wanglab/gogpt-training-data huggingface dataset:
Protein: Ski oncogene (Proto-oncogene c-Ski) (A0A0G2K628)
Organism: Rattus norvegicus (Rat)
Interaction partners:
- Mothers against decapentaplegic homolog 4
- Mothers against decapentaplegic homolog 2
- Mothers against decapentaplegic homolog 3
- Mothers against decapentaplegic homolog 5
- Methyl-CpG-binding protein 2
- Mothers against decapentaplegic homolog 9
- Mothers against decapentaplegic homolog 1
- RING-type E3 ubiquitin transferase
- Nuclear receptor corepressor 1
- Paired amphipathic helix protein Sin3a
Sequence:
MEAAAAGRGGFQPHPGLQKTLEQFHLSSMSSLGGPAAFSARWAQEAYKKESAKEAGAATVPAPVPTAAEPPPVLHLPAIQPPPPVLPGPFFMPSDRSTERCETVLEGETISCFVVGGEKRLCLPQILNSVLRDFSLQQINSVCDELHIYCSRCTADQLEILKVMGILPFSAPSCGLITKTDAERLCNALLYGGAYPPPCKKELAASLALGLELSERSVRVYHECFGKCKGLLVPELYSSPSAACIQCLDCRLMYPPHKFVVHSHKALENRTCHWGFDSANWRAYILLSQDYTGKEEQARLGRCLDDVKEKFDYANKYKRRVPRVSEPPASIRPKTDDTSSQSPASSEKDKQSTWLRTLAGSSNKSLGCAHPRQRLSAFRPWSPAVSASEKETSPHLPALIRDSFYSYKSFETAVAPNVALAPPTQQKVVNSPPCTTVVSRAPEPLTTCIQPRKRKLTMDAPGAPDMLTPVAAAEEDKDSEAEVEVESREEFTSSLSSLSSPSFTSSSSAKDLSSPGMHAPPVAAPDAAAHADAPSGLEAELEHLRQALEGGLDTKEAKEKFLHEVVKMRVKQEEKLTAALQAKRSLHQELEFLRVAKKEKLREATEAKRSLRKEIERLRAENEKKMKEANESRVRLKRELEQARQVRVCDKGCEAGRLRAKYSAQIEDLQAKLQHAEADREQLRADLLREREAREHLEKVVKELQEQLWPRPRPENSGGESNAELDP
Protein: DNA-directed RNA polymerase subunit Rpo4 (EC 2.7.7.6) (DNA-directed RNA polymerase subunit F) (Q4JB12)
Organism: Sulfolobus acidocaldarius (strain ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770)
Function: DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. This subunit is less well bound than the others (Ref.3). Probably not involved in transcription inititation (Probable).
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00864}.
Interaction partners:
- DNA-directed RNA polymerase subunit Rpo5
- DNA-directed RNA polymerase subunit Rpo7
- DNA-directed RNA polymerase subunit Rpo12
- DNA-directed RNA polymerase subunit Rpo1N
- DNA-directed RNA polymerase subunit Rpo10
- DNA-directed RNA polymerase subunit Rpo3
- DNA-directed RNA polymerase subunit Rpo11
- DNA-directed RNA polymerase subunit Rpo2
- DNA-directed RNA polymerase subunit Rpo6
- DNA-directed RNA polymerase subunit Rpo1C
Sequence:
MSYSLKTIEEHFVPYSIAKKYIKELIDTGSSSNLIQKTFDYLNSISRCDEDSASKIMKELEEIVKREDVRAVLASICPTTVEEVRSVLVIDPSTIYSTEQIQKIIEIIKKYVES
Protein: Importin subunit alpha-2 (IMPa-2) (F4JL11)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Binds to conventional NLS motifs and mediates nuclear protein import across the nuclear envelope (By similarity). Acts as cellular receptor for the nuclear import of the virD2 protein of Agrobacterium, but is not essential for Agrobacterium-mediated root transformation.
Subcellular location: Nucleus envelope {ECO:0000250|UniProtKB:Q96321}.
