wanglab/gogpt-training-data huggingface dataset:
Protein: Putative aminodeoxychorismate synthase (ADC synthase) (EC 2.6.1.85) (P-aminobenzoic acid synthase) (PABA synthase) (Para-aminobenzoate synthase) (O94277)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Catalyzes the biosynthesis of 4-amino-4-deoxychorismate (ADC) from chorismate and glutamine. Required for the synthesis of 4-aminobenzoate (PABA), an important component in tetrahydrofolate biosynthesis (By similarity).
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus {ECO:0000269|PubMed:16823372}.
Interaction partners:
- Multifunctional tryptophan biosynthesis protein
- Anthranilate phosphoribosyltransferase
- Tryptophan synthase
- Chorismate synthase
- Putative aminodeoxychorismate lyase
- Folic acid synthesis protein fol1
- Probable dihydrofolate synthetase
- Chorismate mutase
- Pentafunctional AROM polypeptide
- Probable anthranilate synthase component 1
Sequence:
MSEISNRLQILLIDCYDSYTFNLYDLLYKASENACVIVVHWDKMSPDLWEDILQFDAIVVGPGPGHPAEYSSILNRIWQLNIPVMGICLGFQSLALYHGATIERMPNLPWHGRVSSVTTSKTFIFDGISAVKGMRYHSLYANKIPIDSLQILAQSDEDNIVMSIKATKFPHFGILYHPESVGSSKSLKIFKNFLSLADTPNIQCVNSFSKSANGFSHNLNRYDISPAAFILKSGSPSLQIHSVEIPWVEPLALADCIQKSGNPICFLDSAKKPGRYSILGILTGPLARIIHYEKATNTTEIRICKDNSFVRINNDLWSTVADFMNQHKAIKPDTNLPFYGGIMGIIGYECSDLSTKSVSNASFPLDFQQTTVDAELAFVDRSFVFDLEIKKLFVQTLTPLNETCSEWWGELLASTCNTKLDNLSCLHSFDGKQNFGLVQSFPKKEVYCESVKACQEHLLAGDSYEMCLTDTTFVSAPPELSDFEMYMRARSLNPATFAGFVRLNHFTLLCCSPERFLQFRDDRCLFSPIKGTLKREGHMSLEEARKKLLNEKDMGELNMIIDLIRNDLHQLAKKNSVHVPELYSVEEHSNVYSLLSNIYGRIESPITAWDVLSKSFPPGSMTGAPKLRSVRMLEPLEQHGRGIYSGTLGYWDVTGSAEFNVIIRSAFKYKADDYWRIGAGGAVTILSSPEGEYEEMVLKANSILPAFVNLKNKKRSCK
Protein: Uncharacterized protein C16C4.02c (O74447)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Interaction partners:
Sequence:
MHIPHFHLHKGPKGVRTISYEQLLSEDDSYASEKLSEDHVTEVHFVTDKDEDSNASGESRGSMELLENCFSLLHAQDDTSKFVSLTMLAKLLNDHPNLIFKCWERMDMKFLDRLLLSTHYEYVDLGVSILLAFCSEEAILRSYEVKKRVSTLLQCCLKHYDLCIPVICTLSSNPKSAKYLLYYTSFIINEFPFEQAFEILSNALYALDNVQTYMRPIFQGIDKRRGWKLDCTFSFFSDLFSRFPVQSWYSEAIRANLQPLMDAVVERFITDKNLSSATVILSNLLKAAGPASIMPNDGFMILVIGRCSAEIRGSLGMLVKAVGQKGKHGTVSYTVCECYEVLGLLIRYLCENCDVLAQRIEPDKFFQLQRSLTELFSDTMDFLRDAWDNNKNRDNLASHVTVISAVATLCLWLTEDDSQYAQASGLMDIFVYLWRHSWSNGIDYAKWISVALPSMLSNKVFFKAFKDFDAWKVVYDDFIKCNDDLKGDKSFNDYILSTNEEDGEDERLAQAIQDFHILIQLNSLVPQSIWNDDIWQEPYWKNLLESNF
Protein: NPC intracellular sterol transporter 1-related protein 1 (Niemann-Pick type C-related protein 1) (Q12200)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Involved in sphingolipid trafficking. May recycle sphingolipids between cellular membranous compartments.
Subcellular location: Vacuole membrane {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:14970192, ECO:0000269|PubMed:15522102}; Multi-pass membrane protein {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:14970192, ECO:0000269|PubMed:15522102}.
