wanglab/gogpt-training-data huggingface dataset:
Protein: Cdc42-interacting protein 4 (Salt tolerant protein) (Thyroid receptor-interacting protein 10) (TR-interacting protein 10) (TRIP-10) (P97531)
Organism: Rattus norvegicus (Rat)
Function: Required to coordinate membrane tubulation with reorganization of the actin cytoskeleton during endocytosis. Also acts as a link between CDC42 signaling and regulation of the actin cytoskeleton. Binds to lipids such as phosphatidylinositol 4,5-bisphosphate and phosphatidylserine and promotes membrane invagination and the formation of tubules. Also enhances actin polymerization in the vicinity of membrane tubules by recruiting WASL/N-WASP which in turn activates the Arp2/3 complex. Actin polymerization and dynamin may promote the fission of membrane tubules to form endocytic vesicles. Required for the formation of podosomes, actin-rich adhesion structures specific to monocyte-derived cells. Required for translocation of GLUT4 to the plasma membrane in response to insulin signaling. May be required for the lysosomal retention of FASLG/FASL (By similarity).
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000250}. Cytoplasm, cell cortex {ECO:0000250}. Lysosome {ECO:0000250}. Golgi apparatus {ECO:0000250}. Cell membrane {ECO:0000250}. Cell projection, phagocytic cup {ECO:0000250}. Note=Localizes to cortical regions coincident with F-actin, to lysosomes and to sites of phagocytosis in macrophages. Also localizes to the Golgi, and this requires AKAP9. Translocates to the plasma membrane in response to insulin stimulation, and this may require active RHOQ (By similarity). {ECO:0000250}.
Interaction partners:
- Actin nucleation-promoting factor WAS
- Cell division control protein 42 homolog
- Actin nucleation-promoting factor WASL
- Intersectin 2
- Rho-related GTP-binding protein RhoQ
- Rho GTPase-activating protein 44
- F-BAR domain only protein 2
- Rho GTPase-activating protein 17
- tRNA-splicing endonuclease subunit Sen2
- Myc box-dependent-interacting protein 1
Sequence:
MDWGTELWDQFEVLERHTQWGLDLLDKYVKFVKERVEVEQSYAKQLRSLVKKYLPKRPAKDDPEIKFSQQQSFVQLLQEVNDFAGQRELVAESLGIRVCLELAKYSQEMKQERKMHFQEGRRAQQQLENGFKQLENSKRKFERDCREAEKAAHTAERLDQDINATKADVEKAKQQAHLRNHMAEESKNEYAAQLQRFNRDQAHFYFSQMPQIFDKLQDMDERRATRLGAGYGLLSEAELQVVPIIGKCLEGMKVAAESVDAKNDSKVLIELHKSGFARPGDLEFEDFSQVMNRVPSDSSLGTPDGRPELRAASSRSRAKRWPFGKKNKTVVTEDFSHLPPEQQRKRLQQQLEERNRELQKEEDQREALKKMKDVYEKTPQMGDPASLEPRIAETLGNIERLKLEVQKYEAWLAEAESRVLSNRGDSLSRHTRPPDPPTTAPPDSSSSSNNSGSQDNKESSEEPPSEEGQDTPIYTEFDEDFEEPASPIGQCVAIYHFEGSSEGTVSMSEGEDLSLMEEDKGDGWTRVRRKQGGEGYVPTSYLRVTLN
Protein: AP-4 complex accessory subunit Tepsin (ENTH domain-containing protein 2) (Tetra-epsin) (G3V8Y7)
Organism: Rattus norvegicus (Rat)
Function: Associates with the adapter-like complex 4 (AP-4) and may therefore play a role in vesicular trafficking of proteins at the trans-Golgi network.
Subcellular location: Golgi apparatus, trans-Golgi network membrane {ECO:0000269|PubMed:22472443}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q96N21}. Cytoplasmic vesicle {ECO:0000269|PubMed:22472443}. Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q96N21}. Note=Extensively colocalizes with AP-4 which mediates the recruitment of TEPSIN to the trans-Golgi network. {ECO:0000269|PubMed:22472443}.
