wanglab/gogpt-training-data huggingface dataset:
Protein: Platelet glycoprotein Ib alpha chain (GP-Ib alpha) (GPIb-alpha) (GPIbA) (Glycoprotein Ibalpha) (CD antigen CD42b) [Cleaved into: Glycocalicin] (O35930)
Organism: Mus musculus (Mouse)
Function: GP-Ib, a surface membrane protein of platelets, participates in the formation of platelet plugs by binding to the A1 domain of vWF, which is already bound to the subendothelium.
Subcellular location: Membrane; Single-pass type I membrane protein.
Interaction partners:
- Platelet glycoprotein IX
- von Willebrand factor
- Platelet glycoprotein Ib beta chain
- Prothrombin
- P-selectin
- Filamin-A
- Integrin alpha-M
- Platelet glycoprotein V
- Integrin alpha-IIb
- SCO-spondin
Sequence:
MALLILLFLLPSPLHSQHTCSISKVTSLLEVNCENKKLTALPADLPADTGILHLGENQLGTFSTASLVHFTHLTYLYLDRCELTSLQTNGKLIKLENLDLSHNNLKSLPSLGWALPALTTLDVSFNKLGSLSPGVLDGLSQLQELYLQNNDLKSLPPGLLLPTTKLKKLNLANNKLRELPSGLLDGLEDLDTLYLQRNWLRTIPKGFFGTLLLPFVFLHANSWYCDCEILYFRHWLQENANNVYLWKQGVDVKDTTPNVASVRCANLDNAPVYSYPGKGCPTSSGDTDYDDYDDIPDVPATRTEVKFSTNTKVHTTHWSLLAAAPSTSQDSQMISLPPTHKPTKKQSTFIHTQSPGFTTLPETMESNPTFYSLKLNTVLIPSPTTLEPTSTQATPEPNIQPMLTTSTLTTPEHSTTPVPTTTILTTPEHSTIPVPTTAILTTPKPSTIPVPTTATLTTLEPSTTPVPTTATLTTPEPSTTLVPTTATLTTPEHSTTPVPTTATLTTPEHSTTPVPTTATLTTPEPSTTLTNLVSTISPVLTTTLTTPESTPIETILEQFFTTELTLLPTLESTTTIIPEQNSFLNLPEVALVSSDTSESSPFLNSDFCCFLPLGFYVLGLLWLLFASVVLILLLTWTWHVTPHSLDMEQSAALATSTHTTSLEVQRARQVTMPRAWLLFLQGSLPTFRSSLFLWVRPNGRVGPLVAGRRPSALSQGRGQDLLGTVGIRYSGHSL
Protein: Cbb3-type cytochrome c oxidase subunit CcoN1 (EC 7.1.1.9) (Cytochrome CBB3 subunit CcoN1) (D9IA43)
Organism: Stutzerimonas stutzeri (Pseudomonas stutzeri)
Function: Cbb3-type cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Subunits CcoN and CcoO form the functional core of the enzyme complex. Subunits CcoP and CcoQ may optionally bind to the core. CcoN is the catalytic subunit of the enzyme. Electrons originating in cytochrome c or a quinol are transferred to the bimetallic center formed by a high-spin heme and copper B. The complex also functions as a proton pump.
Subcellular location: Cell inner membrane {ECO:0000250|UniProtKB:P0ABI8}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
Sequence:
MNTATSTAYSYKVVRQFAIMTVVWGIVGMGLGVFIAAQLAWPFLNFDLPWTSFGRLRPLHTNAVIFAFGGCALFATSYYSVQRTCQTTLFAPKLAAFTFWGWQLVILLAAISLPLGFTSSKEYAELEWPIDILITIVWVAYAVVFFGTLAKRKVKHIYVGNWFFGAFILTVAILHVVNNLEIPVTAMKSYSLYAGATDAMVQWWYGHNAVGFFLTAGFLGIMYYFVPKQAERPVYSYRLSIVHFWALITVYIWAGPHHLHYTALPDWAQSLGMVMSLILLAPSWGGMINGMMTLSGAWHKLRSDPILRFLVVSLAFYGMSTFEGPMMAIKTVNALSHYTDWTIGHVHAGALGWVAMVSIGALYHLVPKVFGREQMHSIGLINTHFWLATIGTVLYIASMWVNGIAQGLMWRAINDDGTLTYSFVESLEASHPGFVVRMIGGAIFFAGMLVMAYNTWRTVQAAKPAEYDAAAQIA
Protein: Cutinase pbc1 (EC 3.1.1.74) (Cutin hydrolase) (Q9Y7G8)
Organism: Pyrenopeziza brassicae
Function: Catalyzes the hydrolysis of complex carboxylic polyesters found in the cell wall of plants (Probable). Degrades cutin, a macromolecule that forms the structure of the plant cuticle (Probable). Allows pathogenic fungi to penetrate through the cuticular barrier into the host plant during the initial stage of fungal infection (Probable).
