wanglab/gogpt-training-data huggingface dataset:
Protein: RNA-binding protein 20 (RNA-binding motif protein 20) (P0DW16)
Organism: Sus scrofa (Pig)
Function: RNA-binding protein that acts as a regulator of mRNA splicing of a subset of genes encoding key structural proteins involved in cardiac development, such as TTN (Titin), CACNA1C, CAMK2D or PDLIM5/ENH. Acts as a repressor of mRNA splicing: specifically binds the 5'UCUU-3' motif that is predominantly found within intronic sequences of pre-mRNAs, leading to the exclusion of specific exons in target transcripts (By similarity). RBM20-mediated exon skipping is hormone-dependent and is essential for TTN isoform transition in both cardiac and skeletal muscles (By similarity). RBM20-mediated exon skipping of TTN provides substrates for the formation of circular RNA (circRNAs) from the TTN transcripts (By similarity). Together with RBM24, promotes the expression of short isoforms of PDLIM5/ENH in cardiomyocytes (By similarity).
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00130, ECO:0000269|PubMed:33188278}. Cytoplasm, Cytoplasmic ribonucleoprotein granule {ECO:0000269|PubMed:33188278}. Note=The active form that regulates alternative splicing localizes to the nucleus (PubMed:33188278). Also localizes to cytoplasmic ribonucleoprotein granules; localization to cytoplasmic ribonucleoprotein granules plays an important regulatory role (PubMed:33188278). Subcellular localization is regulated by phosphorylation of different parts of the protein: while phosphorylation of the RS (arginine/serine-rich) region promotes nuclear localization, phosphorylation of the C-terminal disordered region promotes localization to cytoplasmic ribonucleoprotein granules (By similarity). {ECO:0000250|UniProtKB:Q5T481, ECO:0000269|PubMed:33188278}.
Interaction partners:
Sequence:
MVLAAAMSQDAEPSGPEQPDRDARSVPGAPAPPAPPGPRGMQPPPPPPPPPPPPPQAGLPQIIQNAAKLLDKTPFSVSNPNPLLPSPASLQLAQLQAQLTLHRLKLAQTAVTNNTAAATVLNQVLSKVAMSQPLFNQLRHPSMISAPHGHTGVPPHATTVPSTRFPSNAITFSAGQTRGPGPSVNLPSQPPNTMVMHPFSGVMPQTPAQPAVILGIGKTGPAPAAAGFYEYGKATSGQAYGSETDSQPSFLPASASTSGSVTYEGHYSHSGQDSQAAFPKDFYGPTSQGSQVAGTFAADTAGGLKGEVGPLLQGPNSQWESPHGFSGQSKPDLTAAPNLWPPHPSQPYELYDPEEPTPDRTPPSLGGRLNHSKQGFSGARRRAKEEQAVLSMRPLQVQELNDFHGVAPLHLPHICSICDKKVFDLKDWELHVKGKLHAQKCLLFSENTGVRCVLGPAEGTLCASPNSTAVYNPAGNEDYASNLGTSYAALPARTFTQSNPAFPSASPGMNFVQRKLGAGRVVHICNLPEGSCTENDVINLGLPFGKVTNYILMKSTNQAFLEMAYTEAAQAMVQYYQEKSAMINGEKLLIRMSKRYKELQLKKPGKTVAAIIQDIHSQRERDMFREADRYGPERPRSRSPVSRSLSPRSHTPSFTSCSSSHSPPGPSRADWGNGRDSWEHSPYARREEERGPAPWRENGEDKRDRTDMWAHDRKHYPRQVDKTELDERLEGGRGYREKHPRSGSPSSLHSVSGYKSREDGYYRKEPKGKSDKYLKQQQEAPGRSRRKDEARLRDGRHPYPDDSGKEDGLEAKGTKSKQSEKNRTKRPDRDQEGADDRKESRMAESEAGKEEQDSMEESPSSVGRQEKETESSDAENTRTRKEQDSESGSEAEGESWYPTNMEELVTVDEVGEEEDFIMEPDIPELEEIVPIDQKDKICPEICPCVTTTLELDLAQDFTKEGVKTIGNGATEISLKSPKEPPSASTSCPSDMDVEMPGLNLDAERKPAECETGLSLEGSGCYEQQAKGAESSDVCLAPMLEQMSSPKPAEERAWQPGPFLDDGKVGGTPEDGAAEGRPLEEKASTPTETDLQSQACQGVSTQENSGYVEMKSLDARSPEYTEVELKQPLSLPSWEPEDVFSELSIPLGVEFVVPRTGFYCKLCGLFYTSEEMAKMSHCRSAVHYRNLQKYLSQLAEEGLKETEGAGSPRPEDSGIVPHFERKKL
Protein: Sodium-independent neutral amino acid transporter LAT1 (Q96QB2)
Organism: Homo sapiens (Human)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004651}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}.