Interaction partners:
- AP complex subunit sigma
- AP-4 complex subunit epsilon
- AP complex subunit beta
- AP-4 complex subunit mu-1
Sequence:
MAAVPPLRDRLSFLHRLPILLKGTSDDDIPCPGYLFEEIAKISHESLGSSQCLLEYLLNRLDSSSGHVKLKVLKILLYLCSHGSSSFMLILRRNSALIQEATAFAGPPDPLHGNSLYQKVRAAAQDLGSTLFSDALPQPPSQPPQILPPAGMGAQARPHSALQGFGYTKESSRTGSAGETFLSTIQRAAEVVVNAVRPGPDNPCTKGPLPHGDAYQPAVTPSASHTHPNPGNLLPAAIQGTRAVKHQPGQAGGGWDEMDSSPSSQNSSCTSNLSRASDSVSRSGSDSHSGASREPGDLAERAEGMAPNDCQQELNLVRTVTQGPRVFLSREETQHFIKECGLLNCEAVLELLLQQLVGTSECEQMRALCAIASFGSADLLPQEHILLLCRQQLQELGAGSPGPVTNKATKILRHLEASCGQQFPTLRPCAQPNSAAAVVGPADLLTSPVPPPGSQVFLQPLSSTAVVPRSPVPTPSPDTLPPALQDPGELRTQLVCSSEPGTGSEQRLENTDTPKDSSSPCPWSPNSLFAGMELVACTRLPCPSFQADLQKVTTEPPVSEPSAFAFLNM
Protein: Tyrosyl-DNA Phosphodiesterase (Tdp1), putative (Q586D1)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- HIT domain-containing protein
- Protein artemis
- KU70 protein
- DNA topoisomerase I
- DNA topoisomerase type IB small subunit
- KU80 protein
Sequence:
MEETKLCPFWVSRVSGLATESPSALTLSDLLHCNIEDPSEVWTHVVLANYLIDLEWVFDMATCLQLSNCHVMIVSGEEGLAERYAASPLAGLLGKERVEIIKPKLPLPFGVHHGKLILCVNSKGVRISVLTANFIESDWGKKTQGIYVQDFPRLVTSSASSNSMGSLQALRRCRGTRFKEEIKRYLSCIGAISSTTGTNCIPLSLLDEVDYSGACVELVSSVPGCHRNSDAYRFGMGRLQEVLRAMQISSPSGENSPTLVWQFSSQGTLTSNFLRSLERVMTISTDNTPLPDTKSPTVRIIYPTEAEVKGSFEGWHGGLSLPVRLRCCHPYVNERLYRWGQRPYAEGADRGRNRAMPHIKTYMRLTENGDGLKWFMLTSANLSRAAWGEWQKGGTQILIRSYELGVVYGTDSFINPADGGLFSATPSKPIPVPSSIGGDGLVRVKIKTLPSESDRDEPTLFLPYNPLNPQPYVSTLQMQQREHRHTGHSCVSQLSSLDVPWLVDLPHRGKDCLGKEFRDVLEGSNRRGEEPDPLRSGGCCVGALGEKRTNRDA
Protein: Floral homeotic protein APETALA 1 (Agamous-like MADS-box protein AGL7) (P35631)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Transcription factor that promotes early floral meristem identity in synergy with LEAFY. Is required subsequently for the transition of an inflorescence meristem into a floral meristem. Is indispensable for normal development of sepals and petals in flowers. Regulates positively the B class homeotic proteins APETALA3 and PISTILLATA with the cooperation of LEAFY and UFO. Interacts with SEPALLATA3 or AP3/PI heterodimer to form complexes that could be involved in genes regulation during floral meristem development. Regulates positively AGAMOUS in cooperation with LEAFY. Displays a redundant function with CAULIFLOWER in the up-regulation of LEAFY. Together with AGL24 and SVP, controls the identity of the floral meristem and regulates expression of class B, C and E genes. Represses flowering time genes AGL24, SVP and SOC1 in emerging floral meristems.
Subcellular location: Nucleus.
Interaction partners:
- Protein LEAFY
- Protein FLOWERING LOCUS T
- Developmental protein SEPALLATA 3
- Protein TERMINAL FLOWER 1
- Transcriptional corepressor SEUSS
- Clathrin interactor EPSIN 1
- Floral homeotic protein APETALA 2
- Brefeldin A-inhibited guanine nucleotide-exchange protein 4
- MADS-box protein SVP
- Developmental protein SEPALLATA 1
Sequence:
MGRGRVQLKRIENKINRQVTFSKRRAGLLKKAHEISVLCDAEVALVVFSHKGKLFEYSTDSCMEKILERYERYSYAERQLIAPESDVNTNWSMEYNRLKAKIELLERNQRHYLGEDLQAMSPKELQNLEQQLDTALKHIRTRKNQLMYESINELQKKEKAIQEQNSMLSKQIKEREKILRAQQEQWDQQNQGHNMPPPLPPQQHQIQHPYMLSHQPSPFLNMGGLYQEDDPMAMRRNDLELTLEPVYNCNLGCFAA
Protein: Transmembrane protein 182 (A0A1D5NY17)
Organism: Gallus gallus (Chicken)
Function: Negatively regulates myogenesis and skeletal muscle regeneration via its association with ITGB1. Modulates ITGB1 activation by decreasing ITGB1-LAMB1 interaction and inhibiting ITGB1-mediated intracellular signaling during myogenesis.
