wanglab/gogpt-training-data huggingface dataset:
Protein: F-box/TPR repeat protein pof3 (O74991)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Has a role in substrate recognition in the Skp1-Cullin-1/Cdc53-F-box (SCF) ubiquitin ligase complex. Required for the maintenance of telomere length and transcriptional silencing at the telomere. Also required for chromosome segregation.
Subcellular location: Mitochondrion. Nucleus.
Interaction partners:
- Minichromosome loss protein 1
- Suppressor of kinetochore protein 1
- Mating-type switching protein swi1
- Swi1-interacting protein swi3
- CENP-A multicopy suppressor protein 2
- Cell division control protein 45 homolog
- F-box protein pof15
- DNA replication complex GINS protein sld5
- DNA replication licensing factor mcm2
- DNA replication licensing factor mcm7
Sequence:
MNNYQVKAIKEKTQQYLSKRKFEDALTFITKTIEQEPNPTIDLFELRAQVYEKSGQYSQAELDAKRMIHLNARNARGYLRLGKLLQLDGFDKKADQLYTQGLRMVHKMDPLRPVLKKVSQRLNERILRTRPVLDLFRILPREVLLCILQQLNFKSIVQCMQVCKHWRDCIKKEPSLFCCLDFSCASPRSVNSRDRNVMAVARYSVYSKDNIQEVIGLEKLGILTPTKALLRSVKSLKVYKTISPLHTQSTDKLYTIWTPFSELHYFYCATPITFSIASKILSCCKKLKQVELVDLIPDLIFDSMDWDKLFNAESVPLALKSLTFIRNQKFPFHHKEQQFLKDLLSASPYLEYLEASYQSDLVAAIKKYKINLRSLIIIDEGVSNTVKDLAFLPQSLTTLIVKPCNPASTILCPYLFPTNVRMESLINLELFLYLRLSQNDIDNVVKFLTSCYKLKKLVLHDSLALAPHFFEIFASLPELEHLEIPDNVALQNKHAIHITDCCPNLKYVNFSNSISLDGSGFIAVLRGLKELKRIDIINCDSVSRDAIDWARSKGMQVTVASSLPNSQPLGTKKIRLI
Protein: GH04034p (Q8MRQ8)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MNEWENQQIRKGVTAAQLVHSQHETVLSRFMIKPAPSGIGTGMDDGDSTAAQSTSTLLEQAYAKNALERTNLAAAVRSSVKTKKEKAKATALRTPQEILAAIQSRLSELKERSADHSASMARISTELKALKLQQLECQQNAPTAAAKYKFYQEIKCYVNDLVDCLSEKAPVIYDLEKRALQQYGKNQRYLVNRRRQDVRDQAKEIAESAKPITAASRRTPDYEEQVRRAAEREGRRTRRRCERERNDLLSSHLDGMSSDDEIADQQQELSVTTMAQIESQSVDALEDVTDDFSKIELILMKFFAWRKTDMSSYQDAFVSLCLPKVLAPLVRHELVLWSPLLDVYADIENMRWYQACMLYASQADETVEQLKIDPDINLVPALIEKIVLPKVTALVTECWDPLSTTQTLRLVGFINRLGREFPLSGTNKQLNKLFESIMERMRLALENDVFIPIFPKQVQEAKTSFFQRQFCSGLKLFRNFLSWQGILADKLLRELAIGALLNRYLLLAMRVCTPNDAINKAYIIVNTLPTVWLLPNSETLKNMELFIGYIKQTLENCDASNPIFMQSSDKAKQILQRLHSL
Protein: Proteasome subunit beta (Q9NHX7)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cytoplasm {ECO:0000256|RuleBase:RU004203}. Nucleus {ECO:0000256|RuleBase:RU004203}.
Interaction partners:
Sequence:
MALAEICKISNAPYMRPNAWSSADVEEEQKGLMCNLANPYTLAAPPFENPLHNLNEIQANGDKTGVKINFDHGTTTLGFKFKGGVLLAVDSRATGGSYIGSQSMKKIVEINQFMLGTLAGGAADCVYWDRVLSKECRLHELRNKERISVAAASKIMANIAHEYKGMGLSMGMMLAGYDKRGPGLYYVDSEGSRTPGNLFSVGSGSLYAYGVLDSGYHWDLEDKEAQELGRRAIYHATFRDAYSGGIIRVYHIKEDGWVNISNTDCMELHYMYQEQLKQQAAK
Protein: Thioredoxin reductase 1 (TR) (TrxR) (EC 1.8.1.9) (Thioredoxin peroxidase 1) (TPx) (Thioredoxin-dependent peroxide reductase 1) (P29509)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Central component in the thioredoxin system. Reduces thioredoxins 1 and 2.