Interaction partners:
Sequence:
MAGAGPKRRALAAPVAEEKEEAREKMLASKRADGAAPAGEGEGVTLQRNITLLNGVAIIVGAIIGSGIFVTPTGVLKEAGSPGLALVMWAACGVFSIVGALCYAELGTTISKSGGDYAYMLDVYGSLPAFLKLWIELLVIRPSSQYIVALVFATYLLKPLFPSCPVPEEAAKLMACHCVLLLTAVNCYSVKAATRVQDAFAAAKLLALALIILLGFVQIGKGDVSNLDPNFSFEGTKLDVGNIVLALYSGLFAYGGWNYLNFVTEEMINPYRNLPLAIIISLPIVTLVYVLTNLAYFTTLSTEQMLSSEAVAVDFGNYHLGVMSWIIPVFVGLSCFGSVNGSLFTSSRLFFVGSREGHLPSILSMIHPQLLTPVPSLVFTCVMTLLYAFSKDIFSVINFFSFFNWLCVALAIIGMIWLRHRKPELERPIKVNLALPVFFILACLFLIAVSFWKTPVECGIGFTIILSGLPVYFFGVWWKNKPKWLLQGIFSTTVLCQKLMQVVPQET
Protein: Magphinin-beta 2 (Q99PH7)
Organism: Mus musculus (Mouse)
Interaction partners:
Sequence:
MDRRNDHGHRVPTFQGPLPPAGSLGLPFSPDVQSETTEKDPPIASRSKKNKNKKNSIKPMDKTTPAPPPVPSANDNASNKPKVTLQALNLPMFTQISQASATTEAPNIQASVTSQTQKAKTMRVTPKVSLTGSEDATTQLKPPLQALNLPVTTPTIQTPVANESANSLASTAVNKSKKASTANNAANKTVPSAAEISLASAATHTATTQGQAAKETGSIQTIAATARSKKNSKGKRTPAKTTNTDNEYVEASNAIEASSRQIGASGRQTEASNRQIEASSRQTEASNRQTEASSRQTEASSRQTETSNRQIGASNRQIMASNRQIGASNRQIEASNRQIGASNRQTEVSSRQIEASNRQIGASNRQTEASNRQIGASNRQTEASNRQIGASNRQTDASNRQTEASSRQTEASSRQTEASSRQTEASSRQIEASAAAVRPKKPRGKKGNNKGSNSASEPSEAPPAIQTVTNHALSVTVRIRRGSRARKAANKNRATESQAQIAEQGAQASEASISALETQVAAAVQALADDYLAQLSLEPTTRTRGKRNRKSKHPNGEERTGNNYRRIPWGRRLPPPRDVAILQERANKLVKYLLVKDQTKIPIKRSDMLKDVIQEYEDYFPEIIERASYALEKMFRVNLKEIDKQNNLYILISTQESSAGIMGTTKDTPKLGLLMVILSVIFMNGNKASEAVIWEVLRKLGLHPGVKHSLFGEVKKLITDEFVKQKYLEYKRVPNSRPPEYEFFWGLRSYHETSKMKVLKFACKVQKKDPKDWAAQYREAVEMDIQAAAVAVAEAKARAEACSPCLQITLTATILPMEPMCSFGIVVHAAA
Protein: V-type proton ATPase subunit D (V-ATPase subunit D) (Vacuolar H(+)-ATPase subunit D) (Vacuolar proton pump subunit D) (Q9XGM1)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Subunit of the peripheral V1 complex of vacuolar ATPase. V-ATPase is responsible for acidifying a variety of intracellular compartments in eukaryotic cells, thus providing most of the energy required for transport processes in the vacuolar system (By similarity).
Subcellular location: Vacuole membrane {ECO:0000269|PubMed:17151019}; Peripheral membrane protein {ECO:0000305}.
Interaction partners:
- V-type proton ATPase subunit B1
- Vacuolar ATP synthase catalytic subunit-related / V-ATPase-related / vacuolar proton pump-like protein
- V-type proton ATPase subunit H
- V-type proton ATPase subunit F
- V-type proton ATPase subunit d2
- V-type proton ATPase catalytic subunit A
- V-type proton ATPase subunit C
- V-type proton ATPase subunit d1
- V-type proton ATPase subunit B2
- V-type proton ATPase subunit G1
Sequence:
MAGQNARLNVVPTVTMLGVMKARLVGATRGHALLKKKSDALTVQFRALLKKIVTAKESMGDMMKTSSFALTEVKYVAGDNVKHVVLENVKEATLKVRSRTENIAGVKLPKFDHFSEGETKNDLTGLARGGQQVRACRVAYVKAIEVLVELASLQTSFLTLDEAIKTTNRRVNALENVVKPKLENTISYIKGELDELEREDFFRLKKIQGYKRREVERQAANAKEFAEEMVLEDISMQRGISINAARNFLVGGAEKDSDIIF
Protein: Latent membrane protein 1 (Protein p63) (A8CSJ8)
Organism: Epstein-Barr virus (strain GD1) (HHV-4) (Human gammaherpesvirus 4)
Subcellular location: Host cell membrane {ECO:0000256|ARBA:ARBA00004598}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004598}.