Subcellular location: Secreted {ECO:0000250|UniProtKB:P11373}.
Interaction partners:
Sequence:
MKVTALGNTLTGFGQALATTLGVDTTSSSPNCAEMMVVFARGTSEPGNVGLFSGPTFFDALEVMMGAGAVSVQGVEYGASIEGFLQGGDPAGSAAMAGIVEGTVQNCPNAKIVMSGYSQGGQLVHNAAAMLPAATMAKISSLVIFGDPNDGKPIANADPSKVMVVCHPGHNICDGRDLVLVEHLTYSRDAVEAATFAAARAKA
Protein: F-box only protein 5 (Early mitotic inhibitor 1) (Q7TSG3)
Organism: Mus musculus (Mouse)
Function: Regulator of APC activity during mitotic and meiotic cell cycle. During mitotic cell cycle plays a role as both substrate and inhibitor of APC-FZR1 complex. During G1 phase, plays a role as substrate of APC-FZR1 complex E3 ligase. Then switches as an inhibitor of APC-FZR1 complex during S and G2 leading to cell-cycle commitment. As APC inhibitor, prevents the degradation of APC substrates at multiple levels: by interacting with APC and blocking access of APC substrates to the D-box co-receptor, formed by FZR1 and ANAPC10; by suppressing ubiquitin ligation and chain elongation by APC by preventing the UBE2C and UBE2S activities. Plays a role in genome integrity preservation by coordinating DNA replication with mitosis through APC inhibition in interphase to stabilize CCNA2 and GMNN in order to promote mitosis and prevent rereplication and DNA damage-induced cellular senescence (By similarity). During oocyte maturation, plays a role in meiosis through inactivation of APC-FZR1 complex. Inhibits APC through RPS6KA2 interaction that increases FBXO5 affiniy for CDC20 leading to the metaphase arrest of the second meiotic division before fertilization. Controls entry into the first meiotic division through inactivation of APC-FZR1 complex. Promotes migration and osteogenic differentiation of mesenchymal stem cells (By similarity).
Subcellular location: Nucleus {ECO:0000250|UniProtKB:Q9UKT4}. Cytoplasm {ECO:0000269|PubMed:15526037}. Cytoplasm, cytoskeleton, spindle {ECO:0000269|PubMed:15526037}. Note=In interphase, localizes in a punctate manner in the nucleus and cytoplasm with some perinuclear concentration. In mitotic cells, localizes throughout the cell, particularly at the spindle. {ECO:0000250|UniProtKB:Q9UKT4}.
Interaction partners:
- Cell division cycle protein 20 homolog
- S-phase kinase-associated protein 1
- Anaphase-promoting complex subunit 4
- Fizzy-related protein homolog
- F-box/WD repeat-containing protein 1A
- Cullin-1
- Serine/threonine-protein kinase PLK1
- F-box/WD repeat-containing protein 11
- E3 ubiquitin-protein ligase RBX1
- Cell division cycle protein 16 homolog
Sequence:
MSRRTCSDLRRPSSCPCRLGARTTVDGCKEESPVLSVTMKCFNCNPDLSELEVVKPEDSGIEASYSPVCLEPSCNDCVRNHERLSFIDSPIVGHDNKENQRVQNTLDSSNETEELEASRLYEDSGYSSFTQSDRDDGILILENFRNSPQARLLPSQSPDQHPNKTLLPVLHFERVVCSTLKKNGKRNPKVDREMLKEVIASGNFRLQNIIGKKMGLEHLDILAELSRRGFVHLLANILTKLSGMDLVNLSKVSRIWKKILENNKGAFQLYSKTMQRVIESSKLSLHATTRGYVVGRAALTCVQKSSTWAPPKKDVQIKSSSQRGQRVSTYSRHNEFVEVAKTLKNNESLKACVRCNFPAKYDHYLERAVCKRESCQFEYCTKCLCAYHNNKDCLNGKILKASCKVGPLPGTKKSKKNLQRL
Protein: Calcineurin binding protein, putative (Q4X0L5)
Organism: Aspergillus fumigatus (strain ATCC MYA-4609 / CBS 101355 / FGSC A1100 / Af293) (Neosartorya fumigata)
Interaction partners:
- Serine/threonine-protein phosphatase 2B catalytic subunit
- Calcineurin subunit B
Sequence:
MADITTTSPPHSLPQSPSFRIHRASRSSSSSRPALSLDLSNLPALSRPTPPSNTLLITDLHDLYLFQPASLASIRSQIESIAPLNSFSPLPSLRRIVCSFHSEDDALRVRKLLDGQSLLNRNVCTKIYFGEPTPLLDEGRPKLLEAPHLDKLFFISPPPSPPHGWVMRTEDPPNKEVHASDLAQALAQLKTEQSAPVSGPVDPGTPMSMSDEKRTGSWPIAMSGQRSRSSTLIYNPEDHGGSPGLPAVMVEDTTVDSDDEDIEMMSPIDMSVRKLPPKTARPPVELMH
Protein: Lysozyme-like protein 3 (Q9XXS1)
Organism: Caenorhabditis elegans
Function: Plays a role in the stress response to heavy metals such as copper, probably in a kgb-1-dependent manner.
