wanglab/gogpt-training-data huggingface dataset:
Protein: Meiotic expression up-regulated protein 23 (O74909)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Interaction partners:
- Meiotic expression up-regulated protein 18
- Meiotic expression up-regulated protein 1/2
- Meiotic coiled-coil protein 3
- Meiotic coiled-coil protein 2
- Meiotic coiled-coil protein 1
- Septin homolog spn5
Sequence:
MPNTESELNEEFSNEFNIPPPTESSSKEGNRFLNDFRVEFEKRRIEARNRILESEGRALENKTHLNEEEIRTNERVKRFQRRVDEWTALEIERESQVQPPLWYQRDREEQNRTLNFLMSGMADLQRTINTMQGTMNTMQGTMNTMQENMINFTNKVNTLDMRSVRAENRDLRKGAYVISPVPFINGNNPDPDLPPITSVQDVDRLSRSQCSRYLQGYGVTFHVNETIGMKKKLASAVGLSAEYDREYPFSGFPN
Protein: E3 ubiquitin-protein ligase TRIM8 (EC 2.3.2.27) (Glioblastoma-expressed RING finger protein) (RING finger protein 27) (RING-type E3 ubiquitin transferase TRIM8) (Tripartite motif-containing protein 8) (Q9BZR9)
Organism: Homo sapiens (Human)
Function: E3 ubiquitin-protein ligase that participates in multiple biological processes including cell survival, differentiation, apoptosis, and in particular, the innate immune response. Participates in the activation of interferon-gamma signaling by promoting proteasomal degradation of the repressor SOCS1. Plays a positive role in the TNFalpha and IL-1beta signaling pathways. Mechanistically, induces the 'Lys-63'-linked polyubiquitination of MAP3K7/TAK1 component leading to the activation of NF-kappa-B. Modulates also STAT3 activity through negative regulation of PIAS3, either by degradation of PIAS3 through the ubiquitin-proteasome pathway or exclusion of PIAS3 from the nucleus. Negatively regulates TLR3/4-mediated innate immune response by catalyzing 'Lys-6'- and 'Lys-33'-linked polyubiquitination of TICAM1 and thereby disrupting the TICAM1-TBK1 interaction.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:23152791, ECO:0000269|PubMed:34871740}. Nucleus {ECO:0000269|PubMed:23152791, ECO:0000269|PubMed:34871740}. Nucleus, nuclear body {ECO:0000269|PubMed:33508234}. Note=Nucleo-cytoplasmic translocation is involved in regulation of NF-kappa-B. {ECO:0000269|PubMed:23152791}.
Interaction partners:
- Suppressor of cytokine signaling 1
- Mitogen-activated protein kinase kinase kinase 7
- T-cell receptor-associated transmembrane adapter 1
- E3 SUMO-protein ligase PIAS3
Sequence:
MAENWKNCFEEELICPICLHVFVEPVQLPCKHNFCRGCIGEAWAKDSGLVRCPECNQAYNQKPGLEKNLKLTNIVEKFNALHVEKPPAALHCVFCRRGPPLPAQKVCLRCEAPCCQSHVQTHLQQPSTARGHLLVEADDVRAWSCPQHNAYRLYHCEAEQVAVCQYCCYYSGAHQGHSVCDVEIRRNEIRKMLMKQQDRLEEREQDIEDQLYKLESDKRLVEEKVNQLKEEVRLQYEKLHQLLDEDLRQTVEVLDKAQAKFCSENAAQALHLGERMQEAKKLLGSLQLLFDKTEDVSFMKNTKSVKILMDRTQTCTSSSLSPTKIGHLNSKLFLNEVAKKEKQLRKMLEGPFSTPVPFLQSVPLYPCGVSSSGAEKRKHSTAFPEASFLETSSGPVGGQYGAAGTASGEGQSGQPLGPCSSTQHLVALPGGAQPVHSSPVFPPSQYPNGSAAQQPMLPQYGGRKILVCSVDNCYCSSVANHGGHQPYPRSGHFPWTVPSQEYSHPLPPTPSVPQSLPSLAVRDWLDASQQPGHQDFYRVYGQPSTKHYVTS
Protein: IgG receptor FcRn large subunit p51 (FcRn) (IgG Fc fragment receptor transporter alpha chain) (Neonatal Fc receptor) (P13599)
Organism: Rattus norvegicus (Rat)
Function: Cell surface receptor that transfers passive humoral immunity from the mother to the newborn. Binds to the Fc region of monomeric immunoglobulin gamma and mediates its selective uptake from milk. IgG in the milk is bound at the apical surface of the intestinal epithelium. The resultant FcRn-IgG complexes are transcytosed across the intestinal epithelium and IgG is released from FcRn into blood or tissue fluids. Throughout life, contributes to effective humoral immunity by recycling IgG and extending its half-life in the circulation. Mechanistically, monomeric IgG binding to FcRn in acidic endosomes of endothelial and hematopoietic cells recycles IgG to the cell surface where it is released into the circulation. In addition of IgG, regulates homeostasis of the other most abundant circulating protein albumin/ALB (By similarity).