Subcellular location: Cell membrane {ECO:0000269|PubMed:34427057}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Kelch like family member 40.
- Creatine kinase S-type, mitochondrial
Sequence:
MKLSVGIFFGGLFAALGVLLFLVAFGTDYWLLATEIGRCSKAPEDAGTEKATFHHEGFFWRCWFSGNVREHNTSMWKFWYTNQSPSKNCTHAYLSPFPHIRDEHNSTSYDSAVIYRGFWTVLMLLGVITIVMASFLIICAAPFASHILYKAGGGFYILAGVLFSLVVVMYVIWVQAMADLENYTNMKKMDCPDFAVYVRYGWSFMLAPIGVFFALLAGMLFLLVGRAIYLNSD
Protein: Cytochrome c oxidase subunit 4 isoform 1, mitochondrial (Cytochrome c oxidase polypeptide IV) (Cytochrome c oxidase subunit IV isoform 1) (COX IV-1) (P10888)
Organism: Rattus norvegicus (Rat)
Function: Component of the cytochrome c oxidase, the last enzyme in the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over the inner membrane that drives transmembrane transport and the ATP synthase. Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Electrons originating from reduced cytochrome c in the intermembrane space (IMS) are transferred via the dinuclear copper A center (CU(A)) of subunit 2 and heme A of subunit 1 to the active site in subunit 1, a binuclear center (BNC) formed by heme A3 and copper B (CU(B)). The BNC reduces molecular oxygen to 2 water molecules using 4 electrons from cytochrome c in the IMS and 4 protons from the mitochondrial matrix.
Subcellular location: Mitochondrion inner membrane {ECO:0000250|UniProtKB:P00423}; Single-pass membrane protein {ECO:0000250|UniProtKB:P00423}.
Interaction partners:
- Cytochrome c oxidase subunit 2
- Cytochrome c1, heme protein, mitochondrial
- Cytochrome b-c1 complex subunit 2, mitochondrial
- Cytochrome c oxidase subunit 5A, mitochondrial
- Cytochrome c oxidase subunit 7C, mitochondrial
- Cytochrome c oxidase subunit 1
- Cytochrome c oxidase subunit 5B, mitochondrial
- Cytochrome c oxidase subunit 6C-2
- Ubiquinol-cytochrome c reductase, complex III subunit X.
- Cytochrome c oxidase subunit 7B, mitochondrial
Sequence:
MLATRALSLIGKRAISTSVCLRAHGSVVKSEDYALPSYVDRRDYPLPDVAHVKLLSASQKALKEKEKADWSSLSRDEKVQLYRIQFNESFAEMNKGTNEWKTVVGLAMFFIGFTALVLIWEKSYVYGPIPHTFDRDWVAMQTKRMLDMKVNPIQGFSAKWDYNKNEWKK
Protein: Spermatogenesis-associated protein 2 (Q9UM82)
Organism: Homo sapiens (Human)
Function: Bridging factor that mediates the recruitment of CYLD to the LUBAC complex, thereby regulating TNF-alpha-induced necroptosis. Acts as a direct binding intermediate that bridges RNF31/HOIP, the catalytic subunit of the LUBAC complex, and the deubiquitinase (CYLD), thereby recruiting CYLD to the TNF-R1 signaling complex (TNF-RSC). Required to activate the 'Met-1'- (linear) and 'Lys-63'-linked deubiquitinase activities of CYLD. Controls the kinase activity of RIPK1 and TNF-alpha-induced necroptosis by promoting 'Met-1'-linked deubiquitination of RIPK1 by CYLD (By similarity).
Subcellular location: Cytoplasm {ECO:0000269|PubMed:10222154, ECO:0000269|PubMed:11079456}. Nucleus {ECO:0000250|UniProtKB:Q66HP6}. Note=Detected in the tubular compartment of the testis and, in the cytoplasm of the Sertoli cells. {ECO:0000269|PubMed:11079456}.