Interaction partners:
- Protein kreg-1
- Invertebrate-type lysozyme 3
- Invertebrate-type lysozyme 2
Sequence:
MKLFALLVSITLCYSFPAPLQTNVSEPFGLLQKVSEQVIDPDYNIPEVKDAPAIPYDERNSPTHAYSVDISFHTTPSDMDCLRDQGYKSVFVRALNPIGNTYFDRNALNTINNAFEAGLGSEVYITPNINSTRSGADQISLVYQNLLANGINVRSIWIQVTSPTNWVAPMAVRIEFIQDMIRSAKNLGLSVGIYTSFYDWLEITGGWNTFSSDVFLWYWHVLSMGTDGETTPTLEDFRPFGPWRQATVKQFGQVEKLCGMIVNRNVYSTGNQHLSQIVHFSTHQENSSSEKKLIRVGGIGF
Protein: U3 small nucleolar RNA-associated protein 22 (U3 snoRNA-associated protein 22) (U three protein 22) (P53254)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Involved in nucleolar processing of pre-18S ribosomal RNA and ribosome assembly.
Subcellular location: Nucleus, nucleolus {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:15590835}.
Interaction partners:
- Nucleolar protein 56
- Ribosome biogenesis protein BMS1
- rRNA biogenesis protein RRP5
- U3 small nucleolar RNA-associated protein 15
- U3 small nucleolar RNA-associated protein 11
- Small ribosomal subunit protein uS4B
- U3 small nucleolar RNA-associated protein 4
- Pre-rRNA-processing protein PNO1
- Small ribosomal subunit protein uS15
- Casein kinase II subunit beta
Sequence:
MATSVKRKASETSDQNIVKVQKKHSTQDSTTDNGSKENDHSSQAINERTVPEQENDESDTSPESNEVATNTAATRHNGKVTATESYDIHIARETAELFKSNIFKLQIDELLEQVKLKQKHVLKVEKFLHKLYDILQEIPDWEEKSLAEVDSFFKNKIVSVPFVDPKPIPQNTNYKFNYKKPDISLIGSFALKAGIYQPNGSSIDTLLTMPKELFEKKDFLNFRCLHKRSVYLAYLTHHLLILLKKDKLDSFLQLEYSYFDNDPLLPILRISCSKPTGDSLSDYNFYKTRFSINLLIGFPYKVFEPKKLLPNRNCIRIAQESKEQSLPATPLYNFSVLSSSTHENYLKYLYKTKKQTESFVEATVLGRLWLQQRGFSSNMSHSGSLGGFGTFEFTILMAALLNGGGINSNKILLHGFSSYQLFKGVIKYLATMDLCHDGHLQFHSNPENSSSSPASKYIDEGFQTPTLFDKSTKVNILTKMTVSSYQILKEYAGETLRMLNNVVQDQFSNIFLTNISRFDNLKYDLCYDVQLPLGKYNNLETSLAATFGSMERVKFITLENFLAHKITNVARYALGDRIKYIQIEMVGQKSDFPITKRKVYSNTGGNHFNFDFVRVKLIVNPSECDKLVTKGPAHSETMSTEAAVFKNFWGIKSSLRRFKDGSITHCCVWSTSSSEPIISSIVNFALQKHVSKKAQISNETIKKFHNFLPLPNLPSSAKTSVLNLSSFFNLKKSFDDLYKIIFQMKLPLSVKSILPVGSAFRYTSLCQPVPFAYSDPDFFQDVILEFETSPKWPDEITSLEKAKTAFLLKIQEELSANSSTYRSFFSRDESIPYNLEIVTLNILTPEGYGFKFRVLTERDEILYLRAIANARNELKPELEATFLKFTAKYLASVRHTRTLENISHSYQFYSPVVRLFKRWLDTHLLLGHITDELAELIAIKPFVDPAPYFIPGSLENGFLKVLKFISQWNWKDDPLILDLVKPEDDIRDTFETSIGAGSELDSKTMKKLSERLTLAQYKGIQMNFTNLRNSDPNGTHLQFFVASKNDPSGILYSSGIPLPIATRLTALAKVAVNLLQTHGLNQQTINLLFTPGLKDYDFVVDLRTPIGLKSSCGILSATEFKNITNDQAPSNFPENLNDLSEKMDPTYQLVKYLNLKYKNSLILSSRKYIGVNGGEKGDKNVITGLIKPLFKGAHKFRVNLDCNVKPVDDENVILNKEAIFHEIAAFGNDMVINFETD
Protein: SUMO1 activating enzyme subunit 1 (M0R054)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MLDHEQVTPEDPGAQFLIRTGSVGRNRAEASLERAQNLNPMVDVKVDTEDIEKKPESFFTQFDAVCLTCCSRDVIVKVDQICHKNSIKFFTGDVFGYHGYTFANLGEHEFVEEKTKVAKVSQGVEDGPDTKRAKLDSSETTMVKKKVVFCPVKEALE