Subcellular location: Cell membrane {ECO:0000269|PubMed:2911353}; Single-pass type I membrane protein {ECO:0000255}. Endosome membrane {ECO:0000250|UniProtKB:P55899}.
Interaction partners:
- Albumin
- Beta-2-microglobulin
- Ig gamma-1 chain C region
- Fc fragment of IgG receptor Ia.
- Tumor necrosis factor receptor superfamily member 8
- Low affinity immunoglobulin gamma Fc region receptor II
- T-cell surface glycoprotein CD4
- Immunoglobulin lambda-like polypeptide 1
- Polymeric immunoglobulin receptor
- CD19 molecule
Sequence:
MGMSQPGVLLSLLLVLLPQTWGAEPRLPLMYHLAAVSDLSTGLPSFWATGWLGAQQYLTYNNLRQEADPCGAWIWENQVSWYWEKETTDLKSKEQLFLEAIRTLENQINGTFTLQGLLGCELAPDNSSLPTAVFALNGEEFMRFNPRTGNWSGEWPETDIVGNLWMKQPEAARKESEFLLTSCPERLLGHLERGRQNLEWKEPPSMRLKARPGNSGSSVLTCAAFSFYPPELKFRFLRNGLASGSGNCSTGPNGDGSFHAWSLLEVKRGDEHHYQCQVEHEGLAQPLTVDLDSPARSSVPVVGIILGLLLVVVAIAGGVLLWNRMRSGLPAPWLSLSGDDSGDLLPGGNLPPEAEPQGVNAFPATS
Protein: Eukaryotic translation initiation factor 3 subunit B (eIF3b) (Eukaryotic translation initiation factor 3 90 kDa subunit homolog) (eIF3 p90) (Translation initiation factor eIF3 p90 subunit homolog) (Q5BGH1)
Organism: Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Function: RNA-binding component of the eukaryotic translation initiation factor 3 (eIF-3) complex, which is involved in protein synthesis of a specialized repertoire of mRNAs and, together with other initiation factors, stimulates binding of mRNA and methionyl-tRNAi to the 40S ribosome. The eIF-3 complex specifically targets and initiates translation of a subset of mRNAs involved in cell proliferation.
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03001}.
Interaction partners:
- Eukaryotic translation initiation factor 2 subunit gamma
- Eukaryotic translation initiation factor 3 subunit G
- Eukaryotic translation initiation factor 2 subunit alpha
- Eukaryotic translation initiation factor 3 subunit M
- Eukaryotic translation initiation factor 3 subunit D
- Eukaryotic translation initiation factor 5, putative
- Eukaryotic translation initiation factor 3 subunit H
- Eukaryotic translation initiation factor 3 subunit C
- Eukaryotic translation initiation factor 3 subunit L
- Eukaryotic translation initiation factor 3 subunit F
Sequence:
MAPSFENLSEQDLHEEEEEEIDFSDLKAQYEVKLEEGLDTFVVIDGLPVVPEENRQKLIKFLLRKLNTVGHTSEDAVFMPLNEKNMSEGFAFVEYETAEQAVAAVKQLHGTPLDKKHTLLVNKLMDIERYGREGRIDEEYKPPNIEPFTEKEHLRSWLGDPNARDQFALYRGDKVGVFWNNKSNPPENVVDRAHWTQLFVQWSPKGTYLASVHPQGVQLWGGPTFSKQKQFPHPFVSLIEFSPGESYLTTWSARPIQVEEGHPVLTYEEDGKNIIVWDIVTGKPLRSFVSHDLAGPESEAQPKKKVQWPAFKWSADEKYVARMLQGQSISIYELPRMNLLGKTSVKIDGVMDFEWSPATVNRDGVKQYEQLLCFWTPEIGSNPARVALMSVPSKEIVRTRNLFNVSDVKLHWQSQGNFVCVKVDRHSKSKKSMATNLEIFRVREKGVPVEVVDSLKDTVINFSWEPNGARFVLITTGDASGAGAPPKTAVSFFAPEKKGVQAGNFKLVRTIEKKTSNAIYWSPKGRFVVVATVHSQSNFDLDFWDMDFEGEKNDNEKDLAANLQLMKTVDHYGVTDIEWDPTGRYVVSGASAWTHQMENGFNLHTFSGETLAENPTDKFKQFLWRPRPPTLLSKEEQKQVRKNLREYSKEFEEEDKYAVDIANTAVVEKRKRVLNEWVAWLKREKELLTEEKEAYGLPEEADQPKAAKDAPTNTEDKGETVVEEIVEEIVEESEEIIG
Protein: Probable pre-mRNA-splicing factor ATP-dependent RNA helicase DEAH6 (EC 3.6.4.13) (DEAH RNA helicase homolog PRP2) (Protein MATERNAL EFFECT EMBRYO ARREST 29) (F4IJV4)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: May be involved in pre-mRNA splicing.