Interaction partners:
- Tumor necrosis factor receptor superfamily member 1A
- Ubiquitin carboxyl-terminal hydrolase CYLD
- E3 ubiquitin-protein ligase RNF31
- RanBP-type and C3HC4-type zinc finger-containing protein 1
- Sharpin
- Tumor necrosis factor
- Spermatogenesis-associated protein 2-like protein
- Tumor necrosis factor receptor type 1-associated DEATH domain protein
- NF-kappa-B essential modulator
- Inhibitor of nuclear factor kappa-B kinase subunit alpha
Sequence:
MGKPSSMDTKFKDDLFRKYVQFHESKVDTTTSRQRPGSDECLRVAASTLLSLHKVDPFYRFRLIQFYEVVESSLRSLSSSSLRALHGAFSMLETVGINLFLYPWKKEFRSIKTYTGPFVYYVKSTLLEEDIRAILSCMGYTPELGTAYKLRELVETLQVKMVSFELFLAKVECEQMLEIHSQVKDKGYSELDIVSERKSSAEDVRGCSDALRRRAEGREHLTASMSRVALQKSASERAAKDYYKPRVTKPSRSVDAYDSYWESRKPPLKASLSLRKEPVATDVGDDLKDEIIRPSPSLLTMASSPHGSPDVLPPASPSNGPALLRGTYFSTQDDVDLYTDSEPRATYRRQDALRPDVWLLRNDAHSLYHKRSPPAKESALSKCQSCGLSCSSSLCQRCDSLLTCPPASKPSAFPSKASTHDSLAHGASLREKYPGQTQGLDRLPHLHSKSKPSTTPTSRCGFCNRPGATNTCTQCSKVSCDACLSAYHYDPCYKKSELHKFMPNNQLNYKSTQLSHLVYR
Protein: 5-hydroxytryptamine (Serotonin) receptor 2B, isoform D (5-hydroxytryptamine (Serotonin) receptor 2B, isoform F) (Serotonin receptor subtype 2B) (Q8INQ6)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004651}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}.
Interaction partners:
Sequence:
MEEDVYASLGAYNDSGGDDWSSSEHLVLWEEDETQRTTANATSRHNQLHVARWNATGNATISATFEDVPFDANNYWALLALVLVLGTAAGNILVCLAIAWERRLQNVTNYFLMSLAITDLMVAVLVMPLGILTLVKGYFPLGSEHCLTWICLDVLFCTASIMHLCTISVDRYLSLRYPMRFGRNKTRRRVTLKIVFVWLLSIAMSLPLSLMYSKNHASVLVNGTCQIPDPVYKLVGSIVCFYIPLGVMLLTYCLTVRLLARQRQNLGGGQQTAAATPGWASGWLGQAPALERRCTWRRLLKPGPGNASSVLHAHSANSTDTDLSTLDNHELWLPDSSIKEPTPTTMTALHQFGAEMLKLSRGLESVASSSTTGSPTKSEFSLSNHLQLQYPSSPQRYAATHQQSHHHNHQQHPAGVYHQQASPKGRHGTTVLGLSTTTLGIERESTRNSLASSRMGGEQSDGTLSQLSQRLRAYKKRRRASSAVPGREKRAGHEDADEDVETPTSTLRRHKRHNSLPKNALYPRHTTVQESLDDDDDEEEESAQQKDQQTKSKICHSDTELDPPQKAKQCHIAGQNHQSDYLQLPSVCTCPYFGDRPLQNCVKSAEVKIISSAFRVTTTTTAVSSSPSEMELLMCSSGNKKSLTSSVSAGITGGPAGAAPATVGSTLSPHSAHNQGSSLTVQSDGSGYLAAPGTPCPGRRKLSISKTASVVTWDSSRHRRRGSSFGGVRTSLLLTPTKTATTSNSSTPLRRSATLRSHQNMNYQGAGECGGKTRTTTSSPCMLQRQQTVRSHHSRNSSVISRNSSRHGRIIRLEQKATKVLGVVFFTFVILWSPFFVLNLLPTVCAECEERISHWVFDVVTWLGYASSMVNPIFYTIFNKVFRQAFKKVLLCRYSSTSAWRPSR
Protein: FKBP prolyl isomerase 8 (A0A0A0MTJ1)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MASCAEPSEPSAPLPAGVPPLEDFEVLDGVEDAEGEEEEEEEEEEEDDLSELPPLEDMGQPPAEEAEQPGALAREFLAAMEPEPAPAPAPEEWLDILVDMTFEEEAQLLQLKVKCLNNLAASQLKLDHYRAALRSCSLVLEHQPDNIKALFRKGKVLAQQGEYSEAIPILRAALKLEPSNKTIHAELSKLVKKHAAQRSTETALYRKMLGNPSRLPAKCPGKGAWSIPWKWLFGATAVALGGVALSVVI
Protein: Ornithine aminotransferase, mitochondrial (EC 2.6.1.13) (Ornithine delta-aminotransferase) (Ornithine--oxo-acid aminotransferase) (Q10G56)
Organism: Oryza sativa subsp. japonica (Rice)
Function: Confers drought and oxidative stress tolerance mainly through enhancing ROS-scavenging capacity and Pro pre-accumulation.