Protein: Histone deacetylase 8 (EC 3.5.1.98) (Q94EJ2)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Responsible for the deacetylation of lysine residues on the N-terminal part of the core histones (H2A, H2B, H3 and H4). Histone deacetylation gives a tag for epigenetic repression and plays an important role in transcriptional regulation, cell cycle progression and developmental events. Histone deacetylases act via the formation of large multiprotein complexes.
Subcellular location: Nucleus {ECO:0000269|PubMed:22363501}. Cytoplasm {ECO:0000269|PubMed:22363501}.
Interaction partners:
- Histone deacetylase 17
- Putative histone deacetylase 10
- AT-rich interactive domain-containing protein 1
- NAD-dependent protein deacetylase SRT1
- NAD-dependent protein deacylase SRT2
- Histone-lysine N-methyltransferase SUVR3
- High mobility group B protein 9
- High mobility group B protein 10
- High mobility group B protein 15
- Putative high mobility group B protein 11
Sequence:
MVTNRVDVFWHEGMLRHDAVEGVFDTGYDPGFLDVLEKHPENADRVRNMLSILRRGPIAPHVNWFTGLPAIVSELLMFHTSEYIEKLVEADKSGERCEIAAGTFMSPGSWEAALLAAGTTLSAMQHILDCHGKIAYALVRPPGHHSQPTQADGYCFLNNAALAVKLALNSGSCSRVAVIDIDVHYGNGTAEGFYTSDKVLTVSLHMNHGSWGSSHPQKGSIDELGEDVGLGYNLNVPLPNGTGDRGYEYAMNELVVPAVRRFGPDMVVLVVGQDSSAFDPNGRQSLTMNGYRRIGQIMRGVAEEHSHGRLLMVQEGGYHVTYAAYCLHAMLEGVLKIPEPHLSDPIAYYPEEEANAVAAVESIKTYHTEFVPFLRGT
Protein: Probable mRNA interferase toxin HicA (EC 3.1.-.-) (Endoribonuclease HicA) (Toxin HicA) (P76106)
Organism: Escherichia coli (strain K12)
Function: Toxic component of a type II toxin-antitoxin (TA) system. A probable translation-independent mRNA interferase. Overexpression causes cessation of cell growth and inhibits cell proliferation via inhibition of translation; this blockage is overcome (after 90 minutes) by subsequent expression of antitoxin HicB. Overexpression causes cleavage of a number of mRNAs and tmRNA, in a translation-independent fashion, suggesting this is an mRNA interferase.
Interaction partners:
- Antitoxin HicB
- mRNA interferase toxin RelE
- mRNA interferase toxin HigB
- Endoribonuclease toxin MazF
- Antitoxin HigA
- Toxin YoeB
- mRNA interferase toxin MqsR
- mRNA interferase toxin YafQ
- Serine/threonine-protein kinase toxin HipA
- Endoribonuclease toxin ChpB
Sequence:
MKQSEFRRWLESQGVDVANGSNHLKLRFHGRRSVMPRHPCDEIKEPLRKAILKQLGLS
Protein: rRNA-processing protein FCF2 (FAF1 copurifying factor 2) (Q12035)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Essential protein involved in pre-rRNA processing and 40S ribosomal subunit assembly. Required for the early cleavage steps of 35S rRNA at the A(0), A(1), and A(2) sites.
Subcellular location: Nucleus, nucleolus {ECO:0000269|PubMed:14562095}.