Interaction partners:
- Peptidyl-prolyl cis-trans isomerase CYP57
- Protein MOS2
- At4g25020
- THO complex subunit 2
- Transducin/WD40 repeat-like superfamily protein
- Pre-mRNA-processing factor 17
- Splicing factor SF3a60 homolog
- Pre-mRNA-splicing factor ATP-dependent RNA helicase DEAH7
- Cell division cycle 5-like protein
- Tetratricopeptide repeat
Sequence:
MGSNDLNTWVSDKLMVLLGFSQTAVVQYLIAMAKQSKSPGELVRELVECGFSLSGDTRAFAEEIYARAPRKTPGVNLYQQQEAEAAMLLKKQKTFSLLEADHDEDENNVKKQSASKTGKSDKGQKRFRKKSEQLEDDDDEVVIVREDKRNVRRKVSEDEDDGTESEEERLRDQREREELEQHLRERDTARTRKLTEPKMSKKEQEEFVRRDSAVDKGDIESLRKFSWQEYMKKRKQKKVLELKDDIEDEPYLFGDEKLTEREIREFRYKREIYELIKKSTQEEDNVGEYRMPDAYDQQGSVDQEKRFAVSVQRYRDMGSAEKMNPFAEQEAWEDHQIENAALKFGAKNKEVSDNYEFVFEDQIDFIKASVLAGDNYEDEMHAKPSQDSAGKSAFHMLQEDRKALPIYTYRDQLLNAVKDHQVLIIVGETGSGKTTQIPQYLHEAGYTKLGKVGCTQPRRVAAMSVAARVAQEMGGKLGHEVGYSIRFEDCTSEKTILKYMTDGMLLRELLGEPDLGSYSVIIVDEAHERTLRTDILFGLVKDIARARPDLKLLISSATMDAEKFSDFFDQAPIFRFPGRRYPVDICFTTAPEADYMDAAITTVLTIHVKEPLGDVLVFLPGQEEIEAVEENLKHKIRGLGTKIRELIICPIYANLPSELQAKIFEPTPEGARKVVLATNIAETSLTIDGIKYVVDPGFSKMKSYNPRTGMESLLVTPISKASATQRTGRAGRTSPGKCYRLYTAFNYYNDLEDNTVPEIQRTNLASVVLSLKSLGIHNLLNFDFMDPPPSEALIKSLELLFALGALNQLGELTKAGRRMAEFPLDPMLSKMIVVSDKYKCSDEIISIAAMLSIGPSIFYRPKDKQVHADNAMKNFHVGNVGDHIAFLKIYNSWKETNYSTQWCYENYIQVRSMKRARDIRDQLEGLLERVEIDVSSNANELDSIRKSIVAGFFPHTAKLQKNGSYRTVKHPQTVHIHPASGLSQVLPRWVVYHQLVLTSKEYMRQVTELKPEWLIEIAPHYYQLKDVEDATSKKMPKTSGRAVV
Protein: Far upstream element-binding protein 3 (FUSE-binding protein 3) (Q96I24)
Organism: Homo sapiens (Human)
Function: May interact with single-stranded DNA from the far-upstream element (FUSE). May activate gene expression.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- Fructose-1,6-bisphosphatase 1
- Heterogeneous nuclear ribonucleoprotein F
- KH domain-containing RNA-binding protein QKI
- Poly
- Far upstream element-binding protein 1
Sequence:
MAELVQGQSAPVGMKAEGFVDALHRVRQIAAKIDSIPHLNNSTPLVDPSVYGYGVQKRPLDDGVGNQLGALVHQRTVITEEFKVPDKMVGFIIGRGGEQISRIQAESGCKIQIASESSGIPERPCVLTGTPESIEQAKRLLGQIVDRCRNGPGFHNDIDSNSTIQEILIPASKVGLVIGRGGETIKQLQERTGVKMVMIQDGPLPTGADKPLRITGDAFKVQQAREMVLEIIREKDQADFRGVRGDFNSRMGGGSIEVSVPRFAVGIVIGRNGEMIKKIQNDAGVRIQFKPDDGISPERAAQVMGPPDRCQHAAHIISELILTAQERDGFGGLAAARGRGRGRGDWSVGAPGGVQEITYTVPADKCGLVIGKGGENIKSINQQSGAHVELQRNPPPNSDPNLRRFTIRGVPQQIEVARQLIDEKVGGTNLGAPGAFGQSPFSQPPAPPHQNTFPPRSSGCFPNMAAKVNGNPHSTPVSGPPAFLTQGWGSTYQAWQQPTQQVPSQQSQPQSSQPNYSKAWEDYYKKQSHAASAAPQASSPPDYTMAWAEYYRQQVAFYGQTLGQAQAHSQEQ
