wanglab/gogpt-training-data huggingface dataset:
Protein: Alpha-monoglucosyldiacylglycerol synthase (Alpha-MGS) (MGlcDAG synthase) (EC 2.4.1.337) (1,2-Diacylglycerol 3-glucosyltransferase) (UDP-glucose:1,2-diacylglycerol 3-alpha-D-glucosyltransferase) (Q8CWR6)
Organism: Streptococcus pneumoniae (strain ATCC BAA-255 / R6)
Function: Glucosyltransferase involved in the biosynthesis of the non-bilayer-prone membrane lipid alpha-monoglucosyldiacylglycerol. This is a major component for maintaining a certain anionic lipid surface charge density, for balancing the bilayer to non-bilayer phase equilibria and for keeping a constant lipid bilayer spontaneous curvature (curvature packing stress). Catalyzes the transfer of a glucosyl residue from UDP-Glc to diacylglycerol (DAG) acceptor to form the corresponding alpha-glucosyl-DAG (1,2-diacyl-3-O-(alpha-D-glucopyranosyl)-sn-glycerol). It can only use UDP-Glc as sugar donor.
Subcellular location: Cell membrane {ECO:0000250}.
Interaction partners:
- Alpha-galactosylglucosyldiacylglycerol synthase
- Phage shock protein PspC N-terminal domain-containing protein
- Extracellular protein
- GTPase Obg
Sequence:
MRIGLFTDTYFPQVSGVATSIRTLKTELEKQGHAVFIFTTTDKDVNRYEDWQIIRIPSVPFFAFKDRRFAYRGFSKALEIAKQYQLDIIHTQTEFSLGLLGIWIARELKIPVIHTYHTQYEDYVHYIAKGMLIRPSMVKYLVRGFLHDVDGVICPSEIVRDLLSDYKVKVEKRVIPTGIELAKFERPEIKQENLKELRSKLGIQDGEKTLLSLSRISYEKNIQAVLVAFADVLKEEDKVKLVVAGDGPYLNDLKEQAQNLEIQDSVIFTGMIAPSETALYYKAADFFISASTSETQGLTYLESLASGTPVIAHGNPYLNNLISDKMFGALYYGEHDLAGAILEALIATPDMNEHTLSEKLYEISAENFGKRVHEFYLDAIISNNFQKDLAKDDTVSQRIFKTVLYLPQQVVAVPVKGSRRMLKASKTQLISMRDYWKDHEE
Protein: Peroxisomal biogenesis factor 11 (O62103)
Organism: Caenorhabditis elegans
Subcellular location: Peroxisome membrane {ECO:0000256|ARBA:ARBA00046271}.
Interaction partners:
- Putative peroxisomal biogenesis factor 19
- Peroxisomal membrane protein PEX13
- Peroxisome assembly protein 12
- Peroxisomal membrane protein PEX14
- TPR_REGION domain-containing protein
- Peroxisomal ATPase PEX1
- Peroxisomal ATPase PEX1
- C-type lectin domain-containing protein
- Peroxisomal biogenesis factor 3
- Bifunctional glyoxylate cycle protein
Sequence:
MVNSTTLAHLNTNIDHLTTVLSSYAGRDKAIRSLAFYLQLKSTTSPDNAKEILGLAKQLSAARLVSRQFNHPGMLKSCRQIMQAFQTGRIGDPLEFLTGAAVTGIYTVYGFVELLAWLSDAKILAFNSARLYKWCLYLWLSELINGIVRQMRVIYRKGIEKSQEDILTLVGLSSDFISGVNSLPHKILWAGKLSMRQSASFSLLASIIGFYKLW
Protein: Uncharacterized protein C31F10.16 (P87317)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Nucleus. Cytoplasm.
