wanglab/gogpt-training-data huggingface dataset:
Protein: BAG family molecular chaperone regulator 6 (Bcl-2-associated athanogene 6) (CaM-binding protein 1) [Cleaved into: Cleaved BAG6] (O82345)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Co-chaperone that regulates diverse cellular pathways, such as programmed cell death and stress responses. Involved in plant basal resistance. Involved in basal heat response through the regulation of the heat induced small HSP (sHSP) transcriptional cascade.
Interaction partners:
- Aspartyl protease APCB1
- Membrane-associated progesterone-binding protein 4
- D111/G-patch domain-containing protein
- Remorin family protein
- At2g46250/T3F17.10
- Aspartic proteinase 39
- BAG family molecular chaperone regulator 4
Sequence:
MMPVYMDPSQPCQMRPQEYYYQGFGNNSQHMAMDAPPPCHGSCVHGNFPAYWPPCYPPQVPYHQCCMNRSAFHPPHASYAPSCYVHPPFPVGYQPWFDVEKDVPGKHHCGKCSSQMCDLKKDRGVVIEEHEPEIEKGEAVLPVRSTNCPYPIIWIPHENARNQEYRSSLGLGKHNQPPAEVRAPDNMTIQKSFPESWRGCFPFDESSMKSLVQNQDSKKAQNGKTVEAPFDISKFKSLLQGQDMKEAQIQKNKEELGQLTYPTSWVPSRRKRDDVEASESSNEDRKKMQNGKTVEYPFDISMIKSLIQGQDVKEAQNQKNKEEPGQVPYPIFWIPSYGKRKDVEASESKESSNEGRNLESCPSDLHRNEGQITQAKGKEGNFECNVLSDAEEKSSVINIPVANHLQEPRNIPVKLSENHLPKPTEPTKRIAKNEPVKSTKKEQSSSSSEASKLPPVCLRVDPLPKERNGGSKSVSHPKRMEKSKETKIAAPLSSKKAESRTVPEACNVKCEDANAEMKMAEGSLNALRTEKGSVESNSNLQEESNGEIIKPCEAKENREQPAKKSFTEEEAARIIQSMYRGYDVRRWEPIKKLKEIATVREQMGDVKKRIEALEASTDQHIEEKEIVVNGELVMNLLLKLDAVEGLHPSIREFRKALATELSSIQDKLDSLKNSCASAEKEAVKEQVEIKSQPSDSPVNLEHSQLTEENKMVSDTNLEKVLRLSPEEHPMSVLNRTDEKQAESAAETEEGYGLFETLATDSKQATENAAAASSTTIPEKIGEVETVVPGNPPSADGNGMTVTNVEENKAMVVESLEEPINELPQMVEETETNSIRDPENASEVSEAETNSSENENRKGEDDIVLHSEKNVELSELPVGVIDEETQPLSQDPSSSYTREGNMTAMDPKTASQEETEVDHSPNNSKGIGQQTSEPQDEKEQSPETEVIVKEQPLETEVILNEQAPEPEITEPGISKETKKLMEENQRFKETMETLVKAGREQLEVISKLTSRVKSLEKKLSHKKKTQIRRRASKPMSVSPTDAVL
Protein: CKLF-like MARVEL transmembrane domain-containing protein 5 (Chemokine-like factor superfamily member 5) (Q96DZ9)
Organism: Homo sapiens (Human)
Subcellular location: Membrane; Multi-pass membrane protein.
Interaction partners:
- Chemokine-like factor
- CKLF-like MARVEL transmembrane domain-containing protein 1
- CKLF-like MARVEL transmembrane domain-containing protein 2
- CKLF-like MARVEL transmembrane domain-containing protein 4
- Trem-like transcript 1 protein
- CKLF-like MARVEL transmembrane domain-containing protein 7
- CKLF-like MARVEL transmembrane domain-containing protein 8
- CKLF-like MARVEL transmembrane domain-containing protein 6
Sequence:
MLSARDRRDRHPEEGVVAELQGFAVDKAFLTSHKGILLETELALTLIIFICFTASISAYMAAALLEFFITLAFLFLYATQYYQRFDRINWPCLLQGHGQSGGPHPLDLLSHSAKVQPQPWPGLTPPGWHTPAAVPWVPAPAPGFWSWLLWFICFHSLGSSDFLRCVSAIIIFLVVSFAAVTSRDGAAIAAFVFGIILVSIFAYDAFKIYRTEMAPGASQGDQQ
Protein: Autophagy-related protein 13 (W0TA43)
Organism: Kluyveromyces marxianus (strain DMKU3-1042 / BCC 29191 / NBRC 104275) (Yeast) (Candida kefyr)
Function: Activates the ATG1 kinase in a nutritional condition dependent manner through the TOR pathway, leading to autophagy. Involved in ATG9 and ATG23 cycling through the pre-autophagosomal structure (By similarity). Also involved in cytoplasm to vacuole transport (Cvt) and more specifically in Cvt vesicle formation. Seems to play a role in the switching machinery regulating the conversion between the Cvt pathway and autophagy (By similarity). Finally, ATG13 is also required for glycogen storage during stationary phase (By similarity).
