVAGSPSSIDEVLNGVLSLPEVSRKQYRLSPNPAENQQLKSEFYYEQAPSASLCVAILTLHSDHAACGQQLIDHCRSLSRKLTNPEVDARLLTDVMRQLLFSAKLMFVNAGCTQEPALCDSYISKVDVLKILVTANYKYIPSLDDIQETAAVTRLRNQLLELEYYQLAVEVSTKSALDPNGVWQAWAMASLKAGNLSGAREKFVRCLKAPVDRNQLNHGPRLLQEIIQHLESTVKLTLSQTMDEDILASLRELEEALSDSAPPEGTESKVQRCNFHQECLFYLFTYGTHLSLISFYLRHDCLKDALTYLQNKGCSDDVFLEGIFQPCLERGRLGALQGLLENLDPTLETWGRYLLSACQLLQRRGHYHSLYQLQQFMMDHIRAAMTCIRFFSHGAQSYLQLGEQQRWLIRAKEHLRTYLQEQQSRRKSHSSSFRKKMSSTDVSRHIHTIELQLEVTRFLHRCESSPSKTAVGSTYTGNSAPPTLFGNSPMKVDVACKVMLGGKNIEEGFGIAYRVIQDFQLEALAVYIRVGQRLVRQRQYSSVRQLHKCVGESGTASKHDCDAIVLSCVSVADKSPADAKELETLILECKNPENKIKAYLQCSKLRAAYLQAVKLKLVKATPLIQEVMRAAESSGDSVMHDICRQWLSEHQEPSSKQR
Protein: Meiotic drive suppressor wtf18 (A0A482ARE1)
Organism: Schizosaccharomyces kambucha (Fission yeast)
Function: Acts as a suppressor component of the dual wtf meiotic drive system, and can suppress but not confer meiotic drive by compatible poisons. Wtf meiotic drive systems promote unequal transmission of alleles from the parental zygote to progeny spores by encoding a poison and an antidote from the same locus; the poison is trans-acting and forms toxic aggregates in all spores within an ascus, wherease the antidote is spore-specific and targets aggregates for degradation by the vacuole (By similarity). Meiotic drive by wtf systems therefore lead to poisoning of all progeny that do not inherit the dual poison/antidote allele, or express a compatible antidote (By similarity).
Subcellular location: Spore membrane {ECO:0000250|UniProtKB:A0A218N034, ECO:0000255}; Multi-pass membrane protein {ECO:0000255}. Vacuole membrane {ECO:0000250|UniProtKB:A0A218N034, ECO:0000255}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
Sequence:
MKNNYTSLKSPLDEEDELKTDHEIDLEKGLLPEYNSEEEGTLPLYSDISKLANPVPEDSSTGPTEIANPNVERRQEFKDSHPNIYFLLRLLISVLAVSVVFFTAWVCVNPLEKSIFGKVAFSVTIGITCPILFIATFCFFETWTQAVAQCIKVTVIFLAQCVKVTVIFLAQCVKVTAVFLAKCVKVIAVGLYNSKKDLVVTIWLAWVVICFILFGCVKDGRLNLNKALICSTCSISAALFFILLLVCIPIWTLKHMLFGLFQVLGVQSCVVIVTKGLMYLFDKHIDATGYEIEASSLFVIGNFLFFYEMERPGALKRMPKFIGNGIASFLGGLGNAFGGIGNAIGRIGNAFRGANDNNDIPLGEMDVESEV
Protein: Aminoacyl-histidine dipeptidase (A8BS90)
Organism: Giardia intestinalis (strain ATCC 50803 / WB clone C6) (Giardia lamblia)
Interaction partners:
- Xaa-Pro dipeptidase
- Glutamate--cysteine ligase