Interaction partners:
- Cell fusion protein cfr1
- ADP-ribosylation factor 1
- Protein transport protein sec13
Sequence:
MSDSFFKDIPEFLETRVNESLDARSKSIAQFKELGPPDQVNTIKVNAKNPSKEVGTYHFVSGVDASSSASLAAYLNTLSYSLDKSQQWFGKGNAWRVSHGVYCCYNVFSQVDVRVEAKIPGGVDTYAIDENGQKHIVDARMWTEAYMSEVLRSLLYSDDTNSRFAGHRRFNPIPNPDAELRFFEAAEQLFTLGYTLGSSSEVRVPTHVNNHLVRGIFAYLKQTCRYSAALNLFEKLRVSIPEVSVLLAELYLLMDHEVHAVRILHDSLLKQRMSASLLIVQVKFLISKERYDLALICAKRAVHASPSEFATWACLADVYLHLEDFKSALLALNSCPMYTYYERDAYPLPPSARAHLPFPVNFPKEELEVENNAQNGYTVSTEITDPYLARLPSPSLRGTFAKAYEMLTLICAKIGWDELLRVRSAVFVMEEEYRSLNDITEGNASPDQNEVAEESVAEEVVGLDKPETSVGSLPKNATVQSKRLCERWLDNLFMVLYEDLRVFTIWRAEYTHFKSQGLAYRKAPAEWEILGEVAFRLHHRVEAVEAFCACLESMFSFKAWKTLLIIYSEDNNIELVLTAIAKLTLYNYRWYQEYSPFLLEQMKNRIMQDGALKMKSILASTRLDPYILNLIHKLYFEWAIAFQIPGHEL
Protein: Phosphatidylinositol polyphosphate 5-phosphatase type IV (72 kDa inositol polyphosphate 5-phosphatase) (Inositol polyphosphate-5-phosphatase E) (Phosphatidylinositol 4,5-bisphosphate 5-phosphatase) (EC 3.1.3.36) (Phosphatidylinositol-3,4,5-trisphosphate 5-phosphatase) (EC 3.1.3.86) (Q9NRR6)
Organism: Homo sapiens (Human)
Function: Phosphatidylinositol (PtdIns) phosphatase that specifically hydrolyzes the 5-phosphate of phosphatidylinositol-3,4,5-trisphosphate (PtdIns(3,4,5)P3), phosphatidylinositol 4,5-bisphosphate (PtdIns(4,5)P2) and phosphatidylinositol 3,5-bisphosphate (PtdIns(3,5)P2) (By similarity). Specific for lipid substrates, inactive towards water soluble inositol phosphates. Plays an essential role in the primary cilium by controlling ciliary growth and phosphoinositide 3-kinase (PI3K) signaling and stability (By similarity).
Subcellular location: Cytoplasm, cytoskeleton, cilium axoneme {ECO:0000269|PubMed:19668215, ECO:0000269|PubMed:19668216, ECO:0000269|PubMed:24166846}. Golgi apparatus, Golgi stack membrane {ECO:0000250|UniProtKB:Q9JII1}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q9JII1}; Cytoplasmic side {ECO:0000250|UniProtKB:Q9JII1}. Cell membrane {ECO:0000250|UniProtKB:Q9WVR1}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q9WVR1}; Cytoplasmic side {ECO:0000250|UniProtKB:Q9WVR1}. Cell projection, ruffle {ECO:0000250|UniProtKB:Q9WVR1}. Cytoplasm {ECO:0000250|UniProtKB:Q9WVR1}. Nucleus {ECO:0000250|UniProtKB:Q9JII1}. Note=Peripheral membrane protein associated with Golgi stacks. {ECO:0000250|UniProtKB:Q9JII1}.
Interaction partners:
- Retinal rod rhodopsin-sensitive cGMP 3',5'-cyclic phosphodiesterase subunit delta
- ADP-ribosylation factor-like protein 13B
- Phosphatidylinositol 4-phosphate 5-kinase type-1 beta
- Inositol polyphosphate-4-phosphatase type I A
- Phosphatidylinositol 4-phosphate 5-kinase type-1 gamma
- Inositol polyphosphate 4-phosphatase type II
- Inositol polyphosphate 5-phosphatase OCRL
- Type II inositol 1,4,5-trisphosphate 5-phosphatase