Protein: Envoplakin (K7EKI0)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
Sequence:
MFKGLSKGSQGKGSPKGSPAKGSPKGSPSRHSRAATQELALLISRMQANADQVERDILETQKRLQQDRLNSEQSQALQHQQETGRSLKEAEVLLKDLFLDVDKARRLKHPQAEEIEKDIKQLHERVTQECAEYRALYEKMVLPPDVGPRVDWARVLEQKQKQVCAGQYGPGMAELEQQIAEHNILQKEIDAYGQQLRSLVGPDAATIRSQYRDLLKAASWRGQSLGSLYTHLQGCTRQLSALAEQQRRILQQDWSDLMADPAGVRREYEHFKQHELLSQEQSVNQLEDDGERMVELRHPAVGPIQAHQEALKMEWQNFLNLCICQETQLQHVEDYRRFQEEADSVSQTLAKLNSNLDAKYSPAPGGPPGAPTELLQQLEAEEKRLAVTERATGDLQRRSRDVAPLPQRRNPPQQPLHVDSICDWDSGEVQLLQGERYKLVDNTDPHAWVVQGPGGETKRAPAACFCIPAPDPDAVARASRLASELQALKQKLATVQSRLKASAVESLRPSQQGTQGGPGRGGCGARRSRFRLPTAPSGSDLANPQAQKLLTQMTRLDGDLGQIERQVLAWARAPLSRPTPLEDLEGRIHSHEGTAQRLQSLGTEKETAQKECEAFLSTRPVGPAALQLPVALNSVKNKFSDVQVLCSLYGEKAKAALDLERQIQDADRVIRGFEATLVQEAPIPAEPGALQERVSELQRQRRELLEQQTCVLRLHRALKASEHACAALQNNFQEFCQDLPRQQRQVRALTDRYHAVGDQLDLREKVVQDAALTYQQFKNCKDNLSSWLEHLPRSQVRPSDGPSQIAYKLQAQKRLTQEIQSRERDRATASHLSQALQAALQDYELQADTYRCSLEPTLAVSAPKRPRVAPLQESIQAQEKNLAKAYTEVAAAQQQLLQQLEFARKMLEKKELSEDIRRTHDAKQGSESPAQAGRESEALKAQLEEERKRVARVQHELEAQRSQLLQLRTQRPLERLEEKEVVEFYRDPQLEGSLSRVKAQVEEEGKRRAGLQADLEVAAQKVVQLESKRKTMQPHLLTKEVTQVERDPGLDSQAAQLRIQIQQLRGEDAVISARLEGLKKELLALEKREVDVKEKVVVKEVVKVEKNLEMVKAAQALRLQMEEDAARRKQAEEAVAKLQARIEDLERAISSVEPKVIVKEVKKVEQDPGLLQESSRLRSLLEEERTKNATLARELSDLHSKYSVVEKQRPKVQLQERVHEIFQVDPETEQEITRLKAKLQEMAGKRSGVEKEVEKLLPDLEVLRAQKPTVEYKEVTQEVVRHERSPEVLREIDRLKAQLNELVNSHGRSQEQLIRLQGERDEWRRERAKVETKTVSKEVVRHEKDPVLEKEAERLRQEVREAAQKRRAAEDAVYELQSKRLLLERRKPEEKVVVQEVVVTQKDPKLREEHSRLSGSLDEEVGRRRQLELEVQQLRAGVEEQEGLLSFQEDRSKKLAVERELRQLTLRIQELEKRPPTVQEKIIMEEVVKLEKDPDLEKSTEALRWDLDQEKTQVTELNRECKNLQVQIDVLQKAKSQEKTIYKEVIRVQKDRVLEDERARVWEMLNRERTARQAREEEARRLRERIDRAETLGRTWSREESELQRARDQADQECGRLQQELRALERQKQQQTLQLQEESKLLSQKTESERQKAAQRGQELSRLEAAILREKDQIYEKERTLRDLHAKVSREELSQETQTRETNLSTKISILEPETGKDMSPYEAYKRGIIDRGQYLQLQELECDWEEVTTSGPCGEESVLLDRKSGKQYSIEAALRCRRISKEEYHLYKDGHLPISEFALLVAGETKPSSSLSIGSIISKSPLASPAPQSTSFFSPSFSLGLGDDSFPIAGIYDTTTDNKCSIKTAVAKNMLDPITGQKLLEAQAATGGIVDLLSRERYSVHKAMERGLIENTSTQRLLNAQKAFTGIEDPVTKKRLSVGEAVQKGWMPRESVLPHLQVQHLTGGLIDPKRTGRIPIQQALLSGMISEELAQLLQDESSYEKDLTDPISKERLSYKEAMGRCRKDPLSGLLLLPAALEGYRCYRSASPTVPRSLR
Protein: Caspase recruitment domain-containing protein 10 (Bcl10-interacting MAGUK protein 1) (Bimp1) (P58660)
Organism: Mus musculus (Mouse)
Function: Scaffold protein that plays an important role in mediating the activation of NF-kappa-B via BCL10 or EGFR.