- Furin/Protein converstase 2
- Cathepsin B
- Dipeptidyl peptidase 3
- Proteasome subunit beta
- Aspartate aminotransferase
Sequence:
MLDANRAVLDTILRSFREAENVWETFFKICEVPHGSYNQEQIIPFYTSFFDNLKTSISGLTYSVDGLKNIIVRVPATPGYERVPGICLQGHSDMVCVKTADSSHDFKKDPLMLRVVQKDGKEWLMATGTTLGADNSIGVAIGIAILLECAKDKTFLHGPLELFITSDEEVGLLGAAGMEENCLTSKYLLNLDSEDFGEICVSCAGGFRVTFTHTIKRVDAGTDPYYKLHLSKLSGGHSGCDIHLYRANTIKLMARLVSKIPGARLCALSGGSAHNAIPGSCQAVITCRSDITPAHIAKIWDEIYIAYKPTDPHAVLSVEKHTQQIKPLSQADSDKILNFITVIPHGPIRFSPTVENFVETSFAATIVKLTEGETEFSLLGSGRSSIESELDGVYERLKALASLAGFSISEQQSRYPGWPANMESVFLKQAIESHETLIGFKPHVGAVHAGLEAGLICKKCPGMDAISIGPTIKNPHSPQEALEISTVAPIYRLTRAIVSELAAKYK
Protein: SnoRNA-binding rRNA-processing protein (Q5A852)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Subcellular location: Nucleus, nucleolus {ECO:0000256|ARBA:ARBA00004604}.
Interaction partners:
- U3 small nucleolar ribonucleoprotein protein IMP4
- SnoRNA-binding rRNA-processing protein
- RNA cytidine acetyltransferase
- rRNA-processing endoribonuclease
- rRNA-processing protein
- Nan1p
- SnoRNA-binding rRNA-processing protein
- Nucleolar protein 56
- Ribosome biosynthesis protein
- Nucleolar protein 58
Sequence:
MKSDFKFSNLLGTVYRKGNLVFNQDGTKLLSPVGNRVSCFDLIKSQSFTFDYQHRKNVQCIALNNQNTLMISIDEDGRAILVNFVSRVVLHHFNFKSKVNDIKFSPCGKYFAIAIDRFIQVWKTPDLTEDRQFAPFVRHRIYSGHFDEVLNISWSLDSRFFISTSKDMTAKIFSLNSDEKDVAMTFSGHRDYVINAFFSHDQEIIYTVSKDGALFKWEYTERPKPENEDSDSEDDATDKPMSWRITAKNFFYADGKLKCACFHPQSKLLVVGFTNGEFRLYEIEDFNLIQSLSMGQNAVNTVNINKTGEWLAFGSAKLGQLLVYEWQSESYILKQQGHFDSMNTLCYSPDGSRLVTGSDDGKIKIWDVRSGFCLMTFTEHTSAVTQVQFAKRGQVLFSSSLDGTIRAWDLIRFRNFKTFTATSRVQFNCLAVDPSGEVIVGGSQDTFEIYVWSVQTGQLLDSLTGHEGPISCLTFGKENSILASASWDKTIRIWNIFSRNQTVEPIEIQSDALCLTMRPDCKELAVSTLDGHVTIFDIEDAKQLHLIDGRKDIVNGRYLEDKFIAKNSNRGKYFSTIAYSFDGLTLLAAGNNNSICMYDIENEVLLKRFIVSENMSLDGTLQFLNSSKITDAGTNSDLIDRAGELSDLEDRVDNSLPGSHRGGDPSERRTRPEVRVTAVEFSPTTAAFAAASTEGLLIFSINQELIFDPFDLDVDVTPEATLESLKEKEYLVALVMAFRLNENYLIHRVIESIPLQDIKLVCQDLPVIYVNRVLNFIGELLTKKESPHIEYYLIMVKNLLIQHGRYISSNKFEFQSSMKLLSRFLNKTAKDVINVGKRNDHLLTYLTVSKDLKTASGHSEGEENIEMNEDSEAEDIDIDEDDDDEEGWLGPNGNSVKAANGIVFSGPADSSDEEDEDELIEV
Protein: Monothiol glutaredoxin-S5 (AtGrxS5) (Protein ROXY 12) (O23420)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: May only reduce GSH-thiol disulfides, but not protein disulfides.