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:Q06628}. Preautophagosomal structure {ECO:0000250|UniProtKB:Q06628}.
Interaction partners:
Sequence:
MSDSDREIIGLINNFFLKAALLLEQCKVVARGGGFDGEEPLRDGNHLFNIETRGDPTLEAQIQPWTTFDGEKSMPPLVLETFLDLRGLHSNQTVYLHDSDGNPWMVCKGGKKSEIVLERWLIELDRQFSSTTGSTDAAEDDEYNEFNDPENLHKQLVLLFRYLYTLTQLLPANDIITKLQASQQGTAQATTTTGTLKPLHIHTRLLDGSKPILSKGRVGLSKPIIASYSNTMNETNIASHLEQRKITPIKTKFGSLRITVSYRKDVDFYVIDQEDPYKRTTNVSALQDTVTATDRRISSNSNISISVSPKTTNMLNANHIPVDSSGGGFARRQSISSKLQPFKVGSVGSGSFVQSGSLQSVTNPNPSLSRNVSSSSVAAALKVQRGSAGSTVLNSDLPPELSSVGSGSKYSSSFGRIRRHSSVRRSESIDRTAKPRKSNETPPEDLLEFVKLLEDKKELNMKPSTILPQQDISSSLIKFQSMKPNNDTLSDNLSMSMSIDQPNMRMGSNSHSPIPSFSPNYGSIPSRLSQGSRNNSNVELITSRKSSLDRHRLSLLNRTGSNVDIRRGSVGTMETTNEDSKEDEDSHVHGLRFNSGTVNDKTEDNNEDDDEEEILIKRSSNAVASSTEHFSVSPRSARSISVSSYTRSQLPLKHPNFSYPTTSATTAHAKFHKSEVIPDQLHREGSHHHNSSHKNDEDDDLLFVMSDMNLTN
Protein: Uncharacterized protein (Q38AY5)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- PTHB1 N-terminal domain-containing protein
- Bardet-Biedl syndrome 8 protein
- Telomerase-associated protein, putative
- FG-GAP repeat protein, putative
- FG-GAP repeat protein, putative
Sequence:
MSVSPEPVVQSNVLYSDEKGEFRYQEGLQYMQNGELEKAILAFSKASFFAPHKPHPFIASAECHVSLYDFQGAVKQYRRSLWLLRSSNGRSNCCSRASGTGRDSRSFFSPQGRPTTAADGSSTAFGSDLMDCNGLDGVSFSVSTDVTGHTIFRRGSSACTTEPYDDASLERAVRRRLAGILDALSIVLFNVEDYEQALRFTDESLELCKDPQVVLHRCAYLIALEREDEAEKVLDKHIEENPSFFILSCSLLVHIYCLRQSFSPAKALLERVPLEERQHPQVLLAQHIFSRTYKTYRNRSIDHSDLQGLTRCISVFPGDSTLLLERAKHYIAKGMDRKAVTDLFRCISASEGRHAHAIDLMTETLFRLGSSNDGQSTTADAIKYYTTSLMWRQDNIPVLLARGECYIKMGDYQKALFDFLTVDRISPKHPEATQRIAVLHDIHGCELHREGKHEEAEREFSTAIATCSTEPVFFYHRARCRFDMNQPRYALRDVLSCYNLNPTDPQIRNFVHAHLSAFDQKVIAGGEHGGDLLGGLPGVTRPSPPNRQNVTKSTGMLRQNRRDKQLVEGKRLILMREGDGLSRAFGDTLTCRKVPLALSDKGSRGHSTTCT
Protein: D-guloside 3-dehydrogenase (EC 1.1.1.-) (P76043)
Organism: Escherichia coli (strain K12)
Function: Catalyzes the NAD(+)-dependent oxidation of the hydroxyl group at C3 of D-gulosides leading to 3-dehydro-D-gulosides. Probably functions in a metabolic pathway that transforms D-gulosides to D-glucosides. Is also able to catalyze the reverse reactions, i.e. the NADH-dependent reduction of the oxo group at C3 of 3-dehydro-D-gulosides leading to D-gulosides. In vitro, can oxidize D-gulose and methyl beta-D-guloside, and reduce methyl alpha-3-dehydro-D-guloside and methyl beta-3-dehydro-D-guloside. However, the actual specific physiological substrates for this metabolic pathway are unknown.