Interaction partners:
- B-cell lymphoma/leukemia 10
- Protein kinase C theta type
- Caspase recruitment domain-containing protein 11
- Caspase recruitment domain-containing protein 14
- Protein kinase C beta type
- Mucosa-associated lymphoid tissue lymphoma translocation protein 1 homolog
Sequence:
MQGRADAGEADEEAGAGSGSEAEEDALWERIEGVRHRLTRALNPAKLTPYLRQCRVLDEQDEEEVLSTYRFPCRANRTGRLIDILRCRGKRGFEAFLEALEFYYPEHFTLLTGQEPAQRCSMILDEEGPEGLTQFLMTEVRRLREARKSQLHREQQLQARGRALEEERAGLEQRLREQQQAQERCQRLREDWEAGSLELLRLKDENYMIAMRLAQLSEEKNSAVLRSRDLQLAVDQLKLKVSRLEEECALLRRARGPPPGAEEKEREPDGADLLSELRAENQRLTASLQELQEGLQQEMSRPGAAGSERILLDILEHDWREAQDSRQELCQKLHAVQGELQWAEELRDKYLQEMEDLRLKHRTLLKDCDLYKHRMATVLAQLEEIEKERDQAIQSRDRIQLQYSQSLIEKDQYRKQVRGLEAERDELLTTVTSLEGTKAMLEAQLQRTQGGSCLKACASSHSLCSNLSSTWSLSEFPSPLGGPEATGEAGGSEPHTSEEATDSEKEINRLSILPFPPSAGSILRRQREEDPEPPKRSFSSMSDITGSVTLKPWSPGLSSSSSSDSVWPLGKPEGLLARGCGLDFLNRSLAIRVSGWSPPAGLDPQDKSPDSMPGLGDRWSGAVVRRVLSGPGSARTEQKEPRAEGTGLEGAGLEAEAQQRTLPWNQSSTLPFLLDSKACHSFHEALDAWAKGPGAEPFYIRANFSLPERSDPHALCVKAQEILRLVDPAHKRRQEWFCTRVDTLTLRDLDRGTVPNYQRAQQLLEVQEKYLISSRHRSPRSNLKKRALGLVRPKPAGGTAGDSAEQLPAEPCSELERSLKPYSLVRPLLVSALRPVVLLPECLAPRLIRNLLDLPSSRLDFQVCPAESLSGEEQCTSSAPGAPKAWPATAGLGSRIRAIQESVGKKHCLLELGARGVRELVHSEVYPIVIHVEVTEKNVREIRGLLGRPGWRDSELLRQCRGSEQWLWGLPCSWVQVPAHAWGHAEELAKVVRGRILQEQARLVWVERGSSRGGSGSSSEA
Protein: Nuclear receptor-binding protein (Q9UHY1)
Organism: Homo sapiens (Human)
Function: May play a role in subcellular trafficking between the endoplasmic reticulum and Golgi apparatus through interactions with the Rho-type GTPases. Binding to the NS3 protein of dengue virus type 2 appears to subvert this activity into the alteration of the intracellular membrane structure associated with flaviviral replication.
Subcellular location: Cytoplasm, cell cortex {ECO:0000269|PubMed:11956649}. Endomembrane system {ECO:0000269|PubMed:11956649}. Cell projection, lamellipodium {ECO:0000269|PubMed:11956649}. Note=Colocalizes with activated RAC3 to endomembranes and at the cell periphery in lamellipodia.