Subcellular location: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
Interaction partners:
Sequence:
MENLQKMISEKSVVIFSKNSCCMSHTIKTLFLDFGVNPTIYELDEINIGREIEQALAQLGCSPTVPVVFIGGQLVGGANQVMSLHLNRSLVPMLKRAGALWL
Protein: Nuclear protein 1 (Protein p8) (O54842)
Organism: Rattus norvegicus (Rat)
Function: Transcription regulator that converts stress signals into a program of gene expression that empowers cells with resistance to the stress induced by a change in their microenvironment. Thereby participates in regulation of many process namely cell-cycle, apoptosis, autophagy and DNA repair responses. Controls cell cycle progression and protects cells from genotoxic stress induced by doxorubicin through the complex formation with TP53 and EP300 that binds CDKN1A promoter leading to transcriptional induction of CDKN1A (By similarity). Protects pancreatic cancer cells from stress-induced cell death by binding the RELB promoter and activating its transcription, leading to IER3 transactivation (By similarity). Negatively regulates apoptosis through interaction with PTMA (By similarity). Inhibits autophagy-induced apoptosis in cardiac cells through FOXO3 interaction, inducing cytoplasmic translocation of FOXO3 thereby preventing the FOXO3 association with the pro-autophagic BNIP3 promoter. Inhibits cell growth and facilitates programmed cell death by apoptosis after adriamycin-induced DNA damage through transactivation of TP53 (By similarity). Regulates methamphetamine-induced apoptosis and autophagy through DDIT3-mediated endoplasmic reticulum stress pathway. Participates in DNA repair following gamma-irradiation by facilitating DNA access of the transcription machinery through interaction with MSL1 leading to inhibition of histone H4' Lys-16' acetylation (H4K16ac) (By similarity). Coactivator of PAX2 transcription factor activity, both by recruiting the EP300 cofactor to increase PAX2 transcription factor activity and by binding PAXIP1 to suppress PAXIP1-induced inhibition on PAX2 (By similarity). Positively regulates cell cycle progression through interaction with COPS5 inducing cytoplasmic translocation of CDKN1B leading to the CDKN1B degradation (By similarity). Coordinates, through its interaction with EP300, the assiociation of MYOD1, EP300 and DDX5 to the MYOG promoter, leading to inhibition of cell-cycle progression and myogenic differentiation promotion (By similarity). Negatively regulates beta cell proliferation via inhibition of cell-cycle regulatory genes expression through the suppression of their promoter activities (By similarity). Also required for LHB expression and ovarian maturation (By similarity). Exacerbates CNS inflammation and demyelination upon cuprizone treatment (By similarity).
Subcellular location: Nucleus {ECO:0000250|UniProtKB:O60356}. Cytoplasm {ECO:0000250|UniProtKB:O60356}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:O60356}.
Interaction partners:
- Tumor protein p53-inducible nuclear protein 1
Sequence:
MATLPPTAHTSQQPVNIEDEDGILDEYDQYSLAQSYVVGGGRKGRTKREAAANTNRPSPGGHERKLLTKFQNSERKKAWR
Protein: E3 ubiquitin-protein ligase BRE1-like 1 (AtBRE1) (EC 2.3.2.27) (Protein HISTONE MONOUBIQUITINATION 1) (AtHUB1) (Protein REDUCED DORMANCY 4) (RING-type E3 ubiquitin transferase BRE1-like 1) (Q8RXD6)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: E3 ubiquitin-protein ligase that monoubiquitinates H2B to form H2BK143ub1. H2BK143ub1 gives a specific tag for epigenetic transcriptional activation and is also prerequisite for H3K4me and maybe H3K79me. It thereby plays a central role in histone code and gene regulation. Forms a ubiquitin ligase complex in cooperation with the E2 enzyme UBC2/RAD6. Required for the regulation of flowering time and defense against necrotrophic fungal pathogens. Involved in the control of seed dormancy and germination.