Subcellular location: Cytoplasm. Mitochondrion intermembrane space {ECO:0000269|PubMed:22984289}.
Interaction partners:
- Thioredoxin reductase 2, mitochondrial
- Thioredoxin-1
- Thioredoxin-2
- Glutathione reductase
- Peroxiredoxin TSA1
- AP-1-like transcription factor YAP1
- Thioredoxin-3
- Transcription factor SKN7
- Cystathionine gamma-lyase
- Peroxiredoxin TSA2
Sequence:
MVHNKVTIIGSGPAAHTAAIYLARAEIKPILYEGMMANGIAAGGQLTTTTEIENFPGFPDGLTGSELMDRMREQSTKFGTEIITETVSKVDLSSKPFKLWTEFNEDAEPVTTDAIILATGASAKRMHLPGEETYWQKGISACAVCDGAVPIFRNKPLAVIGGGDSACEEAQFLTKYGSKVFMLVRKDHLRASTIMQKRAEKNEKIEILYNTVALEAKGDGKLLNALRIKNTKKNEETDLPVSGLFYAIGHTPATKIVAGQVDTDEAGYIKTVPGSSLTSVPGFFAAGDVQDSKYRQAITSAGSGCMAALDAEKYLTSLE
Protein: Mannosylfructose-phosphate phosphatase (EC 3.1.3.79) (A9CK30)
Organism: Agrobacterium fabrum (strain C58 / ATCC 33970) (Agrobacterium tumefaciens (strain C58))
Interaction partners:
- Mannosylfructose-phosphate synthase
Sequence:
MKPLRLLSTDLDGTVVGDNDATRRFRDFWHALPDDLRPVLVFNSGRLIDDQLALLEEVPLPQPDYIIGGVGTMLHAKKRSELETAYTQSLGTGFDPRKIADVMNRIAGVTMQEERYQHGLKSSWFLHDADAAALGEIEAALLAADIDARIVYSSDRDLDILPKAADKGAALAWLCGQLRIGLDESVVSGDTGNDRAMFELKTIRGVIVGNALPELVSLAHQDNRFFHSTAKEADGVIEGLRHWGLNPR
Protein: Protein Shroom4 (Second homolog of apical protein) (Q9ULL8)
Organism: Homo sapiens (Human)
Function: Probable regulator of cytoskeletal architecture that plays an important role in development. May regulate cellular and cytoskeletal architecture by modulating the spatial distribution of myosin II (By similarity).
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000269|PubMed:16249884, ECO:0000269|PubMed:16684770}. Note=Shows partial colocalization with the cytoplasmic pool of F-actin.
Interaction partners:
Sequence:
MENRPGSFQYVPVQLQGGAPWGFTLKGGLEHCEPLTVSKIEDGGKAALSQKMRTGDELVNINGTPLYGSRQEALILIKGSFRILKLIVRRRNAPVSRPHSWHVAKLLEGCPEAATTMHFPSEAFSLSWHSGCNTSDVCVQWCPLSRHCSTEKSSSIGSMESLEQPGQATYESHLLPIDQNMYPNQRDSAYSSFSASSNASDCALSLRPEEPASTDCIMQGPGPTKAPSGRPNVAETSGGSRRTNGGHLTPSSQMSSRPQEGYQSGPAKAVRGPPQPPVRRDSLQASRAQLLNGEQRRASEPVVPLPQKEKLSLEPVLPARNPNRFCCLSGHDQVTSEGHQNCEFSQPPESSQQGSEHLLMQASTKAVGSPKACDRASSVDSNPLNEASAELAKASFGRPPHLIGPTGHRHSAPEQLLASHLQHVHLDTRGSKGMELPPVQDGHQWTLSPLHSSHKGKKSPCPPTGGTHDQSSKERKTRQVDDRSLVLGHQSQSSPPHGEADGHPSEKGFLDPNRTSRAASELANQQPSASGSLVQQATDCSSTTKAASGTEAGEEGDSEPKECSRMGGRRSGGTRGRSIQNRRKSERFATNLRNEIQRRKAQLQKSKGPLSQLCDTKEPVEETQEPPESPPLTASNTSLLSSCKKPPSPRDKLFNKSMMLRARSSECLSQAPESHESRTGLEGRISPGQRPGQSSLGLNTWWKAPDPSSSDPEKAHAHCGVRGGHWRWSPEHNSQPLVAAAMEGPSNPGDNKELKASTAQAGEDAILLPFADRRKFFEESSKSLSTSHLPGLTTHSNKTFTQRPKPIDQNFQPMSSSCRELRRHPMDQSYHSADQPYHATDQSYHSMSPLQSETPTYSECFASKGLENSMCCKPLHCGDFDYHRTCSYSCSVQGALVHDPCIYCSGEICPALLKRNMMPNCYNCRCHHHQCIRCSVCYHNPQHSALEDSSLAPGNTWKPRKLTVQEFPGDKWNPITGNRKTSQSGREMAHSKTSFSWATPFHPCLENPALDLSSYRAISSLDLLGDFKHALKKSEETSVYEEGSSLASMPHPLRSRAFSESHISLAPQSTRAWGQHRRELFSKGDETQSDLLGARKKAFPPPRPPPPNWEKYRLFRAAQQQKQQQQQQKQQEEEEEEEEEEEEEEEEEEEEAEEEEEELPPQYFSSETSGSCALNPEEVLEQPQPLSFGHLEGSRQGSQSVPAEQESFALHSSDFLPPIRGHLGSQPEQAQPPCYYGIGGLWRTSGQEATESAKQEFQHFSPPSGAPGIPTSYSAYYNISVAKAELLNKLKDQPEMAEIGLGEEEVDHELAQKKIQLIESISRKLSVLREAQRGLLEDINANSALGEEVEANLKAVCKSNEFEKYHLFVGDLDKVVNLLLSLSGRLARVENALNSIDSEANQEKLVLIEKKQQLTGQLADAKELKEHVDRREKLVFGMVSRYLPQDQLQDYQHFVKMKSALIIEQRELEEKIKLGEEQLKCLRESLLLGPSNF