Interaction partners:
- Something about silencing protein 10
- U3 small nucleolar RNA-associated protein 7
- Ribosome biogenesis protein BMS1
- U3 small nucleolar RNA-associated protein 11
- U3 small nucleolar ribonucleoprotein protein LCP5
- Protein BFR2
- Nucleolar protein 58
- rRNA-processing protein FCF1
- U3 small nucleolar RNA-associated protein 21
- KRR1 small subunit processome component
Sequence:
MDQSVEDLFGALRDASASLEVKNSAKEQVSLQQEDVLQIGNNDDEVEIESKFQEIETNLKKLPKLETGFDALANKKKKKNVLPSVETEDKRKPNKSDKNDNDWFTLPKPDDNMRREVQRDLLLIKHRAALDPKRHYKKQRWEVPERFAIGTIIEDKSEFYSSRMNRKERKSTILETLMGDEASNKYFKRKYNEIQEKSTSGRKAHYKKMKEMRKKRR
Protein: Glyceraldehyde-3-phosphate:ferredoxin oxidoreductase (GAPOR) (EC 1.2.7.6) (Tungsten-containing glyceraldehyde-3-phosphate ferredoxin oxidoreductase) (Q8U3K2)
Organism: Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1)
Function: Glycolytic enzyme that acts in the place of glyceraldehyde-3-phosphate dehydrogenase (GAPDH) and phosphoglycerate kinase (PGK). Plays a role in anabolic gluconeogenesis.
Interaction partners:
- Glyceraldehyde-3-phosphate dehydrogenase
- Phosphoglycerate kinase
- Fructose-1,6-bisphosphate aldolase/phosphatase
- Non-phosphorylating glyceraldehyde-3-phosphate dehydrogenase
- Triosephosphate isomerase
- Fructose-bisphosphate aldolase class 1
- 2,3-bisphosphoglycerate-independent phosphoglycerate mutase
- Glucose-6-phosphate isomerase
- Transketolase N-terminal section
- Transketolase C-terminal section
Sequence:
MKFSVLKLDVGKREVEAQEIEREDIFGVVDYGIMRHNELRTYEVDPYDPRNIVIFGIGPFAGSVLPGSHRLVFFFRSPLYGGLFPSTMGGAGYQFKNVGVDFVEIHGKAEKPTVIILKNDGEKLSVDFYEIELEKLLDVWKEYKGEEGVYALTQYLLDNLASVFEGMEFRIAVVGPAALNTNMGAIFSQALRNGKRAVGSEDWAARGGPGSVLLRAHNVVAIAFGGKKRKREFPGEDISDVKVAKRVVEGIHKKAQRDVINESTVKYRYNPKLNTGGTFGGNYPAEGDLVPVLNWQMPYIPKEERIKIHELIMKYYWEPFNKESIQPKNWTTCGEPCPVVCKKHRKGHHVEYEPYEANGPLSGSIYLYASDISVHAVDAMGFDAIEFGGTAAWVLELVHKGLLKPAEVGISDVPEFTKDDLITKPVEASEKNAKLVAELAHSIAFGKTEVARIIGMGKRKASKILDEKFKDRLSYGESFKDYGVYTPLGDDGEINPTMYWAIGNFIPLPIQGRYWTFYQFGVFLEPEELAQKIVSSALWEFWYDNVGWCRFHRGWMKKVLKALFMEAYGVSIDMEEHAKKQIRKLIDYLKKAGYEPVFWDSMRVIDLVAKGSEEFGNENWAKKFKEDKIGTAKEYLKRVLDAYSQLIGTEWTL
Protein: PmrA (Two-component response regulator) (Two-component system response regulator BasR) (Q8Z1P4)
Organism: Salmonella typhi
Interaction partners:
- Sensor protein BasS
- Polymyxin B resistance protein
- Phosphoethanolamine transferase EptA
- Virulence sensor histidine kinase PhoQ
- PhoP/PhoQ regulator MgrB
- UDP-4-amino-4-deoxy-L-arabinose--oxoglutarate aminotransferase aminotransferase)
- histidine kinase
- Sensor protein QseC
- Lipid A acyltransferase PagP
- Aerobic respiration control sensor protein
Sequence:
MKILIVEDDTLLLQGLILAAQTEGYACDGVSTARAAEHSLESGHYSLMVLDLGLPDEDGLHFLTRIRQKKYTLPVLILTARDTLNDRISGLDVGADDYLVKPFALEELHARIRALLRRHNNQGESELTVGNLTLNIGRHQAWRDGQELTLTPKEYALLSRLMLKAGSPVHREILYNDIYNWDNEPSTNTLEVHIHNLRDKVGKSRIRTVRRFGYMLVATEES
Protein: Spindle pole body-associated protein CIK1 (Chromosome instability and karyogamy protein 1) (Q01649)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: A developmentally regulated protein important for microtubule functions. Targets KAR3 to the cytoplasmic microtubules during mating. Essential for KAR3 function during prophase of meiosis I. Required for interhomolog recombination, synapsis of homologous chromosomes and establishment of a meiosis I spindle.