Subcellular location: Nucleus {ECO:0000269|PubMed:17329563, ECO:0000269|PubMed:19286969}.
Interaction partners:
- Ubiquitin-conjugating enzyme E2 1
- Ubiquitin-conjugating enzyme E2 2
- Ubiquitin-conjugating enzyme E2 3
- Histone H2B.6
- Histone H2B.5
- Histone H2B.4
- Histone H2B.8
- Histone H2B.7
- Histone H2B.9
- Histone H2B.2
Sequence:
MASTGEPDRKRRHFSSISPSEAAAAVKKQPFFWPSSEDKLDTAVLQFQNLKLSQKLEAQQVECSILEDKLSQIKEKQLPYNSSLKTVHKSWEKLTASVESCSVRVSDSSSGAHRFVNKEDGSSPAVKNDFINRLLETGATESSSSNICSNQMEENGVNTSSQMTQTLYNLVAATEDLRCLKDELYPTVLRTNLGKDLCGQLALSELESEIKSFRGDLDDVLVKFKSLSRELQSHRDADAKVRVDLKRIRGELEDEVVELQQCNGDLSALRAERDATAGAFFPVLSLGNKLATSDRERDKQRDLQDMETVLKELTVLASGRLQQLKNLHEERTKMLGKMSNLQNKSKSVRCISSSQACLSLKDQLEKSKEAVFQYMALLEKLQVEKDSIVWKEREINIKNELGDVSRKTSAVTDSRMASLDSEIQKQLDEKMRIKTRLGNISRERGRKEIFADMKALISSFPEEMSSMRSQLNNYKETAGGIHSLRADVQSLSGVLCRKTKEYEALQLRSADYASQLGDLNATVCDLKNSHEELKLFLDMYKRESTDARDIAEAKEQEYRAWAHVQSLKSSLDEQNLELRVKAANEAEAVSQQMLAAAEAEIADLRQKMDDCKRDVAKHSDILKSKHEEHGTYLSEIQTIGSAYEDIVPQNQQLLLQVTERDDYNIKLFLEGITSRQMQDTLLIDKYIMDKDIQQGSAYASFLSKKSSRIEDQLRFCTDQFQKLAEDKYQKSVSLENLQKKRADIGNGLEQARSRLEESHSKVEQSRLDYGALELELEIERFNRRRIEEEMEIAKKKVSRLRSLIEGSSAIQKLRQELSEFKEILKCKACNDRPKEVVITKCYHLFCNPCVQKLTGTRQKKCPTCSASFGPNDIKPIYI
Protein: Ribonuclease III domain-containing protein RNC1, chloroplastic (Chloroplast ribonuclease III domain protein) (A6YSL1)
Organism: Zea mays (Maize)
Function: Binds specific group II introns in chloroplasts and facilitates their splicing. Acts on both subgroup IIA and subgroup IIB introns. The substrates of the subgroup II also require the CRM domain proteins CAF1 or CAF2. Binds both single-stranded and double-stranded RNA non-specifically, but lacks endonuclease activity. Required for plastid ribosome biogenesis.
Subcellular location: Plastid, chloroplast stroma {ECO:0000269|PubMed:17693527}.