Interaction partners:
- Transcription factor TYE7
- Probable transcription factor HMS1
- Phosphatidylglycerol/phosphatidylinositol transfer protein
- Protein NSG2
- Protein NSG1
- Chromatin assembly factor 1 subunit A
Sequence:
MNVLWIIALVGQLMRLVQGTATCAMYGNCGKKSVFGNELPCPVPRSFEPPVLSDETSKLLVEVCGEEWKEVRYACCTKDQVVALRDNLQKAQPLISSCPACLKNFNNLFCHFTCAADQGRFVNITKVEKSKEDKDIVAELDVFMNSSWASEFYDSCKNIKFSATNGYAMDLIGGGAKNYSQFLKFLGDAKPMLGGSPFQINYKYDLANEEKEWQEFNDEVYACDDAQYKCACSDCQESCPHLKPLKDGVCKVGPLPCFSLSVLIFYTICALFAFMWYYLCKRKKNGAMIVDDDIVPESGSLDESETNVFESFNNETNFFNGKLANLFTKVGQFSVENPYKILITTVFSIFVFSFIIFQYATLETDPINLWVSKNSEKFKEKEYFDDNFGPFYRTEQIFVVNETGPVLSYETLHWWFDVENFITEELQSSENIGYQDLCFRPTEDSTCVIESFTQYFQGALPNKDSWKRELQECGKFPVNCLPTFQQPLKTNLLFSDDDILNAHAFVVTLLLTNHTQSANRWEERLEEYLLDLKVPEGLRISFNTEISLEKELNNNNDISTVAISYLMMFLYATWALRRKDGKTRLLLGISGLLIVLASIVCAAGFLTLFGLKSTLIIAEVIPFLILAIGIDNIFLITHEYDRNCEQKPEYSIDQKIISAIGRMSPSILMSLLCQTGCFLIAAFVTMPAVHNFAIYSTVSVIFNGVLQLTAYVSILSLYEKRSNYKQITGNEETKESFLKTFYFKMLTQKRLIIIIFSAWFFTSLVFLPEIQFGLDQTLAVPQDSYLVDYFKDVYSFLNVGPPVYMVVKNLDLTKRQNQQKICGKFTTCERDSLANVLEQERHRSTITEPLANWLDDYFMFLNPQNDQCCRLKKGTDEVCPPSFPSRRCETCFQQGSWNYNMSGFPEGKDFMEYLSIWINAPSDPCPLGGRAPYSTALVYNETSVSASVFRTAHHPLRSQKDFIQAYSDGVRISSSFPELDMFAYSPFYIFFVQYQTLGPLTLKLIGSAIILIFFISSVFLQNIRSSFLLALVVTMIIVDIGALMALLGISLNAVSLVNLIICVGLGVEFCVHIVRSFTVVPSETKKDANSRVLYSLNTIGESVIKGITLTKFIGVCVLAFAQSKIFDVFYFRMWFTLIIVAALHALLFLPALLSLFGGESYRDDSIEAED
Protein: aldehyde dehydrogenase (NAD(+)) (EC 1.2.1.3) (A0A1B0GUA1)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MWRLPRALCVHAAKTSKLSGPWSRPAAFMSTLLINQPQYAWLKELGLREENEGVYNGSWGGRGEVITTYCPANNEPIARVRQASVADYEETVKKAREAWKIWADIPAPKRGEIVRQIGDALREKIQVLGSLVSLEMGKILVEGVGEVQEYVDICDYAVGLSRMIGGPILPSERSGHALIEQWNPVGLVGIITAFNFPVAVYGWNNAIAMICGNVCLWKGAPTTSLISVAVTKIIAKVLEDNKLPGAICSLTCGGADIGTAMAKDERVNLLSFTGSTQVGKQVGLMVQERFGRSLLELGGNNAIIAFEDADLSLVVPSALFAAVGTAGQRCTTARRLFIHESIHDEVVNRLKKAYAQIRVGNPWDPNVLYGPLHTKQAVSMFLGAVEEAKKEGGTVVYGGKVMDRPGNYVEPTIVTGLGHDASIAHTETFAPILYVFKFKNEEEVFAWNNEVKQGLSSSIFTKDLGRIFRWLGPKGSDCGIVNVNIPTSGAEIGGAFGGEKHTGGGRESGSDAWKQYMRRST
Protein: Ubiquilin-2 (Chap1) (DSK2 homolog) (Protein linking IAP with cytoskeleton 2) (PLIC-2) (hPLIC-2) (Ubiquitin-like product Chap1/Dsk2) (Q9UHD9)
Organism: Homo sapiens (Human)
Function: Plays an important role in the regulation of different protein degradation mechanisms and pathways including ubiquitin-proteasome system (UPS), autophagy and the endoplasmic reticulum-associated protein degradation (ERAD) pathway. Mediates the proteasomal targeting of misfolded or accumulated proteins for degradation by binding (via UBA domain) to their polyubiquitin chains and by interacting (via ubiquitin-like domain) with the subunits of the proteasome. Plays a role in the ERAD pathway via its interaction with ER-localized proteins FAF2/UBXD8 and HERPUD1 and may form a link between the polyubiquitinated ERAD substrates and the proteasome. Involved in the regulation of macroautophagy and autophagosome formation; required for maturation of autophagy-related protein LC3 from the cytosolic form LC3-I to the membrane-bound form LC3-II and may assist in the maturation of autophagosomes to autolysosomes by mediating autophagosome-lysosome fusion. Negatively regulates the endocytosis of GPCR receptors: AVPR2 and ADRB2, by specifically reducing the rate at which receptor-arrestin complexes concentrate in clathrin-coated pits (CCPs).
Subcellular location: Cytoplasm {ECO:0000269|PubMed:18199683}. Nucleus {ECO:0000269|PubMed:9853615}. Membrane {ECO:0000250|UniProtKB:Q9QZM0}. Cytoplasmic vesicle, autophagosome {ECO:0000269|PubMed:19148225}. Note=Colocalizes with a subset of proteasomes, namely those that are cytoskeleton associated or free in the cytosol. Associated with fibers in mitotic cells. {ECO:0000269|PubMed:10983987}.
Interaction partners:
- Polyubiquitin-C
- Desumoylating isopeptidase 1
- Heat shock 70 kDa protein 13
- Ubiquitin-ribosomal protein eS31 fusion protein
- Proteasomal ubiquitin receptor ADRM1
- 26S proteasome non-ATPase regulatory subunit 4
- Polyubiquitin-B
- Ubiquitin-ribosomal protein eL40 fusion protein
- TAR DNA-binding protein 43
- Optineurin
Sequence:
MAENGESSGPPRPSRGPAAAQGSAAAPAEPKIIKVTVKTPKEKEEFAVPENSSVQQFKEAISKRFKSQTDQLVLIFAGKILKDQDTLIQHGIHDGLTVHLVIKSQNRPQGQSTQPSNAAGTNTTSASTPRSNSTPISTNSNPFGLGSLGGLAGLSSLGLSSTNFSELQSQMQQQLMASPEMMIQIMENPFVQSMLSNPDLMRQLIMANPQMQQLIQRNPEISHLLNNPDIMRQTLEIARNPAMMQEMMRNQDLALSNLESIPGGYNALRRMYTDIQEPMLNAAQEQFGGNPFASVGSSSSSGEGTQPSRTENRDPLPNPWAPPPATQSSATTSTTTSTGSGSGNSSSNATGNTVAAANYVASIFSTPGMQSLLQQITENPQLIQNMLSAPYMRSMMQSLSQNPDLAAQMMLNSPLFTANPQLQEQMRPQLPAFLQQMQNPDTLSAMSNPRAMQALMQIQQGLQTLATEAPGLIPSFTPGVGVGVLGTAIGPVGPVTPIGPIGPIVPFTPIGPIGPIGPTGPAAPPGSTGSGGPTGPTVSSAAPSETTSPTSESGPNQQFIQQMVQALAGANAPQLPNPEVRFQQQLEQLNAMGFLNREANLQALIATGGDINAAIERLLGSQPS
Protein: Rho-related BTB domain containing, isoform B (M9PG08)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Rho GDP-dissociation inhibitor 3
- Rho-type guanine nucleotide exchange factor, isoform F
- Rho-associated protein kinase
- Formin 3, isoform B
- FI11917p
- Protein diaphanous
- Insulin receptor substrate 53 kDa, isoform A
- IP04855p
- Cofilin/actin-depolymerizing factor homolog
- Cullin 3, isoform F
Sequence:
MPKMDNEQPHQELVKCVLVGDTAVGKTRLICARACNKHVSLSQLLSTHVPTVWAIDQYRIYKDVLERSWEVVDGVNVSLRLWDTFGDHDKDRRFAYGRSDVVLLCFSIASPISLRNCKMMWYPEIRRFCPDVPVILVGCKNDLRYMYRDENYLSYFGEKGTFVRAALKSDLVMPDEARAVAKELGVAYYETSVFTYFGVNEVFENAIRSALIARRQQRFWMTNLKKVQKPLLQAPFRPPKPPPPEVTVMVGNYRQDIYNMFLSQAYTDLVLVGAGGTKFAVHRFMLAAASSIFQRLLSTELTDMGGRSSSESSMVSSTFGEATIADFNDDTEALIRYESRTQRMWEHLKRRSSYQALPLMESKRSNDLYRELHHPVLQSIRLVHVENHRGVNGLQTIVTLSKLISPQALHQCLRFIYTGTIDKDCDNIEEIREAADLLELPQLTQLLSRPQTVMENSSDEPNPHICLRIKESMERHCIGDGCFSDVTFELDDGLMKAHRAVLVGRCDVMRAMLLGDFREAHSNVIVFPGVTIYTFHKLLCYLYTDQIPPISAVKCLNLLELANRLCLPRLLNLVECRVIEDLTLISQNETNETVDHCLKLLEPVKLHNAHQLAEWCMSYLCVNYNLICKFSLKGLKALHQDNQEYLREHRWPPVWYLKDYDYYQRCLNELNKELKLKTSRRESPSDDEGCLCFTGVFSCWLLGKSKRSADVSGTTDNSNADNQIFNSAGNSLNHIDLEADMDLNLXHPALGQGRSLRFIVILPVLICFICTILSILILFQIHT