- Type 2 phosphatidylinositol 4,5-bisphosphate 4-phosphatase
- Synaptojanin-2
Sequence:
MPSKAENLRPSEPAPQPPEGRTLQGQLPGAPPAQRAGSPPDAPGSESPALACSTPATPSGEDPPARAAPIAPRPPARPRLERALSLDDKGWRRRRFRGSQEDLEARNGTSPSRGSVQSEGPGAPAHSCSPPCLSTSLQEIPKSRGVLSSERGSPSSGGNPLSGVASSSPNLPHRDAAVAGSSPRLPSLLPPRPPPALSLDIASDSLRTANKVDSDLADYKLRAQPLLVRAHSSLGPGRPRSPLACDDCSLRSAKSSFSLLAPIRSKDVRSRSYLEGSLLASGALLGADELARYFPDRNVALFVATWNMQGQKELPPSLDEFLLPAEADYAQDLYVIGVQEGCSDRREWETRLQETLGPHYVLLSSAAHGVLYMSLFIRRDLIWFCSEVECSTVTTRIVSQIKTKGALGISFTFFGTSFLFITSHFTSGDGKVAERLLDYTRTVQALVLPRNVPDTNPYRSSAADVTTRFDEVFWFGDFNFRLSGGRTVVDALLCQGLVVDVPALLQHDQLIREMRKGSIFKGFQEPDIHFLPSYKFDIGKDTYDSTSKQRTPSYTDRVLYRSRHKGDICPVSYSSCPGIKTSDHRPVYGLFRVKVRPGRDNIPLAAGKFDRELYLLGIKRRISKEIQRQQALQSQNSSTICSVS
Protein: Candida glabrata strain CBS138 chromosome L complete sequence (Q6FL73)
Organism: Candida glabrata (strain ATCC 2001 / BCRC 20586 / JCM 3761 / NBRC 0622 / NRRL Y-65 / CBS 138) (Yeast) (Nakaseomyces glabratus)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
- ATP synthase subunit a
Sequence:
MELRRRLSRVQTLTQFNFSYNKSFGHKFRDFIAKSGHHVKPIQKYIFPNFIAVHYFYIIFMTILASILLYPVKNFSYIDILFLAAGATTQGGLNTVNINELTLYQQMIIYIICCLCTPIAIHGTLAFVRLYWFERYFDNIRDTSKRNYKMRRTKTILEREKTARTLSRLRTNTTIPIHKSNQENSQRSNFQEKLFSGEFVNRDEQNSIESQQDAMDSQSTQNSLPTFKGLGPSKIQKTASPRSLNSTLPSGSVLEDGESRTPYEQPIDYTIPNSNPNLTVPVERFKRRRSRDISPQDMYRSIMMLQDKHSNIDDNEEGPALVIGSPQDRQNIKPTVQSQSMGHNALTPVHSISDKEVSPKHVDANEINMGMKVKDKHGNQGPSRRSGSQSPSSENAFPNENDEEENFSPYTNSRKIKLNKHPTGRNYDNSSDDLNSAGNYNSEEGLEGENATQSTEEVSPLDSDDAYSDGDSHEYENTEVNEDSDSIQDIQSGNNRLYRRRTDQERNLNYESEASITQDNIERHNNDSINSENAASDDSESNGENTNDRNARTPNKGGEPKIQFNITEPPRKRRTQNFHIMEATRPNIPHNAHKRTSSNLFLKQLSKGKRIRHNLKRRLSSGPFEKNESPFNPSIKNVNKQKGSQKETNQDNGEDYFADNESDDDDNNPASSDYNGLSKTVSYNNTEDRKPDPVRLTMERAMTMDNITPEDLNKLAQKPDFQKMVYKNWKRKHRKNKKNRKLGWNKKFDFEDTLPTVFDSHNEGHQRTMSNDEDNEDIRNGNIDRYNTIDYNDGYQIDPDMNEEGYFGVSFNNDYNFSRHPFSRTMSANYLSWEPTVGRNSLFVDLSRAQKEELGGVEYRSIKLLCKILVIYYLGFHIMSFTMLLPWITHKTKYKHIVRDDGVSPGWWGFFTAMSAFNDLGLTLTPDSMSSFNRAAYPLIVMIWFIIIGNTGFPVLLRFIIWVMYHLSSDLSQLRESLAFLLDHPRRCFTLLFPSTATWWLFGILVGLNITDWILFIILDFNNVVVKPNPKGYRVLMGLFQAVSTRTAGFSVVDLSQLNSAVQVSYMIMMYVSVLPLAISIRRTNVYEEQSLGLYGNVEDDDSSDSDYEDHLSSEEELLAKNGDNDDDEETLDSQYYSKSIRGRNDSDESSSNEGGSNSSAKKRKRTAKKESSKGKKKKRRVSEKKSKSFIGAHLRRQLSFDLWFLFLGLFVICICENGKIKDVARPAFNVFPILFEIVSAYGTVGLSLGYPNTSQSLSGQFTTLSKLVIIAMLIRGRNRGLPYTLDRAIILPSDRLERIDHIEDLKLKRTAGLHARHQPRPEDERKKSIAKKSFKYIKKGGKGLLYPSKLL
Protein: RNA-binding protein (Q382D7)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MAPKSATKSAAATKASAPKNDPKKNAPKAAAPKPAATAPKAAAAKEAKARPAAGTHNGVYVKNWGQGSVTDATRIFSAAGKVVSAQIRRRRYAIIFFENAAAVRKAIDLFNEKEVLGAKVTVSPAKTSPKPDPHEGSSVVFLSPIFRTSTTNGQIRELFTGMRVLRIRTYHQNYAYVYLDSAAAAQKFVKEKNGTEFRGKKLRVALSTRSLQKEKDRAERANLLSDAHNFKKDAKKDIKRDDKKDPKKDSRRNEKKDAKRKQ
