wanglab/gogpt-training-data huggingface dataset:
Protein: Probable 26S proteasome complex subunit sem1 (Q9VM46)
Organism: Drosophila melanogaster (Fruit fly)
Function: Subunit of the 26S proteasome which plays a role in ubiquitin-dependent proteolysis.
Interaction partners:
- 26S proteasome non-ATPase regulatory subunit 14
- Probable 26S proteasome non-ATPase regulatory subunit 3
- 26S proteasome non-ATPase regulatory subunit 6
- 26S proteasome non-ATPase regulatory subunit 4
- 26S proteasome non-ATPase regulatory subunit 2
- GH11341p
- 26S proteasome non-ATPase regulatory subunit 7
- 26S proteasome non-ATPase regulatory subunit 11
- PCI domain-containing protein 2 homolog
- 26S proteasome non-ATPase regulatory subunit 1
Sequence:
MSAPDKEKEKEKEETNNKSEDLGLLEEDDEFEEFPAEDFRVGDDEEELNVWEDNWDDDNVEDDFSQQLKAHLESKKMET
Protein: Kinetochore protein NDC80 (A8K031)
Organism: Homo sapiens (Human)
Subcellular location: Chromosome, centromere, kinetochore {ECO:0000256|RuleBase:RU368072}. Nucleus {ECO:0000256|RuleBase:RU368072}.
Interaction partners:
Sequence:
MKRSSVSSGGAGRLSMQELRSQDVNKQGLYTPQTKEKPTFGKLSINKPTSERKVSLFGKRTSGHGSRNSQLGIFSSSEKIKDPRPLNDKAFIQQCIRQLCEFLTENGYAHNVSMKSLQAPSVKDFLKIFTFLYGFLCPSYELPDTKFEEEVPRIFKDLGYPFALSKSSMYTVGAPHTWPHIVAALVWLIDCIKIHTAMKESSPLFDDGQPWGEETEDGIMHNKLFLDYTIKCYESFMSGADSFDEMNAELQSKLKDLFNVDAFKLESLEAKNRALNEQIARLEQEREKEPNRLESLRKLKASLQGDVQKYQAYMSNLESHSAILDQKLNGLNEEIARVELECETIKQENTRLQNIIDNQKYSVADIERINHERNELQQTINKLTKDLEAEQQKLWNEELKYARGKEAIETQLAEYHKLARKLKLIPKGAENSKGYDFEIKFNPEAGANCLVKYRAQVYVPLKELLNETEEEINKALNKKMGLEDTLEQLNAMITESKRSVRTLKEEVQKLDDLYQQKIKEAEEEDEKCASELESLEKHKHLLESTVNQGLSEAMNELDAVQREYQLVVQTTTEERRKVGNNLQRLLEMVATHVGSVEKHLEEQIAKVDREYEECMSEDLSENIKEIRDKYEKKATLIKSSEE
Protein: lysozyme (EC 3.2.1.17) (Q6X3T9)
Organism: Bacillus phage Bam35c (Bacillus thuringiensis bacteriophage Bam35c)
Interaction partners:
Sequence:
MGVIADLSHHEIVNWSRASKQLDFTILRVQDGSRVIDREYQKNVTGCKAYGVPFGNYAFCRFVSENDARVEARDFWERGDKDATIWFADIEVTTMDDMRAGTQAFIDELRRLGAKRVGIYVAHHKYKEFQADKINADAVWIPRYPNKPLFPCDLWQYSETGRVDGISGDVDLNYLTGTKPLKWFTGSVNTNFQIHIGDFDELTWAGDSKREVKEFLEGYGVWDMRLEKNAYRLIVGDFCNEEWCDETLQRLKERFPGYGMWKVNI
Protein: Dioxygenase FUM3 (EC 1.14.11.-) (Fumonisin biosynthesis cluster protein 3) (W7LKX6)
Organism: Gibberella moniliformis (strain M3125 / FGSC 7600) (Maize ear and stalk rot fungus) (Fusarium verticillioides)
Function: Dioxygenase; part of the gene cluster that mediates the biosynthesis of fumonisins B1 (FB1), B2 (FB2), B3 (FB3), and B4 (FB4), which are carcinogenic mycotoxins. On the basis of the chemical structures of fumonisins and precursor feeding studies, fumonisin biosynthesis is predicted to include at least five groups of biochemical reactions: synthesis of a linear polyketide with a single terminal carbonyl function and methyl groups at C-10 and C-14; condensation of the polyketide with alanine; reduction of the polyketide carbonyl to a hydroxyl; hydroxylation of 2-4 polyketide