Interaction partners:
- 3-dehydro-D-guloside 4-epimerase
- D-glucoside 3-dehydrogenase
- Putative ABC transporter periplasmic-binding protein YcjN
- Inner membrane ABC transporter permease protein YcjO
- Inner membrane ABC transporter permease protein YcjP
- Kojibiose phosphorylase
- Glucosylglycerate phosphorylase
- Beta-phosphoglucomutase
- Uncharacterized HTH-type transcriptional regulator YcjW
- Galactitol 1-phosphate 5-dehydrogenase
Sequence:
MKKLVATAPRVAALVEYEDRAILANEVKIRVRFGAPKHGTEVVDFRAASPFIDEDFNGEWQMFTPRPADAPRGIEFGKFQLGNMVVGDIIECGSDVTDYAVGDSVCGYGPLSETVIINAVNNYKLRKMPQGSSWKNAVCYDPAQFAMSGVRDANVRVGDFVVVVGLGAIGQIAIQLAKRAGASVVIGVDPIAHRCDIARRHGADFCLNPIGTDVGKEIKTLTGKQGADVIIETSGYADALQSALRGLAYGGTISYVAFAKPFAEGFNLGREAHFNNAKIVFSRACSEPNPDYPRWSRKRIEETCWELLMNGYLNCEDLIDPVVTFANSPESYMQYVDQHPEQSIKMGVTF
Protein: Delta(24)-sterol reductase (EC 1.3.1.72) (24-dehydrocholesterol reductase) (3-beta-hydroxysterol Delta-24-reductase) (Q5BQE6)
Organism: Rattus norvegicus (Rat)
Function: Catalyzes the reduction of the delta-24 double bond of sterol intermediates during cholesterol biosynthesis. In addition to its cholesterol-synthesizing activity, can protect cells from oxidative stress by reducing caspase 3 activity during apoptosis induced by oxidative stress. Also protects against amyloid-beta peptide-induced apoptosis.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q15392}; Single-pass membrane protein {ECO:0000255}. Golgi apparatus membrane {ECO:0000250|UniProtKB:Q15392}; Single-pass membrane protein {ECO:0000255}.
Interaction partners:
- Lanosterol 14-alpha demethylase
- 7-dehydrocholesterol reductase
- Lathosterol oxidase
- Lanosterol synthase
- Methylsterol monooxygenase 1
- 3-keto-steroid reductase/17-beta-hydroxysteroid dehydrogenase 7
- 3-beta-hydroxysteroid-Delta
- Transmembrane 7 superfamily member 2.
- Sterol O-acyltransferase 1
- Sterol O-acyltransferase 2
Sequence:
MEPAVSLAVCALLFLLWVRVKGLEFVLIHQRWVFVCLFLLPLSLIFDIYYYVRAWVVFKLSSAPRLHEQRVQDIQKQVREWKEQGSKTFMCTGRPGWLTVSLRVGKYKKTHKNIMINLMDILEVDTKKQIVRVEPLVSMGQVTALLNSIGWTLPVLPELDDLTVGGLIMGTGIESSSHKYGLFQHICTAYELILADGSFVRCTPSENSDLFYAVPWSCGTLGFLVAAEIRIIPAKKYVKLRFEPVRGLEAICEKFTHESQRLENHFVEGLLYSLDEAVIMTGVMTDDVEPSKLNSIGSYYKPWFFKHVENYLKTNREGLEYIPLRHYYHRHTRSIFWELQDIIPFGNNPIFRYLFGWMVPPKISLLKLTQGETLRKLYEQHHVVQDMLVPMKCLSQALHTFQNDIHVYPIWLCPFILPSQPGLVHPKGDEAELYVDIGAYGEPRVKHFEARSCMRQLEKFVRSVHGFQMLYADCYMNREEFWEMFDGSLYHKLRKQLGCQDAFPEVYDKICKAARH
Protein: Serine (Or cysteine) peptidase inhibitor, clade B, member 9b (Q6P217)
Organism: Mus musculus (Mouse)
Interaction partners:
Sequence:
MSTLSEANGTFAIHLLKMLCQSNPSKNVCFSPVSISSALAMVLLGAKEQTAVQISQALGLKKEKGIHQGFLKLLRKLNKPDRKYSLIVANRLFADKTCEVLQTFKESCFRFYDSEMEQVNFFKAAVESRQCINTWVSKQTEGKIPELLADDSVNFQTRLVLVNALYFKGMWACQFCKESTREMPFYINKDEKRPVQMMCQTDTFMFAFVDELPARLLVMPYEGMELSLMVLLPEKGVDLSKVENDLTFEKLIAWTKPDIMWSTEVKVFLPKFKLQEDYEMKSVLQCLGIVDVFEKEKADLSAMSPERNLCLSKFIHKSVVEVNEEGTEAAAASSAEGIIPLCLGGGPSWFCADHPFLFFIRHNQTNSILFCGRFSSP
Protein: Penicillin-binding protein 3 (PBP 3) (EC 3.4.16.4) (PSPB20) (Penicillin-binding protein C) (P42971)
Organism: Bacillus subtilis (strain 168)
Function: Penicillin-binding proteins (PBPs) function in the late steps of murein biosynthesis (Probable). Probably required for both cortical and vegetative peptidoglycan synthesis (Probable). Although not usually required for cell division, in the absence of PBP 2B (pbpB) it becomes essential. Confers resistance to oxacillin and cephalexin.