Protein: Inhibitor of nuclear factor kappa-B kinase subunit alpha (EC 2.7.11.10) (Nuclear factor NF-kappa-B inhibitor kinase alpha) (A0A8I6ANR6)
Organism: Rattus norvegicus (Rat)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}. Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MERPPGLRPGAGGPWEMRERLGTGGFGNVSLYQHRELDLKIAIKSCRLELSTKNRERWCHEIQIMKKLNHANVVKACDVPEELNFLINDVPLLAMEYCSGGDLRKLLNKPENCCGLKESQILSLLSDIGSGIRYLHENKIIHRDLKPENIVLQDVGGKIMHKIIDLGYAKDVDQGSLCTSFVGTLQYLAPELFENKPYTATVDYWSFGTMVFECIAGYRPFLHHLQPFTWHEKIKKKDPKCIFACEEMTGEVRFSSHLPQPNNLCSLIVEPMESWLQLMLNWDPQQRGGPIDPPLKQPKCFVLMDNILNLKIVHILNMTSAKIISFLLPYDESLHSLQSRIERETGINTGSQELLSETGISLDPRKPASQCVLDGVRGCDSYMVYLFDKSKTVYEGPFASRSLSDCVNYIVQDSKIQLPVTQLRKVWAEAVHYVSGLKEDYSRLFQGQRAAMLSLLRYNANLTKMKNTLISASQQLKAKLEFFRKSIQLDLERYSEQMTYGISSEKMLKAWKEMEEKAIHYSEVGVIGYLEDQIMSLHTEIMELQKSPYGRRQGDLMESLEQRAIDLYKQLKHRPTDHSYSDSTEMVKIIVHTVQSQDRVLKELFGHLSKLLGCKQKIIDLLPKVEVALSNIKEADNTVMFMQGKRQKEIWHLLKIACTQSSARSLVGSSLEGTVTPPVSAWLPPTLADREHPLTCVVTPQDGVRCAWSEALC
Protein: LD41005p (TATA box-binding protein-associated factor RNA polymerase I subunit C-like) (Q9W2G5)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Homeobox protein goosecoid
- CKII-alpha subunit interactor-3, isoform B
- GEO04452p1
- TATA box-binding protein-associated factor RNA polymerase I subunit B
Sequence:
MPRRYQTALNSAKYSAQVKTKTSDNESDSEDDLPPDQDAEDNNEPDNLRSILENAPHFSYPGLNTGMLGQLLYDHQDNPKQDLPNCSVTVPLPLFLAKDGQTPRVEACVQRPFRYDDWTRQLQLGKAIFDRRLKNMRQRVQKQEQGVHDASLFEMAEHIAQQENSFFRDSYDYYYTGGNLNTIPFDGNDQLAMHVSGNKLRDLHFSRDYGEAEFWQPLHSATIEESSSEVFELLPLHNLNRSQMFLARLLKEVSLYELKCKDEQDSDSDYELIRHCMFSSQVAPFTSAAQSLANANTLALASQDRSLRFVDISTQQDIAKLDVCLLKGLKKTSSTWAQLKQAEESTFHCLTQPVLFTVDVRCNLPLNPCFASGVHSKACERFSCLAKGVNPNLLYVASNHNFHCLDIRCLGKKLTDRAVVTWTHQMTYPPCFIDTSVHQDSEYIALGGLLPKDLRICELQGAQAKSVDEMFSPAIPFAPVTLEEALIDARLGGFVDVYADIAERVTTCITGMRFIGLEGASDQAFTQLLTSNSLGDVYCQRLTLRDEEEHVQQIRTGTHTTEAIRYLANAVNERVQRENIRCTQVQSIPEIRDIFRDGAKRSKPEEKPLIVEEIEIDYGIEDTDVSEDESPASEKVKEEPSESKKGGKKTPKKKTKVKPKRQPKRKAASKRNVKKQKSISRGPWQKSAYKLSHYTDMMSTRLLDVWDMEEYDTTRDVTREMFDERIKGKELEPEQRMANWLEQLPSQTVVPTEDEVTEGNPDMVPGTSLPKLYGATTANYSVIPALNSDQDIGERLLSPKKESPVEFGREYSILLPGQNTIIEDYPCAPPAKRPKVKHVKGF
Protein: Peroxisomal membrane protein 11A (HsPEX11p) (28 kDa peroxisomal integral membrane protein) (PMP28) (Peroxin-11A) (Peroxisomal biogenesis factor 11A) (Protein PEX11 homolog alpha) (PEX11-alpha) (O75192)
Organism: Homo sapiens (Human)
Function: May be involved in peroxisomal proliferation and may regulate peroxisomes division. May mediate binding of coatomer proteins to the peroxisomal membrane (By similarity). Promotes membrane protrusion and elongation on the peroxisomal surface.
Subcellular location: Peroxisome membrane {ECO:0000269|PubMed:20826455, ECO:0000269|PubMed:9714566, ECO:0000269|PubMed:9792670}; Multi-pass membrane protein {ECO:0000269|PubMed:9714566, ECO:0000269|PubMed:9792670}.