Protein: Glucose-6-phosphatase catalytic subunit 1 (EC 3.1.3.9) (Glucose-6-phosphatase) (G-6-Pase) (G6Pase) (Glucose-6-phosphatase alpha) (G6Pase-alpha) (P35575)
Organism: Homo sapiens (Human)
Function: Hydrolyzes glucose-6-phosphate to glucose in the endoplasmic reticulum. Forms with the glucose-6-phosphate transporter (SLC37A4/G6PT) the complex responsible for glucose production in the terminal step of glycogenolysis and gluconeogenesis. Hence, it is the key enzyme in homeostatic regulation of blood glucose levels.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000303|PubMed:9497333}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Hexokinase-4
- Glucose-6-phosphate exchanger SLC37A4
- Hexokinase-3
- Hexokinase-2
- Hexokinase HKDC1
- GDH/6PGL endoplasmic bifunctional protein
- Glucose-6-phosphate 1-dehydrogenase
- Hexokinase-1
- Phosphoenolpyruvate carboxykinase, cytosolic
- Glucose-6-phosphate isomerase
Sequence:
MEEGMNVLHDFGIQSTHYLQVNYQDSQDWFILVSVIADLRNAFYVLFPIWFHLQEAVGIKLLWVAVIGDWLNLVFKWILFGQRPYWWVLDTDYYSNTSVPLIKQFPVTCETGPGSPSGHAMGTAGVYYVMVTSTLSIFQGKIKPTYRFRCLNVILWLGFWAVQLNVCLSRIYLAAHFPHQVVAGVLSGIAVAETFSHIHSIYNASLKKYFLITFFLFSFAIGFYLLLKGLGVDLLWTLEKAQRWCEQPEWVHIDTTPFASLLKNLGTLFGLGLALNSSMYRESCKGKLSKWLPFRLSSIVASLVLLHVFDSLKPPSQVELVFYVLSFCKSAVVPLASVSVIPYCLAQVLGQPHKKSL
Protein: 5'-3' exoribonuclease Rnm (EC 3.1.13.-) (3',5'-nucleotide bisphosphate phosphatase) (EC 3.1.3.97) (RNase AM) (P77766)
Organism: Escherichia coli (strain K12)
Function: Exoribonuclease that catalyzes the last steps of 5S, 16S and 23S rRNA 5'-end maturation. Removes 3 nucleotides (nt) from the 5' end of 5S, 16S and 23S rRNA precursors to generate the mature 5' ends. Precursors with longer extensions are not processed (7 nt at the 5' end of pre-23S rRNA or 66 nt at the 5'-end of 16S rRNA are not processed). 5S and 23S rRNA maturation occurs more efficiently and accurately on ribosomal particles as compared to free RNA; the enzyme overdigests free RNA but generates the correct 5'-end in ribosomes from rnm deletion strains. Efficiently catalyzes the hydrolysis of the 3'-phosphate from 3',5'-bis-phosphonucleotides as well as the successive hydrolysis of 5'-phosphomononucleotides from the 5'-end of short pieces of RNA and DNA, with no specificity toward the identity of the nucleotide base. Is more efficient at hydrolyzing RNA oligonucleotides than DNA oligonucleotides. This enzyme can also hydrolyze annealed DNA duplexes, albeit at a catalytic efficiency approximately 10-fold lower than that of the corresponding single-stranded oligonucleotides.