Interaction partners:
- Importin subunit beta-1
- Transcription factor VIP1
- Nuclear cap-binding protein subunit 1
- Exportin-2
- Nuclear pore complex protein NUP50A
- Transportin
- Ran-binding protein 1 homolog a
- F-box protein VBF
- Nucleoporin
- Nuclear cap-binding protein subunit 2
Sequence:
MSLRPNAKTEVRRNRYKVAVDAEEGRRRREDNMVEIRKSKREESLQKKRREGLQANQLPQFAPSPVPASSTVEKKLESLPAMVGGVWSDDRSLQLEATTQFRKLLSIERSPPIEEVIDAGVVPRFVEFLTREDYPQLQFEAAWALTNIASGTSENTKVVIEHGAVPIFVQLLASQSDDVREQAVWALGNVAGDSPRCRDLVLGQGALIPLLSQLNEHAKLSMLRNATWTLSNFCRGKPQPPFDQVRPALPALERLIHSTDEEVLTDACWALSYLSDGTNDKIQSVIEAGVVPRLVELLQHQSPSVLIPALRSIGNIVTGDDLQTQCVISHGALLSLLSLLTHNHKKSIKKEACWTISNITAGNRDQIQAVCEAGLICPLVNLLQNAEFDIKKEAAWAISNATSGGSPDQIKYMVEQGVVKPLCDLLVCPDPRIITVCLEGLENILKVGEAEKVTGNTGDVNFYAQLIDDAEGLEKIENLQSHDNSEIYEKAVKILETYWLEEEDETLPPGDPSAQGFQFGGGNDAAVPPGGFNFQ
Protein: Eukaryotic translation initiation factor 4E homologous protein, isoform B (E1JIV5)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Eukaryotic translation initiation factor 4G1, isoform B
- GIGYF family protein Gyf
- Eukaryotic translation initiation factor 4 gamma 2
- Cytoplasmic FMR1-interacting protein
- Eukaryotic initiation factor 4A
- Eukaryotic translation initiation factor 4E1
- eIF-4F 25 kDa subunit
- eIF-4F 25 kDa subunit
- eIF-4F 25 kDa subunit
- eIF-4F 25 kDa subunit
Sequence:
MSMEKVANKQYETKNWPDIVDSDDSDVDNQIDVDNLPPLEVGPGENRLQHTYCLWFSRKETQRAAADYSKSLHMVGRCASVQQWWSLYSHLIRPTALKPYRELLLFKQGIIPMWEDPANSKGGQWLIRLRKNKVDRAWENVCMAMLGEQFLVGDEICGVVLQTKYPNPSIQVACSSRPIICIIYTRFVVQFGKCKIIIVTNNNKRNVYEFLTIIVIKIHEEMLSLLSRKCKFVNAPNELVTRIGRFLF
Protein: Potassium voltage-gated channel subfamily E member 4 (MinK-related peptide 3) (MiRP3) (Minimum potassium ion channel-related peptide 3) (Potassium channel subunit beta MiRP3) (Q8WWG9)
Organism: Homo sapiens (Human)
Function: Ancillary protein that assembles as a beta subunit with a voltage-gated potassium channel complex of pore-forming alpha subunits. Modulates the gating kinetics and enhances stability of the channel complex. May associate with KCNQ1/KVLTQ1 and inhibit potassium current.
Subcellular location: Membrane {ECO:0000305|PubMed:27162025}; Single-pass membrane protein {ECO:0000255}.
Interaction partners:
- Potassium voltage-gated channel subfamily KQT member 4
- Potassium voltage-gated channel subfamily E member 3
- Potassium voltage-gated channel subfamily KQT member 1
- Potassium voltage-gated channel subfamily E member 1
- Potassium voltage-gated channel subfamily KQT member 5
- Potassium voltage-gated channel subfamily E member 2
- Voltage-gated inwardly rectifying potassium channel KCNH2
- Voltage-gated potassium channel KCNC4
- Potassium voltage-gated channel subfamily E regulatory beta subunit 5
- Sodium channel regulatory subunit beta-1
Sequence:
MHFLTIYPNCSSGVVRAQSRTEQKNPLGLDDLGIQNLGQTVSLAPAVEAASMLKMEPLNSTHPGTAASSSPLESRAAGGGSGNGNEYFYILVVMSFYGIFLIGIMLGYMKSKRREKKSSLLLLYKDEERLWGEAMKPLPVVSGLRSVQVPLMLNMLQESVAPALSCTLCSMEGDSVSSESSSPDVHLTIQEEGADDELEETSETPLNESSEGSSENIHQNS
Protein: Profilin (E0XJL2)
Organism: Gossypium hirsutum (Upland cotton) (Gossypium mexicanum)
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000256|ARBA:ARBA00004245}.
Interaction partners:
- Actin
- Actin
- Actin
- actin
- Actin depolymerizing factor 7
- Actin-depolymerizing factor
- Actin-depolymerizing factor 2-like
- Actin depolymerizing factor 2
Sequence:
MSWQAYVDDHLMCEIEGNHLSAAAIIAHDGSVWAQSANFPQFKPEEINAIMNDFNEPGTLAPTGLHLGGTKYMVIQGEPGAVIRGKKGPGGVTVKKTNMALIIGIYDEPMTPGQCNMIVERLGDYLLDQGY
Protein: Nipped-B protein (A0A590UJS4)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|RuleBase:RU364107}.