Interaction partners:
- Peroxisomal membrane protein 11C
- Mitochondrial fission 1 protein
- Dynamin-1-like protein
- Peroxisomal biogenesis factor 19
- Peroxisomal membrane protein PEX13
- Peroxisomal membrane protein 11B
- Peroxisome proliferator-activated receptor alpha
- Peroxisome assembly protein 12
- Peroxisome biogenesis factor 10
- Peroxisomal biogenesis factor 3
Sequence:
MDAFTRFTNQTQGRDRLFRATQYTCMLLRYLLEPKAGKEKVVMKLKKLESSVSTGRKWFRLGNVVHAIQATEQSIHATDLVPRLCLTLANLNRVIYFICDTILWVRSVGLTSGINKEKWRTRAAHHYYYSLLLSLVRDLYEISLQMKRVTCDRAKKEKSASQDPLWFSVAEEETEWLQSFLLLLFRSLKQHPPLLLDTVKNLCDILNPLDQLGIYKSNPGIIGLGGLVSSIAGMITVAYPQMKLKTR
Protein: L-galactonate dehydratase (EC 4.2.1.146) (Q0QWS4)
Organism: Hypocrea jecorina (Trichoderma reesei)
Function: Mediates the conversion of L-galactonate to 2-dehydro-3-deoxy-L-galactonate, the second step in D-galacturonate catabolic process.
Interaction partners:
Sequence:
MSEVTITGFRSRDVRFPTSLDKTGSDAMNAAGDYSAAYCILETDSAHSGHGMTFTIGRGNDIVCAAINHVADRLKGKKLSSLVADWGKTWRYLVNDSQLRWIGPEKGVIHLALGAVVNAVWDLWAKTLNKPVWRIVADMTPEEYVRCIDFRYITDAITPEEAVAMLREQEAGKAKRIEEALQNRAVPAYTTSAGWLGYGEDKMKQLLRETLAAGYRHFKVKVGGSVEEDRRRLGIAREILGFDKGNVLMVDANQVWSVPEAIDYMKQLSEYKPWFIEEPTSPDDIMGHKAIRDALKPYGIGVATGEMCQNRVMFKQLIMTGAIDICQIDACRLGGVNEVLAVLLMAKKYGVPIVPHSGGVGLPEYTQHLSTIDYVVVSGKLSVLEFVDHLHEHFLHPSVIKDGYYQTPTEAGYSVEMKPESMDKYEYPGKKGVSWWTTDEALPILNGEKI
Protein: Zinc finger protein ush (Protein U-shaped) (Q9VPQ6)
Organism: Drosophila melanogaster (Fruit fly)
Function: Transcription regulator that modulates expression mediated by transcription factors of the GATA family such as pnr and srp. Represses transcription of proneural achaete-scute complex (AS-C), which is usually activated by pnr. Involved in cardiogenesis, blood, and eye development. During hematopoiesis, it is required to restrict the number of crystal cells, probably via its interaction with the isoform SrpNC of srp. Negatively regulates expression of sr. Probably acts by interacting with the GATA-type zinc finger of proteins such as pnr and srp, possibly antagonizing the interaction between the GATA-type zinc finger and some cofactor.
Subcellular location: Nucleus {ECO:0000269|PubMed:9367989}.
Interaction partners:
- Grain, isoform C
- Box A-binding factor
- GATA-binding factor A
- Pebbled, isoform A
- Insulin gene enhancer protein ISL-1
- FI19405p1
Sequence:
MLSSNTRGDCSDTAEEMTVDSRDSKDLSAQDIGEQKQQQMEDQLEDQLNDSRDPQNNNNNIDDDADEDAEFEEPEKANPQQDQDLGETEMEQEHDLQQEDLQQELPANSPSTPPRSPSSPQLIPKLEQPATPPSEPEASPCPSPSPCPTPKYPKVRLNALLASDPALKPDAKELTLPDSRLLAPPPLVKPDTQAQPEVAEPLLKPARFMCLPCGIAFSSPSTLEAHQAYYCSHRIKDTDEAGSDKSGAGGSGATAGDAAGLTGGSTEPPAKMARTGKQYGCTQCSYSADKKVSLNRHMRMHQTSPAAPTLAGLPSLLQNGIAPPGVTPNPMEDSSSQQTDRYCSHCDIRFNNIKTYRAHKQHYCSSRRPEGQLTPKPDASPGAGSGPGSAGGSIGVSAQAATPGKLSPQARNKTPTPAMVAVAAAAAAAAASLQATPHSHPPFLALPTHPIIIVPCSLIRAASFIPGPLPTPNSGIVNPETTCFTVDNGTIKPLATALVGATLEPERPSAPSSAAEATEAKSSPPEPKRKEAGLTRESAPLDLSLRRSPITLNSLSLRQRQLRNALLDVEEVLLAGVGTGKENVETPRGGGSVTPEQIVCAPSLPSSPSMSPSPKRRAISPRSSGAGSASSMSPPGLNVAVPHLLDMRSMLPADFGLSESLLAKTNPELALKLAAAAAAAAVAGSSGAAAFPPASLPAQTSSGNPGSGGSAGGAQQPQIYVKKGVSKCMECNIVFCKYENYLAHKQHYCSARSQEGASEVDVKSAVSPSIAGAGGLGAGAAEAASSVETTPVAYQQLICAACGIKYTSLDNLRAHQNYYCPKGGAVAAPAATPTDPGQLGMPKEKCGKCKTLHEIGLPCPPPVANPLAAPTVNPQPATNSLNKCPVCGVVSPTAALAKKHMEMHGTVKAYRCSICQYKGNTLRGMRTHIRTHFDKKTSDVNEELYMTCIFEEDASALSQELVTPTGASTTTGHDSMDHPSQMFNCDYCNYVSTYKGNVLRHMKLMHPHVAINSPSISPDTRDQDVTSNPTTNQHSNSDVSNGEAPSFHIKSEPLDPPPTVNLVHENNNSPIATPHIKAEPIEVGADAAPGGLVPPMTSPLGNSSSVAAAAAAAAEVMKKYCSTCDISFNYVKTYLAHKQFYCKNKPIRPEASDSPSPNHLGGGVAVGLGIGGLVGGHGQQKNKENLQEAAI