Interaction partners:
- Uncharacterized protein YciO
- Ribonuclease 3
- Sugar phosphatase YidA
- Ribosomal large subunit pseudouridine synthase B
- trp operon leader peptide
Sequence:
MSDTNYAVIYDLHSHTTASDGCLTPEALVHRAVEMRVGTLAITDHDTTAAIAPAREEISRSGLALNLIPGVEISTVWENHEIHIVGLNIDITHPLMCEFLAQQTERRNQRAQLIAERLEKAQIPGALEGAQRLAQGGAVTRGHFARFLVECGKASSMADVFKKYLARGKTGYVPPQWCTIEQAIDVIHHSGGKAVLAHPGRYNLSAKWLKRLVAHFAEHHGDAMEVAQCQQSPNERTQLAALARQHHLWASQGSDFHQPCPWIELGRKLWLPAGVEGVWQLWEQPQNTTEREL
Protein: E3 ubiquitin-protein ligase RNF187 (A0A1X7SBW3)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
LALPAGPAEAACALCQRAPREPVRADCGHRFCRACVVRFWAEEDGPFPCPECADDCWQRAVEPGRPPLSRRLLALEEAAAAPARDGPASEAALQLLCRADAGPLCAACRMAAGPEPPEWEPRWRKALRGKENKGSVEIMRKDLNDARDLHGQAESAAAVWKGHVMDRRKKALTDYKKLRAFFVEEEEHFLQEAEKEEGLPEDELADPTERFRSLLQAVSELEKKHRNLGLSMLLQ
Protein: Aspartate-beta-hydroxylase (A0A8I6GM10)
Organism: Rattus norvegicus (Rat)
Subcellular location: Sarcoplasmic reticulum membrane {ECO:0000256|ARBA:ARBA00004157}; Single-pass type II membrane protein {ECO:0000256|ARBA:ARBA00004157}.
Interaction partners:
Sequence:
ASPRPTGSPGGGRWNWAGLLLFVCDSCFCTSSLSLTFPNIAKHGGHKNGRRGGISGGSFFTWFMVIALLGVWTSVAVVWFDLVDYEEVLGKLGVYDADGDGDFDVDDAKVLLGLKERSTSERTFPPEEAETQAELEEQAPEGAEAQNVEDEVKEQIQSLLQESVHTDHDLEADGPAGEPQSEVEDFLTATDSDDRFEALEPGTQNNGTDKKQIKWKFSLSLSLSLSLSLSLLSVKKKKPKLLNKFDKTIKAELDAAEKLRKRGKIEEAVSAFEELVRRYPQSPRARYGKAQCEDDLAEKQRSNEVLRRAIETYQEAASLPDAPTDLVKLSLKRRSERQQFLGHMRGSLLTLQRLVQLFPSDTTLKNDLGVGYLLMGDNDSAKKVYEEVLNVTPNDGFAKVHYGFILKAQNRIAESIPYLKEGIESGDPGTDDGRFYFHLGDAMQRVGNKEAYKWYELGHKRGHFASVWQRSLYNVNGLKAQPWWTPRETGYTELVKSLERNWKLIRDEGLMVMDKAKGLFLPEDENLREKGDWSQFTLWQQGRKNENACKGAPKTCTLLEKFSETTGCRRGQIKYSIMHPGTHVWPHTGPTNCRLRMHLGLVIPKEGCKIRCANETRSWEEGKVLIFDDSFEHEVWQDASSFRLIFIVDVWHPELTPQQRRSLPAI
Protein: Embryonic growth/differentiation factor 1 (GDF-1) (P20863)
Organism: Mus musculus (Mouse)
Function: May mediate cell differentiation events during embryonic development.
Subcellular location: Secreted.