Protein: Integrase catalytic domain-containing protein (P71644)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Interaction partners:
- Possible transposase
Sequence:
MVSTTGMGRSTARRMLTGPGLPEPAEQVDGRRLRARGFSDDARALLEHVWALMGMPCGKYLVVMLELWLPLEAAAGDLDKPFATEAAVAELKAMSAATVDRYLKPARERMRIKGISTTKPSPLLRNSITIHTCSDEAPKVPGVIEADTVAHCGPSLIGEFARTLTMTDLVTGWTENASIRNNAAKWILEGIKECQQRFPFPMTVFDSDCGGEFINHDVAGWLQARDIAQTRSRPYQKNDQAHVESKNNHVVRKHAFYWRYDTGEELELLNRLWPLVSLRCNFFTPTKKPVGYTSTVNGRRKRIYDKPATPWQRLQASGVLDAQQLSTVAARIEGFNPADLTRQINAIQMQLLDLAKTKTEALATARHIDLQSLQPSINRLAKAK
Protein: Sprouty-related, EVH1 domain-containing protein 3 (Spred-3) (Q6P6N5)
Organism: Mus musculus (Mouse)
Function: Tyrosine kinase substrate that inhibits growth-factor-mediated activation of MAP kinase. Inhibits fibroblast growth factor (FGF)-induced retinal lens fiber differentiation, probably by inhibiting FGF-mediated phosphorylation of ERK1/2. Inhibits TGFB-induced epithelial-to-mesenchymal transition in lens epithelial cells.
Subcellular location: Cell membrane {ECO:0000269|PubMed:12646235, ECO:0000269|PubMed:24705354}; Peripheral membrane protein {ECO:0000269|PubMed:12646235}.
Interaction partners:
- GTPase HRas
- GTPase KRas
- Neurofibromin
Sequence:
MVRVRAVVMARDDSSGGWLPVGGGGLSQVSVCRVRGARPEGGARQGHYVIHGERLRDQKTTLECTLRPGLVYNKVNPIFHHWSLGDCKFGLTFQSPAEADEFQKSLLAALAALSRGSLTPSSSSSSSSPSQDTAETPCPLTSHVDSDSSSSHSRQETPPTAPIATVESAAAFPLATRPQRRRSSAQSYPPLLPFTGIPEPSESLAGAGSQGWGSRGYEDYRRSGPPPPPLALSTCVVRFAKTGALRGAALGPPVSLPAPLTEAAPPAPPARPPPGPGPTPAPAKASPEAEEAARCVHCRALFRRRADGRGGRCAEAPDPGRLLVRRLSCLWCAESLLYHCLSDAEGDFSDPCACEPGHPRPAARWAALAALSLAVPCLCCYAPLRACHWVAARCGCAGCGGRHEEAAR
Protein: Adenine DNA glycosylase (EC 3.2.2.31) (MutY homolog) (hMYH) (Q9UIF7)
Organism: Homo sapiens (Human)
Function: Involved in oxidative DNA damage repair. Initiates repair of A*oxoG to C*G by removing the inappropriately paired adenine base from the DNA backbone. Possesses both adenine and 2-OH-A DNA glycosylase activities.
Subcellular location: Nucleus {ECO:0000269|PubMed:25820570}. Mitochondrion {ECO:0000250|UniProtKB:Q99P21}.