Subcellular location: Mitochondrion matrix {ECO:0000250}.
Interaction partners:
- Delta-1-pyrroline-5-carboxylate synthase 1
- Delta-1-pyrroline-5-carboxylate synthase 2
- Arginase 1, mitochondrial
- Arginine biosynthesis bifunctional protein ArgJ
- Os05g0536400 protein
- Probable N-acetyl-gamma-glutamyl-phosphate reductase, chloroplastic
- Probable N-acetyl-gamma-glutamyl-phosphate reductase, chloroplastic
- argininosuccinate synthase
- argininosuccinate synthase
- Proline dehydrogenase
Sequence:
MAAALARRGGGGLARALARGRGMCSATAAERAAGAALTSEELMRMERERSAHNYHPIPVVFSKGEGSHILDPEGNKYIDFLSAYSAVNQGHCHPKVLRALKEQAERLTLSSRAFYNDKFPIFAEYLTSMFGYEMMLPMNTGAEGVETAIKLVRKWGYEKKKIPKNEALIVSCCGCFHGRTLGVISMSCDNDATRGFGPLVPGHLKVDFGDTDGLEKIFKDHGERICGFLFEPIQGEAGVIIPPDGYLKAVRDLCSRHNILMIADEIQTGIARTGKMLACDWENIRPDVVILGKALGAGVVPVSAVLADKDIMLCIKPGEHGSTFGGNPLASAVAVASLKVVTDEGLVERAAKLGQEFRDQLQKVQQRFPQIIREVRGRGLLNAVDLSNEALSPASAYDICIKLKERGVLAKPTHDTIIRLAPPLSISPEELAEASKAFSDVLEHDLPQLQKQIKKTESAAEKQSCDRCGRDLY
Protein: Sperm transmembrane protein 9 (Fertilization defective 9) (Spermatogenesis defective 9) (Q9TVY6)
Organism: Caenorhabditis elegans
Function: Required for fertilization. May be required for cell adhesion and/or function as a signaling molecule.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:14653860, ECO:0000305}. Membrane {ECO:0000269|PubMed:14653860, ECO:0000305}; Single-pass type I membrane protein {ECO:0000269|PubMed:14653860}.
Interaction partners:
- Uncharacterized protein
- Dendritic cell-specific transmembrane protein-like domain-containing protein
- TRP homologous cation channel protein
- Ig-like domain-containing protein
- LDL receptor repeat-containing protein egg-2
- Dendritic cell-specific transmembrane protein-like domain-containing protein
- Sperm vesicle fusion protein fer-1
- LDL receptor repeat-containing protein egg-1
Sequence:
MNVILVLVVLFFAGDCAKIRKIIDFLEKDAPNDIEKTPNYNEESLAVKRNKNFNPCLENPKICSNRGKCLHENGNFYCICPVTHYGKTCEHVSDQTNCEKHLCQNNSTCVSIKSLRTIVNTVLLRQIRVQRKVNGSKAALTNEELAEIDLEVNYECICQKGYFGGLCDESEADRTCQEVYCLGRGKGAINATGKCECECENQFFGDRCEQISACFDTQCDNGGICEDVVDWKTKTVTATCKCPSAIELIGGTVTGENCETLQIPSTAPKEFIPCAEGSNSTMFFKKFIANISLEYMDDISELEAIKNDYNDGKNVNGTMTDGWCRNDGKCVPEVVRVNSSRAYYIYRCECTNPLTDGYYCEYKRHDSCSLTREEVARGDRWDEKCTDSQHGACVDISGVAHCVCKPDYTGEKCEIFDPCARQPCKHGDCIPIPNTADVAFGTSRYQCLCPLSAKLNPESQACMEINEKKCAPGACGNGRCVPCESDADDLMPLCNDNDNRQGFRCLCEAGYLPPFCKVHTNPCYQNLCQNSATCHIDPKQRSYDCQCVNGTRGSLCENVDDSCDAFGNKICVHGTCINDEYFHRGFSCECDDGFEGLDCNVEIAWSSVMTNRLMKNYEFSLPLVACFVSLAILLPVIVISRRRQGRVEEAKKTSEVKTENP
Protein: mRNA-capping enzyme subunit beta (EC 3.6.1.74) (mRNA 5'-phosphatase) (mRNA 5'-triphosphate monophosphatase) (O93803)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Function: First step of mRNA capping. Converts the 5'-triphosphate end of a nascent mRNA chain into a diphosphate end.