Interaction partners:
- TSC22 domain family protein 2
- TSC22 domain family protein 4
- TSC22 domain family protein 1
- TSC22 domain family protein 3
- Elongin-C
- Elongin-B
- Nuclear receptor-binding protein 2
- Myeloid leukemia factor 1
Sequence:
MSEGESQTVLSSGSDPKVESSSSAPGLTSVSPPVTSTTSAASPEEEEESEDESEILEESPCGRWQKRREEVNQRNVPGIDSAYLAMDTEEGVEVVWNEVQFSERKNYKLQEEKVRAVFDNLIQLEHLNIVKFHKYWADIKENKARVIFITEYMSSGSLKQFLKKTKKNHKTMNEKAWKRWCTQILSALSYLHSCDPPIIHGNLTCDTIFIQHNGLIKIGSVAPDTINNHVKTCREEQKNLHFFAPEYGEVTNVTTAVDIYSFGMCALEMAVLEIQGNGESSYVPQEAISSAIQLLEDPLQREFIQKCLQSEPARRPTARELLFHPALFEVPSLKLLAAHCIVGHQHMIPENALEEITKNMDTSAVLAEIPAGPGREPVQTLYSQSPALELDKFLEDVRNGIYPLTAFGLPRPQQPQQEEVTSPVVPPSVKTPTPEPAEVETRKVVLMQCNIESVEEGVKHHLTLLLKLEDKLNRHLSCDLMPNENIPELAAELVQLGFISEADQSRLTSLLEETLNKFNFARNSTLNSAAVTVSS
Protein: Proliferating cellular nuclear antigen 1 (PCNA 1) (Q9M7Q7)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: This protein is an auxiliary protein of DNA polymerase delta and is involved in the control of eukaryotic DNA replication by increasing the polymerase's processibility during elongation of the leading strand.
Subcellular location: Nucleus.
Interaction partners:
- DNA polymerase eta
- Replication factor C subunit 2
- Replication factor C subunit 3
- DNA ligase 6
- Replication factor C subunit 5
- DNA polymerase delta small subunit
- Probable DNA primase large subunit
- Replication factor C subunit 4
- DNA replication licensing factor MCM7
- Chromosome transmission fidelity protein 18 homolog
Sequence:
MLELRLVQGSLLKKVLESIKDLVNDANFDCSSTGFSLQAMDSSHVALVSLLLRSEGFEHYRCDRNLSMGMNLGNMSKMLKCAGNDDIITIKADDGGDTVTFMFESPTQDKIADFEMKLMDIDSEHLGIPDAEYHSIVRMPSNEFSRICKDLSSIGDTVVISVTKEGVKFSTAGDIGTANIVLRQNTTVDKPEDAIVIEMKEPVSLSFALRYMNSFTKATPLSDTVTISLSSELPVVVEYKVAEMGYIRYYLAPKIEEEEDTNP
Protein: Thiamine transporter 2 (ThTr-2) (ThTr2) (Solute carrier family 19 member 3) (Q99PL8)
Organism: Mus musculus (Mouse)
Function: High-affinity transporter for the intake of thiamine.
Subcellular location: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
- Thiamine transporter 1
- Mitochondrial thiamine pyrophosphate carrier
- Thiamine pyrophosphokinase 1
Sequence:
MDSSCRTPPSNSWVYPTVILCLFGFFSMFRPSEAFLIPFLSEPSKNLTSPEMTNEILPVWTYSYLATLPPVFVLTDYLRYKPVIMLHVVAFATSYLFLLFGQGVMLMQTAEFFFGVVSATEIAYFAYIYSMVSPEHYQKVSSYCRSITLVAYTAGSVLAQLLVSLTNLPYSSLFYISLACVSVAFFFSLFLPMPKKSMFFHAKSDRDDCPKPLEQCTVPKEAQSNRTHSELFANSKNLEDREMSNPDPENSALRHFAHWFQDLKECYSSKHLVYWSLWWAFATAGYNQILNYVQVLWEHKAPSQDSSIYNGAVEAIATFGGALASFSVGYLKVNWDLLGELGLAVFSAVIAGSLFLMNYSRSIWVCYAGYLLVKSSYSFLITIAVFQIAVNLSLERYALVFGIDTFIALVIQTIMTMIVVDQRGLQLPVTTQFLVYGSYFAVIAGVFLMRSIYILCSAKCRKEVQNLATTRSPNEPHPQEPSNVSTKF
Protein: Zinc finger protein 614 (Q8N883)
Organism: Homo sapiens (Human)
Function: May be involved in transcriptional regulation.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
Sequence:
MIKTQESLTLEDVAVEFSWEEWQLLDTAQKNLYRDVMVENYNHLVSLGYQTSKPDVLSKLAHGQEPWTTDAKIQNKNCPGIGKVDSHLQEHSPNQRLLKSVQQCNGQNTLRNIVHLSKTHFPIVQNHDTFDLYRKNLKSSLSLINQKRRHGINNPVEFIGGEKTLLHGKHERTHTKTRFSENAKCIHTKFQVFKHQRTQKIEKPHACIECEQTFLRKSQLIYHENICIQENPGSGQCEKLSRSVLFTKHLKTNTTDKICIPNEYRKGSTVKSSLITHQQTHTEEKSYMCSECGKGFTMKRYLIAHQRTHSGEKPYVCKECGKGFTVKSNLIVHQRTHTGEKPYICSECGKGFTMKRYLVVHQRTHTGEKPYMCSECGKGFTVKSNLIVHQRSHTGEKSYICSECGKGFTVKRTLVIHQRTHTGEKSYICNECGKGFTTKRTLIIHQRTHTGEKPYECNECGKAFSQKICLIQHERCHTGKTPFVCTECGKSYSHKYGLITHQRIHTGEKPYECNECGKAFTTKSVLNVHQRTHTGERPYGCSDCEKAFSHLSNLVKHKKMHTREMGRISQVENSCNGESQLLPYK
Protein: Clathrin light chain A (Lca) (O08585)
Organism: Mus musculus (Mouse)
Function: Clathrin is the major protein of the polyhedral coat of coated pits and vesicles. Acts as component of the TACC3/ch-TOG/clathrin complex proposed to contribute to stabilization of kinetochore fibers of the mitotic spindle by acting as inter-microtubule bridge (By similarity).