Interaction partners:
- DNA mismatch repair protein Msh6
- DNA repair nuclease/redox regulator APEX1
- N-glycosylase/DNA lyase
- Cell cycle checkpoint control protein RAD9A
- DNA mismatch repair protein Msh2
- Oxidized purine nucleoside triphosphate hydrolase
- DNA mismatch repair protein Mlh1
- Mismatch repair endonuclease PMS2
- Endonuclease III-like protein 1
- DNA polymerase delta catalytic subunit
Sequence:
MTPLVSRLSRLWAIMRKPRAAVGSGHRKQAASQEGRQKHAKNNSQAKPSACDGMIAECPGAPAGLARQPEEVVLQASVSSYHLFRDVAEVTAFRGSLLSWYDQEKRDLPWRRRAEDEMDLDRRAYAVWVSEVMLQQTQVATVINYYTGWMQKWPTLQDLASASLEEVNQLWAGLGYYSRGRRLQEGARKVVEELGGHMPRTAETLQQLLPGVGRYTAGAIASIAFGQATGVVDGNVARVLCRVRAIGADPSSTLVSQQLWGLAQQLVDPARPGDFNQAAMELGATVCTPQRPLCSQCPVESLCRARQRVEQEQLLASGSLSGSPDVEECAPNTGQCHLCLPPSEPWDQTLGVVNFPRKASRKPPREESSATCVLEQPGALGAQILLVQRPNSGLLAGLWEFPSVTWEPSEQLQRKALLQELQRWAGPLPATHLRHLGEVVHTFSHIKLTYQVYGLALEGQTPVTTVPPGARWLTQEEFHTAAVSTAMKKVFRVYQGQQPGTCMGSKRSQVSSPCSRKKPRMGQQVLDNFFRSHISTDAHSLNSAAQ
Protein: FI20146p1 (Q9VLN6)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004370}.
Interaction partners:
- LD11139p
- GEO02653p1
Sequence:
MQSLKTADLPENPREHCNFISAACFWYTMPTFIKGRKRTLDTKDLYRALKEHKSETLGNKLCASWELELEKTKGKPNLLRALLRVFGWYFALLGLVLFLLELGLRTLQPIFLLKLIAYYTHGSESIESAYYYAAGVILCSALNVIIMHPYMLGTMHVGLKMRVGMCSMIYRKALRLSKSALGDTTAGHVVNLMSNDVGRLDLATIFVHYLWVGPLETLFITYLMYREIGIAAVFGVAFMLLFIPLQAYLGKRTSVLRLRTALRTDERVRMMNEIISGIQVIKMYAWELPFEHMVAFARKKEINAIRHVSYIRGILLSFIIFLTRVSIFLSLVGYVLLGTFLTPEVAFLITAYYNILRTTMTVFFPQGISQMAETLVSIKRVQKYMQSDETNVMDMSVDLTEDFQGSNQETVHADGDEERDEAEDKLLGPPIATVNENAKLSEAGISISGLMAKWDVNSPDYSLNGVNLRVQPGTMLGIVGRTGSGKSSLIQAILGELPAESGEIKVNGSMSYASQEPWLFSGTVRQNILFGQPMDRRRYAKVVKKCALERDFELLPFKDKTIVGERGASLSGGQKARISLARAVYRETSIYLLDDPLSAVDTHVARHLFEQCMRGYLRERIVILATHQLQFLQHADQIVIMDKGRVSAVGTYESLRESGLDFASMLADPERDEQSEERSRSRSGSYTHSHSDQRRNSEQSLLSMADSCMDDLEAEQANNQERQEAGQIGLRLYSKYFKAGGGFFAFFVMMGFCVLSQGLASLGDYFLSYWVTKKGNVAYRADNNDTTRSEELEPRLSTWLRDIGLSVDAEMLDTYIFTVITVLTILVTVARSFLFFNLAMKASIRLHNSMFRGITRAAMYFFNTNPSGRILNRFSKDMGQVDEILPAVMMDVIQIFLALAGIVIVIAVVNPLFLIPTVVLGIIFYQLRTFYLKTSRDVKRMEAITRSPVYSHLAASLTGLSTIRAFGAQRVLEAEFDNYQDMHSSAFYMFISTSRAFGYWLDCFCVIYIAIITLSFFIFPPANGGDVGLAITQAMGMTGMVQWGMRQSAELENTMTAVERVVEYEDIEPEGALEAPADKKPPKSWPEQGKIVFDELSLRYTPDPKSENVLKSLSFVIKPKEKVGIVGRTGAGKSSLINALFRLSYNDGSVLIDKRDTSEMGLHDLRSKISIIPQEPVLFSGTMRYNLDPFDEYSDDKLWRSLEEVKLKEVVADLPSGLQSKITEGGTNFSVGQRQLVCLARAILRENRILVMDEATANVDPQTDGLIQTTIRNKFKECTVLTIAHRLHTIMDSDKVLVMDAGRAVEFGTPYELLTLADSKVFHGMVKQTGHATYESLLKIAQKAFENRQNHSLSS
Protein: Keratin-associated protein 6-2 (Q3LI66)
Organism: Homo sapiens (Human)
Function: In the hair cortex, hair keratin intermediate filaments are embedded in an interfilamentous matrix, consisting of hair keratin-associated proteins (KRTAP), which are essential for the formation of a rigid and resistant hair shaft through their extensive disulfide bond cross-linking with abundant cysteine residues of hair keratins. The matrix proteins include the high-sulfur and high-glycine-tyrosine keratins.