carbons; and esterification of six-carbon tricarboxylic acids to two of the hydroxyls. The biosynthesis starts with the polyketide synthase FUM1-catalyzed carbon chain assembly from one molecule of acetyl CoA, eight molecules of malonyl CoA, and two molecules of methionine. The C-18 polyketide chain is released from the enzyme by a nucleophilic attack of a carbanion, which is derived from R-carbon of alanine by decarboxylation, on the carbonyl carbon of polyketide acyl chain. This step is catalyzed by a pyridoxal 5'-phosphate-dependent aminoacyl transferase FUM8. The resultant 3-keto intermediate 2-amino-3-oxo-12,16-dimethylicosane is then stereospecifically reduced to the 3-hydroxyl product 2-amino-3-hydroxy-12,16-dimethylicosane by reductase FUM13. Subsequent oxidations at C-5, C-10, C-14 and C-15 followed by tricarballylic esterification of the hydroxyl groups on C-14 and C-15 furnish the biosynthesis of fumonisins. The C-10 hydroxylation is performed by the cytochrome P450 monooxygenase FUM2 and occurs early in the biosynthesis. The C-5 hydroxylation is performed by the dioxygenase FUM3 and occurs late in the biosynthesis. Cytochrome P450 monooxygenases FUM6 and FUM15 may be responsible for the two remaining hydroxylations at positions C-14 and C-15. The FUM11 tricarboxylate transporter makes a tricarboxylic acid precursor available for fumonisin biosynthesis via its export from the mitochondria. If the precursor is citrate, the FUM7 dehydrogenase could remove the C-3 hydroxyl of citrate to form tricarballylic acid either before or after the CoA activation by the FUM10 acyl-CoA synthetase and FUM14 catalyzed esterification of CoA-activated tricarballylic acid to the C-14 and C-15 hydroxyls of the fumonisin backbone. Alternatively, if the precursor is cis-aconitate, FUM7 may function to reduce the double bond. In this alternate proposal, feeding studies with tetradehydro-fumonisin B1 suggests that FUM7 cannot function on the tricarballylic ester and must therefore act before the FUM14-mediated esterification.
Interaction partners:
Sequence:
MNKEKVPQNAVPNGRTKLRQVTSATPLDEVFQYWEEDGAIVIKGLLTSAQVEQLNQEMGPILQKVAIGGHASDVRLQNFHGMKTKRAGDLTNNSAVFRDHLLDNDFIHAVSQRCFAYRGKMGPDAYWLGSASTIHVGPGQKPQTLHRDLGSYPIFWMLGPQGPESQINFLVATTDFTEANGATRIIPGSHKWEFNQHGDRDMTIPAEMKAGDCLLISGKVIHGTGGNKTDQERGCLAVTMCANFLAPEEAHPFIVSMGTAKKLPVRSQRCLGFRSQWPQSSPGLWTKDYSELALHLGLDD
Protein: AT14886p (Q8MTA5)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MGQLSGYETVIERLTKSLNSGVGNDMAVPRDVSLRWLLKLICEHLEKIPTTVQVSKVDENPYRVTCSRFMDISNIFKCEFVDPNIQVCFKTDLGISRSLSSSPKGEITFLTSSSSSKENFDPHSRKLLLAQNSKLKKATQVSQSQKKQGKNATEVAQSSLNSTAAIIDEFPAKDLDFLHNFSSLDITKRNKTTEDSSDWFKTDTLVRVRSVQSPEDFYVQGIHAAQRLREELDTFAHTLSDSSSVPPTIVVGQNYIIHHKDKDRYYRALVSQKLTNENLYNVFLTDIGVHLHVRCSDFRVVPERISHLPYSAVHCSLSELMPKNGESEWDSKASAFLKQIVQNNPVRVIVKKALTYELHGVDLITSNYDTNISVRDSFLYCGLAISRDGAPLWLPPAPTALRLPRISFRFGDVYMVQMLHVEDPQEFYVMRHDYEKKRLWLQFSLQEAMDRINISQLQNIFLGQLHLGCVLQSGGQWKRASIEQILPDGYVLVHLVDEGPSQKVFWDQLFVLPQKFWDTGLAIKCCLADVETRAEHSYTWTPEGTTLFKQLTSNPRLYMDVISCTEDLVYVSLHFERSNSETTSVGVQLVAHGHCTSSGESSRMIKPTVSNRSVRFDEETKKFIAQQKVRPVELSPYRMPDNTERNKRTTVNILYVRKPDEFYVTLPHFQQAINNLQKSVQKAAAAMYQNMLPRTDWQVGDMCYARVQANCDSQALWYRGVVTGVIPPGITCPIVRYQVHLRDLGELIDDVHSSSLANIDEADMRISSSAKRCHLHGIRPIGDEWSKDAIDFFMDQLKAYNEIHVTGRGRTENSLSVILWGSLSILTGPFSPATIKYVNINKALLMAGMAEKDHNSDSEDDQQSMPENVSVNSEEAAKANDWESCLSKIDGTSKTNDSLNLIESRSVTVGFEHNEDMPPLALLEDLGNTKNTTGETTPPAGWTTRRKCDKSVFTAIATNVTYECCIYLTLASDKPFIEHMGNLLVREYKPLMDKQKERSTSYTYKMGQAVVVTYHMDNMIYRGIVQRLENNHNEYTVYYVDYGNMELVKADEMLPYAPFPDLNAMCFLVELHGVRSKQGKYSLKEMDTVHLNLVMKLSGVRIVDDETVGPNKIPKCQIKVGNVDIATMMIDSGMSVPIEKQTIKNNTKYLPSQKFLEDFKVFDELDHLAAGEGELSDKEAPPTQRKHDSISSVQQPPTKKFLVDQEEVEAFECDQDFDCQQAAQKMHLNNNFYLGDFGKYADETTARDEDEPHSNSSKSIDMEVFANVNDSQLEPLNSFATEQLIRRIALRQQEIKDSITFSPIDTSSVRSFYDASASFKTLSLPNGVKEFYCTVDNVLSDTELQIAPCLSEFTKHEISLIQETSTLIKDAEPLMEPKVGDLCLARYSRDKQWYRANIKEISPILSPTSEQVTVFYIDFHDTEKVSFNHLKVMPSQLFMFPLRSFCVKLHGIKRNKSFKEKSVRQALQACLCQHPLVFARVHYPLNYYPNRPNCDADLIEVELYENRHEKKLVYQSLCENWMFLKKS
Protein: Cytoplasmic polyadenylation element binding protein 1 (A0A087WXG7)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MFSGIATSTSSSMSGTGLEHSSLSDCLLLIPLEEEAGRIKDCWDNQEAPALSTCSNANIFRRINAILDNSLDFSRVCTTPINRGIHDHLPDFQDSEETVTSRMLFPTSAQESSRGLPDANDLCLGLQSLSLTGWDRPWSTQDSDSSAQSSTHSVLSMLHNPLGNVLGKPPLSFLPLDPLGSDLVDKFPAPSVRGSRLDTRPILDSRSSSPSDSDTSGFSSGSDHLSDLISSLRISPPLPFLSLSGGGPRDPLKMGVGSRMDQEQAALAAVTPSPTSASKRWPGASVWPSWDLLEAPKDPFSIEREARLHRQAAAVNEATCTWSGQLPPRNYKNPIYSCKVFLGGVPWDITEAGLVNTFRVFGSLSVEWPGKDGKHPRCPPKGYVYLVFELEKSVRSLLQACSHDPLSPDGLSEYYFKMSSRRMRCKEVQVIPWVLADSNFVRSPSQRLDPSRTVFVGALHGMLNAEALAAILNDLFGGVVYAGIDTDKHKYPIGSGRVTFNNQRSYLKAVSAAFVEIKTTKFTKKVQIDPYLEDSLCHICSSQPGPFFCRDQVCFKYFCRSCWHWRHSMEGLRHHSPLMRNQKNRDSS
Protein: Major outer membrane protein (Q2GIE4)
Organism: Anaplasma phagocytophilum (strain HZ)
Interaction partners:
Sequence:
MKLVERIVGRKSVSALVIFCTILCVPFQAFSHESTDNFKSKNRLYFAGTYKISVPNFGSLEVEESNSHVPNVGTVLRKSMKGNVLVNTGKHKSFDAYYKEEFYSNDYFGFSGSIGYAINNFRIEVEGMNSEFKIKAGKGSVHKDDAFYIALVRERTISNNNYVVVKNKSVAVTSVALSLCYDIKSLSDIVISYLCFGVSGNAVDLLETRKLTHGYYGRIGAGFLVTRDILLSVGGYYHRLHANEFSGLKLFIPAATAREMRPAPTSAHAKMDIAYLGVEMSLRYSF
Protein: Phosphatidylinositol 5-phosphate 4-kinase type-2 gamma (EC 2.7.1.149) (Phosphatidylinositol 5-phosphate 4-kinase type II gamma) (PI(5)P 4-kinase type II gamma) (PIP4KII-gamma) (Q8TBX8)
Organism: Homo sapiens (Human)
Function: Phosphatidylinositol 5-phosphate 4-kinase with low enzymatic activity. May be a GTP sensor, has higher GTP-dependent kinase activity than ATP-dependent kinase activity. PIP4Ks negatively regulate insulin signaling through a catalytic-independent mechanism. They interact with PIP5Ks and suppress PIP5K-mediated PtdIns(4,5)P2 synthesis and insulin-dependent conversion to PtdIns(3,4,5)P3.
Subcellular location: Endoplasmic reticulum {ECO:0000250|UniProtKB:O88370}. Cytoplasm {ECO:0000250|UniProtKB:O88370}.