Subcellular location: Cell membrane {ECO:0000269|PubMed:20713508, ECO:0000269|PubMed:22882210, ECO:0000269|PubMed:3080407}; Single-pass membrane protein {ECO:0000305}. Forespore inner membrane {ECO:0000269|PubMed:3080407}; Single-pass membrane protein {ECO:0000255}. Forespore outer membrane {ECO:0000269|PubMed:3080407}; Single-pass membrane protein. Membrane raft {ECO:0000269|PubMed:20713508, ECO:0000269|PubMed:22882210}; Single-pass membrane protein {ECO:0000255}. Note=Localizes at mid cell; localization requires FtsZ and PBP 2B (pbpB) (PubMed:28792086). Present in detergent-resistant membrane (DRM) fractions that may be equivalent to eukaryotic membrane rafts; these rafts include proteins involved in signaling, molecule trafficking and protein secretion (PubMed:20713508, PubMed:22882210). {ECO:0000269|PubMed:20713508, ECO:0000269|PubMed:22882210, ECO:0000269|PubMed:28792086}.
Interaction partners:
- Probable peptidoglycan glycosyltransferase FtsW
- Peptidoglycan glycosyltransferase RodA
- Cell shape-determining protein MreB
- Cell division protein FtsZ
- Penicillin-binding protein 4
- Cell division protein FtsA
- Cell shape-determining protein MreC
- D-alanyl-D-alanine carboxypeptidase DacA
- Rod shape-determining protein MreD
- Uncharacterized oxidoreductase YcsN
Sequence:
MLKKCILLVFLCVGLIGLIGCSKTDSPEDRMEAFVKQWNDQQFDDMYQSLTKDVKKEISKKDFVNRYKAIYEQAGVKNLKVTAGEVDKDDQDNKTMKHIPYKVSMNTNAGKVSFKNTAVLKLEKTDDEESWNIDWDPSFIFKQLADDKTVQIMSIEPKRGQIYDKNGKGLAVNTDVPEIGIVPGELGDKKEKVIKELAKKLDLTEDDIKKKLDQGWVKDDSFVPLKKVKPDQEKLVSEATSLQGVTRTNVSSRYYPYGEKTAHLTGYVRAITAEELKKKKEGTYSDTSNIGIAGLENVYEDKLRGTTGWKIYVPQTGEVIAEKKAKDGEDLHLTIDIKTQMKLYDELKDDSGAAVALQPKTGETLALVSAPSYDPNGFIFGWSDKEWKKLNKDKNNPFSAKFNKTYAPGSTIKPIAAAIGIKNGTLKADEKKTIKGKEWQKDSSWGGYSVTRVSERLQQVDLENALITSDNIYFAQNALDMGADTFTKGLKTFGFSEDVPYEFPIQKSSIANDKLDSDILLADTGYGQGQMQMSPLHLATAYTPFVDNGDLVKPTLIKKDSQTADVWHKQVVTKEGAADITKGLKGVVEDERGSAYQPVVKGITVAGKTGTAELKTSKDDKDGTENGWFVGYDYENKDLLVAMMIQNVQDRGGSHYVVEKAKKQFQSN
Protein: Barrier-to-autointegration factor (Q9VLU0)
Organism: Drosophila melanogaster (Fruit fly)
Function: Plays fundamental roles in nuclear assembly, chromatin organization, gene expression and gonad development. May potently compress chromatin structure and be involved in membrane recruitment and chromatin decondensation during nuclear assembly. Functions are required in both M phase and interphase of the cell cycle.
Subcellular location: Nucleus {ECO:0000269|PubMed:12902403}. Cytoplasm {ECO:0000269|PubMed:12902403}. Chromosome {ECO:0000269|PubMed:12902403}. Note=Colocalizes with chromosomes during both interphase and mitosis.