Subcellular location: Nucleus {ECO:0000269|PubMed:11729143}. Cytoplasm, cytoskeleton, microtubule organizing center, spindle pole body {ECO:0000269|PubMed:11729143}. Cytoplasm, cytoskeleton, spindle {ECO:0000269|PubMed:11729143, ECO:0000269|PubMed:25313961}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:8106549}. Note=Localization to the spindle pole body is infrequent in meiotic cells (PubMed:11729143). Localizes to cytoplasmic microtubules during mating (PubMed:8106549). {ECO:0000269|PubMed:11729143, ECO:0000269|PubMed:8106549}.
Interaction partners:
- Kinesin-like protein KAR3
- Kinesin-like protein KIP1
- Kinesin-like protein KIP3
- Spindle pole body-associated protein VIK1
- Kinesin-like protein KIP2
- Protein BIM1
- Cell division control protein KAR1
- Kinesin-like protein CIN8
- Cell division control protein 31
- Shugoshin
Sequence:
MNNSKIPKLSFHSDPNNVTRDFPKTKRQKVQKREMDMILTPNNNKLNILHSSGSGIRRCYTDDTSATYTKKLTFGGDPKIIERVKNNERKVRKDIDSLLNAISEIEKESVRIHARELPAITLELDAKVKACRELQNEIDGLSTEMDLKDNQCDLQRKNVELSSKNIVSMHAVKVQEFENDLEEELSNAKREWTYKLMEVENLKPDERLTDEMRQLKTEFEEVNRKLFILQNENENECKNYKKELDKKFEIFKKVKNDARIELDGEQERLSKVLKDLQDTHGELKENIKTCRDEFNDFEKRIGEAEVNFHSMELAVVPLKKKLASTSQALTQVQEEKKQVEGEANNWKKKYVNELEKVQQELYTRQNLATSIEEIKGYTRCFAYANERQMPDEFHINYVDRCICENSGEKRVQVFDRVVLEEIHKDHKRLYNECIPFLEKYISKLINCSIIVVSQQPTAPMKKTLLKQLIEQYGENYKMTLNILHLDGSIKHSDVGLDNPTEIRDLSQDEECMNILTLDTKLGKDEESHSMNIYIGSMSTVQLNRELDDAPSVLSHILTKTKQCFVFKINAGENIEKALALAGKLKRTITLPQLD
Protein: Epsin-1 (EPS-15-interacting protein 1) (O88339)
Organism: Rattus norvegicus (Rat)
Function: Binds to membranes enriched in phosphatidylinositol 4,5-bisphosphate (PtdIns(4,5)P2). Modifies membrane curvature and facilitates the formation of clathrin-coated invaginations. Regulates receptor-mediated endocytosis (By similarity).
Subcellular location: Cytoplasm. Cell membrane; Peripheral membrane protein. Nucleus. Membrane, clathrin-coated pit. Note=Associated with the cytoplasmic membrane at sites where clathrin-coated pits are forming. Colocalizes with clathrin and AP-2 in a punctate pattern on the plasma membrane. Colocalizes with clathrin at the Golgi complex. Detected in presynaptic nerve terminals and in synaptosomes. May shuttle to the nucleus when associated with ZBTB16/ZNF145.