Interaction partners:
Sequence:
MNGDMPHVPITTLAGIASLTDLLNQLPLPSPLPATTTKSLLFNARIAEEVNCLLACRDDNLVSQLVHSLNQVSTDHIELKDNLGSDDPEGDIPVLLQAVLARSPNVFREKSMQNRYVQSGMMMSQYKLSQNSMHSSPASSNYQQTTISHSPSSRFVPPQTSSGNRFMPQQNSPVPSPYAPQSPAGYMPYSHPSSYTTHPQMQQASVSSPIVAGGLRNIHDNKVSGPLSGNSANHHADNPRHGSSEDYLHMVHRLSSDDGDSSTMRNAASFPLRSPQPVCSPAGSEGTPKGSRPPLILQSQSLPCSSPRDVPPDILLDSPERKQKKQKKMKLGKDEKEQSEKAAMYDIISSPSKDSTKLTLRLSRVRSSDMDQQEDMISGVENSNVSENDIPFNVQYPGQTSKTPITPQDINRPLNAAQCLSQQEQTAFLPANQVPVLQQNTSVAAKQPQTSVVQNQQQISQQGPIYDEVELDALAEIERIERESAIERERFSKEVQDKDKPLKKRKQDSYPQEAGGATGGNRPASQETGSTGNGSRPALMVSIDLHQAGRVDSQASITQDSDSIKKPEEIKQCNDAPVSVLQEDIVGSLKSTPENHPETPKKKSDPELSKSEMKQSESRLAESKPNENRLVETKSSENKLETKVETQTEELKQNESRTTECKQNESTIVEPKQNENRLSDTKPNDNKQNNGRSETTKSRPETPKQKGESRPETPKQKSDGHPETPKQKGDGRPETPKQKGESRPETPKQKNEGRPETPKHRHDNRRDSGKPSTEKKPEVSKHKQDTKSDSPRLKSERAEALKQRPDGRSVSESLRRDHDNKQKSDDRGESERHRGDQSRVRRPETLRSSSRNEHGIKSDSSKTDKLERKHRHESGDSRERPSSGEQKSRPDSPRVKQGDSNKSRSDKLGFKSPTSKDDKRTEGNKSKVDTNKAHPDNKAEFPSYLLGGRSGALKNFVIPKIKRDKDGNVTQETKKMEMKGEPKDKVEKIGLVEDLNKGAKPVVVLQKLSLDDVQKLIKDREDKSRSSLKPIKNKPSKSNKGSIDQSVLKELPPELLAEIESTMPLCERVKMNKRKRSTVNEKPKYAEISSDEDNDSDEAFESSRKRHKKDDDKAWEYEERDRRSSGDHRRSGHSHEGRRSSGGGRYRNRSPSDSDMEDYSPPPSLSEVARKMKKKEKQKKRKAYEPKLTPEEMMDSSTFKRFTASIENILDNLEDMDFTAFGDDDEIPQELLLGKHQLNELGSESAKIKAMGIMDKLSTDKTVKVLNILEKNIQDGSKLSTLLNHNNDTEEEERLWRDLIMERVTKSADACLTTINIMTSPNMPKAVYIEDVIERVIQYTKFHLQNTLYPQYDPVYRLDPHGGGLLSSKAKRAKCSTHKQRVIVMLYNKVCDIVSSLSELLEIQLLTDTTILQVSSMGITPFFVENVSELQLCAIKLVTAVFSRYEKHRQLILEEIFTSLARLPTSKRSLRNFRLNSSDMDGEPMYIQMVTALVLQLIQCVVHLPSSEKDSNAEEDSNKKIDQDVVITNSYETAMRTAQNFLSIFLKKCGSKQGEEDYRPLFENFVQDLLSTVNKPEWPAAELLLSLLGRLLVHQFSNKSTEMALRVASLDYLGTVAARLRKDAVTSKMDQGSIERILKQVSGGEDEIQQLQKALLDYLDENTETDPSLVFSRKFYIAQWFRDTTLETEKAMKSQKDEESSEGTHHAKEIETTGQIMHRAENRKKFLRSIIKTTPSQFSTLKMNSDTVDYDDACLIVRYLASMRPFAQSFDIYLTQILRVLGENAIAVRTKAMKCLSEVVAVDPSILARLDMQRGVHGRLMDNSTSVREAAVELLGRFVLCRPQLAEQYYDMLIERILDTGISVRKRVIKILRDICIEQPTFPKITEMCVKMIRRVNDEEGIKKLVNETFQKLWFTPTPHNDKEAMTRKILNITDVVAACRDTGYDWFEQLLQNLLKSEEDSSYKPVKKACTQLVDNLVEHILKYEESLADSDNKGVNSGRLVACITTLFLFSKIRPQLMVKHAMTMQPYLTTKCSTQNDFMVICNVAKILELVVPLMEHPSETFLATIEEDLMKLIIKYGMTVVQHCVSCLGAVVNKVTQNFKFVWACFNRYYGAISKLKSQHQEDPNNTSLLTNKPALLRSLFTVGALCRHFDFDLEDFKGNSKVNIKDKVLELLMYFTKHSDEEVQTKAIIGLGFAFIQHPSLMFEQEVKNLYNNILSDKNSSVNLKIQVLKNLQTYLQEEDTRMQQADRDWKKVAKQEDLKEMGDVSSGMSSSIMQLYLKQVLEAFFHTQSSVRHFALNVIALTLNQGLIHPVQCVPYLIAMGTDPEPAMRNKADQQLVEIDKKYAGFIHMKAVAGMKMSYQVQQAINTCLKDPVRGFRQDESSSALCSHLYSMIRGNRQHRRAFLISLLNLFDDTASMVKDKRKERKSSPSKENESSDSEEEVSRPRKSRKRVDSDSDSDSEDDINSVMKCLPENSAPLIEFANVSQGILLLLMLKQHLKNLCGFSDSKIQKYSPSESAKVYDKAINRKTGVHFHPKQTLDFLRSDMANSKITEEVKRSIVKQYLDFKLLMEHLDPDEEEEEGEVSASTNARNKAITSLLGGGSPKNNTAAETEDDESDGEDRGGGTSGVRRRRSQRISQRITH