Interaction partners:
- Inner nuclear membrane protein Man1
- Polybromo
- Lamin-B receptor
- Lamin-C
- Nucleosomal histone kinase 1
- Lamin Dm0
- Histone H3.3A
- Histone H3
- Brahma associated protein 111kD
- Bromodomain containing 7/9
Sequence:
MSGTSQKHRNFVAEPMGNKSVTELAGIGETLGGRLKDAGFDMAYTVLGQYLVLKKDEELFKDWMKEVCHASSKQASDCYNCLNDWCEEFL
Protein: Acyltransferase 3 domain-containing protein (Q389C9)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MPGSLNSCPNNPNTQHCVLFSTVSHWTGPQSLYYCFPRSRTLLQIARFILDDPDLSTQLGYGALLGSNRSTELLKQYIYCSAHVPAASSNERYHAASWCIASVGITLILVATVCDYKWRVGTSSVTHEADETGNEGASELNPRATPACLPLISAEEVREDSTKLPTTPSPDCSRQCPRAGGLSRFHQIYGVHSPLLTPEEQLTAQSAVDSSSASIPSAQEASVFSSLTQQRLGFQGTSMRSDEQFLGIKAGVALASVPTLMQESGDGGNSCVTKLHALNVEKLNRSLQKDPLRGSDAPVLRSGVAHVVQCLSLVSSFQKWRGYPESESDLNLFNGLRVITFLWVTIFGTFWFTQQISPVNSSVVPSDSMLYAFLQKRIFSACAISTFLVIAGFLTLHRLHIYEEWQMKSPAVRAKWSRGTRRQWLLKGALSYTRYVVSRFVRVIPVALTVTLLVPNILPATSKGPLWMALSNAPALHKNCEDYWWTNLLLINNMVPTDGSKCCFPWSYYVALEFQLVATGPLIYRLARSLHTRVYTAGSIACVMIGVALRYSAFMSKKGKHLEKSEAAPYTFDAGALYEWPHLMFIPFLAGAILHRIYIAVKHRAQTLLMFGPDMFTVMHRCPESTTTEDRLSYFILEKLRLRSMRFLIMWGGIGMMCLCVFWGWSVLHLSQETTQVSVCRAAYESLILLFWCLGLCMLVFPLLFGYGGATRRFLVHPLWCGLSRLVLVGYLLTPIVIGIVNAHWGPTNVGVMLLLMLRWLGCTFLTFLAAFVLHMLVERPFLYISSQGKY
Protein: Myosin IXB (M0R300)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
Sequence:
MSVKEAGSSGRREQAAYHLHIYPQLSTTESQASCRVTATKDSTTSDVIKDAIASLRLDGTKCYVLVEVKESGGEEWVLDANDSPVHRVLLWPRRAQDEHPQEDGYYFLLQERNADGTIKYVHMQLVAQATATRRLVERGLLPRQQADFDDLCNLPELTEGNLLKNLKHRFLQQKIYTYAGSILVAINPFKFLPIYNPKYVKMYENQQLGKLEPHVFALADVAYYTMLRKRVNQCIVISGESGSGKTQSTNFLIHCLTALSQKGYASGVERTILGAGPVLEAFGNAKTAHNNNSSRFGKFIQVSYLESGIVRGAVVEKYLLEKSRLVSQEKDERNYHVFYYLLLGVSEEERQEFQLKQPEDYFYLNQHNLKIEDGEDLKHDFERLKQAMEMVGFLPATKKQIFAVLSAILYLGNVTYKKRATGREEGLEVGPPEVLDTLSQLLKVKREILVEVLTKRKTVTVNDKLILPYSLSEAITARDSMAKSLYSALFDWIVLRINHALLNKKDVEEAVSCLSIGVLDIFGFEDFERNSFEQFCINYANEQLQYYFNQHIFKLEQEEYQGEGITWHNIGYTDNVGCIHLISKKPTGLFYLLDEESNFPHATSQTLLAKFKQQHEDNKYFLGTPVMEPAFIIQHFAGKVKYQIKDFREKNMDYMRPDIVALLRGSDSSYVRELIGMDPVAVFRWAVLRAAIRAMAVLREAGRLRAERAEKAAGMSSPGAQSHPEELPRGASTPSEKLYRDLHNQMIKSIKGLPWQGEDPRSLLQSLSRLQKPRAFILKSKGIKQKQIIPKNLLDSKSLKLIISMTLHDRTTKSLLHLHKKKKPPSISAQFQTSLNKLLEALGKAEPFFIRCIRSNAEKKELCFDDELVLQQLRYTGMLETVRIRRSGYSAKYTFQDFTEQFQVLLPKDAQPCREVISTLLEKMKIDKRNYQIGKTKVFLKETERQALQETLHREVVRKILLLQSWFRMVLERRHFLQMKRAAVTIQACWRSYRVRRALERTQAAVYLQASWRGYWQRKLYRHQKQSIIRLQSLCRGHLQRKSFSQMISEKQKAEEKEREALEAARAGAEEGGQGQAAGGQQVAEQGPEPAEDGGHLASEPEVQPSDRSPLEHSSPEKEAPSPEKTLPPQKTVAAESHEKVPSSREKRESRRQRGLEHVKFQNKHIQSCKEESALREPSRRVTQEQGVSLLEDKKESREDETLLVVETEAENTSQKQPTEQPQAMAVGKVSEETEKTLPSGSPRPGQLERPTSLALDSRVSPPAPGSAPETPEDKSKPCGSPRVQEKPDSPGGSTQIQRYLDAERLASAVELWRGKKLVAAASPSAMLSQSLDLSDRHRATGAALTPTEERRTSFSTSDVSKLLPSLAKAQPAAETTDGERSAKKPAVQKKKPGDASSLPDAGLSPGSQVDSKSTFKRLFLHKTKDKKYSLEGAEELENAVSGHVVLEATTMKKGLEAPSGQQHRHAAGEKRTKEPGGKGKKNRNVKIGKITVSEKWRESVFRQITNANELKYLDEFLLNKINDLRSQKTPIESLFIEATEKFRSNIKTMYSVPNGKIHVGYKDLMENYQIVVSNLATERGQKDTNLVLNLFQSLLDEFTRGYTKNDFEPVKQSKAQKKKRKQERAVQEHNGHVFASYQVSIPQSCEQCLSYIWLMDKALLCSVCKMTCHKKCVHKIQSHCSYTYGRKGEPGVEPGHFGVCVDSLTSDKASVPIVLEKLLEHVEMHGLYTEGLYRKSGAANRTRELRQALQTDPAAVKLENFPIHAITGVLKQWLRELPEPLMTFAQYGDFLRAVELPEKQEQLAAIYAVLEHLPEANHNSLERLIFHLVKVALLEDVNRMSPGALAIIFAPCLLRCPDNSDPLTSMKDVLKITTCVEMLIKEQMRKYKVKMEEISQLEAAESIAFRRLSLLRQNANKSPKTRDIQEEELEVLLEEEAAGGDEDREKEILIERIQSIKEEKEDITYRLPELDPRGSDEENLDSETSASTESLLEERAGRGASEGPPAPALPCPGAPTPSPLPTVAAPPRRRPSSFVTVRVKTPRRTPIMPTANIKLPPGLPSHLPRWAPGA
Protein: Splicing factor MUD2 (P36084)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Splicing factor that contacts pre-mRNA directly and is a component of the pre-mRNA-U1 snRNP complex (commitment complex 2) that forms during early spliceosome assembly in yeast extracts.
Interaction partners:
- Protein HSH49
- U2 small nuclear ribonucleoprotein A'
- Branchpoint-bridging protein
- U1 small nuclear ribonucleoprotein A
- Small nuclear ribonucleoprotein E
- Small nuclear ribonucleoprotein Sm D2
- Pre-mRNA-processing protein PRP40
- Protein NAM8
- U1 small nuclear ribonucleoprotein component SNU71
- U1 small nuclear ribonucleoprotein 70 kDa homolog
Sequence:
MADEKRLEDLRSKIMESIGKSEKDVVPIENKRFNTDNAVIDTHFKRQKSDGELPKAPKSRNVSHSNNRGPSSIITMSTNRTTYEQTRAGPHRQSYRDASGRSYNRENRYSSHNTGPQWNNNPYNRQRDERRGRNERFDRRGRNGNGNYDRFNYQRKNEGSKFNGDRDKRQLQTNKYDMNYNSQNVMYPGSSFDSPAYYNMASSKANSRLVISGLSQSSDPSIVARLKDLLENFISGLQKTESNAEDFKISNFYIGEGRPDHIIVEFSSQICSTMVLACRSFFNAKLGTFDLKWRRPNDYVQQLDHLVDFCRGTVIALENLENIGEGEDYRMKELFSSLNVTNGTAKPLFYKCSSNTNNTGKESEFTKCILLSFEVVTQDILDKLKPYKWFKPNDGKISQVTSWITFQSLPNLVTQSVRVESRVLLLLNCLDPLDLKDETFITEIKETLKYSIAGADTIKICQPGVDYRLNFENLASGAGNIYIKFKTLEAAKHAMEELPGTQFNDRTVLCTYIDEDDFDMMEATQLS
Protein: Small nuclear ribonucleoprotein-associated protein B (snRNP-B) (snRPB) (SM11) (Sm protein B) (Sm-B) (SmB) (P17136)
Organism: Rattus norvegicus (Rat)
Function: Plays a role in pre-mRNA splicing as a core component of the spliceosomal U1, U2, U4 and U5 small nuclear ribonucleoproteins (snRNPs), the building blocks of the spliceosome (By similarity). Component of both the pre-catalytic spliceosome B complex and activated spliceosome C complexes (By similarity). Is also a component of the minor U12 spliceosome (By similarity). As part of the U7 snRNP it is involved in histone pre-mRNA 3'-end processing (By similarity).
Subcellular location: Cytoplasm, cytosol {ECO:0000250|UniProtKB:P14678}. Nucleus {ECO:0000250|UniProtKB:P14678}. Note=SMN-mediated assembly into core snRNPs occurs in the cytosol before SMN-mediated transport to the nucleus to be included in spliceosomes. {ECO:0000250|UniProtKB:P14678}.