Interaction partners:
- Phosphatidylinositol 5-phosphate 4-kinase type-2 alpha
- Phosphatidylinositol 5-phosphate 4-kinase type-2 beta
- 1-phosphatidylinositol 3-phosphate 5-kinase
- Phosphatidylinositol 4,5-bisphosphate 3-kinase catalytic subunit gamma isoform
- Phosphatidylinositol polyphosphate 5-phosphatase type IV
- Phosphatidylinositol 3-kinase regulatory subunit beta
- Phosphatidylinositol 3-kinase regulatory subunit gamma
- Inositol polyphosphate 5-phosphatase OCRL
- Type 2 phosphatidylinositol 4,5-bisphosphate 4-phosphatase
- Phosphatidylinositol 4,5-bisphosphate 3-kinase catalytic subunit alpha isoform
Sequence:
MASSSVPPATVSAATAGPGPGFGFASKTKKKHFVQQKVKVFRAADPLVGVFLWGVAHSINELSQVPPPVMLLPDDFKASSKIKVNNHLFHRENLPSHFKFKEYCPQVFRNLRDRFGIDDQDYLVSLTRNPPSESEGSDGRFLISYDRTLVIKEVSSEDIADMHSNLSNYHQYIVKCHGNTLLPQFLGMYRVSVDNEDSYMLVMRNMFSHRLPVHRKYDLKGSLVSREASDKEKVKELPTLKDMDFLNKNQKVYIGEEEKKIFLEKLKRDVEFLVQLKIMDYSLLLGIHDIIRGSEPEEEAPVREDESEVDGDCSLTGPPALVGSYGTSPEGIGGYIHSHRPLGPGEFESFIDVYAIRSAEGAPQKEVYFMGLIDILTQYDAKKKAAHAAKTVKHGAGAEISTVHPEQYAKRFLDFITNIFA
Protein: Fatty acid-binding protein 5 (Epidermal-type fatty acid-binding protein) (E-FABP) (Fatty acid-binding protein, epidermal) (Keratinocyte lipid-binding protein) (Psoriasis-associated fatty acid-binding protein homolog) (PA-FABP) (Q05816)
Organism: Mus musculus (Mouse)
Function: Intracellular carrier for long-chain fatty acids and related active lipids, such as endocannabinoids, that regulate the metabolism and actions of the ligands they bind. In addition to the cytosolic transport, selectively delivers specific fatty acids from the cytosol to the nucleus, wherein they activate nuclear receptors (By similarity). Delivers retinoic acid to the nuclear receptor peroxisome proliferator-activated receptor delta; which promotes proliferation and survival. May also serve as a synaptic carrier of endocannabinoid at central synapses and thus controls retrograde endocannabinoid signaling. Modulates inflammation by regulating PTGES induction via NF-kappa-B activation, and prostaglandin E2 (PGE2) biosynthesis during inflammation. May be involved in keratinocyte differentiation (By similarity).
Subcellular location: Cytoplasm {ECO:0000269|PubMed:17512406, ECO:0000269|PubMed:29531087}. Nucleus {ECO:0000269|PubMed:17512406}. Synapse {ECO:0000269|PubMed:29531087}. Postsynaptic density {ECO:0000269|PubMed:29531087}. Secreted {ECO:0000269|PubMed:29531087}. Note=Localizes primarily to the cytoplasm. Upon certain ligand binding, a conformation change exposes a nuclear localization motif and the protein is transported into nucleus (By similarity). Secreted by astrocytes, but not by neurons (PubMed:29531087). {ECO:0000250|UniProtKB:Q01469, ECO:0000269|PubMed:29531087}.
Interaction partners:
- Peroxisome proliferator-activated receptor delta
- Aspartate aminotransferase, mitochondrial
- Platelet glycoprotein 4
- Scavenger receptor class B member 1
- Peroxisome proliferator-activated receptor alpha
- Hormone-sensitive lipase
Sequence:
MASLKDLEGKWRLMESHGFEEYMKELGVGLALRKMAAMAKPDCIITCDGNNITVKTESTVKTTVFSCNLGEKFDETTADGRKTETVCTFQDGALVQHQQWDGKESTITRKLKDGKMIVECVMNNATCTRVYEKVQ
Protein: Protein NETWORKED 1B (F4JIF4)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Plant-specific actin binding protein. May be part of a membrane-cytoskeletal adapter complex.