Protein: Homeobox protein engrailed-like (A0A0G2JT82)
Organism: Rattus norvegicus (Rat)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|PROSITE-ProRule:PRU00108, ECO:0000256|RuleBase:RU000682}.
Interaction partners:
- Hepatocyte nuclear factor 3-beta
- Nuclear receptor subfamily 4 group A member 2
- Paired box 2
Sequence:
MEEQQPEPKSQRDSGLGAVAAAAPGGLSLSLSPGASGSSGSDGDSVPVSPQPAPPSPPAAPCLPPLAHHPHLPPHPPPPPPPPPPPPPPQHLAAPAHQPQPAAQLHRTTNFFIDNILRPDFGCKKEQPLPQLLVASAAAGGGAAGGGSRVERDRSQTGAGRDPVHSLGTRASGAASLLCAPDANCGPPDGSQPATAVGAGASKAGNPAAAAAAAAAAAAAAVAAAAAAASKPSDSGGGSGGSAGSPGAQGAKFPEHNPAILLMGSANGGPVVKTDSQQPLVWPAWVYCTRYSDRPSSGPRTRKLKKKKNEKEDKRPRTAFTAEQLQRLKAEFQANRYITEQRRQTLAQELSLNESQIKIWFQNKRAKIKKATGIKNGLALHLMAQGLYNHSTTTVQDKDESE
Protein: Protein shisa-2 homolog (Shisa-like protein 2) (mShisa) (Transmembrane protein 46) (Q8QZV2)
Organism: Mus musculus (Mouse)
Function: Plays an essential role in the maturation of presomitic mesoderm cells by individual attenuation of both FGF and WNT signaling.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}.
Interaction partners:
- Protein shisa-7
Sequence:
MWGGRCSPSTSSRHRASLLQLLLAALLAAGARASGEYCHGWLDAQGVWRIGFQCPERFDGGDATICCGSCALRYCCSSAEARLDQGGCDNDRQQGVGEPGRTDREGPDSSAVPIYVPFLIVGSVFVAFIILGSLVAACCCRCLRPKQDPQQSRAPGANRLMETIPMIPSASTSRGSSSRQSSTAASSSSSANSGARAPPTRSQTNCCLPEGTMNNVYVNMPTNFSVLNCQQATQIVPHQGQYLHTPYVGYAVQHDSVPMTPVPPFMDGLQPGYRPVQPPFAHTNSEQKMFPAVTV
Protein: Serine/threonine-protein kinase 16 (EC 2.7.11.1) (Myristoylated and palmitoylated serine/threonine-protein kinase) (MPSK) (Protein kinase PKL12) (TGF-beta-stimulated factor 1) (TSF-1) (Tyrosine-protein kinase STK16) (EC 2.7.10.2) (P57760)
Organism: Rattus norvegicus (Rat)
Function: Membrane-associated protein kinase that phosphorylates on serine and threonine residues. In vitro substrates include DRG1, ENO1 and EIF4EBP1. Also autophosphorylates (By similarity). May be involved in secretory vesicle trafficking or intracellular signaling. May have a role in regulating stromal-epithelial interactions that occur during ductal morphogenesis in the mammary gland. May be involved in TGF-beta signaling. Able to autophosphorylate on Tyr residue; it is however unclear whether it has tyrosine-protein kinase toward other proteins.