Protein: Heat shock cognate protein HSP 90-beta (Q6AZV1)
Organism: Xenopus laevis (African clawed frog)
Function: Molecular chaperone that promotes the maturation, structural maintenance and proper regulation of specific target proteins involved for instance in cell cycle control and signal transduction. Undergoes a functional cycle linked to its ATPase activity. This cycle probably induces conformational changes in the client proteins, thereby causing their activation. Interacts dynamically with various co-chaperones that modulate its substrate recognition, ATPase cycle and chaperone function. Engages with a range of client protein classes via its interaction with various co-chaperone proteins or complexes, that act as adapters, simultaneously able to interact with the specific client and the central chaperone itself. Recruitment of ATP and co-chaperone followed by client protein forms a functional chaperone. After the completion of the chaperoning process, properly folded client protein and co-chaperone leave HSP90 in an ADP-bound partially open conformation and finally, ADP is released from HSP90 which acquires an open conformation for the next cycle.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:P08238}. Dynein axonemal particle {ECO:0000269|PubMed:30561330, ECO:0000269|PubMed:33263282}.
Interaction partners:
- CS domain-containing protein.
- SGT1 homolog, MIS12 kinetochore complex assembly cochaperone L homeolog isoform X1
- Uncharacterized protein.
- Stress-induced-phosphoprotein 1
- Serine/threonine-protein kinase TOR
- Protein kinase domain-containing protein
- receptor-interacting Serine/threonine-protein kinase 3 isoform X1
- Protein kinase domain-containing protein
- Heat shock 70 kDa protein
- Glucocorticoid receptor
Sequence:
MPEVAHNGEEEVETFAFQAEIAQLMSLIINTFYSNKEIFLRELISNASDALDKIRYESLTDPSKLDSGKDLKIDIIPNRLERTLTMIDTGIGMTKADLINNLGTIAKSGTKAFMEALQAGADISMIGQFGVGFYSAYLVAEKVVVITKHNDDEQYAWESSAGGSFTVKVDTGEPIGRGTKVILHLKEDQTEYLEEKRVKETVKKHSQFIGYPITLYLEKEREKEISDDEAEEEKEEKKEEEGENDKPKIEDVGSDEEEEGKDKKKKTKKIKEKYIDQEELNKTKPIWTRNPDDITQEEYGEFYKSLTNDWEDHLAVKHFSVEGQLEFRALLFIPRRAPFDLFENKKKKNNIKLYVRRVFIMDSCDELIPEYLNFVRGVVDSEDLPLNISREMLQQSKILKVIRKNIVKKCLELFCELAEDKENYKKFYEGFSKNLKLGIHEDSTNRKKLSELLRYHTSQTGDEMASLTEYVSRMKENQKSIYYITGESKDQVANSAFVERVRKRGFEVVYMTEPIDEYCVQQLKEFDGKTLVSVTKEGLELPEDEEEKKTMEENKTKFESLCKLMKEILDKKVEKVTVSNRLVSSPCCIVTSTYGWTANMERIMKAQALRDNSTMGYMMAKKHLEINPEHPIVETLRQKADTDKNDKAVKDLVVLLFETALLSSGFSLDDPQTHSNRIYRMIKLGLGIDDDDAPIEEASPSVPDDIPPLEGEEDASRMEEVD
Protein: Cyclin D (Q9GTQ8)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MADIMDLLCSEIIVYDSDPSLYRLNKRQQQMSSPAIIRDQSSICSSLGDAESDSHPDAQNNAVVCNMKELVYIYASVDSAAKNPEQLEPPPPPPPPPPPPPTATQSIQSYPRYISQEPPTSHCQRLDERLTTTADPPATDNVNTAIGDPTLYSDRCLENFLKVEEKHHKIPDTYFSIQKDITPPMRKIVAEWMMEVCAEENCQEEVVLLALNYMDRFLSSKSVRKTQLQILAAACLLLASKLREPSCRALSVDLLVVYTDNSIYKDDLIKWELYVLSRLGWDLSSVTPLDFLELLMMRLPIGSKNFPDINIGKVRGHAQAFISLAAKEHKFAKFSASTIAASSIAASMNGLKWHLRSGHNLHFLLSLMTDLTSVEQAQVRDCMLHMEDIFKEHSRNLEPFLVNIDPKEMSTLYYKRRFQIHQSQHLSQISIRPLPLPKAPAECVEQHQQQHNFGSAAPHRTHTCKMQAQAQAQNEIQDVTF
Protein: Thymosin beta-4 (T beta-4) [Cleaved into: Hemoregulatory peptide AcSDKP (Ac-Ser-Asp-Lys-Pro) (N-acetyl-SDKP) (AcSDKP) (Seraspenide)] (P62326)
Organism: Bos taurus (Bovine)
Function: Plays an important role in the organization of the cytoskeleton. Binds to and sequesters actin monomers (G actin) and therefore inhibits actin polymerization.