Interaction partners:
- Protein WHAT'S THIS FACTOR 1
- CRS2-associated factor 2, chloroplastic
- CRM-domain containing factor CFM3, chloroplastic/mitochondrial
- Chloroplastic group IIA intron splicing facilitator CRS1, chloroplastic
- Chloroplast RNA splicing2
- peptidyl-tRNA hydrolase
- Tha8
- Chloroplastic group IIB intron splicing facilitator CRS2, chloroplastic
- Single-stranded DNA-binding protein WHY1, chloroplastic
Sequence:
MGPPAMAFQALTLTPLPFSLHSSSRRVRVLAVAADQTPPPAPPSEPANSPSRLLRELAQRKKAVSPKKKHPPRRFILKPPLDDERLTRRFLSSPQLSLKALPLLSSCLPSAPLSTADRTWMDEYLLEAKQALGYPLAPSETLGEGDDCPARHFDVLFYLAFQHLDPSSERTRMRHVRNGHSRLWFLGQYVLELAFCEFFLQRYPRESPGPMRERVFALIGKKVLPRWLKAASLHNLVFPYDDLDKMIRKDREPPSKAVFWAIFGAIYLCFGMPEVYRVLFEAFGMDPDDESCQPKLRRQLEDVDYVSVEFEKRQLTWQDVAAYRPPPDALFAHPRLFRACVPPGMHRFRGNIWDFDSRPKVMTTLGYPLPMNDRIPEITEARNIELGLGLQLCFLHPSKHKFEHPRFCYERLEYVGQKIQDLVMAERLLMKHLDAPGRWLAEKHRRTLMNKYCGRYLRDKHLQHYIIYGETVQDRFEHNRRLRNPSTTSVQQALHGLAYCVYGKPDVRRLMFEVFDFEQVQPKAV
Protein: Adhesion G protein-coupled receptor G3 (G-protein coupled receptor 97) (G-protein coupled receptor PGR26) (Q86Y34)
Organism: Homo sapiens (Human)
Function: Orphan receptor that regulates migration of lymphatic endothelial cells in vitro via the small GTPases RhoA and CDC42. Regulates B-cell development (By similarity). Seems to signal through G-alpha(q)-proteins.
Subcellular location: Cell membrane {ECO:0000269|PubMed:22575658}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein G
Sequence:
MATPRGLGALLLLLLLPTSGQEKPTEGPRNTCLGSNNMYDIFNLNDKALCFTKCRQSGSDSCNVENLQRYWLNYEAHLMKEGLTQKVNTPFLKALVQNLSTNTAEDFYFSLEPSQVPRQVMKDEDKPPDRVRLPKSLFRSLPGNRSVVRLAVTILDIGPGTLFKGPRLGLGDGSGVLNNRLVGLSVGQMHVTKLAEPLEIVFSHQRPPPNMTLTCVFWDVTKGTTGDWSSEGCSTEVRPEGTVCCCDHLTFFALLLRPTLDQSTVHILTRISQAGCGVSMIFLAFTIILYAFLRLSRERFKSEDAPKIHVALGGSLFLLNLAFLVNVGSGSKGSDAACWARGAVFHYFLLCAFTWMGLEAFHLYLLAVRVFNTYFGHYFLKLSLVGWGLPALMVIGTGSANSYGLYTIRDRENRTSLELCWFREGTTMYALYITVHGYFLITFLFGMVVLALVVWKIFTLSRATAVKERGKNRKKVLTLLGLSSLVGVTWGLAIFTPLGLSTVYIFALFNSLQGVFICCWFTILYLPSQSTTVSSSTARLDQAHSASQE
Protein: N-acetylglucosamine repressor (P0AF20)
Organism: Escherichia coli (strain K12)
Function: Acts as a repressor of the nagEBACD operon and acts both as an activator and a repressor for the transcription of the glmSU operon.