Interaction partners:
- Keratin-associated protein 6-1
- Keratin-associated protein 6-3
- Keratin-associated protein 22-1
- Keratin-associated protein 24-1
- Keratin-associated protein 26-1
- Keratin-associated protein 20-2
- Small cysteine and glycine repeat-containing protein 1
- Keratin-associated protein 13-3
- Keratin-associated protein 20-1
- Keratin-associated protein 7-1
Sequence:
MCGSYYGNYYGDHGYGCCGYEGLGYGYGSLRCGYSSCCGYGHGYGSRFFCGCGYGCGSGYYY
Protein: Protein phosphatase 2C, putative (EC 3.1.3.16) (Q38B45)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Serine/threonine protein phosphatase, putative
- Phosphotyrosine protein phosphatase I domain-containing protein
- Serine/threonine-protein phosphatase
- Serine/threonine-protein phosphatase
Sequence:
MSGQGNLLRMFPLQHKKMSQFSLRFLSVGVCEMMNCAEREYMSSFTVHNKFNRSAYAGINPLSSSSTIQSPLMADVVAAGLFDSYTGHSCSRFISKYLARALSMHSTLPEEIAWLRGELKDDPLVTVMTSSLSRSRAMHGTQIDKQGGNGDMHTIRPLFSEWDMQQYAMLADIAFLRACEDSKFESSLPATELANEGSRAVWFTATAAPFSLHEQRRCERSREEASHCGMAPPPLRSLDMPQVASESQRRASADGKVGKKSPKFAADEKEDFEREFCVDVLVSNVGDSRAFGIARNPLTWGQRSLLDSTRERVVPLSVDHKPLRTPEFQRIVSAGGEVRSEVGDMIDANPFYNVSRSFGHWSMKRNPKRAPSEQKITAVPTCSSWEMLPGDVLVLCNHAVFETRSQEDTSIDEAAKVVAREIKHGASPGEAAGALCDYALRFGAGHSLQVLVALATDGGEHCQQDKSGEPYRYDSVIPGPIYVQPCRHSLSYSAALLADCRRCGITLPDLLEKRWLHVRDELCSRYKLPLMYCYGKECSALQQQMEEEALLFSGVSFPPGKRELSELTEKELRCVREEFEKVARSIMPSKNRLPERKV
Protein: Eukaryotic translation initiation factor 2A (eIF-2A) (D3ZUV3)
Organism: Rattus norvegicus (Rat)
Interaction partners:
- Eukaryotic translation initiation factor 3 subunit B
- Eukaryotic translation initiation factor 2 subunit 1
- Eukaryotic translation initiation factor 2 subunit 3, X-linked
- Eukaryotic translation initiation factor 2 subunit 3, Y-linked
- RNA-binding protein 4B
- eIF-2-alpha kinase GCN2
- Eukaryotic translation initiation factor 2, subunit 2
- X-box-binding protein 1
- Translation initiation factor eIF2B subunit alpha
Sequence:
MAPSTPLLTVRGSEGLYMVNGPPHFTESTVLPREPGKNCKVYTFSKDGTLFAWSNGEKVNIINVANKGLLHSFDLPKAVCLEFSPNNTVLATWQPYTTSKDGTAGTPNLQLYDVKTGTCLKSFIQKKMQNWCPSWSDDEIICARNVNNEVHFFENNNFNTIANKLHLQKVNDFNLSPGTQPFKVAVYVPGSKGAPSFVRLYQYPNFAGPQAALANKSFFKADKVTMLWNKKATAVLVIASTDVDKTGASYYGEQTLHYIATNGESAVVQLPKNGPIYDVAWNPSSTEFCAVYGFMPAKATVFNLKCDPVFDFGTGPRNAAFYSPHGHILVLAGFGNLRGQMEVWDVKNYKLISKPVASDSTYFAWCPDGEHILTATCAPRLRVNNGYKIWHYTGSLLYKYDVPSNGELWQVSWQPFLDGIFPAKTITYQAVPSEVPSEEPKVATAYRPPALRNKPVTSSKLHEEEPPQNMKPHPSSDKPLSKTALKNQRKHEAKKAAKQEARNDLAPTPVPQSAPRSTVTQSASGDPEVDKKIKNLKKKLKAIEQLKEQAAAGKQLEKNQLEKIQKETALLQELEDLELGV
Protein: Cofilin-1 (Cofilin, non-muscle isoform) (P18760)
Organism: Mus musculus (Mouse)
Function: Binds to F-actin and exhibits pH-sensitive F-actin depolymerizing activity. In conjunction with the subcortical maternal complex (SCMC), plays an essential role for zygotes to progress beyond the first embryonic cell divisions via regulation of actin dynamics. Required for the centralization of the mitotic spindle and symmetric division of zygotes. Plays a role in the regulation of cell morphology and cytoskeletal organization in epithelial cells (By similarity). Required for the up-regulation of atypical chemokine receptor ACKR2 from endosomal compartment to cell membrane, increasing its efficiency in chemokine uptake and degradation (By similarity). Required for neural tube morphogenesis and neural crest cell migration.