Interaction partners:
Sequence:
MERDLERGPPGPPRPPLGPPLSSSIGLALLLLLLALLFWLYIVMSNWTGGALLVLYSFALMLIIIILIIFIFRRDLLCPLGGLGLLLLMITLLLIALWNLHGQALYLGIVLFIFGCLLVIGLWIYFLEILWRLGATIWQLLAFILAFFLAIILLIIALYLQQNWWTLLVDLLWLLLFMAILIWMYYHGPRHTDEHHHDDSLPHPQQATDDSSHESDSNSNDGRHHLLVSGAGDGPPLCSQNLGAPGGGPDNGPQDPDNTDDNGPQDPDNTDDNGPQDPDNTDDNGPQDPDNTDDNGPQDPDNTDDNGPQDPDNTDDNGPQDPDNTDDNGPHDPLPHNPSDSAGNDGGPPNLTEEVENKGGDWDPPSMTDGGGGDPHLPTLLLGTSGSGGDDDDPHGPVQLSYYD
Protein: 4-alpha-glucanotransferase (EC 2.4.1.25) (Amylomaltase) (Disproportionating enzyme) (D-enzyme) (P15977)
Organism: Escherichia coli (strain K12)
Subcellular location: Cytoplasm.
Interaction partners:
- Glycogen debranching enzyme
- Maltodextrin phosphorylase
- 1,4-alpha-glucan branching enzyme GlgB
- Glycogen phosphorylase
- Glycogen synthase
- Glucose-1-phosphate adenylyltransferase
- Maltodextrin glucosidase
- Periplasmic alpha-amylase
- Phosphoglucomutase
- Cytoplasmic alpha-amylase
Sequence:
MESKRLDNAALAAGISPNYINAHGKPQSISAETKRRLLDAMHQRTATKVAVTPVPNVMVYTSGKKMPMVVEGSGEYSWLLTTEEGTQYKGHVTGGKAFNLPTKLPEGYHTLTLTQDDQRAHCRVIVAPKRCYEPQALLNKQKLWGACVQLYTLRSEKNWGIGDFGDLKAMLVDVAKRGGSFIGLNPIHALYPANPESASPYSPSSRRWLNVIYIDVNAVEDFHLSEEAQAWWQLPTTQQTLQQARDADWVDYSTVTALKMTALRMAWKGFAQRDDEQMAAFRQFVAEQGDSLFWQAAFDALHAQQVKEDEMRWGWPAWPEMYQNVDSPEVRQFCEEHRDDVDFYLWLQWLAYSQFAACWEISQGYEMPIGLYRDLAVGVAEGGAETWCDRELYCLKASVGAPPDILGPLGQNWGLPPMDPHIITARAYEPFIELLRANMQNCGALRIDHVMSMLRLWWIPYGETADQGAYVHYPVDDLLSILALESKRHRCMVIGEDLGTVPVEIVGKLRSSGVYSYKVLYFENDHEKTFRAPKAYPEQSMAVAATHDLPTLRGYWECGDLTLGKTLGLYPDEVVLRGLYQDRELAKQGLLDALHKYGCLPKRAGHKASLMSMTPTLNRGLQRYIADSNSALLGLQPEDWLDMAEPVNIPGTSYQYKNWRRKLSATLESMFADDGVNKLLKDLDRRRRAAAKKK
Protein: Transcription factor COE2 (Early B-cell factor 2) (EBF-2) (Q9HAK2)
Organism: Homo sapiens (Human)
Function: Transcription factor that, in osteoblasts, activates the decoy receptor for RANKL, TNFRSF11B, which in turn regulates osteoclast differentiation. Acts in synergy with the Wnt-responsive LEF1/CTNNB1 pathway. Recognizes variations of the palindromic sequence 5'-ATTCCCNNGGGAATT-3' (By similarity).