Subcellular location: Cytoplasmic vesicle membrane; Peripheral membrane protein; Cytoplasmic side. Membrane, coated pit; Peripheral membrane protein; Cytoplasmic side. Cytoplasm, cytoskeleton, spindle {ECO:0000250|UniProtKB:P09496}. Note=Cytoplasmic face of coated pits and vesicles. In complex with TACC3 and CKAP5 (forming the TACC3/ch-TOG/clathrin complex) localized to inter-microtubule bridges in mitotic spindles. {ECO:0000250|UniProtKB:P09496}.
Interaction partners:
- Clathrin heavy chain 1
- Cyclin-G-associated kinase
- Clathrin light chain B
- AP-2 complex subunit alpha-1
- Unconventional myosin-VI
- Auxilin
- AP-2 complex subunit mu
- AP-2 complex subunit sigma
- AP-1 complex subunit beta-1
- AP-2 complex subunit beta
Sequence:
MAELDPFGAPAGAPGGPALGNGVAGAGEEDPAAAFLAQQESEIAGIENDEAFAILDGGAPGRATRRAAGGPDAVDGVMNGEYYQESNGPTDSYAAISEVDRLQSEPESIRKWREEQTERLEALDANSRKQEAEWKEKAIKELEEWYARQDEQLQKTKANNRVADEAFYKQPFADLIGYVAAEEAFVNDIDESSPGTEWERVARLCDFNPKSSKQAKDVSRMRSVLISLKQAPLVH
Protein: Cytochrome c oxidase subunit 2 (EC 7.1.1.9) (Cytochrome c oxidase polypeptide II) (P00405)
Organism: Mus musculus (Mouse)
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:0000269|PubMed:34616041, ECO:0000269|PubMed:38575788}; Multi-pass membrane protein {ECO:0000269|PubMed:34616041, ECO:0000269|PubMed:38575788}.
Interaction partners:
- Cytochrome c oxidase subunit 7C, mitochondrial
- Cytochrome b
- Cytochrome c oxidase subunit 4 isoform 1, mitochondrial
- Cytochrome b-c1 complex subunit Rieske, mitochondrial
- Cytochrome c oxidase subunit 3
- NADH-ubiquinone oxidoreductase chain 1
- Cytochrome c oxidase subunit 6C
- Cytochrome c oxidase subunit 5A, mitochondrial
- Cytochrome c oxidase subunit 6B1
- Cytochrome c oxidase subunit 5B, mitochondrial
Sequence:
MAYPFQLGLQDATSPIMEELMNFHDHTLMIVFLISSLVLYIISLMLTTKLTHTSTMDAQEVETIWTILPAVILIMIALPSLRILYMMDEINNPVLTVKTMGHQWYWSYEYTDYEDLCFDSYMIPTNDLKPGELRLLEVDNRVVLPMELPIRMLISSEDVLHSWAVPSLGLKTDAIPGRLNQATVTSNRPGLFYGQCSEICGSNHSFMPIVLEMVPLKYFENWSASMI
Protein: Interferon-induced GTP-binding protein Mx1 (Myxoma resistance protein 1) (Myxovirus resistance protein 1) (P79135)
Organism: Bos taurus (Bovine)
Function: Interferon-induced dynamin-like GTPase with antiviral activity against rabies virus (RABV), vesicular stomatitis virus (VSV) and murine pneumonia virus (MPV). Isoform 1 but not isoform 2 shows antiviral activity against vesicular stomatitis virus (VSV).