Interaction partners:
- Activin receptor type-1C
- Activin receptor type-2B
- Activin receptor type-2A
- Activin receptor type-1B
- Nodal
- Ceramide synthase 2
- Ceramide synthase 4
- Ceramide synthase 5
- Ceramide synthase 3
- Ceramide synthase 6
Sequence:
MLPVCHRFCDHLLLLLLLPSTTLAPAPASMGPAAALLQVLGLPEAPRSVPTHRPVPPVMWRLFRRRDPQEARVGRPLRPCHVEELGVAGNIVRHIPDSGLSSRPAQPARTSGLCPEWTVVFDLSNVEPTERPTRARLELRLEAESEDTGGWELSVALWADAEHPGPELLRVPAPPGVLLRADLLGTAVAANASVPCTVRLALSLHPGATAACGRLAEASLLLVTLDPRLCPLPRLRRHTEPRVEVGPVGTCRTRRLHVSFREVGWHRWVIAPRGFLANFCQGTCALPETLRGPGGPPALNHAVLRALMHAAAPTPGAGSPCCVPERLSPISVLFFDNSDNVVLRHYEDMVVDECGCR
Protein: Membrane associated guanylate kinase, WW and PDZ domain containing 1 (H7C4U7)
Organism: Homo sapiens (Human)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004170}; Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004170}.
Interaction partners:
Sequence:
AGGSLGTGRRRQRLPATGGTTRSPREGEVPGVDYNFLTVKEFLDLEQSGTLLEVGTYEGNYYGTPKPPSQPVSGKVITTDALHSLQSGSKQSTPKRTKSYNDMQNAGIVHAENEEEDDVPEMNSSFTADSGEQEEHTLQETALPPVNSSIIAAPITDPSQKFPQYLPLSAEDNLGPLPENWEMAYTENGEVYFIDHNTKTTSWLDPRCLNKQQKPLEECEDDEGVHTEELDSELELPAGWEKIEDPVYGIYYVDHINRKTQYENPVLEAKRKKQLEQQQQQQQQQQQQQQQQQQQQTEEWTEDHSALVPPVIPNHPPSNPEPAREVPLQGKPFFTRNPSELKGKFIHTKLRKSSRGFGFTVVGGDEPDEFLQIKSLVLDGPAALDGKMETGDVIVSVNDTCVLGHTHAQVVKIFQSIPIGASVDLELCRGYPLPFDPDDPNTSLVTSVAILDKEPIIVNGQETYDSPASHSSKTGKVNGMKDARPSSPADVASNSSHGYPNDTVSLASSIATQPELITVHIVKGPMGFGFTIADSPGGGGQRVKQIVDSPRCRGLKEGDLIVEVNKKNVQALTHNQVVDMLVECPKGSEVTLLVQRGGLPVPKKSPKSQPLERKDSQNSSQHSVSSHRSLHTASPSHSTQVLPEFPPAEAQAPDQTDSSGQKKPDPFKIWAQSRSMYENRPMSPSPASGLSKGEREREINSTNFGECPIPDYQEQDIFLWRKETGFGFRILGGNEPGEPIYIGHIVPLGAADTDGRLRSGDELICVDGTPVIGKSHQLVVQLMQQAAKQGHVNLTVRRKVVFAVPKTENEVPSPASSHHSSNQPASLTEEKRTPQGSQNSLNTVSSGSGSTSGIGSGGGGGSGVVSTVVQPYDVEIRRGENEGFGFVIVSSVSRPEAGTTFAGNACVAMPHKIGRIIEGSPADRCGKLKVGDRILAVNGCSITNKSHSDIVNLIKEAGNTVTLRIIPGDESSNATLLTNAEKIATITTTHTPSQQGTQETRNTTKPKQESQFEFKAPQATQEQDFYTVELERGAKGFGFSLRGGREYNMDLYVLRLAEDGPAERCGKMRIGDEILEINGETTKNMKHSRAIELIKNGGRRVRLFLKRGDGSVPEYGGSNYENIPSFPGMTP
Protein: NADPH-dependent 1-acyldihydroxyacetone phosphate reductase (ADR) (EC 1.1.1.101) (1-acyl DHAP reductase) (Acyl/alkyl DHAP reductase) (Acylglycerone-phosphate reductase) (Triacylglycerol lipase AYR1) (TAG lipase) (EC 3.1.1.3) (P40471)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Can convert acyl and alkyl dihydroxyacetone-phosphate (DHAP) into glycerolipids and ether lipids, respectively. Required for the biosynthesis of phosphatidic acid via the DHAP pathway, where it reduces 1-acyl DHAP to lysophosphatidic acid (LPA). Also has triacylglycerol (TAG) lipase activity. Involved in the mobilization of the non-polar storage lipids triacylglycerols (TAGs) from lipid particles by hydrolysis of TAGs. Required for spore germination. Plays a role in cell wall biogenesis, but this effect may be indirect by affecting the activities of cell wall synthesis enzymes. Lipolysis of TAG by AYR1 is essential for starvation-induced autophagy. Forms an NADPH-regulated cation-selective channel in the mitochondrial outer membrane.