Subcellular location: Nucleus {ECO:0000250}.
Interaction partners:
- mRNA-capping enzyme subunit alpha
- mRNA cap guanine-N
- choline-phosphate cytidylyltransferase
- SIR4-interacting protein SIF2
- Transcription initiation factor TFIID subunit 5
- Transcription initiation factor TFIID subunit 9
- Deubiquitination module subunit
- Histone acetyltransferase
- Transcription initiation factor TFIID subunit 6
- Transcription initiation factor TFIID subunit 10
Sequence:
MNVGSILNDDPPSSGNANGNDDNTKIIKSPTAYHKPSVHERHSITSMLNDTPSDSTPTKKPEPTISPEFRKPSISSLTSPSVAHKPPPLPPSSSSVGSSEHSSARSSPAITKRNSIANIIDAYEEPATKTEKKAELNSPKINQSTPVPKLEEHENDTNKVEKVVDSAPEPKPKKEPQPVFDDQDDDLTKIKKLKQSKKPRRYETPPIWAQRWVPPNRQKEETNVDDGNEAITRLSEKPVFDYTTTRSVDLECSITGMIPPSSITRKIAEWVYANFSNVEEKSKRNVELELKFGKIIDKRSGNRIDLNVVTECIFTDHSSVFFDMQVEEVAWKEITKFLDELEKSFQEGKKGRKFKTLESDNTDSFYQLGRKGEHPKRIRVTKDNLLSPPRLVAIQKERVADLYIHNPGSLFDLRLSMSLEIPVPQGNIESIITKNKPEMVREKKRISYTHPPTITKFDLTRVIGNKTEDKYEVELEAGVMEIFAAIDKIQKGVDNLRLEELIEVFLNNARTLNNRLNKIC
Protein: Cleavage and polyadenylation specificity factor subunit 2 (Cleavage and polyadenylation specificity factor 100 kDa subunit) (CPSF 100 kDa subunit) (O35218)
Organism: Mus musculus (Mouse)
Function: Component of the cleavage and polyadenylation specificity factor (CPSF) complex that play a key role in pre-mRNA 3'-end formation, recognizing the AAUAAA signal sequence and interacting with poly(A) polymerase and other factors to bring about cleavage and poly(A) addition. Involved in the histone 3' end pre-mRNA processing (By similarity).
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- Symplekin
- pre-mRNA 3' end processing protein WDR33
- Cleavage and polyadenylation specificity factor subunit 1
- Cleavage and polyadenylation specificity factor subunit 4
- Cleavage and polyadenylation specificity factor subunit 3
- Pre-mRNA 3'-end-processing factor FIP1
- Pre-mRNA cleavage complex 2 protein Pcf11
- Cleavage stimulation factor subunit 1
- Cleavage stimulation factor subunit 2
- WD repeat-containing protein 82
Sequence:
MTSIIKLTTLSGVQEESALCYLLQVDEFRFLLDCGWDEHFSVDIIDSLRKHVHQIDAVLLSHPDPLHLGALPFAVGKLGLNCAIYATIPVYKMGQMFMYDLYQSRHNTEDFTLFTLDDVDAAFDKIQQLKFSQIVNLKGKGHGLSITPLPAGHMIGGTIWKIVKDGEEEIVYAVDFNHKREIHLNGCSLEMLSRPSLLITDSFNATYVQPRRKQRDEQLLTNVLETLRGDGNVLIAVDTAGRVLELAQLLDQIWRTKDAGLGVYSLALLNNVSYNVVEFSKSQVEWMSDKLMRCFEDKRNNPFQFRHLSLCHGLSDLARVPSPKVVLASQPDLECGFSRDLFIQWCQDPKNSIILTYRTTPGTLARFLIDNPTEKVTEIELRKRVKLEGKELEEYVEKEKLKKEAAKKLEQSKEADIDSSDESDVEEDVDQPSAHKTKHDLMMKGEGSRKGSFFKQAKKSYPMFPAPEERIKWDEYGEIIKPEDFLVPELQATEEEKSKLESGLTNGEEPMDQDLSDVPTKCVSATESIEIKARVTYIDYEGRSDGDSIKKIINQMKPRQLIIVHGPPEASQDLAECCRAFGGKDIKVYMPKLHETVDATSETHIYQVRLKDSLVSSLQFCKAKDAELAWIDGVLDMRVSKVDTGVILEEGELKDDGEDSEMQVDAPSDSSAMAQQKAMKSLFGEDEKELGEETEIIPTLEPLPPHEVPGHQSVFMNEPRLSDFKQVLLREGIQAEFVGGVLVCNNQVAVRRTETGRIGLEGCLCQDFYRIRDLLYEQYAIV
Protein: S-methyl-5'-thioadenosine phosphorylase (EC 2.4.2.28) (5'-methylthioadenosine phosphorylase) (MTA phosphorylase) (MTAP) (MTAPase) (B4DUC8)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03155}. Nucleus {ECO:0000256|HAMAP-Rule:MF_03155}.