Interaction partners:
- Epidermal growth factor receptor pathway substrate 15
- Clathrin heavy chain 1
- Epidermal growth factor receptor substrate 15-like 1
- Intersectin-1
- AP-2 complex subunit beta
- Clathrin coat assembly protein AP180
- AP-2 complex subunit alpha-2
- Epsin-3
- Clathrin light chain A
- Epsin-2
Sequence:
MSTSSLRRQMKNIVHNYSEAEIKVREATSNDPWGPSSSLMSEIADLTYNVVAFSEIMSMIWKRLNDHGKNWRHVYKAMTLMEYLIKTGSERVSQQCKENMYAVQTLKDFQYVDRDGKDQGVNVREKAKQLVALLRDEDRLREERAHALKTKEKLAQTATASSAAVGSGPPPEAEQAWPQSSGEEELQLQLALAMSKEEADQPPSCGPEDDVQLQLALSLSREEHDKEERIRRGDDLRLQMAIEESKRETGGKEESSLMDLADVFTTPAPPQASDPWGGPASVPTAVPVAAAASDPWGAPAVPPAADPWGGAAPTPASGDPWRPAAPTGPSVDPWGGTPAPAAGEGPTSDPWGSADGGAPVSGPPSSDPWAPAPAFSDPWGGSPAKPSSNGTAVGGFDTEPDEFSDFDRLRTALPTSGSSTGELELLAGEVPARSPGAFDMSGVGGSLAESVGSPPPAATPTPTPPTRKTPESFLGPNAALVDLDSLVSRPGPTPPGAKASNPFLPSGAPATGPSVTNPFQPAPPATLTLNQLRLSPVPPVPGAPPTYISPLGGGPGLPPMMPPGPPAPNTNPFLL
Protein: YY1 associated protein 1 (B0QZ55)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MAGVGRSGGPWGRTRGGRSGRLGVSLGALSSLPLEELPRPLCCRRCRRHFGFALRGETIPVSVAGSASSQFAPLALHLSLLLSRISASRLTRWPPPDKREGSAVDPGKRRSLAATPSSSLPCTLIALGLRHEKEANELMEDLFETFQDEMGFSNMEDDGPEEEERVAEPQANFNTPQALRFEELLANLLNEQHQIAKELFEQLKMKKPSAKQQKEVEKVKPQCKEVHQTLILDPAQRKRLQQQMQQHVQLLTQIHLLATCNPNLNPEASSTRICLKELGTFAQSSIALHHQYNPKFQTLFQPCNLMGAMQLIEDFSTHVSIDCSPHKTVKKTANEFPCLPKQVAWILATSKVFMYPELLPVCSLKAKNPQDKILFTKAEDNLLALGLKHFEGTEFLNPLISKYLLTCKTARQLTVRIKNLNMNRAPDNIIKFYKKTKQLPVLGKCCEEIQPHQWKPPIEREEHRLPFWLKVQPSSSKSVGGRRSLKVLREYQGLP
Protein: Protein naked cuticle homolog 1 (Naked-1) (mNkd) (mNkd1) (Q99MH6)
Organism: Mus musculus (Mouse)
Function: Cell autonomous antagonist of the canonical Wnt signaling pathway. May activate a second Wnt signaling pathway that controls planar cell polarity. Required for spermatogenesis.
Subcellular location: Cell membrane {ECO:0000250}. Cytoplasm {ECO:0000250}.
Interaction partners:
- Segment polarity protein dishevelled homolog DVL-1
- Segment polarity protein dishevelled homolog DVL-3
- Segment polarity protein dishevelled homolog DVL-2
- Protein naked cuticle homolog 2
- Serine/threonine-protein phosphatase 2A 55 kDa regulatory subunit B beta isoform
- Axin-2
- Serine/threonine-protein phosphatase 2A regulatory subunit B'' subunit delta
- Serine/threonine-protein phosphatase 2A catalytic subunit alpha isoform
- 3222402P14Rik protein
- Serine/threonine-protein phosphatase 2A 65 kDa regulatory subunit A alpha isoform
Sequence:
MGKLHSKPAAVCKRRESPEGDSFAVSAAWARKGIEEWIGRQRCPGSVSGPRQLRLAGTVGRGTRELVGDTSREALGEEDEDDFPLEVALPPEKIDSLGSGDEKRMERLSEPGQASKKQLKFEELQCDVSVEEDSRQEWTFTLYDFDNNGKVTREDITSLLHTIYEVVDSSVNHSPTSSKTLRVKLTVAPDGSQSKRSVLFNHTDLQSTRPRADTKPAEELRGWEKKQRAPLRFQGDSHLEQPDCYHHCVDENIERRNHYLDLAGIENYTSQFGPGSPSVAQKSELPPRISNPTRSRSHEPEAAHIPHRRPQGVDPGSFHLLDTPFAKASELQQRLRGTQDGSKHFVRSPKAQGKNMGMGHGARGARSKPPLVPTTHTVSPSAHLATSPALLPTLAPLGHKKHKHRAKESQASCRGLQGPLAAGGSTVMGREQVRELPAVVVYESQAGQAVQRHEHHHHHEHHHHYHHFYQP
Protein: Glutamate receptor IIA (RE27895p) (Q9VMP4)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}. Postsynaptic cell membrane {ECO:0000256|ARBA:ARBA00034100}.