Subcellular location: Lipid droplet {ECO:0000269|PubMed:10515935, ECO:0000269|PubMed:10617610, ECO:0000269|PubMed:21820081, ECO:0000269|PubMed:24868093}. Mitochondrion outer membrane {ECO:0000269|PubMed:16407407, ECO:0000269|PubMed:28916712}. Endoplasmic reticulum {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:28916712}.
Interaction partners:
- Glycerol-3-phosphate O-acyltransferase 2
- Glycerol-3-phosphate O-acyltransferase 1
- Lysophosphatidic acid:oleoyl-CoA acyltransferase 1
- Triacylglycerol lipase 5
- Lysophospholipid acyltransferase
- Triacylglycerol lipase 4
- 1-acyl-sn-glycerol-3-phosphate acyltransferase
- Double-strand break repair protein MRE11
- Triacylglycerol lipase 3
- Very long-chain fatty acid transport protein
Sequence:
MSELQSQPKKIAVVTGASGGIGYEVTKELARNGYLVYACARRLEPMAQLAIQFGNDSIKPYKLDISKPEEIVTFSGFLRANLPDGKLDLLYNNAGQSCTFPALDATDAAVEQCFKVNVFGHINMCRELSEFLIKAKGTIVFTGSLAGVVSFPFGSIYSASKAAIHQYARGLHLEMKPFNVRVINAITGGVATDIADKRPLPETSIYNFPEGREAFNSRKTMAKDNKPMPADAYAKQLVKDILSTSDPVDVYRGTFANIMRFVMIFVPYWLLEKGLSKKFKLDKVNNALKSKQKNKDD
Protein: GTP-binding protein YPT31/YPT8 (Rab GTPase YPT31) (P38555)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Required for protein transport in the secretory pathway. Probably involved in regulation of secretory vesicle formation at the trans-Golgi compartment. Plays a role in autophagy.
Subcellular location: Golgi apparatus membrane {ECO:0000269|PubMed:9151665}; Lipid-anchor {ECO:0000269|PubMed:9151665}.
Interaction partners:
- Rab GDP-dissociation inhibitor
- Myosin-2
- Phosphatidylinositol 4-kinase PIK1
- GTP-binding protein YPT32/YPT11
- Trafficking protein particle complex II-specific subunit 130
- Rab guanine nucleotide exchange factor SEC2
- Protein transport protein YIP1
- Trafficking protein particle complex II-specific subunit 120
- Exocyst complex component SEC15
- ADP-ribosylation factor guanine nucleotide-exchange factor SEC7
Sequence:
MSSEDYGYDYDLLFKIVLIGDSGVGKSNLLSRFTKNEFNMDSKSTIGVEFATRTLEIDGKRIKAQIWDTAGQERYRAITSAYYRGAVGALIVYDISKSSSYENCNHWLSELRENADDNVAVGLIGNKSDLAHLRAVPTEESKTFAQENQLLFTETSALNSENVDKAFEELINTIYQKVSKHQMDLGDSSANGNANGASAPNGPTISLTPTPNENKKANGNNCC
Protein: Histone H2AX (H2a/x) (Histone H2A.X) (Q54WG6)
Organism: Dictyostelium discoideum (Social amoeba)
Function: Core component of nucleosome which plays a central role in DNA double strand break (DSB) repair. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling (By similarity). Phosphorylation of H2AX seems to be performed by atr1 and/or possibly dnapkcs, as ATM ortholog is absent in the genome of this organism.
Subcellular location: Nucleus {ECO:0000250}. Chromosome {ECO:0000250}.