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- Zinc finger protein 423
- Protein O-mannosyl-transferase TMTC1
- Histone-lysine N-methyltransferase PRDM16
- Peroxisome proliferator-activated receptor gamma
Sequence:
MFGIQDTLGRGPTLKEKSLGAEMDSVRSWVRNVGVVDANVAAQSGVALSRAHFEKQPPSNLRKSNFFHFVLALYDRQGQPVEIERTAFVDFVENDKEQGNEKTNNGTHYKLQLLYSNGVRTEQDLYVRLIDSVTKQPIAYEGQNKNPEMCRVLLTHEVMCSRCCEKKSCGNRNETPSDPVIIDRFFLKFFLKCNQNCLKTAGNPRDMRRFQVVLSTTVNVDGHVLAVSDNMFVHNNSKHGRRARRLDPSEATPCIKAISPSEGWTTGGAMVIIIGDNFFDGLQVVFGTMLVWSELITPHAIRVQTPPRHIPGVVEVTLSYKSKQFCKGAPGRFIYTALNEPTIDYGFQRLQKVIPRHPGDPERLAKEMLLKRAADLVEALYGTPHNNQDIILKRAADIAEALYSVPRNPSQLPALSSSPAHSGMMGINSYGSQLGVSISESTQGNNQGYIRNTSSISPRGYSSSSTPQQSNYSTSSNSMNGYSNVPMANLGVPGSPGFLNGSPTGSPYGIMSSSPTVGSSSTSSILPFSSSVFPAVKQKSAFAPVIRPQGSPSPACSSGNGNGFRAMTGLVVPPM
Protein: Transcriptional activator VP30 (Minor nucleoprotein VP30) (P35258)
Organism: Lake Victoria marburgvirus (strain Musoke-80) (MARV) (Marburg virus (strain Kenya/Musoke/1980))
Function: Acts as a transcription anti-termination factor immediately after transcription initiation, but does not affect transcription elongation. This function has been found to be dependent on the formation of an RNA secondary structure at the transcription start site of the first gene (By similarity).
Subcellular location: Virion. Host cytoplasm {ECO:0000250}. Note=Tightly bound in the nucleocapsid.
Interaction partners:
Sequence:
MQQPRGRSRTRNHQVTPTIYHETQLPSKPHYTNYHPRARSMSSTRSSAESSPTNHIPRARPPSTFNLSKPPPPPKDMCRNMKIGLPCADPTCNRDHDLDNLTNRELLLLMARKMLPNTDKTFRSPQDCGSPSLSKGLSKDKQEQTKDVLTLENLGHILSYLHRSEIGKLDETSLRAALSLTCAGIRKTNRSLINTMTELHMNHENLPQDQNGVIKQTYTGIHLDKGGQFEAALWQGWDKRSISLFVQAALYVMNNIPCESSISVQASYDHFILPQSQGKGQ
Protein: Dedicator of cytokinesis protein 1 (180 kDa protein downstream of CRK) (DOCK180) (Q8BUR4)
Organism: Mus musculus (Mouse)
Function: Involved in cytoskeletal rearrangements required for phagocytosis of apoptotic cells and cell motility. Along with DOCK1, mediates CRK/CRKL regulation of epithelial and endothelial cell spreading and migration on type IV collagen. Functions as a guanine nucleotide exchange factor (GEF), which activates Rac Rho small GTPases by exchanging bound GDP for free GTP. Its GEF activity may be enhanced by ELMO1.
Subcellular location: Cytoplasm {ECO:0000250}. Membrane {ECO:0000250}. Note=Recruited to membranes via its interaction with phosphatidylinositol 3,4,5-trisphosphate. {ECO:0000250}.
Interaction partners:
- Engulfment and cell motility protein 2
- Engulfment and cell motility protein 1
- Adapter molecule crk
- Breast cancer anti-estrogen resistance protein 1
- Rho-related GTP-binding protein RhoG
- Crk-like protein
- Engulfment and cell motility protein 3
- Focal adhesion kinase 1
- Ras-related C3 botulinum toxin substrate 2
- Ras-related C3 botulinum toxin substrate 3
Sequence:
MTRWVPTKREEKYGVAFYNYDARGADELSLQIGDTVHILETYEGWYRGYTLRKKSKKGIFPASYIHLKEAIVEGKGQHETVIPGDLPLIQEVTTTLREWSTIWRQLYVQDNREMFRSVRHMIYDLIEWRSQILSGTLPQDELKELKKKVTAKIDYGNRILDLDLVVRDEDGNILDPELTSTISLFRAHEVASKQVEERLQEEKSQKQNMDINRQAKFAATPSLALFVNLKNVVCKIGEDAEVLMSLYDPMESKFISENYLVRWSSSGLPKDIDRLHNLRAVFTDLGSKDLKREKISFVCQIVRVGRMELRDSNTRKLTSGLRRPFGVAVMDVTDIINGKVDDEDKQHFIPFQAVAGENDFLQTVINKVIAAKEVNHKGQGLWVTLKLLPGDIHQIRKEFPHLVDRTTAVARKTGFPEIIMPGDVRNDIYVTLVQGDFDKGSKTTAKNVEVTVSVYDEDGKRLEHVIFPGAGDEAISEYKSVIYYQVKQPRWFETLKVAIPIEDVNRSHLRFTFRHRSSQDSKDKSEKIFALAFVKLMRYDGTTLRDGEHDLIVYKAEAKKLEDAATYLSLPSTKGELEEKGHSATGKGMQSLGSCTISKDSFQISTLVCSTKLTQNVDLLGLLKWRSNTNLLQQNLRQLMKVDGGEVVKFLQDTLDALFNIMMENSESETFDTLVFDALVFIIGLIADRKFQHFNPVLETYIKKHFSATLAYTKLTKVLRTYVASAEKPGVNEQLYKAIKALEYIFKFIVRSRVLFNQLYENKGEADFVESLLQLFRSINDMMSSLSELTVRVKGAALKYLPTIVNDVKLVFDPKELSKMFTEFILNVPAGLLTVQKLSCLIEIVHSDLFTQHDCREILLPMMTDQLKYHLERQEELEACCQLLSNILEVLYRKDVGPTQRHVQIIMETLLRTVNRTVISMGRDSELIGNFVACMTAILRQMEDYHYAHLIKTFGKMRTDVVDFLMETFIMFKNLIGKNVYPFDWVIMNTMQNKVFLRAINQYADMLNKRFLDQANFELQLWNNYFHLAVAFLTQESLQLENFSSAKRAKILNKYGDMRRQIGFEIRDMWYNLGQHKIKFIPEMVGPILEMTLIPETELRKATLPIFFDMMQCEFHSTRSFQMFENEIITKLDHEVEGGRGDEQYKVLFDKILLEHCRKHKYLAKTGETFVKLVVRLMERLLDYRTIMHDENKDNRMSCTVNVLNFYKEIEREEMYIRYLYKLCDLHKECDNYTEAAYTLLLHAKLLKWSEDVCAAHLTQRDGFQATTQGQLKEQLYQEIIHYFDKGKMWEEAIALGKELAEQYETEMFDYEQLSELLKKQAQFYENIVKVIRPKPDYFAVGYYGQGFPSFLRGKVFIYRGKEYERREDFEARLLTQFPNAEKMKTTSPPGDDIKTSPGQYIQCFTVKPKLDLPPRFHRPVSEQIVSFYRVNEVQRFEYSRPIRKGEKNPDNEFANMWIERTIYTTAYKLPGILRWFEVKSVFMVEISPLENAIETMQLTNDKISSMVQQHLDDPGLPINPLSMLLNGIVDPAVMGGFANYEKAFFTDRYLQEHPEAHGQIEKLKDLIAWQIPFLAEGIRIHGDKVTEALRPFHERMEACFKQLKEKVEKQYGVRTMPSGLDDRRGSRPRSMVRSFTMPSSSRPLSVASVSSFSSDSTPSRPGSDGFALEPLLPKKMHSRSQDKLDKDDPDKEKKDKKKEKRNSKHQEIFDKEFKPADSSLQQSEAVILSETISPLRPQRPKSQVINVIGNERRFSVSPASPSSQQTPPPVTPRAKLSFSIQPSLELNGMMGMDVADVPPPLPLKGNMADYGNLMENQDMMVSPTSPPPPPPQRQQPPPLPSKTPPPPPPKTTRKQTSVDSGIVQ
Protein: Cytochrome P450, family 76, subfamily C, polypeptide 6 (Putative cytochrome P450) (Q9LQ25)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- At1g25400
- O-fucosyltransferase 20
- ABC transporter C family member 2
Sequence:
MDIISGQPLFLIFCFILSCLLFFTTARSRRSPCQLSKSPPGPPRLPIIGNIHLVGKNPHHSFTDLSKTYGPVMSLKLGCLNSVVIASRDAVREVLKTHDQILSGRYISEATKSNNHHEFSVGWIHPSSSRFRMLRKLSATQLFSPQCIQATKALRMKKVQELVNFLSESCEREEAVDISHVSFVTALNIISNILFSVNLGSYDSKNSSAFQEMVIGYQESIGNPDLANFFPFMRFLDLQGNSKKMRESSGRLLQVFREFYDARIVEKSSRSVEKDVSSKDFLDVLIDLQQGDETEINIDEIEHLLLDMFVAGTDTNSSTVEWAMAELLGNPKTMTKVQDEINHVIGQNGDFQESDISKLPYLKAVVKETFRLHPAAPFLLQRKAETNVEILGFTVLKDSQVLVNVWAIGRDPLVWENPTHFEPERFLGKEIDVKGTDYELTPFGAGRRICPGLPLAMKTVHLMLASLLYTFEWKLPNGVGSEDLDMEETFGLTVHKTNPLLAVPLKKRAIN
Protein: Intradiol ring-cleavage dioxygenases domain-containing protein (G8BJM5)
Organism: Candida parapsilosis (strain CDC 317 / ATCC MYA-4646) (Yeast) (Monilia parapsilosis)
Interaction partners:
- Phenol 2-monooxygenase
Sequence:
MPSSTKVKINDEPQINPKGPIITEMNEDTITKNAILVNSQHTNMRLLFLLQKVVQHLHDFAIETRLTTEEWEVAIQFLTDTGKMCSDIRQEYVLLSDILGLSVLVDAISHPKPPNATIGTLLGPFHTHDAEEKHQGDSISSEGRGEPLLIEGLLTEPDGTPIPDASIDLWHCDNKGMYDTQYANRDHPDMRGIIKTKEDGSFVIKCSRPVPYPIPHDGPVGKLLQKINRHPYRPSHIHFIIEKPGYDRLITALYAKGDPYETSDVVFGVKDSLLYTLDKLGTEKAKKYDMNPDDWYLKWHFKIISEEEAKKLRYEKNKEALTRAAANLVLNSDGVPEHCPLD
Protein: Cell-cycle checkpoint serine-threonine kinase (Eurofung) (C8V3Z7)
Organism: Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Interaction partners:
- DNA damage and replication checkpoint protein Rfx1, putative
- non-specific serine/threonine protein kinase