Interaction partners:
- Small nuclear ribonucleoprotein Sm D3
- Small nuclear ribonucleoprotein Sm D1
- Small nuclear ribonucleoprotein Sm D2
- Small nuclear ribonucleoprotein Sm D2
- Small nuclear ribonucleoprotein E
- Small nuclear ribonucleoprotein F
- Small nuclear ribonucleoprotein G
- U1 small nuclear ribonucleoprotein A
- U1 small nuclear ribonucleoprotein 70 kDa
- U1 small nuclear ribonucleoprotein C
Sequence:
MTVGKSSKMLQHIDYRMRCILQDGRIFIGTFKAFDKHMNLILCDCDEFRKIKPKNSKQAEREEKRVLGLVLLRGENLVSMTVEGPPPKDTGIARVPLAGAAGGPGIGRAAGRGIPAGVPMPQAPAGLAGPVRGVGGPSQQVMTPQGRGTVAAAAAAATASIAGAPTQYPPGRGGPPPPMGRGAPPPGMMGPPPGMRPPMGPPMGIPPGRGTPMGMPPPGMRPPPPGMRGLL
Protein: Prefoldin subunit 2 (cDNA, FLJ96845, Homo sapiens prefoldin 2 (PFDN2), mRNA) (B1AQP2)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MAENSGRAGKSSGSGAGKGAVSAEQVIAGFNRLRQEQRGLASKAAELEMELNEHSLVIDTLKEVDETRKCYRMVGGVLVERTVKEVLPALENNKEQIQKIIETLTQQLQAKGKELNEFREKHNIRLMGEDEKPAAKENSEGAGAKASSAGVLVS
Protein: Transcription factor NF-E4 (Q86UQ8)
Organism: Homo sapiens (Human)
Function: Functions as part of the SSP (stage selector protein) complex, a complex that contributes to the preferential expression of the gamma-gene in fetal erythroid cells by facilitating the interaction of the gamma-globin genes with enhancer elements contained in the locus control region (LCR). The complex binds to the stage selector element (SSE) in the proximal gamma-globin promoter. In contrast, isoform 2 acts as a repressor of gamma-globin gene expression by preventing NFE2 and RNA polymerase II recruitment to the promoter.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- Alpha-globin transcription factor CP2
Sequence:
MPRVVCWHTLKSLNGYKNLSSGAETREGLRSSSPVDLPLRPRKQATAAGQRKLLSLQLLLCACTSVTDLTYWGPAGHGATAPHRSLLAIHLHLVPASSAAMKATGPHNAQTQVNPQGHAPSAEDPTGTWTVSGPCKDHPHPFLSQSNPPTRISSALPLKTDSALEQTPQQLPSLHLSQG
Protein: Centrosomal protein 290 (A0A0G2K715)
Organism: Rattus norvegicus (Rat)
Subcellular location: Cytoplasm, cytoskeleton, cilium basal body {ECO:0000256|ARBA:ARBA00004120}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000256|ARBA:ARBA00004300}.
Interaction partners:
Sequence:
MPPNIKWKELIKVDPDELPRQEELADKLLISLSKVEVNELKNEDQENMIHLFRITQSLMKMKAQEVELALEEVEKAGEEQAKFENQLKTKVMKLENELEMAQQSAGGRDTRFLRDEIRQLEKQLEQKDRELEDMEKELDKEKKVNEQLALRNEEAENENSKLRRENKRLKKKNEQLRQDIIDYQKQIDSQKESLLSRRGEDSDYRSQLSKKNYELVQYLDEIQTLTEANEKIEVQNQEMRKNLEESVQEMEKMTDEYNRMKAIVHQTDTVMDQIKKENEHYRLQVRELTDLLKAKDEEDDPVMMAVNAKVEEWKLILSSKDDEIIEYQQMLQSLRGKLKNAQLDADKSNIMALKQGIQERDSQIKMLTEQVEQYTKEMEKNTFIIEDLKNELRKDKGTSNIYQQTHYMKIHSKVQILEEKTKEAERTAELAEADAREKDKELVEALKRLKDYESGVYGLEDAVIEIKNYKAQIKIRDGEIEVLTKEINKLEMKINDVLDENEALRERAGLEPKTMIDLTEFRNSKRVKQQQYRAENQILLKEIESLEEERLDLKRKIRQMAQERGKRSAASGLTIDDLNLTETFSHGDKIGERKLNFISFNNMNETQSKNEFLSRELIEKEKDLERSRTVITKFQNKLKELVEENKQLEEGMKEILQAIKDMPKDSDVKGSETSLIIPSLERLVNAMESKNAEGIFDASLHLKAQVDQLTGRNEELRQELRESRKEAVNYSQQLVKANLKIDHLEKETDLLRQSSGSNVVYKGIDLPDGIAPSSAYIINSQNEYLIHLLQELDNKEKKLKHLEDSLEDYNRKFAVIRHQQSLLYKEYLSEKDVWKADSEMIKEEKRKLEDQAQQDAVKVKEYNNLLNALQMDSNEMKKMLSENSRKITVLQVNEKSLIRQYTTLVEIERQLRKENGKHKNDVISMEAEVTEKIGNLQRFKEMATFRIAALQKVVDNSVSLSELELANKQYSELTAKYRDVLQKDNMLVQRASNLEHLACENASLKEQMEGLSKELEITKEKLHTIEQAWEQETKLGNESNMDKAKKSMTNSDIVSISKKITVLEMKELNERQRAEHCQKMYEHLRTSLKHMEERNFELETKFTELTKINLDAQKVEQMLRDELADSVNKAVSDADRQRILELEKREVELKVEVSKLREISDIAKRQVDFLNSQQQSREKEVESLRMQLLDFQAQSDEKALIAKLHQHVVSLQISEATALGKLESVTSKLQKMEACNLRLEQKLDEKEQALYYARLEGRNRANHLRQTIQSLRRQFSGALPLAQQEKFSKTMIQLQNDKLKIMQEMKNSQQEHRNMENKTLEMELKLKGLEELISTLKDARGAQKVINWHVKIEELRLQELKLNRELVKGKEEIKYLNNIISEYEHTISSLEEDIVQQSKFHEERQMAWDQREVELERQLDIFDRQQNEILSAAQKFEDATGSMPDPSLPLPNQLEIALRKIKENIQIILKTQATCKSLEEKLKEKESALRLAEQNILSRDKVINELRLQLPATADREKLIAELNRTELEPKSHHTMKIAHQTIANMQARLNHKEEVLKKYQHLLEKAREEQREIVKKHEEDLHVLHHKLEQQADNSLSKFKQTAQDLIKQSPAPVPTNKHFIRLAEMEQTVAEQDDSLSSLLTKLKRVSRDLERQKEVTEFKVREFETTKLRLQETHANEVKKVKAEVEDLRHALAQAQKDSQNLKSELQAQKEANSRAPTTTMRNLVDRLKSQLALKEKQQKALSRALLELRSEMTAAAEERIIAVTSQKEANLNVQQVVERHTKELKSQIEDLNENLLKLKEALKTSKNKENSLADDLNDLNNELQKKQKAYNKILREKDGIDQENDELRRQIKRLSSGLQSKTLIDNKQSLIDELQKKVKKLESQLERQVDDVDIKPIKEKSGKEELIRWEEGKKWQTKVEGMRNKLKEKEGEVHSLTKQLSTLKELFAKADKEKLTLQKKLKTTGMTVDQVLGVRALESEKELEELKRRNLDLENDIVYMRTHQALPRDSVVEDLHLQNRYLQEKLHTLENKLSKDAYSQSLTSEIESDDHCQKEQELQRENLKLSSENIELKFQLEQAKKDLPRLKNQVRDLKEMCEILKKGKMELERKLGQVRGSGRSGKTIPELEKTIGLMKKVVEKVQRENEQLKKASGLLTSEKMATLEEENGKLKAELEKLKAHFGRQLSMQFESKSKGTERIMAENERLRKELKKEMQASEKLRIAKNNLELVNDKMAGQLEETGKRLQFAESRGPQLEGADSQSWKSIVVSRIYDTKIKDLESDIAKKNQSITDLKQLVREATEREQKAKKYTEDLEQQIEILKNVPEGAETEQELIQQLQLLRLANNQLDKEKAELIHQIEVIKDQTGAESSTPDSDQLKKKINDLETHLRKSEPEKQHLKEEIKKLKKELENFDPSFFEEIEDLKYNYKEEVKKNILLEEKLNKLSEQFGFELPSPLAASEQREDGESPNGVPIY
Protein: E3 ubiquitin-protein ligase hrd-like protein 1 (P90859)
Organism: Caenorhabditis elegans
Function: Proposed to have a role in neuroprotection.
Subcellular location: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
- RING-type E3 ubiquitin transferase
- Derlin-1
- Derlin-2
- UBX domain-containing protein 1
- Ubiquitin-conjugating enzyme E2 G2
- S5 DRBM domain-containing protein
- Transitional endoplasmic reticulum ATPase homolog 2
- 3-hydroxy-3-methylglutaryl coenzyme A reductase
- Peptide-N
- UV excision repair protein RAD23
Sequence:
MGVVNLLSRSSFPSVDSYLALSVLVAIVASVTVFTTFRSQPELQKLIEEELRNNTRLSSAYGLNIEALSGHTFFQIAHYILSDTTLIWVAINSYFAILAVCTRLIIKLTFKELARQEENVARQAFFCYVLLTIVYLSVVIGPQKGHRVMPWMIWGGICAFLSHLQFITCQRLKHISPSCDRGSQKISFLSLFLFFVSIAMTFLISRFQHHLTWQPAVLLYFDCLLAVFRSTYILFRCISSSRVFSFNPDSVRHFNYWLELITNFVCELIQMLSFAQLLAFSPGLNLTSIFFLYHMKLTYNCMTEQLSRHRNHKKIFEHIERSYPSVKCANGDDRCVVCWELLGTSRRLPCSHQFHDWCLMWWLAQDSSCPTCRCTIPSPQDQIRQPPEVGNSTRLRFNGGSFGFVHFPAFTLEVAANFGPFFGRAAEPTEEQLQTMLEQVREMFPQMSVDIIMTDLRQSGSAQSTIENILEGRIGMNASFMPGGVLDDELSDESENEIEYEEPAEIVQEPDNGRQRTWTKLSSSSGDEDLSYYEIQRAKMIETYRRKYLESDKAADLRAMGITE