Interaction partners:
- Kinase-interacting family protein
- Pollen receptor-like kinase 1
Sequence:
MASLSQSESGRLYSWWWDSHIPKNSKWIQDNLADMDSKVKTMIKLIEADADSFARRADMYFKKRPELMKLVEELYRAYRALAERYDHTTVELRRAHKVMVEAFPNQMSFDMIEDSASSSSEPRTEADTEALQKDGTKSKRSFSQMNKLDGTSDSHEADSEVETLKRTLLELQTEKEALNLQYQLILSKVSRFEKELNDAQKDVKGFDERACKADIEIKILKESLAKLEVERDTGLLQYSQAIERIADLEASISHGQEYAKGLTNRVSEAEREAMSLKKELSRLQSEKEAGLLRYNKSLELISSLEKTIRDAEESVRVFRDQSEQAETEIKALKQELLKLNEVNEDLNVRYQQCLETISKLEREVSHAQDNAKRLSSEVLAGAAKIKTVEEQCALLESFNQTMKVEAENLAHKMSAKDQELSQKQNEIEKLQAVMQEEQLRFSELGASLRNLESLHSQSQEEQKVLTSELHSRIQMLRELEMRNSKLEGDISSKEENRNLSEINDTSISLEIQKNEISCLKKMKEKLEEEVAKQMNQSSALQVEIHCVKGNIDSMNRRYQKLIDQVSLTGFDPESLSYSVKKLQDENSKLVELCTNQRDENNAVTGKLCEMDSILKRNADLEKLLLESNTKLDGSREKAKDLIERCESLRGEKSELAAERANLVSQLQIMTANMQTLLEKNSVLEKSLSCANIELESLRDKSKCFDDFFQFLKNDKSELMKERESLVSQLCKVEEKLGVLEKKYTELEVRYTDLQRDNKLKSHQVEELQVSLAAEKQESANYKRSTESRLADLQKNVSFLREECRSRKREYEDELDRVVNKQVEIFILQKLIEDLEQKNFSLLIECQKHVEASEFSEKLIAELESENLEQQMEAEIFLDEIDSLRGAIYQVIKALQVEADCKTEQKITKDQISVSRALGEIDSLKGSLSSAEYEMHRLVVENSVLLSLLGQFQSDGLVLESEKNILEKDLKTKIHQCGMLEKDKQDLQEANRLLKSKLIKREQQEQKLRAELKFENLKFESLHDSYMVLQQDYSYTLNDNKTLLLKFSEFKDGMHVVEEENDAILQEAVALSNTCVVYRSFGSEMAEEVEDFVETVSSLREISTGLKRKVETLEKKLEGKEKESQGLNKMLENLQEGLEEDNFLTGLLEHQVSNVDEILEHREMEILEAEHMLKATNNENEELHKEVEELRKDYEDSRRMRANLEWQISELSDVAGRQEEEIRKLNALNENLESEVQFLNKEIQRQQVREEYLSLELQEKSNEIGLWDSAATSFYFDLQVSAIRELILENKVNELSGVCENLNDEVVTKTTKIKQMKETVGFLESQVTELKSQLSAYDPVIASLAGDVKALEKSTHALTKFPATAYQQRVGNNLEESGSTTSPCNGIVILKEINPSIKTIEQAFVKEKGRLSRQITRSTSQKRRDRRKIENIQPDDQVTGESRQPRLRPEMTEVKNELLMKDNPRDQVTDSLTYGRSQGTSHGSNDMFEFWDESAESETSVNFLINSNKPQRSLNSNLRHQSRNPSIESDKAVGVVDKLELSRNIEDKAKILERLLSDSRRLSSLRISLTDLKRKLEMNEKQRRFSNADLVIVKRQLKEMEEAVSQLENTNEILSKEIEETGDARDIYRKVVVEKSRSGSEKIEQLQNKMQNIEQTVLKLEDGTKSKGRKMFSETRTVILLRDIIHKGGKRSARKKKNRFCGCIRSSTKEE
Protein: BHLH transcription factor (Barren stalk1) (Q5MP56)
Organism: Zea mays (Maize)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MDPYHYQTMYDPRGFPIIHPQPYLQHPVAGALGDSRVRGGGSGARRRPGAKLSTDPQSVAARERRHRISDRFRVLRSLVPGGSKMDTVSMLEQAIHYVKFLKTQISLHQAALMQHEEGCHAELAAYSAVAVVGDNEVTLASHGRTGACDEMMQLQVAAEEALSYGVDAHQPYGLDPRQLSGGHELPPLPASCIFLEEPADACYSVCDLDDGDTGLPGSY
Protein: Killer cell lectin-like receptor subfamily C, member 2 (Natural killer cell protein group 2-C1) (Natural killer cell receptor NKG2C) (Q9WTJ9)
Organism: Mus musculus (Mouse)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004401}; Single-pass type II membrane protein {ECO:0000256|ARBA:ARBA00004401}.