Subcellular location: Cytoplasm, perinuclear region. Membrane {ECO:0000250}; Lipid-anchor {ECO:0000250}. Note=Associates with Golgi and Golgi-derived vesicles. {ECO:0000250}.
Interaction partners:
Sequence:
MGHALCVCSRGTVIIDNKRYLFVQKLGEGGFSYVDLVEGLHDGHFYALKRILCHEQQDQEEAQREADMHRLFQHPNILRLMAYSLKERGAKHEAWLLLPFFKRGTLWNEIERLKDQGNFLTEDQILPLLLGICRGLEAIHAKGYAHRDLKPTNILLGDEGQPVLMDLGSMNQACIQVEGSRQALALQDWAAQRCTISYRAPELFSVQSHCVIDERTDVWSLGCVLYAMMFGEGPYDMVFQKGDSVALAVQNDLSIPQSPRHSSALRQLLASMMTVDPQQRPHIPVLLSQLEALQPPAPGQHTTQI
Protein: S-adenosylmethionine synthase (EC 2.5.1.6) (Q5BE08)
Organism: Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Interaction partners:
- 5-methyltetrahydropteroyltriglutamate--homocysteine S-methyltransferase
- Homocysteine S-methyltransferase
- NAD dependent epimerase/dehydratase family protein
- S-adenosylmethionine decarboxylase
- DNA
- SPEE_NEUCR Spermidine synthase
- Methionine synthase, vitamin-B12 independent, putative
- GAF domain nucleotide-binding protein
- Aromatic-amino-acid transaminase, hypothetical
- aromatic-amino-acid transaminase
Sequence:
MGSVATPNGTFLFTSESVGRGHPDKIADQISDAILDACLAEDPLSKVACETATKTGMIMVFGEITTQARLDYQAIIRGAIKDIGYDDSEKGFDYKTCNVLVAIEQQSPDIAQGLHYEEALEKLGAGDQGIMFGYATDETPELLPLTLVLSHKLNAAMTTARNDGSIPWLRPDTKTQVTVEYAHDNGAVKPLRVDTVVVSAQHSDDVTTEELRAVIKEKIIKKVIPAELLDDRTVYHIQPSGRFVIGGPQGDAGLTGRKIIVDTYGGWGAHGGGAFSGKDYSKVDRSAAYVGRWIAKSLVAAGLARRALVQLSYAIGVAEPLSLYVDTYGTSEKTSEELVQIIRNNFDLRPGVIVRELDLAKPIYFETAQNGHFTNQKFSWEQPKALKF
Protein: Serine/threonine-protein kinase YPK1 (EC 2.7.11.1) (Sphingosine-like immunosuppressant resistant protein 2) (Yeast protein kinase 1) (P12688)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Plays an essential role in the proliferation of yeast cells. Involved in a signaling pathway, required for optimal cell wall integrity, that acts in parallel with the PKC1-SLT2-dependent pathway. Downstream kinase in the sphingolipid-mediated signaling pathway. Its phosphorylation is regulated by the intracellular sphingolipid concentration. Cooperates with SLI1 in mediating resistance to the sphingolipid biosynthesis inhibitor drug myriocin (ISP-1). Its kinase activity is essential for the resistance. Required for both receptor-mediated and fluid-phase endocytosis, but is not necessary for receptor phosphorylation or ubiquitination. Necessary for the internalization of plasma membrane proteins carrying different types of internalization signals. Acts downstream of the PKH kinases to control endocytosis by phosphorylating components of the endocytic machinery. Phosphorylation of residue Thr-504 in the activation loop is essential for activity. phosphorylates and down-regulates flippase activator FPK1.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:10825204, ECO:0000269|PubMed:12221112, ECO:0000269|PubMed:14562095}. Cell membrane {ECO:0000305}; Peripheral membrane protein {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Note=Intracellular localization is regulated by the intracellular sphingolipid levels. During the yeast cell cycle, distributed both on the plasma membrane and in the cytosol. Greater accumulation was detected on the plasma membrane, such as in the budding area, a daughter cell and the neck region of the mother cell in the S phase, and the septum between a mother cell and a daughter cell in the G2 phase.