Interaction partners:
- Histone H2B.v3
- Histone H4
- Histone H2A.z
- PWWP domain-containing protein
- Histone H3.3 type c
- Histone H3.3 type a
- ATP-dependent DNA helicase ku70
- Histone H3.3 type b
- Suppressor of Mek1
- Histone H1
Sequence:
MSETKPASSKPAAAAKPKKVIPRVSRTGEPKSKPESRSARAGITFPVSRVDRLLREGRFAPRVESTAPVYLAAVLEYLVFEILELAHNTCSISKKTRITPQHINWAVGNDLELNSLFQHVTIAYGGVLPTPQQSTGEKKKKPSKKAAEGSSQIY
Protein: Thrombospondin 2 (D4A2G6)
Organism: Rattus norvegicus (Rat)
Interaction partners:
- Platelet glycoprotein 4
- Platelet glycoprotein 4
- Syndecan-4
- Integrin subunit alpha 3
- Integrin beta-1
- Syndecan-1
- Integrin subunit alpha 2b
- Lysosome membrane protein 2
- Scavenger receptor class B member 1
- Matrix metalloproteinase-9
Sequence:
MLWALALLALGIGPRAYAGDHGEDTAFDLFSISNINRKTIGAKQFRGPDPGVPAYRFVRFDYVPPVNTDDLNRIVKLARRKEGFFLTAQLKQDRKSRGTLLVLEGPGTSQRQFEIVSNGPGDTLDLNYWVEGHQHTNFLEDVGLADSQWKNVTVQVASDTYSLYVGCDLIDSVTLEEPFYEQLEADKSRMYVAKGASRESHFRGLLQNVHLVFADSVEDILSKKGCQHSQGAEVNTISEHTETLHLSPHITTDLVVQGVEKAQEVCTHSCEELSNMMNELSGLHVMVNQLSKNLERVSSDNQFLLELIGGPLKTRNMSACVQEGRIFAENETWVVDSCTTCTCKKFKTVCNQITCSPATCANPSLVEGECCPSCSHSADNDEGWSPWAEWTECSVTCGSGTQQRGRSCDVTSNTCLGPSIQTRTCSLGKCDTRIRQNGGWSHWSPWSSCSVTCGVGNVTRIRLCNSPVPQMGGKNCKGSGRETKACQRAPCPIDGRWSPWSPWSACTVTCAGGIRERTRVCNSPEPQYGGKDCVGDVTEHQMCNKRSCPIDGCLSNPCFPGAKCNSFPDGSWSCGSCPVGFLGNGTHCEDLDECAVVADICFSINKASRCVNTNPGFHCLPCPPRYKGTQPFGIGLEDAKTEKQVCEPENPCKDKTHNCHKHAECIYLGHFSDPMYKCECQTGYAGDGLICGEDSDLDGWPNSNLVCATNATYHCVKDNCPKLPNSGQEDFDKDGIGDACDEDDDNDGVSDEKDNCPLLFNPRQLDYDKDEVGDRCDNCPYVHNQAQIDTDNNGEGDACSVDIDGDDVFNERDNCPYVYNTDQRDTDGDGVGDHCDNCPLMHNPDQMDQDNDLVGDQCDNNEDIDDDGHQNNQDNCPYISNSNQADHDNDGKGDACDSDDDNDGVPDDRDNCRLVFNPDQEDSDGDGRGDICKDDFDNDNVPDIDDVCPENNAITETDFRNFQMVPLDPKGTTQIDPNWVIRHQGKELVQTANSDPGIAVGFDEFGSVDFSGTFYVNTDRDDDYAGFVFGYQSSSRFYVVMWKQVTQTYWEDKPSRAYGYSGVSLKVVNSTTGTGEHLRNALWHTGNTEGQVRTLWHDPKNIGWKDYTAYRWHLIHRPKTGYMRVLVHEGKQVMADSGPIYDQTYAGGRLGLFVFSQEMVYFSDLKYECRDA
Protein: CSD domain-containing protein (P91398)
Organism: Caenorhabditis elegans
Interaction partners:
- ATP-dependent RNA helicase cgh-1
- CSD domain-containing protein
- Protein LSM14 homolog car-1
- HTH OST-type domain-containing protein
- Polyadenylate-binding protein
- Female germline-specific tumor suppressor gld-1
- RRM domain-containing protein
- K Homology domain-containing protein
- RRM domain-containing protein
- PUM-HD domain-containing protein
Sequence:
MSDTANTAVEVDEQVIEKKLDDLSIGKKRSPSKDDTSKHRLPAAERIRIWEEEQKAKIVLTAGLQGKVKWYSVLRRYGFISRSDGEKDVFVHQTAISKSDTEKFYLRTLADEEEVLFDLVDGKNGPEAANVTGPAGVNVSGSKYRHQLLSRFRKNRKPKIVVGEDFDSKETEKLVEAPAVAMEKKKQRKQRKNKNRKQKDQKGAGDAADSSATTESLGTSSETASPDSKSCTKIISEEAGLSKIDRCDSALDDAGLGAQLIDAQI
Protein: Putative ABC transporter arginine-binding protein 2 (P30859)
Organism: Escherichia coli (strain K12)
Function: Part of the ABC transporter complex ArtPIQMJ involved in arginine transport.