Subcellular location: Nucleus matrix {ECO:0000250|UniProtKB:P10668}. Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:P10668}. Cell projection, ruffle membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250|UniProtKB:P10668}; Cytoplasmic side {ECO:0000250|UniProtKB:P10668}. Cell projection, lamellipodium membrane {ECO:0000250|UniProtKB:P10668}; Peripheral membrane protein {ECO:0000250|UniProtKB:P10668}; Cytoplasmic side {ECO:0000250|UniProtKB:P10668}. Cell projection, lamellipodium {ECO:0000269|PubMed:25107909}. Cell projection, growth cone {ECO:0000269|PubMed:27723745}. Cell projection, axon {ECO:0000269|PubMed:27723745}. Note=Colocalizes with the actin cytoskeleton in membrane ruffles and lamellipodia. Detected at the cleavage furrow and contractile ring during cytokinesis. Almost completely in nucleus in cells exposed to heat shock or 10% dimethyl sulfoxide. {ECO:0000250|UniProtKB:P23528}.
Interaction partners:
- LIM domain kinase 1
- Actin, cytoplasmic 1
- Actin nucleation-promoting factor WASL
- LIM domain kinase 2
- Src substrate cortactin
- Hematopoietic lineage cell-specific protein
- Actin, cytoplasmic 2
- Protein phosphatase Slingshot homolog 1
- WD repeat-containing protein 1
- Protein phosphatase Slingshot homolog 3
Sequence:
MASGVAVSDGVIKVFNDMKVRKSSTPEEVKKRKKAVLFCLSEDKKNIILEEGKEILVGDVGQTVDDPYTTFVKMLPDKDCRYALYDATYETKESKKEDLVFIFWAPENAPLKSKMIYASSKDAIKKKLTGIKHELQANCYEEVKDRCTLAEKLGGSAVISLEGKPL
Protein: Segregation and condensation protein B (P35155)
Organism: Bacillus subtilis (strain 168)
Function: Participates in chromosomal partition during cell division. May act via the formation of a condensin-like complex containing Smc and ScpA that pull DNA away from mid-cell into both cell halves.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:12897137}. Note=Associated with two foci at the outer edges of the nucleoid region in young cells, and at four foci within both cell halves in older cells.
Interaction partners:
- Segregation and condensation protein A
- Stage 0 sporulation protein J
- Chromosome partition protein Smc
- Uncharacterized protein YpuI
- Ribosomal large subunit pseudouridine synthase B
- Uncharacterized protein YpuF
- Cytidylate kinase
- Protein RibT
- Uncharacterized RNA pseudouridine synthase YtzG
- DNA topoisomerase 3
Sequence:
MGLDIVNWKAIVEALLYAAGDEGLTKKQLLTVLEIEEPELNTIMADVADEYRGDTRGIELIEYADTYMLSTKKDFAPYLKKLIEVPSKGLSQASLEVLAIVSYKQPITRAEIEEIRGVKSERILHSLVAKALLCEVGRADGPGRAILYGTTPTFLEQFGLKTLDELPPLPENAEEDVLQEEADLFFENFNQTFEDIK
Protein: Inclusion body clearance protein IML2 (O94699)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Inclusion body (IB) resident protein that interacts strongly with lipid droplet (LD) proteins. Involved in LD-mediated IB clearing after protein folding stress, probably by enabling access to the IBs of an LD-stored soluble sterol derivative that acts as chaperone in inclusion clearing.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:P47031}. Nucleus {ECO:0000250|UniProtKB:P47031}. Note=Localized exclusively in cytoplasmic inclusion bodies under protein folding stress conditions. {ECO:0000250|UniProtKB:P47031}.