Interaction partners:
Sequence:
MRPARASLAAAGRDWGAALGTHLPREERIGIIGGTGLDDPEILEGRTEKYVDTPFGKPSDALILGKIKNVDCVLLARHGRQHTIMPSKVNYQANIWALKEEGCTHVIVTTACGSLREEIQPGDIVIIDQFIDRTTMRPQSFYDGSHSCARGVCHIPMAEPFCPKTREVLIETAKKLGLRCHSKGTMVTIEGPRFSSRAESFMFRTWGADVINMTTVPEVVLAKEAGICYASIAMATDYDCWKEHEEAVSVDRVLKTLKENANKAKSLLLTTIPQIGSTEWSETLHNLKNMAQFSVLLPRH
Protein: FHA domain-containing protein (Q385C1)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MEIAIVAAHNLKALADLGGLSATVSQPTKCLEETPSGLLPMRVRSSSVSGYKRCRLVARFLSRSTENGCSLPSQNFNSTGGGNRCGMANLPLVCLLPLGRDPRENSGVIQFEGELLGSFLSRRHCVVQLAGREPLRGSPDAGLWCALSVRDCGSKNGTFVNGKRLATGDTSPSVLFDPSSGTSWKQPLLTIEFGPGSKLGAEESLSSDQLLLRFHVFARCLCEGEHIQRIQQFLCCLPTAMDYLPTPPFVSSPCSLAESANTEAKGEGEASSMGSPAVAPLKDNGDVNTRAVGSAERASNTDKPVVNIHCSPSGTSGKVTRSQSPIVIKRRRVGGGSLASSQRARFDGNSAACSGEGGRSRGMKGGGERALPSRTPSHGEAPDALKRDSVKREPTRTSLEGWDDIFLSADVNEQDVVLPRSGTARSGQLVPDNGSCGIADFFFPFELPGLTAVKKGIKRKRAAGR
Protein: RING-type E3 ubiquitin transferase (EC 2.3.2.27) (Q7K231)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- RNA helicase
- Pre-mRNA-processing factor 17
- Spliceosome-associated protein CWC27 homolog
- CG4973 protein
- FI23980p1
- Pre-mRNA-splicing factor CWC22 homolog
- Serine/arginine repetitive matrix protein 1
- Microfibrillar-associated protein 1
- RNA helicase
- Cwc25
Sequence:
MGKRQHQKDKMYLTYTEWSELYGGKKVESLENDHVKFKRLPFEHCCITMAPYEMPYCDLQGNVFEYEAILKFLKTFKVNPITGQKMDSKSLVKLNFHRNANDEYHCPALFKPFSKNSHIVAVATTGNVYCWEAIDQLNIKTKNWKDLVDDTPFQRKDIITIQDPQKLEKYDISTFYHIKKNLRVLTEEEQQERKNPASGRIKTMNLETKETLEQLQQDYQPAEEEASTSKRTADKFNAAHYSTGAVAASFTSTAMVPVSQIEAAIIDDDLVKYERVKKKGYVRLNTNLGPLNLELFCDQTPRACDNFIKHCANGYYNNVMFHRSIRNFIVQGGDPTGSGSGGESIWGKKFEDEFKPNLTHTGRGVLSMANSGPNTNGSQFFITYRSCKHLDGKHTIFGKLVGGLDTLQKMENIEVDNKDRPIEDIIIESSQVFVNPFAEAAEQLAKEREEEAAGKEEIVKKEEQQKRMKEPLKVYREGVGKYLKLQTVAKKPEAPLTSAQAAKKKKLANGFGDFSSW
Protein: Cyclic AMP receptor 4 (cAMP receptor 4) (Q9TX43)
Organism: Dictyostelium discoideum (Social amoeba)
Function: Receptor for cAMP. Regulates axial patterning and cellular differentiation during late development. The activity of this receptor is mediated by G proteins.