Subcellular location: Periplasm {ECO:0000269|PubMed:8801422}.
Interaction partners:
- Arginine ABC transporter permease protein ArtM
- Arginine ABC transporter permease protein ArtQ
- Arginine transport ATP-binding protein ArtP
- Histidine/lysine/arginine/ornithine transport system permease protein HisM
- Histidine/lysine/arginine/ornithine transport system permease protein HisQ
- Glutamate/aspartate import permease protein GltK
- L-cystine transport system permease protein TcyL
- Glutamine transport system permease protein GlnP
- Inner membrane amino-acid ABC transporter permease protein YhdY
- Glutamate/aspartate import permease protein GltJ
Sequence:
MKKVLIAALIAGFSLSATAAETIRFATEASYPPFESIDANNQIVGFDVDLAQALCKEIDATCTFSNQAFDSLIPSLKFRRVEAVMAGMDITPEREKQVLFTTPYYDNSALFVGQQGKYTSVDQLKGKKVGVQNGTTHQKFIMDKHPEITTVPYDSYQNAKLDLQNGRIDGVFGDTAVVTEWLKDNPKLAAVGDKVTDKDYFGTGLGIAVRQGNTELQQKLNTALEKVKKDGTYETIYNKWFQK
Protein: Tro protein (Q7TSJ9)
Organism: Mus musculus (Mouse)
Interaction partners:
Sequence:
DWAAQYREAVEMDIQAAAVAVAEAKARAEARAQMGIGEEAVAGPWNWDDMDINCLTREELGDDAQAWSRFSFEIEPRAQENADPTTNVLFNQGATTRNSFSDGAGISFGGITNPSGGFGGISNPSGGFGGISNPSGGFGGISNPSGGFGGISNPSGGFGGISNPSGGFGGISNPSGGFGGISNPSGGFGGISNPSGGFGGISNPSGGFGGISNPSGGFGGISNPSGGFGGISNPSGGFGGISNPSGGFGGRNSITFGSVPNTSANFSSAPSISFGDTPNTSTSFSGGANSSFSGTPSTSAPFCNTASISFGGAPSTSTSFSTASISFGGAPSTSTSLSTASISFGGAPSTSTSFSTASISFGGAPSTSTSLSTASISFGGAPSINSSSGGSSVSFGGAPTTSTSFSGGPCISFGGAPCTTASISGGASSGFGSTLCSTNPGFSALSTNTSFGSAPTTSTVFSGAVSTTTGFGGTLSTSVCFGSSPYSGAGFGGTLSTSISFGGSPSTNTGFGGTLSTSVSFGASSSTSSDFGGTLSTSVSFGGSSGANAGFGGTLNSSTSFGGAISTSTGFGSALNNSANFGGAISTSFSGVLNSSASFGGAINTSAGFGSTLNSSASFGSALSTSASFGGVLNGSAGFGGALNTNATFGGVLNGSAGFGGAMNTNATFGGALNSNAGFGGAISTSTNFGGALNNSAGFGGAMNTSASFGGALNNSAGFGGAISTNATFGGALNNSAGFGGAISTNATFGGALNNSAGFGGAISTSASFGGTLNNSASFGGAINTSASFGGVLNNSAGFGGAINTSANFGGALTNSAGFGGAISTSASFGGALNNSAGFGGAISTSASFGGALNNSAGFGGAISTNASFGGAISNSPDFGGAFSTSVGFGGTLNTTDFGSTHSNSISFGSAPTTSVSFGGSHSTNLCFGGAPSTSLCFGSASNTNLCFGGSNSTNCFSGATSANFNEGHSISFGNGLSTSAGFGNGLGTSAGFGSSLGTSTGFGGSLGPSASFNGGLGTSTGFGGGLGTSTDFSGGLNHNADFNGGLGNSAGFNGGLNTNTDFGGELGTSAGFGDGLGSSTSFGAGLVTSDGFAGNLGTNTGFGGTLGTGAGFSVSLNNGNGFGNGPNASFNRGLNTIIGFGSGSNTSNGFTGEPNTGSSFSNGPSSIVGFSGGPSTGAGFCSGPSTGGFGGGPSTGPGFGGPSTGPGFGGPSTGGGFGGPNTGGGFGGPSTGGGFGGPSTGGGFGGPSTGGGFGGPSTAAGFGSGLSTSTGFGGGLNTSAGFSGGPPSTGTGFGGGASSHGGCGFPYG