Interaction partners:
- Serine/threonine-protein kinase TOR2
- Target of rapamycin complex 2 subunit TSC11
- Protein ORM2
- Target of rapamycin complex 2 subunit AVO1
- Serine/threonine-protein kinase PKH2
- cAMP-dependent protein kinase regulatory subunit
- Serine/threonine-protein kinase BCK1/SLK1/SSP31
- Flippase kinase 1
- Protein ORM1
- Serine/threonine-protein kinase TOR1
Sequence:
MYSWKSKFKFGKSKEEKEAKHSGFFHSSKKEEQQNNQATAGEHDASITRSSLDRKGTINPSNSSVVPVRVSYDASSSTSTVRDSNGGNSENTNSSQNLDETANIGSTGTPNDATSSSGMMTIKVYNGDDFILPFPITSSEQILNKLLASGVPPPHKEISKEVDALIAQLSRVQIKNQGPADEDLISSESAAKFIPSTIMLPGSSTLNPLLYFTIEFDNTVATIEAEYGTIAKPGFNKISTFDVTRKLPYLKIDVFARIPSILLPSKTWQQEMGLQDEKLQTIFDKINSNQDIHLDSFHLPINLSFDSAASIRLYNHHWITLDNGLGKINISIDYKPSRNKPLSIDDFDLLKVIGKGSFGKVMQVRKKDTQKVYALKAIRKSYIVSKSEVTHTLAERTVLARVDCPFIVPLKFSFQSPEKLYFVLAFINGGELFYHLQKEGRFDLSRARFYTAELLCALDNLHKLDVVYRDLKPENILLDYQGHIALCDFGLCKLNMKDDDKTDTFCGTPEYLAPELLLGLGYTKAVDWWTLGVLLYEMLTGLPPYYDEDVPKMYKKILQEPLVFPDGFDRDAKDLLIGLLSRDPTRRLGYNGADEIRNHPFFSQLSWKRLLMKGYIPPYKPAVSNSMDTSNFDEEFTREKPIDSVVDEYLSESVQKQFGGWTYVGNEQLGSSMVQGRSIR
Protein: DDRGK domain-containing protein 1 (UFM1-binding and PCI domain-containing protein 1) (Q80WW9)
Organism: Mus musculus (Mouse)
Function: Substrate adapter for ufmylation, the covalent attachment of the ubiquitin-like modifier UFM1 to substrate proteins, which plays a key role in reticulophagy (also called ER-phagy) (By similarity). In response to endoplasmic reticulum stress, promotes recruitment of the E3 UFM1-protein ligase UFL1 to the endoplasmic reticulum membrane: in turn, UFL1 mediates ufmylation of proteins such as RPN1 and RPL26/uL24, promoting reticulophagy of endoplasmic reticulum sheets (By similarity). Ufmylation-dependent reticulophagy inhibits the unfolded protein response (UPR) by regulating ERN1/IRE1-alpha stability. Ufmylation in response to endoplasmic reticulum stress is essential for processes such as hematopoiesis or inflammatory response. Required for TRIP4 ufmylation, thereby regulating nuclear receptors-mediated transcription. May play a role in NF-kappa-B-mediated transcription through regulation of the phosphorylation and the degradation of NFKBIA, the inhibitor of NF-kappa-B. Plays a role in cartilage development through SOX9, inhibiting the ubiquitin-mediated proteasomal degradation of this transcriptional regulator.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:37795761}; Single-pass membrane protein {ECO:0000250|UniProtKB:Q96HY6}.
Interaction partners:
- E3 UFM1-protein ligase 1
- CDK5 regulatory subunit-associated protein 3
- Ubiquitin-fold modifier 1
- Ubiquitin-fold modifier-conjugating enzyme 1
- Ufm1-specific protease 2
- Ubiquitin-like modifier-activating enzyme 5
- Ufm1-specific protease 1
Sequence:
MVGPWVYLVAAVLLIGLILFLTRSRGRAAAADGEPLHNEEERAGAGQVGRSLPQESEEQRTGSRPRRRRDLGSRLQAQRRAQRVAWEDGDENVGQTVIPAQEEEGIEKPAEVHPTGKIGAKKLRKLEEKQARKAQREAEEAEREERKRLESQREAEWKKEEERLRLKEEQKEEEERKAQEEQARREHEEYLKLKEAFVVEEEGVSETMTEEQSHSFLTEFINYIKKSKVVLLEDLAFQMGLRTQDAINRIQDLLTEGTLTGVIDDRGKFIYITPEELAAVANFIRQRGRVSITELAQASNSLISWGQDLPAQASA
Protein: T3SS secreted effector EspL (A0A0H3JP21)
Organism: Escherichia coli O157:H7
Interaction partners:
- Protein-arginine N-acetylglucosaminyltransferase NleB1
- Effector protein NleF
- T3SS secreted effector NleH
- Cysteine S-methyltransferase NleE
- T3SS secreted effector NleA/EspI
Sequence:
MPIINKSASNYVEYISKNNPPYLSKKRDASINLNGKVSDCNGEIIWCRHIASYWSEFFCSNSGKIDYETFSSPQLLSKAIVIQENKGTNNIKGDVYFVENESWGSVIYNLFLQLEKENKSHTSLEVHSPGHAMALGIKIKNDKENKFVINFYDPNQTATHKRVFFCTNNICDIINLTAYDFLSEQCLKCYGLKEDTLSLFVDKTKSNDNNNVFIKKLPDNILQGVVINFAMGAGLREIIKKVYNDTRFTDLTKSQMKILCESKNVNNVPGLLLALQNGHDNVIDEYGTLIKKSNLNKEELIHILSARTLDGTIPGLYQALQNGHAQAIKSYGNLVLDTINKNIDLEYLLSAFKYEAHSSNKYTPGLFSAFQNGHADAIKAYCGVLGNSNLKRGEIIRMLEARNYDGAPGLLLAYQNGDINTIQSFFDSLIMLDISKDFIEELLTAKHYDFTGLSLAISHRHDHVVKLYGKLFKKLDTSPYKMSIILALAIDCERNNANIIIDSEYKSNKAVKEYVEILKEFNICPEKVAEYLSEFSGKHFLDVYNYYSN
Protein: TSSK6-activating co-chaperone protein (Q9DA44)
Organism: Mus musculus (Mouse)
Function: Co-chaperone that facilitates HSP-mediated activation of TSSK6.