Interaction partners:
- N-acetylglucosamine-6-phosphate deacetylase
- Glucosamine-6-phosphate deaminase
- Ribonucleotide monophosphatase NagD
- PTS system N-acetylglucosamine-specific EIICBA component
- HTH-type transcriptional regulator ChbR
- HTH-type transcriptional repressor NanR
Sequence:
MTPGGQAQIGNVDLVKQLNSAAVYRLIDQYGPISRIQIAEQSQLAPASVTKITRQLIERGLIKEVDQQASTGGRRAISIVTETRNFHAIGVRLGRHDATITLFDLSSKVLAEEHYPLPERTQQTLEHALLNAIAQFIDSYQRKLRELIAISVILPGLVDPDSGKIHYMPHIQVENWGLVEALEERFKVTCFVGHDIRSLALAEHYFGASQDCEDSILVRVHRGTGAGIISNGRIFIGRNGNVGEIGHIQVEPLGERCHCGNFGCLETIAANAAIEQRVLNLLKQGYQSRVPLDDCTIKTICKAANKGDSLASEVIEYVGRHLGKTIAIAINLFNPQKIVIAGEITEADKVLLPAIESCINTQALKAFRTNLPVVRSELDHRSAIGAFALVKRAMLNGILLQHLLEN
Protein: Nucleoporin (Q57XP4)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MFAFLPPAKAARTERSPLGSTELGCDVSQLTTPSVTAVSPFPVGQVRPVTIAEADIRVGGVSVRPSIFLSGIGTNSCWMVDENTRLLRVWDMRKPFWHRTAPRVAHIPFFTESEGLPLFVTELGPNDESIAFCTDYGVVSSLDHSVEFQVSTENEPVKVSAFACRREQQATLTAVGTLSGAIFVAIKIDGERFVISFERTSCNVSVRTSTSSSGGSWWSSFLPKRLLSTDSRESNNDEADGSRLEFTLLRFRGEHPTQLWAVNAASEFFLLDIGPLRRRRPKNNGSAEGGIRAKWITNISSVLQRRGRVVAFDETPLSLCCLVYLFSCSRWDASLEVVTMEPSTGAVRRVVSMQSIALLAHSVASAPLHHTKIYLDESSHMITILSGQCCVFLNNDLGVRNPCSSEDVHMLRNVEFPIVSALLPDGHIVTMGINGPVVSNTRADELLHEAAEDSREAADDRGSRGSGIRQNSDAWKQSRFTGGRDGLNDVTRLLNNLLDSLRIDCKMSIDSAVLDAGEAICLYSTPHKGNWARADLNIEDDNIIMHVTHSVVQRQQEHRRFLLTVLLHKEIALRLQPQTIARLLSMQEALLVMVAIRRLQNDTTHCSSSATTTVEGFEVMTPLYQLASAGSNNINSSLLAANLSQNGDSCSVEDYRRLVRSAVERERCQLLLRRAINCVADQARSELSSANSMCAQATSAEIVFGDPSRLSQLLQVLCDNLHETQGSVLIDRRSKFDDALSVASVFVLVARAIDESREDIESLCPIPQNVRALMWTSSDASDYGIQLHLSSAAKCFSDALAGSLMWSKSEMETMSAPADPLSEKMNTSELSSWLVPVQDQLRLLDFIAVIIHFTFRNHSEGGPTFFASAMRSTLFREPFLIEPLGYPFGAPVPTETTVGACVLRLCEELALDFVVDDVVSAFCLAEPVENPLQPSGKYDRLGLYCERNPKIFEVALRTLLTQRREWELQLLPELLPQYEAGAVARDEFLAKEAPQLLWLMRPQAFYSLVEEGARLPSSSSASYFLYGDDLVTHRSRCLALSRLAWVASGSGNSSSYYGLELDTAVVAAQKRFLMPDTKNVVLGPAELVQRLLQLPSPDAWMSATGVVCLVEEELRKDLLTQIARRAKQHDGEVLLQIKREGTSELEVARALEVTAIGRILLAATGRGEGCATATAKACAGIFDNAEQQLLMSWLRARSAGLVS
Protein: Endoplasmic reticulum chaperone BiP (EC 3.6.4.10) (Immunoglobulin heavy chain-binding protein homolog) (A0A1D8PG96)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Interaction partners:
- protein disulfide-isomerase
- Hsp70 family chaperone
- non-specific serine/threonine protein kinase
- Hsp70 chaperone Ssb
- Derlin
- Nucleoporin
- Nucleoporin NSP1
- Protein-transporting protein
- Nucleotide exchange factor SIL1
- Calnexin
Sequence:
MRSSQSSWLPRIGLLYVALVILIPFLVSPKHAFAVAAVSDDESSTDNYGTVIGIDLGTTYSCVGVMKNGKVEILANDQGNRITPSYVSFNGDERLVGDAAKNQASSNVNNTVFDIKRLIGLKYNDDTVQKELKHLPYKIENKGNKPVVKVEYQGEEKTFSPEEISSMVLGKMKSIAEDYLGKKVTHAVVTVPAYFNDAQRQATKDAGTIAGLNVLRIVNEPTAAAIAYGLDKGDQEKQIIVYDLGGGTFDVSLLSIEGGVFEVLATAGDTHLGGEDFDFKIVRYLAKQFKKKHNIDITANAKAISKLKREAEKAKRTLSSQMSTRVEIDSFVDGIDFSETLSRAKFEELNIAAFRKTLKPVEQVLKDGGVKKSDIDDIVLVGGSTRIPKVQELLEGFFDGKKASKGINPDEAVAYGAAVQAGVLSGEEGVDDIVLLDVNPLTLGIETSGGVMTTLIKRNTAIPTKKSQIFSTAADNQPTVLIQVYEGERTMAKDNNRLGKFELTGIPPAPRGVPQIEVTFSLDANGILKVEAADKGTGKSESITITNEKGRLSKDEIDRMVEEAEKYAQQDQELKEKIEARNSLENYAHVLRGQLSDTSETGLGSKLDDDDKETLDDAIKETLEFIEDNFDTATAEEFEEQKQKLIDVANPITAKLYGGAAGEGAGGAGDAKFGDDDSDDEFDHDEL