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:P62328}.
Interaction partners:
- Actin, cytoplasmic 1
- Actin, cytoplasmic 2
- Thymosin beta
- Profilin-1
- Profilin-4
- Profilin-2
- Profilin
- Profilin
- Profilin-3
- Prothymosin alpha
Sequence:
MSDKPDMAEIEKFDKSKLKKTETQEKNPLPSKETIEQEKQAGES
Protein: Thiamin biosynthesis protein (Thi-4), putative (AFU_orthologue AFUA_2G10740) (C8V3I9)
Organism: Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Interaction partners:
- Thiamine biosynthetic bifunctional enzyme, putative
- Cytosolic regulator Pianissimo, putative
- ATP-dependent RNA helicase dbp2
- Thiamine thiazole synthase
- pyridoxal kinase
- DNA polymerase
Sequence:
MSVGRVLVIAGSDSSGGAGLEADQRVLTAHGCYALTATTGLTAQNTLGVQDIFVVPADFVEKQIRAGLDDVGADVVKLGMLSSATTIDVVADALTSYQIPSVVLDPVMISTSGSQLLPEAAVQGLRTKLLPLTTILTPNIPEAQLLLKDAGQEPTNPEDLQGLIDLAKRVAALGPRAVLLKGGHLPLTKDYTAAKGSDDASRVIDILYAGEEVTQFETEYLVSKNTHGTGCSLASAIAANLALGKDLKRAVRNGVRFVEAGIKTSYDIGKGSGPINHFHSVYSLPFAPGRFLEYVLDRPDVQSVWKRFTEHEFVLGLGSGTLPVERFKEYLVQDYLYLVQFARSNALASYKAKDMESIAASAKIVLHIQQETALHIDYCASFGLSKEEMEKVPETTACTAYSRYILDVGQSEDWLALQVALAPCLIGYGAIAQRLHAEEKTLREGNRYWKWIENYVAEDYTEAVRLGSELLETHMRKVSLSRMEELVKIFIKATELEIMFWDMGLGAGHS
Protein: Krueppel-like factor 4 (Epithelial zinc finger protein EZF) (Gut-enriched krueppel-like factor) (Q60793)
Organism: Mus musculus (Mouse)
Function: Transcription factor; can act both as activator and as repressor. Binds the 5'-CACCC-3' core sequence. Binds to the promoter region of its own gene and can activate its own transcription. Regulates the expression of key transcription factors during embryonic development. Plays an important role in maintaining embryonic stem cells, and in preventing their differentiation. Required for establishing the barrier function of the skin and for postnatal maturation and maintenance of the ocular surface. Involved in the differentiation of epithelial cells and may also function in skeletal and kidney development. Contributes to the down-regulation of p53/TP53 transcription (By similarity).
Subcellular location: Nucleus {ECO:0000269|PubMed:10431239, ECO:0000269|PubMed:24161396, ECO:0000269|PubMed:35922041}. Cytoplasm {ECO:0000269|PubMed:35922041}.
Interaction partners:
- Catenin beta-1
- Transcription factor SOX-2
- POU domain, class 5, transcription factor 1
- Homeobox protein NANOG
- Myc proto-oncogene protein
- CCAAT/enhancer-binding protein beta
- Cellular tumor antigen p53
- Zinc finger protein 750
- Protein lin-28 homolog A
- Transcriptional coactivator YAP1
Sequence:
MRQPPGESDMAVSDALLPSFSTFASGPAGREKTLRPAGAPTNRWREELSHMKRLPPLPGRPYDLAATVATDLESGGAGAACSSNNPALLARRETEEFNDLLDLDFILSNSLTHQESVAATVTTSASASSSSSPASSGPASAPSTCSFSYPIRAGGDPGVAASNTGGGLLYSRESAPPPTAPFNLADINDVSPSGGFVAELLRPELDPVYIPPQQPQPPGGGLMGKFVLKASLTTPGSEYSSPSVISVSKGSPDGSHPVVVAPYSGGPPRMCPKIKQEAVPSCTVSRSLEAHLSAGPQLSNGHRPNTHDFPLGRQLPTRTTPTLSPEELLNSRDCHPGLPLPPGFHPHPGPNYPPFLPDQMQSQVPSLHYQELMPPGSCLPEEPKPKRGRRSWPRKRTATHTCDYAGCGKTYTKSSHLKAHLRTHTGEKPYHCDWDGCGWKFARSDELTRHYRKHTGHRPFQCQKCDRAFSRSDHLALHMKRHF
Protein: Dehydrodolichyl diphosphate synthase complex subunit nus1 (EC 2.5.1.87) (Q9Y7K8)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: With SPAC4D7.04c, forms the dehydrodolichyl diphosphate synthase (DDS) complex, an essential component of the dolichol monophosphate (Dol-P) biosynthetic machinery. Adds multiple copies of isopentenyl pyrophosphate (IPP) to farnesyl pyrophosphate (FPP) to produce dehydrodolichyl diphosphate (Dedol-PP), a precursor of dolichol which is utilized as a sugar carrier in protein glycosylation in the endoplasmic reticulum (ER).