Interaction partners:
- Glutamate receptor IIB
- Bruchpilot, isoform J
- FI23915p1
- FI04462p
- Neuropilin and tolloid-like, isoform B
- Glutamate receptor IIC
- Fasciclin-2
- Vesicular glutamate transporter, isoform A
- NMDA receptor 2, isoform C
- Glutamate [NMDA] receptor subunit 1
Sequence:
MRLCPVVIYAFIIIIGFLEGIIALGGDDRNEITVGAIFYENEKEIELSFDQAFREVNNMKFSELRFVTIKRYMPTNDSFLLQQITCELISNGVAAIFGPSSKAASDIVAQIANATGIPHIEYDLKLEATRQEQLNHQMSINVAPSLSVLSRAYFEIIKSNYEWRTFTLIYETPEGLARLQDLMNIQALNSDYVKLRNLADYADDYRILWKETDETFHEQRIILDCEPKTLKELLKVSIDFKLQGPFRNWFLTHLDTHNSGLRDIYNEDFKANITSVRLKVVDANPFERKKTRLTKVDQILGNQTMLPILIYDAVVLFASSARNVIAAMQPFHPPNRHCGSSSPWMLGAFIVNEMKTISEDDVEPHFKTENMKLDEYGQRIHFNLEIYKPTVNEPMMVWTPDNGIKKRLLNLELESAGTTQDFSEQRKVYTVVTHYEEPYFMMKEDHENFRGREKYEGYAVDLISKLSELMEFDYEFMIVNGNGKYNPETKQWDGIIRKLIDHHAQIGVCDLTITQMRRSVVDFTVPFMQLGISILHYKSPPEPKNQFAFLEPFAVEVWIYMIFAQLIMTLAFVFIARLSYREWLPPNPAIQDPDELENIWNVNNSTWLMVGSIMQQGCDILPRGPHMRILTGMWWFFALMMLSTYTANLAAFLTSNKWQSSIKSLQDLIEQDKVHFGSMRGGSTSLFFSESNDTDYQRAWNQMKDFNPSAFTSTNKEGVARVRKEKGGYAFLMETTSLTYNIERNCDLTQIGEQIGEKHYGLAVPLGSDYRTNLSVSILQLSERGELQKMKNKWWKNHNVTCDSYHEVDGDELSIIELGGVFLVLAGGVLIGVILGIFEFLWNVQNVAVEERVTPWQAFKAELIFALKFWVRKKPMRISSSSDKSSSRRSSGSRRSSKEKSRSKTVS
Protein: Degringolade, isoform D (A0A0B4LHT4)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MANLSVSTEDAHSQIRSLTQDVIQMEAELDRMNRYCEEVVAQIDTFATRTSTPTTRRIRRRTSPVEVIDLSHLDRAPPVRSARNRDPDAFIDLCTPEGPRSRTVNLHSNDSLTILPRRSAENDPVVDLDVASPPKRVNRDIDESQKEELYKCPICMDSVSKREPVSTKCGHVFCRECIETAIRATHKCPICNKKLTARQFFRIYL
Protein: E3 ubiquitin-protein ligase NEURL1B (EC 2.3.2.27) (Neuralized-2) (NEUR2) (Neuralized-like protein 1B) (Neuralized-like protein 3) (RING-type E3 ubiquitin transferase NEURL1B) (A8MQ27)
Organism: Homo sapiens (Human)
Function: E3 ubiquitin-protein ligase involved in regulation of the Notch pathway through influencing the stability and activity of several Notch ligands.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:19723503}.
Interaction partners:
- E3 ubiquitin-protein ligase MIB2
- Protein jagged-1
Sequence:
MGNTVHRTLPDPSPPARLLATRPCCGPGPERRPVLGEAPRFHAQAKGKNVRLDGHSRRATRRNSFCNGVTFTQRPIRLYEQVRLRLVAVRPGWSGALRFGFTAHDPSLMSAQDIPKYACPDLVTRPGYWAKALPENLALRDTVLAYWADRHGRVFYSVNDGEPVLFHCGVAVGGPLWALIDVYGITDEVQLLESAFADTLTPARLSQARFSACLPPSSHDAANFDNNELENNQVVAKLGHLALGRAPGPPPADAAAAAIPCGPRERPRPASSPALLEADLRFHATRGPDVSLSADRKVACAPRPDGGRTLVFSERPLRPGESLFVEVGRPGLAAPGALAFGITSCDPGVLRPNELPADPDALLDRKEYWVVARAGPVPSGGDALSFTLRPGGDVLLGINGRPRGRLLCVDTTQALWAFFAVRGGVAGQLRLLGTLQSSPATTTPSGSLSGSQDDSDSDMTFSVNQSSSASESSLVTAPSSPLSPPVSPVFSPPEPAGIKNGECTVCFDGEVDTVIYTCGHMCLCHSCGLRLKRQARACCPICRRPIKDVIKIYRP