- Serine/threonine-protein kinase tel1
- Transcriptional corepressor
- Protein kinase domain-containing protein
- M-phase inducer phosphatase
- non-specific serine/threonine protein kinase
- DNA damage checkpoint effector kinase
- DNA replication checkpoint mediator MRC1 domain-containing protein
- G1/S regulator
Sequence:
MVPRNEQSSLKRSRVTADHESQDQKKPRRSERISSQQQSQTPVIQSYLPTPLTHHDSTATDLRNEMTATPPSQALPRSPSDLGSPPGDTQALSQFVYPPRAFADDVEDEAAEGVWGYLIPLDDKVRDALVLRKRDGCDAKPTKERSSKERKSRESSTKHAANRRPGGYLIGRHPECDLSLNIPTVSNRHFLVFPENRRGDTVAILEDLSSNGTFINDAIVGRNKHRELEDGDEVTVLDEVRFVFRAPRTKNISGFRQQYRVLQQLGKGHFATVYLCVERTTGAKFAVKVFEKRADSKSQNDALMQEIGLLMSVSHPNLLCLKDTFDESDGVYLVLELAPEGELFNMIIRKQKFTEKETRHIFRQLFEGLKYLHDRGIVHRDIKPENILVADNKLTVKLGDFGLAKIIGEDSFTTTLCGTPSYVAPEILQESRRRKYTKAVDIWSLGVVLYICLCGFPPFSDELYTPENPYTLAQQIKLGRFDYPSPYWDSVGDPALDLIDRMLTVDVDKRITVDECLQHPWLTGELPSVTDSTDGLTGALGNLDFSKRKIARERTLLSGINDVRSSQQKTGDGASVKVYHKNIAGQRMHNQRATRQHEFPNKNSGPKDFVNLGECGDPVLFEEEPTSRHN
Protein: Peroxisome biogenesis factor 10 (EC 2.3.2.27) (PER10) (Peroxin-10) (Peroxisomal biogenesis factor 10) (AtPEX10) (AthPEX10) (Peroxisome assembly protein 10) (Pex10p) (Q9SYU4)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: E3 ubiquitin-protein ligase component of a retrotranslocation channel required for peroxisome organization by mediating export of the PEX5 receptor from peroxisomes to the cytosol, thereby promoting PEX5 recycling. The retrotranslocation channel is composed of PEX2, PEX10 and PEX12; each subunit contributing transmembrane segments that coassemble into an open channel that specifically allows the passage of PEX5 through the peroxisomal membrane (By similarity). PEX10 also regulates PEX5 recycling by acting as a E3 ubiquitin-protein ligase. When PEX5 recycling is compromised, PEX10 catalyzes polyubiquitination of PEX5 during its passage through the retrotranslocation channel, leading to its degradation (By similarity).
Subcellular location: Peroxisome membrane {ECO:0000269|PubMed:14576288, ECO:0000269|PubMed:16169966}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Peroxisome biogenesis protein 12
- Peroxisome biogenesis protein 5
- Peroxisomal membrane protein PEX14
- Peroxisome biogenesis protein 7
- Peroxisomal ATPase PEX6
- Peroxisome biogenesis protein 19-1
- Peroxisome biogenesis protein 19-2
- Pollen-specific leucine-rich repeat extensin-like protein 1
- Pollen-specific leucine-rich repeat extensin-like protein 2
- Peroxisome biogenesis protein 16
Sequence:
MRLNGDSGPGQDEPGSSGFHGGIRRFPLAAQPEIMRAAEKDDQYASFIHEACRDAFRHLFGTRIALAYQKEMKLLGQMLYYVLTTGSGQQTLGEEYCDIIQVAGPYGLSPTPARRALFILYQTAVPYIAERISTRAATQAVTFDESDEFFGDSHIHSPRMIDLPSSSQVETSTSVVSRLNDRLMRSWHRAIQRWPVVLPVAREVLQLVLRANLMLFYFEGFYYHISKRASGVRYVFIGKQLNQRPRYQILGVFLLIQLCILAAEGLRRSNLSSITSSIQQASIGSYQTSGGRGLPVLNEEGNLITSEAEKGNWSTSDSTSTEAVGKCTLCLSTRQHPTATPCGHVFCWSCIMEWCNEKQECPLCRTPNTHSSLVCLYHSDF
Protein: Phospholipid-transporting ATPase (EC 7.6.2.1) (Q7JPE3)
Organism: Caenorhabditis elegans
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141, ECO:0000256|RuleBase:RU362033}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141, ECO:0000256|RuleBase:RU362033}.