Interaction partners:
- TYRO protein tyrosine kinase-binding protein
- Natural killer cells antigen CD94
- Killer cell lectin-like receptor subfamily C, member 1
- Killer cell lectin-like receptor subfamily C, member 3
- CD226 antigen
- Natural cytotoxicity triggering receptor 1
- NKG2-D type II integral membrane protein
- High affinity immunoglobulin epsilon receptor subunit gamma
- T-cell surface glycoprotein CD3 zeta chain
- Nectin-2
Sequence:
MSHLLGTEQASEPRKATKKTQAQFRFSNAAGDRLLEFSLQHASQKHLKASRHGYCKNFASPPEKLIAGILGTIWFTLLIALVISTRIVSPYAELKKQIHPFLVRTQKGSHALLSKAQPCPHCPKEWISYSHNCYFIGMERKSWNDSLGSCLSKNCSLLHIDSEEEQDFLQSLSLVSWTGILRKGRGQAWDWKKDSIFKPKIAEISHDECNCAMMSASGLTADNCTTLHPYLCKCKFPI
Protein: Eukaryotic translation initiation factor 4E-2 (eIF-4E-2) (eIF4E-2) (eIF-4F 25 kDa subunit 2) (mRNA cap-binding protein 2) (O74743)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Recognizes and binds the 7-methylguanosine-containing mRNA cap during an early step in the initiation of protein synthesis and facilitates ribosome binding by inducing the unwinding of the mRNAs secondary structures.
Interaction partners:
- Eukaryotic translation initiation factor 4 gamma
- ATP-dependent RNA helicase eIF4A
- Eukaryotic translation initiation factor 4E-1
- UPF0321 protein C569.02c
- Polyadenylate-binding protein, cytoplasmic and nuclear
- ATP-dependent RNA helicase ded1
- Putative cell agglutination protein pfl4
- Thiamine pyrophosphokinase
- Probable eukaryotic translation initiation factor 5
- Nuclear cap-binding protein subunit 1
Sequence:
MADAEDSRHSKNEGFPNTSLITEKLDLLDLFGSPKVKTEREGRPARLLEGLSAVNAETAFVKTHPLQHEWTLWFLKPPTQGLEWSDLLKEIISFKTVEEFWGIFKTISKASMLPAKSDYSYFLKGIRPEWEDPQNMNGGKWAYQSKHKGSNLDELWLYMVLAAIGETLDPTGKEVTGVVCNMRKGFYRIAVWTRNCNDKDVLEKIGLRFKEVLGISDKETIEYSAHEDSSKAGSMRAKTRMSL
Protein: Interferon, alpha-inducible protein 27 (G3V761)
Organism: Rattus norvegicus (Rat)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
Sequence:
MALSGTGTLVASIASKVASSVAVVKAGGAVSSTILASSQGLNLLAQTALGSGASALGSALGALKAGTVLSSLPASALAVCPIGVKTAVAMLGGAMTVAAVPPVLSAVGFTGSGIAASSLAAKLMSVSAIANGGGVPAGGLVATLQSAGAAGLSMTSKVLVGSTGSAVVASVMGVCKHLYSFL
Protein: Protein CHROMATIN REMODELING 5 (AtCHR5) (EC 3.6.4.-) (F4IV99)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: DNA-binding helicase that specifically binds to the promoter of target genes, leading to chromatin remodeling, possibly by promoting deposition of histone H3.3 (By similarity). Probable chromatin remodeling factor.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00768}.
Interaction partners:
- Chromatin structure-remodeling complex protein SYD
- Histone H4
- FACT complex subunit SSRP1
- PHD-finger and DNA binding domain-containing protein
- At5g20670)
Sequence:
MAFFRNYSNDTVSHNVLDENEERQNAATFQSSPLNEDVDGTYSERGFDMNMDVQYQSDPEPGCSIRQPNETAVDNVADPVDSHYQSSTKRLGVTGRWGSTFWKDCQPMGQREGSDPAKDSQSGYKEAYHSEDNHSNDRSEKLDSENENDNENEEEDNEMNKHQSGQADVPADEMLSDEYYEQDEDNQSDHVHYKGYSNPTNSRSLPKAGSAVHSNSRTSRAIHKNIHYSDSNHDHNGDADMDYEEEEDEDDPEDADFEPYDAADDGGASKKHGQGWDVSDEDPESDEEIDLSDYEDDYGTKKPKVRQQSKGFRKSSAGLERKSFHVSSRQKRKTSYQDDDSEEDSENDNDEGFRSLARRGTTLRQNNGRSTNTIGQSSEVRSSTRSVRKVSYVESEDSEDIDDGKNRKNQKDDIEEEDADVIEKVLWHQLKGMGEDVQTNNKSTVPVLVSQLFDTEPDWNEMEFLIKWKGQSHLHCQWKTLSDLQNLSGFKKVLNYTKKVTEEIRYRTALSREEIEVNDVSKEMDLDIIKQNSQVERIIADRISKDGLGDVVPEYLVKWQGLSYAEATWEKDVDIAFAQVAIDEYKAREVSIAVQGKMVEQQRTKGKASLRKLDEQPEWLIGGTLRDYQLEGLNFLVNSWLNDTNVILADEMGLGKTVQSVSMLGFLQNTQQIPGPFLVVVPLSTLANWAKEFRKWLPGMNIIVYVGTRASREVCQQYEFYNEKKVGRPIKFNALLTTYEVVLKDKAVLSKIKWIYLMVDEAHRLKNSEAQLYTALLEFSTKNKLLITGTPLQNSVEELWALLHFLDPGKFKNKDEFVENYKNLSSFNESELANLHLELRPHILRRVIKDVEKSLPPKIERILRVEMSPLQKQYYKWILERNFHDLNKGVRGNQVSLLNIVVELKKCCNHPFLFESADHGYGGDINDNSKLDKIILSSGKLVILDKLLVRLRETKHRVLIFSQMVRMLDILAEYLSLRGFQFQRLDGSTKAELRQQAMDHFNAPASDDFCFLLSTRAGGLGINLATADTVVIFDSDWNPQNDLQAMSRAHRIGQQEVVNIYRFVTSKSVEEEILERAKRKMVLDHLVIQKLNAEGRLEKRETKKGSNFDKNELSAILRFGAEELFKEDKNDEESKKRLLSMDIDEILERAEQVEEKHTDETEHELLGAFKVANFCNAEDDGSFWSRWIKPDSVVTAEEALAPRAARNTKSYVDPSHPDRTSKRKKKGSEPPEHTERSQKRRKTEYFVPSTPLLEGTSAQVRGWSYGNLPKRDAQRFYRTVMKFGNHNQMACIAEEVGGVVEAAPEEAQVELFDALIDGCKESVETGNFEPKGPVLDFFGVPVKANELLKRVQGLQLLSKRISRYNDPISQFRVLSYLKPSNWSKGCGWNQIDDARLLLGILYHGFGNWEKIRLDESLGLTKKIAPVELQHHETFLPRAPNLKERATALLEMELAAAGGKNTNAKASRKNSKKVKDNLINQFKAPARDRRGKSGPANVSLLSTKDGPRKTQKAEPLVKEEGEMSDDGEVYEQFKEQKWMEWCEDVLADEIKTLGRLQRLQTTSADLPKEKVLFKIRRYLEILGRRIDAIVLEHEEDLYKQDRMTMRLWNYVSTFSNLSGDRLNQIYSKLKQEKEEEEGVGPSHLNGSRNFQRQQKFKTAGNSQGSQQVHKGIDTAKFEAWKRRRRTENDVQTERPTITNSNSLGILGPGPLDRSHRARQTGFPPR
Protein: Cofilin-1A (P0DJ26)
Organism: Dictyostelium discoideum (Social amoeba)
Function: Controls reversibly actin polymerization and depolymerization in a pH-sensitive manner. It has the ability to bind G- and F-actin in a 1:1 ratio of cofilin to actin. It is the major component of intranuclear and cytoplasmic actin rods (By similarity).
Subcellular location: Nucleus matrix {ECO:0000250}. Cytoplasm, cytoskeleton {ECO:0000250}.
Interaction partners:
- Actin-interacting protein 1
- Severin
- HP domain-containing protein
- Profilin-3
- Adenylyl cyclase-associated protein
- Profilin-1
- Profilin-2
- Twinfilin
- Gelation factor
- Probable vinculin
Sequence:
MSSGIALAPNCVSTFNDLKLGRKYGGIIYRISDDSKEIIVDSTLPAGCSFDEFTKCLPENECRYVVLDYQYKEEGAQKSKICFVAWCPDTANIKKKMMATSSKDSLRKACVGIQVEIQGTDASEVKDSCFYEKCTKI
Protein: Sugar baby, isoform F (Q7KUF9)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
Sequence:
MKATIDKELLPMKAHYFLFNAGTAPVVPFMPTLAGQLGYSPAVVGTMYTILPIIGMLAKPLFGYIADRYHRHRPLFLGGQVLTGIAFFLIMFVPGMEKPLPKVEFHCHQGVSDIPRFCSEYGECVERNLERYYGNRTLECELNCEAQPFMWDIVCEDWLKNNTENCAANRTNTQMEFGASITMQKIENDGSCMFFMIPHDQGQIAGQNVTLYCPKEKEYFKSNCTMDCREDYLKEQLAESAVINTSSAVTMPQFWLFFGLLIFSWIGMAVVVSIGDAICFGILGDRHHLYGKQRLCGSLGWGVFALLAGLLVDHMSLGEVNKNYTAVFWMALLIMGFDVFASSKLRHTPTHLSSNILKDVGQMFLSVRCVIFFLWCVAIGLGTALIWNFLFIYLEELDKAFEGCDSSIKTLEGLVMGIQCFGGELPFFFLSGWILKKIGHVNAMSVVLFGFGVRFILYSMLQNPWYILPIELMNGVTFGLFYATMASYASIVAPPGTDATMQSLVGAIFEGVGVSMGSLIAGQLFESVTARTTFEIFGIGAFIVFVIHVCIQLYLQRNSNIDENGKGTVKYFAPTDAMHMLNDQEYSRVS
Protein: Tyrosine-protein kinase Yes (EC 2.7.10.2) (Proto-oncogene c-Yes) (p61-Yes) (P07947)
Organism: Homo sapiens (Human)
Function: Non-receptor protein tyrosine kinase that is involved in the regulation of cell growth and survival, apoptosis, cell-cell adhesion, cytoskeleton remodeling, and differentiation. Stimulation by receptor tyrosine kinases (RTKs) including EGRF, PDGFR, CSF1R and FGFR leads to recruitment of YES1 to the phosphorylated receptor, and activation and phosphorylation of downstream substrates. Upon EGFR activation, promotes the phosphorylation of PARD3 to favor epithelial tight junction assembly. Participates in the phosphorylation of specific junctional components such as CTNND1 by stimulating the FYN and FER tyrosine kinases at cell-cell contacts. Upon T-cell stimulation by CXCL12, phosphorylates collapsin response mediator protein 2/DPYSL2 and induces T-cell migration. Participates in CD95L/FASLG signaling pathway and mediates AKT-mediated cell migration. Plays a role in cell cycle progression by phosphorylating the cyclin-dependent kinase 4/CDK4 thus regulating the G1 phase. Also involved in G2/M progression and cytokinesis. Catalyzes phosphorylation of organic cation transporter OCT2 which induces its transport activity.