Protein: Histone H1.9 (H1.9 linker histone) (Spermatid-specific linker histone H1-like protein) (TISP64) (Q9QYL0)
Organism: Mus musculus (Mouse)
Function: DNA-binding protein that may be implicated in chromatin remodeling and/or transcriptional regulation during spermiogenesis, the process of spermatid maturation into spermatozoa.
Subcellular location: Nucleus {ECO:0000269|PubMed:12920187, ECO:0000269|PubMed:14636221}. Chromosome {ECO:0000269|PubMed:12920187, ECO:0000269|PubMed:14636221}.
Interaction partners:
- Testis-specific H1 histone
- Histone H1.8
- H1 histone family, member X
- Transmembrane protein 190
- Histone H2A
- Histone H2A-like 1
Sequence:
MAQMVAGDQDAGTLWVPSQSESQTESDISTQSLRKPTMSYVILKTLADKRVHNCVSLATLKKAVSITGYNMTHNTWRFKRVLQNLLDKGMIMHVTCCKGASGSLCLCKERALKSNHRAKRCQDRQKSQKPQKPGQRESEPCQLLLSSKKKNDQLFKGVRRVAKGNRHCHY
Protein: Ubiquitin-ribosomal protein eS31 fusion protein (Ubiquitin carboxyl extension protein 80) [Cleaved into: Ubiquitin; Small ribosomal subunit protein eS31 (40S ribosomal protein S27a)] (P79781)
Organism: Gallus gallus (Chicken)
Function: Ubiquitin Exists either covalently attached to another protein, or free (unanchored). When covalently bound, it is conjugated to target proteins via an isopeptide bond either as a monomer (monoubiquitin), a polymer linked via different Lys residues of the ubiquitin (polyubiquitin chains) or a linear polymer linked via the initiator Met of the ubiquitin (linear polyubiquitin chains). Polyubiquitin chains, when attached to a target protein, have different functions depending on the Lys residue of the ubiquitin that is linked: Lys-6-linked may be involved in DNA repair; Lys-11-linked is involved in ERAD (endoplasmic reticulum-associated degradation) and in cell-cycle regulation; Lys-29-linked is involved in proteotoxic stress response and cell cycle; Lys-33-linked is involved in kinase modification; Lys-48-linked is involved in protein degradation via the proteasome; Lys-63-linked is involved in endocytosis, DNA-damage responses as well as in signaling processes leading to activation of the transcription factor NF-kappa-B. Linear polymer chains formed via attachment by the initiator Met lead to cell signaling. Ubiquitin is usually conjugated to Lys residues of target proteins, however, in rare cases, conjugation to Cys or Ser residues has been observed. When polyubiquitin is free (unanchored-polyubiquitin), it also has distinct roles, such as in activation of protein kinases, and in signaling (By similarity).