Interaction partners:
Sequence:
MEQHTSNPTKEKAKEEDSVACFCPAKSSPSYIDLPANFTPANFLTIQTKLSSGAGQKPKGCLGVLECMYANLQLQTQLAQRQIAILENLQASLSQPGSGRESKNCSLPGLCCKLLLNHLPQFHK
Protein: Telomere length regulation protein elg1 (Telomere elongation suppressor elg1) (O43086)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Involved in the negative control of telomere length and in telomeric silencing through a replication-mediated pathway. May have a role in Okazaki fragment maturation. Required for S-phase progression. An RFC-like complex (elg1-RFC) is formed where elg1 replaces rfc1 in the RFC complex. This complex appears to have a role in DNA replication, replication fork re-start, recombination and repair.
Subcellular location: Nucleus {ECO:0000305}. Chromosome, telomere {ECO:0000305}.
Interaction partners:
- Replication factor C subunit 2
- Replication factor C subunit 5
- Replication factor C subunit 3
- Replication factor C subunit 4
- Chromosome transmission fidelity protein 18
- ATP-dependent DNA helicase srs2
- Proliferating cell nuclear antigen
- ATP-dependent DNA helicase pfh1
- Replication factor C subunit 1
- DNA repair and recombination protein rad22
Sequence:
MQIVGYLSADSQSNPDLKSENEAKEEKPIGRRHTMSPVPATSENKYFGKSPLSGSRKPRRSRSLHKERSYMRKFFDMDMEESKDFENDQSLLVTLKVSTSLGQKIENILHPKLSNDTNSTAFPPAKSSGEASDTNILVENINSQETVNSSPLVSELHYSNLADSPSNLRNTVTSMHPFFMSKSVKKNSEIKFVSEERGGTKPERLLDPLWPTPDSQSMLEYAGSIEPSVFWFPKKHLEEAILEETSHLSFKEVLSSTTANMITPLAEKNKTEVLQVTPSKLHTFALESLCFSPAPFIQKVLSRLLPSDPNVEMPMIPQILEKGLWVSKYAPSKTQDCCAFSQCLSKIADWLRSCRLTKPESSSVPPSSSISRSSTIHSCTSSKRNEDSLSESDFEPDIIEEEDDSDEFNPSVSRKKAKLTSSQFSNWMLVTGVTGIGKTSCLYAICRELNFEVVEIHPGMRRSGKELLERIGELTQSHIVDKSRLNNTPDILILLEEVDILFQDDRGFWQAVSTLIEKSKRPVVMTCNETDFLPSAFLQEDHIVQFQSISSALLTDYISSVLYADRCIISRNVVESISYRYGSDLRGILMQLNFWSLVNFPSLPSKDKQDDSHEPFIEATISAFDEGVGVYNPRIQTSEDLLQTYSEEQMGDIGLLFMPNLVNWRKVCVPKSEMEEKEAIMEKLIYSHQYADSLSYVDYRFSSQPTIYETYELMNDSASFEDMSLECRDNCANAFQDNLVGFPTISNPFHANAPPEPHELKLQYHSFCFINNLFSKSSLKAISSNDSIVPKALNNRELQLSALASTIGYKLDPDDVYNILSFLSFANSQVTSYTPPNSIDRPNDILILEVAPFVRCMRRYDRIRLNSYKLLLSSKGRSASHISRRGAASILRSAGYNYGRLQYLEGSDRILSTWFSTTLD
Protein: Receptor expression-enhancing protein (A0A1L5BXV2)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasmic vesicle, clathrin-coated vesicle membrane {ECO:0000256|ARBA:ARBA00029431}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00029431}. Endoplasmic reticulum membrane {ECO:0000256|ARBA:ARBA00004477}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004477}. Membrane {ECO:0000256|RuleBase:RU362006}; Multi-pass membrane protein {ECO:0000256|RuleBase:RU362006}.