Subcellular location: Cytoplasm {ECO:0000269|PubMed:19951175}. Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P20591}; Peripheral membrane protein {ECO:0000250|UniProtKB:P20591}; Cytoplasmic side {ECO:0000250|UniProtKB:P20591}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:P20591}. Note=Binds preferentially to negatively charged phospholipids. Colocalizes with CCHFV protein N in the perinuclear region. {ECO:0000250|UniProtKB:P20591}.; SUBCELLULAR LOCATION: [Isoform 2]: Nucleus {ECO:0000269|PubMed:19951175}.
Interaction partners:
- Ubiquitin-like protein ISG15
- Interferon-induced GTP-binding protein Mx2
- Interferon-induced, double-stranded RNA-activated protein kinase
- Interferon regulatory factor 9
- Uncharacterized protein
- USP domain-containing protein
- S-adenosylmethionine-dependent nucleotide dehydratase RSAD2
- Interferon induced protein with tetratricopeptide repeats 1
- Interferon-induced transmembrane protein 3
- 2'-5' oligoadenylate synthase
Sequence:
MVHSDLGIEELDSPESSLNGSEDMESKSNLYSQYEEKVRPCIDLIDSLRSLGVEQDLALPAIAVIGDQSSGKSSVLEALSGVALPRGSGIVTRCPLVLRLKKLGNEDEWKGKVSFLDKEIEIPDASQVEKEISEAQIAIAGEGTGISHELISLEVSSPHVPDLTLIDLPGITRVAVGNQPPDIEYQIKSLIRKYILRQETINLVVVPANVDIATTEALRMAQEVDPQGDRTIGILTKPDLVDKGTEDKVVDVVRNLVFHLKKGYMIVKCRGQQDIKHRMSLDKALQRERIFFEDHAHFRDLLEEGKATIPCLAERLTSELIMHICKTLPLLENQIKETHQRITEELQKYGKDIPEEESEKMFCLIEKIDTFNKEIISTIEGEEFVEQYDSRLFTKVRAEFSKWSAVVEKNFEKGYEAIRKEIKQFENRYRGRELPGFVNYKTFETIIKKQVRVLEEPAVDMLHTVTDIIRNTFTDVSGKHFNEFFNLHRTAKSKIEDIRLEQENEAEKSIRLHFQMEQLVYCQDQVYRRALQQVREKEAEEEKNKKSNHYFQSQVSEPSTDEIFQHLTAYQQEVSTRISGHIPLIIQFFVLRTYGEQLKKSMLQLLQDKDQYDWLLKERTDTRDKRKFLKERLERLTRARQRLAKFPG
Protein: Trehalase (EC 3.2.1.28) (Alpha,alpha-trehalase) (Alpha,alpha-trehalose glucohydrolase) (Q9W2M2)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- BcDNA.GH08860
- Trehalose 6-phosphate phosphatase
- Trehalose 6-phosphate phosphatase
- Trehalase
- Phosphotransferase
- Hexokinase type 2
- Phosphoacetylglucosamine mutase
- Glycogen phosphorylase
- Glucose-6-phosphate isomerase
- Phosphoglucomutase 1
Sequence:
MFKLPTISLLLVSWSCLVALSQAKTYSLPDLTTDYNNAIPVDEEEAQDPFASCKIYCEGNLLHTIQTAVPKLFADSKTFVDMKLNNSPDKTLEDFNAMMEAKNQTPSSEDLKQFVDKYFSAPGTELEKWTPTDWKENPSFLDLISDPDLKQWGVELNSIWKDLGRKMKDEVSKNPEYYSIIPVPNPVIVPGGRFIEFYYWDSYWIIRGLLYSQMFDTARGMIENFFSIVNRFGFIPNGGRVYYHGRSQPPLLTGMVKSYVDFTNDDKFAIDALDTLEHEFEFFVNNHNVTVKNHSLCVYRDSSSGPRPESYREDVETGEEFPTDEAKELHYSELKAGAESGMDFSSRWFISPTGTNDGNRSALSTTSIVPVDLNAYLYWNAKLIAEFHSKAGNTKKVTEYETKAEKLLLGIQEVLWNEEAGVWLDYDMINQKPRDYYTPTNLSPLWVKAFNISESEKISASVMAYIERNKLDSFPGGVPNTLSYTGEQWDAPNVWAPMQYILVEGLNNLNTPEAKNMSLKWATRWVKTNFAAFSKDRHMYEKYNADEFGVGGGGGEYEVQTGFGWSNGVIIEWLSKHGRDISIGSGCGCLAGEKRQ