Subcellular location: [Ubiquitin]: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.; SUBCELLULAR LOCATION: [Small ribosomal subunit protein eS31]: Nucleus, nucleolus {ECO:0000250|UniProtKB:P62979}.
Interaction partners:
- Small ribosomal subunit protein uS2
- Ubiquitin-ribosomal protein eL40 fusion protein
- 60S ribosomal protein L6
- Ribosomal protein L36a like
- Ribosomal protein L37
- 60S ribosomal protein L29
- Small ribosomal subunit protein uS15
- Ribosomal protein S10
- Large ribosomal subunit protein uL2
- 40S ribosomal protein S30
Sequence:
MQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQQRLIFAGKQLEDGRTLSDYNIQKESTLHLVLRLRGGAKKRKKKSYTTPKKNKHKRKKVKLAVLKYYKVDENGKISRLRRECPSEECGAGVFMASHFDRHYCGKCCLTYCFNKPEDK
Protein: Protein DIA1 (Digs into agar protein 1) (P54005)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Involved in regulation of invasive growth.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:14562095}.
Interaction partners:
- Calcium/calmodulin-dependent protein kinase II
- E3 ubiquitin-protein ligase RSP5
- Uncharacterized protein YOR385W
Sequence:
MGSISRYLLKKAADGLKDEQRLKIEMSDSKSVPECFHFNRERRMPIAEINGEDGFFMFPSQQSLENFENTKKYSNELSPDAIGIPLFQIINCTLPFGKRGHSNTVVGNVPYYKIFKFILRTADEPPPYTVAKIVCSNNGLILYKVPLYDIYKNVSQANVTYSFVGTTSTEPNLLAMAHREGHRDLDTKVNNLNLRWHVTYSPVVTNDHYKLILLADYEVNRLDEDVIRAAKNKMSIDQKDQKVQRFVAAHYTREFETSLFRWVAQEGHLILGEYSTDQGSFGLNNIPPLTEELGCQSLLIHYIEYMKRQRKKIAKEARRQNKRNVANTTNMNMNLM
Protein: Putative 2-hydroxyacid dehydrogenase YGL185C (EC 1.-.-.-) (P53100)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Interaction partners:
Sequence:
MCDSPATTGKPTILFIADPCETSATLNSKAFKEKFRILRYQLDTKEAFLNFLERHEQDKICAIYAGFPAFKKIGGMTRSIIEHKSFPRKNLKCIVLCSRGYDGWDLDTLRKHEIRLYNYQDDENEKLIDDLKLHQVGNDVADCALWHILEGFRKFSYYQKLSRETGNTLTARAKAAEKSGFAFGHELGNMFAESPRGKKCLILGLGSIGKQVAYKLQYGLGMEIHYCKRSEDCTMSQNESWKFHLLDETIYAKLYQFHAIVVTLPGTPQTEHLINRKFLEHCNPGLILVNLGRGKILDLRAVSDALVTGRINHLGLDVFNKEPEIDEKIRSSDRLTSITPHLGSATKDVFEQSCELALTRILRVVSGEAASDEHFSRVV