Interaction partners:
Sequence:
MTTPRPTHLHRRSSSKWVPPSAPLHNPISIFRGRSNRETGSRVIRPNHLFESPRYELNNYRDFTDNRISTTKYTFWNFIPLNIWHQVSTKYANLYFIFIAILNWVPFFDAYTRYVGLIPICFVLGTTLIKDGIEDYRRYKFDNQINKKTCHVWDRDRCAFRKTEWRYILVGDFVHISNNQDVPADIILLRSSSESGTCYIETCNLDGETSLKQRMVPAKVIDYSKKDSTFKPPDFTGVVTCEKPDKSIYTIRAKVEFEPGQSDVIIKENMLLRGSRIKNTTFVEGIVVYAGHDTKVMQNNGRAPHKTSGIEKLTNKFIIACFIMLLLMVLYGAITSAVWVGQHPVDEQIPFILSNTPRPFIEGFIGIGAFFINYQLLVPISLYITVEIIKALQIYFISNDIQLYDQKSDRAIDCRSLSIPEELGTVTHVLSDKTGTLTENMMIFRNCAFDETDYGSNGSQSNPDKPVKSDELYQRILTSMQNPVQKHFFANILLNNSVVVNHIPHTDVLELGNFDGGVYNIGNSCFYDVTEEKYKQKLAAIGKGGVDDDDVSRPDELGLPTTSIQFDDRLTVIVEEDTPSDSPAPDASPRDLPETPTPTSPIYRPLSSLSSFSRKLSTVVRRSILRPISDIIPVRKRLISFKQQAMNPYEAESPDELALIEGAALYDYVLLERAATSVTISTPEKAEKRYEILLTLPFDATRKRMSVIVNSQKGPLMYCKGADSAIISRLSSDSLESKRVQDLKDHLDNYAKKGLRTLCFAMKYISKEDFEDFLDSYRFLMEDATSEREKMLSEKADELETNLKLSGVTGIEDRLQDGVPDTLRALRDAGIQVWVLTGDKLETAQNIATSSGLFHPQRSLKVIETETDAEEASESAGLNIIMSPAAIRLAQDGNAHLMEALKKAKTVLCYRMTPSEKATIVNTVKKRIKGNVLAIGDGANDVPMIQAAHVGIGIAGKEGLQAAMACDFAIARFKFLSRLLLVHGHWSYYRLANTFLYFLYKNANAVFIIFYYQFYNGASGTNIVDPIWGVIYPIIFTSVQPVVVGVLDQDYDDQTLMNKPELYVIGRENQLYTWKHFFRDVIDGIYQAAVIYYVAYLTLDNSTSSLWEMGFYIATSSILVNSGHLALQVRYWHWQLVALFSFFILFNFAFFFAECLTAAAAMVPDPPVWMPIHAMGDPRFWYYQFITVIVALCPRFTSMCLMSSLKSETSKR
Protein: Homeobox protein PKNOX1.1 (Homeodomain transcription factor Prep1) (Pbx/knotted 1 homeobox 1.1) (Pbx/knotted-1 homeobox Prep1.1) (Q90VY7)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Nucleus {ECO:0000256|PROSITE-ProRule:PRU00108}.