Subcellular location: Cell membrane. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome. Cytoplasm, cytosol. Cell junction {ECO:0000250|UniProtKB:Q28923}. Note=Newly synthesized protein initially accumulates in the Golgi region and traffics to the plasma membrane through the exocytic pathway. Localized to small puncta throughout the cytoplasm and cell membrane when in the presence of SNAIL1 (By similarity). {ECO:0000250|UniProtKB:Q28923}.
Interaction partners:
- Tyrosine-protein kinase Fyn
- Transcriptional coactivator YAP1
- Proto-oncogene tyrosine-protein kinase Src
- Catenin delta-1
- SHC-transforming protein 1
- E3 ubiquitin-protein ligase CBL-C
- Fibronectin
- Tyrosine-protein kinase Fer
- Epidermal growth factor receptor
- Tyrosine-protein phosphatase non-receptor type 11
Sequence:
MGCIKSKENKSPAIKYRPENTPEPVSTSVSHYGAEPTTVSPCPSSSAKGTAVNFSSLSMTPFGGSSGVTPFGGASSSFSVVPSSYPAGLTGGVTIFVALYDYEARTTEDLSFKKGERFQIINNTEGDWWEARSIATGKNGYIPSNYVAPADSIQAEEWYFGKMGRKDAERLLLNPGNQRGIFLVRESETTKGAYSLSIRDWDEIRGDNVKHYKIRKLDNGGYYITTRAQFDTLQKLVKHYTEHADGLCHKLTTVCPTVKPQTQGLAKDAWEIPRESLRLEVKLGQGCFGEVWMGTWNGTTKVAIKTLKPGTMMPEAFLQEAQIMKKLRHDKLVPLYAVVSEEPIYIVTEFMSKGSLLDFLKEGDGKYLKLPQLVDMAAQIADGMAYIERMNYIHRDLRAANILVGENLVCKIADFGLARLIEDNEYTARQGAKFPIKWTAPEAALYGRFTIKSDVWSFGILQTELVTKGRVPYPGMVNREVLEQVERGYRMPCPQGCPESLHELMNLCWKKDPDERPTFEYIQSFLEDYFTATEPQYQPGENL
Protein: Dolichol-phosphate mannosyltransferase subunit 1 (EC 2.4.1.83) (A0A1D8PEA2)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Subcellular location: Endoplasmic reticulum {ECO:0000256|RuleBase:RU365083}.
Interaction partners:
- Dolichol-phosphate mannosyltransferase subunit 3
- Dolichol phosphate-mannose biosynthesis regulatory protein
- Dol-P-Man:Man
- UDP-N-acetylglucosamine--dolichyl-phosphate N-acetylglucosaminephosphotransferase
- Chitobiosyldiphosphodolichol beta-mannosyltransferase
- dolichol kinase
- dolichyl-phosphate beta-glucosyltransferase
- Cwh8p
- Mannose-1-phosphate guanyltransferase
- GPI mannosyltransferase 3
Sequence:
MTQNKYSVILPTYNEKRNLPILIYLLNKTFTANKLDWEVIIVDDNSPDGTQEIAKKLIDIFGPEHIQLRPRAGKLGLGTAYVHGLQFVTGNFVIIMDADFSHHPEAIPEFIAKQKSQDYDIVTGTRYAGDGGVFGWDFKRKLISRGANFLASVVLRPHVSDLTGSFRLYKTDVLRKIIDVTQSKGYVFQMEMMVRAKAMGFTVGEVPISFVDRLYGESKLGGDEIVQYAKGVWTLFTSV