Interaction partners:
Sequence:
MDGLRQRVEHFLEQRNLVTEVLGALEAKTGVEKRYLAAGAVTLLSLYLLFGYGASLLCNLIGFVYPAYASIKAIESPSKDDDTVWLTYWVVYALFGLAEFFSDLLLSWFPFYYVGKCAFLLFCMAPRPWNGALMLYQRVVRPLFLRHHGAVDRIMNDLSGRALDAAAGITRNVKPSQTPQPKDK
Protein: 16.0 kDa heat shock protein, peroxisomal (OsHsp16.0) (Q652V8)
Organism: Oryza sativa subsp. japonica (Rice)
Subcellular location: Peroxisome {ECO:0000305}.
Interaction partners:
Sequence:
MADLFFGGPFRRILYGRPFPPDWASASATAAMDWVETPTSHVLRINVPGLGKDDVKVQVEDGNVLTVRGAAPHAAAEKEREREKDVVWHVAERGRPEFAREVALPAEVRVEQIRASVDNGVLTVVVPKEPAPARPRTRPIAVSSKL
Protein: Chaperone protein DnaK (HSP70) (Heat shock 70 kDa protein) (Heat shock protein 70) (P0C922)
Organism: Borreliella burgdorferi (strain ATCC 35210 / DSM 4680 / CIP 102532 / B31) (Borrelia burgdorferi)
Function: Acts as a chaperone.
Interaction partners:
- Chaperone protein DnaJ
- Chaperone protein HtpG
- Protein GrpE
- Chaperonin GroEL
- Co-chaperonin GroES
- Heat shock protein
- ATP-dependent Clp protease, subunit A
- ATP-dependent Clp protease, subunit C
- Uncharacterized protein BB_0085
- Chaperonin, putative
Sequence:
MGKIIGIDLGTTNSCVAIMEHGKPVVIQNSEGGRTTPSIVAYTNKGERLVGQVAKNQMVTNPENTIYSIKRFMGRRFEEVASEIKMVPYKIEKGLNGDARVNISNIKKQMSPPEISAATLTKMKETAEAYLGEKVTEAVITVPAYFNDAQRQATKDAGKIAGLEVKRIVNEPTAAALAYGIEKKHEEIVAVYDLGGGTFDISILELGDGVFEVKSTNGDTHLGGDNFDDEIIKHLISEFKKESAIDLSNDKMALQRLKEAAEKAKIELSGAQEASINLPFITADANGPKHLQYTLTRAKFEQMVDHLVQKTKEPCLKAIKDAGLKASDINEVILVGGSTRIPAIQKIVKDIFGQDPNKGVNPDEAVAIGAAIQGGILTGETKDMVLLDVTPLSLGIETLGGVMTKLIERNTTIPTKKSQVFSTAADNQTSVDIKVLQGEREMAAQNRILGNFILDGIPAAPRGVPQIEVSFDIDANGIVHVSAKDMGTGKEQKIRIESSSGLSESEIDRMVKDAEAHAEEDKKLKENIEAKNTANSLIYQTEKSLKEYSEKISSEDKEAIESKIKELKESLEKEDISLIKSRTEELQKASYKIAEMMYKDSSQQNANSQQENGPQSNTSEEGKEADYEVVDEDKK
Protein: Testicular tissue protein Li 180 (A0A024QZT4)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
METLSNASGTFAIRLLKILCQDNPSHNVFCSPVSISSALAMVLLGAKGNTATQMAQALSLNTEEDIHRAFQSLLTEVNKAGTQYLLRTANRLFGEKTCQFLSTFKESCLQFYHAELKELSFIRAAEESRKHINTWVSKKTEGKIEELLPGSSIDAETRLVLVNAIYFKGKWNEPFDETYTREMPFKINQEEQRPVQMMYQEATFKLAHVGEVRAQLLELPYARKELSLLVLLPDDGVELSTVEKSLTFEKLTAWTKPDCMKSTEVEVLLPKFKLQEDYDMESVLRHLGIVDAFQQGKADLSAMSAERDLCLSKFVHKSFVEVNEEGTEAAAASSCFVVAECCMESGPRFCADHPFLFFIRHNRANSILFCGRFSSP
Protein: AMMECR1 domain-containing protein (Q382F0)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Protein MEMO1
Sequence:
MVNATPDMARYCCAVIHSKLRGEKTPEPPASITNEPSPIFVSLKTLDGDLRGCIGNFSAEPLHKQLRDYAVAAAFQDNRFPSVTLAELPMLSCSVCLLHSFEKAHRWDDWEIGVHGIRIRYKNYSATYLPSVMPEQRWDHIQAIRSLMRKAGCGEEVSDAILNELDVTRYQESKSTVAFKSANLGSLPC