Interaction partners:
- Homeobox protein Hox-B2a
- Homeobox protein Hox-B1a
- Pbxy homeodomain protein
- Homeobox protein Hox-A2b
Sequence:
MMAAQSVSIDKYPEGDQQMQVMEQSENDLKKGFSNGNTGNTSSPVSNEPQTQMDIDKACIYRHPLFPLLALLFEKCEQSTLGSDCVTSASFDVDIENFVRSQEKDGKAFFSEDPDLDNLMVKAIQVLRIHLLELEKVSDLCKDFCSRYISCLKAKMNSETLLSGDPGSPYSPVHDQLSNPFSGPLSPQSLLIPSSGLQQGSVTVTTVNSSQVATGNTVYQPVTVVTPQGQVVTQAISPGALHIQNSQLQLQLNQDLSFFGGDDSSPKNKRGVLPKQATNVMRSWLFQHIAHPYPTEEEKKQIATQTNLTLLQVNNWFINARRRILQPMLDANSTEASKSKKKVAQSRPLHRFWSDSIASTGSQQQLTMPDGSLVTVGMNVDGFQALSSDGATLAMQQVLMGNHSEDETDESGNEDDTDMSTANMPGLGLDVSD
Protein: Uncharacterized protein (Q57YB5)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Uncharacterized protein
- Uncharacterized protein
- Uncharacterized protein
- Uncharacterized protein
- Uncharacterized protein
- Uncharacterized protein
- Uncharacterized protein
- Uncharacterized protein
- Ubiquitin-like domain-containing protein
- Manganese/iron superoxide dismutase C-terminal domain-containing protein
Sequence:
MFRVRRLAGFIQCSPCGKMGPLKQQTRRYTPIWKSDPAVDNVAPLRDEDERRTLWAEVGPISDVGSAVTAWIRFGNDPVLHTAVPTMLGGKFRNQQREKESLLPNSSSPFAYVEDYMGTNLVFGSPVHAKESAAVWATYFERRYASRLRLSRRTVANYVGLINSPEVFDDESDRPETRWSQDTFFRECAYLSEKFLKEKVSNMQQFEAALKRASPEAYLAFFDAFQQQTQTQIPLPSPSVWHYEGERRKQWAEKFISISHKAQAFFKDVLSEDVKKYQEVPGKLLQKVKPVLADVGKILVKRHERWLKGRVWTSLTEEEREAYCMKEVKRQQMQVEDGEFDPMMEDDVDDTELEEWQREHDAIMELMNSPIDGLHFTTLELWLHAMRCEELETEHIYTSARVRAVQVAARKKLYDTTSYEEVIQAVVESIARGTLDLGAGVLRPHFNEVWCQLNYAKFGSSTITQHTTTSRRQLLFFHAGSLKDIAATATLYYATKPLSNSLDYASPYKYRRSLITLCSNYGVETAYTTQRPLLRSAANLARAEDLIHAVVTAAAQPFGERRRAATRDLHMEFQRLAVPVERVIVANPVSALLESGADPDEKPVEGEKVNMWPLGAKRVVLYKWSAPNVEKLKAMESDAAPAVSGSSLTAERLREIQELKRRGFLEVSLWRRVTAQERKQRNEIVEAKKKQVEEVVRTVPSLAHLHQYATSLYSRIEERVAFPTETSTVTDTTNMKEETNKPLEDSEWEFAVLLDDRVLLNKEESVELYLPYRDANGELLAQGEYRALVRAFDLEANPNLHPAYCSVGYSESFHVFDALPQLIAQFFRVKDATAEAAGVTHIPAADFTPFCAFLRDAGLDVPLRCEFEAGQAVTTDGDVYMDYFLQLLRGEAFHQSHAQAGLTEAQRAIEPLCRAHWVVHHPGADESEWATARRSVLDHAMQHEREWWFPNEMLDVKDVVTGSTNGLTPQMYPAAVRYGVELCTVLTAEGKFVDERGSGLSARCVVNGTGAAESVVFDTANCNGTNTTSVEDALRVAHGALRSAQDRHNTLAAFRLGPLSKQSQVLLFCGVNAYEFGGKYARTYAYAFEKAKKELEVTAASGFMAPSLSHEDIERLSDQPTTSPSVDRFASTTHPEQRKAQFVPRVGPGSTPLEDPAADQKSEWS
Protein: Clathrin light chain 3 (F4J5M9)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Clathrin is the major protein of the polyhedral coat of coated pits and vesicles.
Subcellular location: Cytoplasmic vesicle membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Membrane, coated pit {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Note=Cytoplasmic face of coated pits and vesicles. {ECO:0000250}.
Interaction partners:
- Clathrin heavy chain 1
- AP-1 complex subunit sigma-2
- AP-2 complex subunit sigma
- AP-1 complex subunit sigma-1
- AP-1 complex subunit mu-2
- At5g57460
- Phragmoplastin DRP1C
- Exocyst complex component EXO84B
- LanC-like protein GCL2
- Style cell-cycle inhibitor 1
Sequence:
MSSTLSNEESGLGDSNRSTEVDGGDGGNFTAYESRFQSQRFDSSFSNFDSQPEKESDLPCGDSSPRPETQSPPSINSFDDTNDSILPPPSAMEKEEGFALREWRRLNALRLEEKEKEEKEMVQQILEAAEQYKAEFYSKRNVTIENNKKLNREKEKFFLENQEKFYAEADKNNWKAIAELIPREVPVIENRGNKKKTATITVIQGPKPGKPTDLSRMRQVLTKLKHNPPTHMKPKLPSPSGADPNVSVSEQVTVTEKL