Interaction partners:
- Vacuolar segregation protein 7
- Large ribosomal subunit protein eL20B
- Vacuolar protein sorting-associated protein 3
- Vacuolar fusion protein mon1
- Vitamin H transporter 1
Sequence:
MSKSQEQRLQNFVTVIQGLNDILDDKMDEATEKFKSGNSSFHLSGQAVVAFIQAVLTFEPSRFKDSQNRIDIAIKALSADKDDASKNNTFLSTFDPGVEYRVSIGLMLLLSALIGFCSESIVTSVKSVYKLRKAHSIFSKINKRHFDHFSAAFHSTGRSDVDLANEYVQTGTLLCTGLFTLLISLLPPKMITILNVFGYKGDRDWALQCMWMPALQRPTSFFAAVAFAALIQYYSGAVQLCSIYKKTPEEPDGWPDKRCFEILEKVEKAHPDGPMWPLHRAKLLSMVKKQDEAIVVLEELMAKPPPRLKQLEVLIVFEHALDCAFSHRYVDGANSFLKLSSLNDSSTALYSYFAAACFLQDVHVNANVEALEKASKLLEPLHDLVANKTAPLDVHIRRKVGKLIKRRASAGNQGGLAEYVGFSPLYELVYVWNGFRRMTDDELSKFDVERMEPWQDQDDDICQALIKATVLRNLGRTDEVFPILQKICAVTRTTETWAVAFAHYEMAVAFFESNGSKKEGLKHCDAYLRKARDFGGDNEFESRLIIRVQLARHVVRKCLQSMS
Protein: Uncharacterized protein (Q387I1)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MGDKVEYGTSTVKSLGDTCRLVRALQGSTDPRLVSINSLLEGVVKSAQSLVKGTDSQKRFNMEFAEFCGVALMGLPDLEDAVDDLRVQENCANAAVNDQDDFDGISPAIFMREIIGYVVSRNTNVGAQYLEHIGRSAMAKFAGQESSEVTPKRLKSGMNDERHVQSVARKKQRTRPVAGKMGRAPTDDKSGVAATGRVFGVDGDEPKQRYKQSRPKGPPMLSRWVKPWTLLNQRVQGIILEHASNENTRRPPVCNYPPGKRSNITPFDICTAPSGPEMLNLWHARESMTSSSVGHCDPVGVAFDETALDHDSKGSEPSFFPSGDKKVCAFVSSELMANLVRYGVSSLEAPFKGAK
Protein: CAAX prenyl protease 1 homolog (EC 3.4.24.84) (Farnesylated proteins-converting enzyme 1) (FACE-1) (Prenyl protein-specific endoprotease 1) (Zinc metalloproteinase Ste24 homolog) (O75844)
Organism: Homo sapiens (Human)
Function: Transmembrane metalloprotease whose catalytic activity is critical for processing lamin A/LMNA on the inner nuclear membrane and clearing clogged translocons on the endoplasmic reticulum. Proteolytically removes the C-terminal three residues of farnesylated proteins. Plays also an antiviral role independently of its protease activity by restricting enveloped RNA and DNA viruses, including influenza A, Zika, Ebola, Sindbis, vesicular stomatitis, cowpox, and vaccinia. Mechanistically, controls IFITM antiviral pathway to hinder viruses from breaching the endosomal barrier by modulating membrane fluidity.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:23539603}; Multi-pass membrane protein {ECO:0000255}. Nucleus inner membrane {ECO:0000269|PubMed:23539603}; Multi-pass membrane protein {ECO:0000255}. Early endosome membrane {ECO:0000269|PubMed:35283811}; Multi-pass membrane protein {ECO:0000255}. Late endosome membrane {ECO:0000269|PubMed:35283811}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Protein-S-isoprenylcysteine O-methyltransferase
- CAAX prenyl protease 2
- Protein farnesyltransferase subunit beta
- Prelamin-A/C
- Protein farnesyltransferase/geranylgeranyltransferase type-1 subunit alpha
- Seipin
- 1-acyl-sn-glycerol-3-phosphate acyltransferase beta
- SUN domain-containing protein 1
- Emerin
- Lamin-B1
Sequence:
MGMWASLDALWEMPAEKRIFGAVLLFSWTVYLWETFLAQRQRRIYKTTTHVPPELGQIMDSETFEKSRLYQLDKSTFSFWSGLYSETEGTLILLFGGIPYLWRLSGRFCGYAGFGPEYEITQSLVFLLLATLFSALTGLPWSLYNTFVIEEKHGFNQQTLGFFMKDAIKKFVVTQCILLPVSSLLLYIIKIGGDYFFIYAWLFTLVVSLVLVTIYADYIAPLFDKFTPLPEGKLKEEIEVMAKSIDFPLTKVYVVEGSKRSSHSNAYFYGFFKNKRIVLFDTLLEEYSVLNKDIQEDSGMEPRNEEEGNSEEIKAKVKNKKQGCKNEEVLAVLGHELGHWKLGHTVKNIIISQMNSFLCFFLFAVLIGRKELFAAFGFYDSQPTLIGLLIIFQFIFSPYNEVLSFCLTVLSRRFEFQADAFAKKLGKAKDLYSALIKLNKDNLGFPVSDWLFSMWHYSHPPLLERLQALKTMKQH