Subcellular location: Membrane; Multi-pass membrane protein.
Interaction partners:
- Guanine nucleotide-binding protein alpha-2 subunit
- Adenylate cyclase, aggregation specific
Sequence:
MKVLQEINLTYSILVIADFSSIFGCLLVLIAFKKLKLLRNHITRVIACFCVSSLLKDIISTGLTLSLGPQNEAGSTSFQCYLYAITITYGSLACWLWTLCLAFSIYNLIVKREPEPEKYEKFYHGVCWTIPLICVIVMLAKKTIEPVGNWCWISEKYVGYRFGLFYGPFFAIWIISAVLVGLTSRYTYSVIRNSVSDNKDKHMTYQFKLINYIIVFLLCWVFAIVNRILNGLGYYPTLPNILHTYFSVSHGFFASVTFIYNNPLMWRYWGSKIFLIFAKFGYFVELQRRLDRNKNNNNPSPILNSYAATVYHSSTIESLSLQHNNDISNDNQQQQQQQQTPQQPQQQFQQQQSPTVIEMQNLKQDQNIENNEQNENCYNTIDTNIEINTNKLNDNSFEITQPSNDLNTIENNNNYNNNNNNNNNNSLVIEKEKDEREKKDNKF
Protein: Deubiquitinase OTUD6B (EC 3.4.19.12) (DUBA-5) (OTU domain-containing protein 6B) (Q8N6M0)
Organism: Homo sapiens (Human)
Function: Deubiquitinating enzyme that may play a role in the ubiquitin-dependent regulation of protein synthesis, downstream of mTORC1. May associate with the protein synthesis initiation complex and modify its ubiquitination to repress translation. May also repress DNA synthesis and modify different cellular targets thereby regulating cell growth and proliferation. May also play a role in proteasome assembly and function.
Interaction partners:
- Zinc finger-containing ubiquitin peptidase 1
- Ubiquitin thioesterase OTUB1
Sequence:
MEAVLTEELDEEEQLLRRHRKEKKELQAKIQGMKNAVPKNDKKRRKQLTEDVAKLEKEMEQKHREELEQLKLTTKENKIDSVAVNISNLVLENQPPRISKAQKRREKKAALEKEREERIAEAEIENLTGARHMESEKLAQILAARQLEIKQIPSDGHCMYKAIEDQLKEKDCALTVVALRSQTAEYMQSHVEDFLPFLTNPNTGDMYTPEEFQKYCEDIVNTAAWGGQLELRALSHILQTPIEIIQADSPPIIVGEEYSKKPLILVYMRHAYGLGEHYNSVTRLVNIVTENCS
Protein: Mitochondrial uncoupling protein Bmcp (Brain mitochondrial carrier protein 1) (Bmcp-1) (Mitochondrial uncoupling protein 5) (Q7K566)
Organism: Drosophila melanogaster (Fruit fly)
Function: Regulates metabolic homeostasis in response to nutritional cues and may therefore be involved in adaptation to dietary variations. May not function in creating mitochondrial proton leaks across the inner mitochondrial membrane (i.e. mitochondrial uncoupling).
Subcellular location: Mitochondrion inner membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- RH64870p
Sequence:
MGEVKDWRPFVYGGVASITAEFGTFPIDTTKTRLQIQGQKIDQSFSQLRYRGMTDAFVKISREEGLRALYSGIWPAVLRQATYGTIKFGTYYTLKKLANERGLLINEDGSERVWSNILCAAAAGAISSAIANPTDVLKVRMQVHGKGQHKGLLGCFGEIYKYEGVRGLWRGVGPTAQRAVVIASVELPVYDFCKLQLMNAFGDHVGNHFISSFIASLGSAIASTPIDVIRTRLMNQRPVSITMNGVVTAAATPKLYSGSLDCAVQTIRNEGLPALYKGFIPTWVRMGPWNIIFFITYEQLKKY