Subcellular location: Endoplasmic reticulum membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}.
Interaction partners:
- Dehydrodolichyl diphosphate synthase complex subunit SPAC4D7.04c-farnesyl diphosphate specific))
- Farnesyl pyrophosphate synthase
- Decaprenyl-diphosphate synthase subunit 1
- Geranylgeranyl pyrophosphate synthase
- Protein farnesyltransferase/geranylgeranyltransferase type-1 subunit alpha
- Protein farnesyltransferase subunit beta
- Squalene synthase
- tRNA
- Putative ribosomal recycling factor
- Isopentenyl-diphosphate delta-isomerase
Sequence:
MYDDIFFYLALWVIQSVYGAWDWAKNWVFWTCSYLLNFLYHHHCSRDLIRRDTKKLKKKPKHIAVIIECVEDGGIEGLIHDACELSAWCVCSNIRELTIYERKGFLKQSPEAVEKAIYSHLPFYLGGDKCTVHVTNPCSPDEKNQNDCVDLKVHLIAKEDGRDAIIDLTRGLADLCTKKVISSTQVTLELIDKELKESVIPEPDLLIIFAPLLKLQGFPPWQLRLCEIFHDPILYTTNYLTFFKALVHYSNAEMRLGH
Protein: AP-1 complex subunit gamma (A0A8I5Y697)
Organism: Rattus norvegicus (Rat)
Subcellular location: Cytoplasmic vesicle membrane {ECO:0000256|ARBA:ARBA00004156}. Endomembrane system {ECO:0000256|ARBA:ARBA00029433}; Peripheral membrane protein {ECO:0000256|ARBA:ARBA00029433}; Cytoplasmic side {ECO:0000256|ARBA:ARBA00029433}. Golgi apparatus {ECO:0000256|ARBA:ARBA00004555}.
Interaction partners:
Sequence:
MTPLELINKLYHISAGFSKSCVLKNQPIFYMYEWFWGQNIRTFLFYVFFHMQRMPAPIRLRELIRTIRTARTQAEEREMIQKECAAIRSSFREEDNTYRCRNVAKLLYMHMLGYPAHFGQLECLKLIASQKFTDKRIGYLGAMLLLDERQDVHLLMTNCIKNDLNHSTQFVQGLALCTLGCMGSSEMCRDLAGEVEKLLKTSNSYLRKKAALCAVHVIRKVPELMEMFLPATKNLLNEKNHGVLHTSVVLLTEMCERSPDMLAHFRKLVPQLVRILKNLIMSGYSPEHDVSGISDPFLQVRILRLLRILGRNDDDSSEAMNDILAQVATNTETSKNVGNAILYETVLTIMDIKSESGLRVLAINILGRFLLNNDKNIRYVALTSLLKTVQTDHNAVQRHRSTIVDCLKDLDVSIKRRAMELSFALVNGNNIRGMMKELLYFLDSCEPEFKADCASGVFLAAEKYAPSKRWHIDTIMRVLTTAGSYVRDDAVPNLIQLITNSVEMHAYTVQRLYKAILGDYSQQPLVQVAAWCIGEYGDLLVSGQCEEEEPIQVTEDEVLDILESVLISNMSTSVTRGYALTAIMKLSTRFTCTVNRIKKVVSIYGSSIDVELQQRAVEYNALFKKYDHMRSALLERMPVMEKVTTNGPSEIVQTNGETEPAPLETKPPPSGPQPTSQANDLLDLLGGNDITPVIPTAPTSKPASAGGELLDLLGDITLTGAPAAAPTPASVPQITQPPFLLDGLSSQPLFNDIAPGIPSITAYSKNGLKIEFTFERSNTNPSVTVITIQASNSTELDMTDFVFQAAVPKTFQLQLLSPSSSVVPAFNTGTITQVIKVLNPQKQQLRMRIKLTYNHKGSAMQDLAEVNNFPPQSWQ