wanglab/gogpt-training-data huggingface dataset:
Protein: NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 9, mitochondrial (Complex I-39kD) (CI-39kD) (NADH-ubiquinone oxidoreductase 39 kDa subunit) (Sperm flagella protein 3) (Q5BK63)
Organism: Rattus norvegicus (Rat)
Function: Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed not to be involved in catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone.
Subcellular location: Mitochondrion matrix {ECO:0000250|UniProtKB:Q16795}.
Interaction partners:
- NADH dehydrogenase 1 beta subcomplex subunit 5, mitochondrial
- NADH-ubiquinone oxidoreductase 75 kDa subunit, mitochondrial
- NADH dehydrogenase 1 alpha subcomplex subunit 5
- NADH dehydrogenase iron-sulfur protein 8, mitochondrial
- NADH dehydrogenase iron-sulfur protein 4, mitochondrial
- NADH dehydrogenase iron-sulfur protein 6, mitochondrial
- NADH-ubiquinone oxidoreductase chain 4
- NADH:ubiquinone oxidoreductase subunit V3
- NADH dehydrogenase 1 alpha subcomplex subunit 12
- NADH dehydrogenase 1 beta subcomplex subunit 11, mitochondrial
Sequence:
MAAAVRFQVVRALPMSRPAISAAATSVFCSSSHRQLHHAVIPHGKGGRSSVSGVVATVFGATGFLGRYVVNHLGRMGSQVIIPYRCDIYDTMHLRLMGDLGQLIFLEWDARDKDSIRKAVQHSNVVINLIGREWETRNFDFEDVFVNIPRAIAQASKEAGVERFIHVSHLNASMKSSAKSLRSKAVGEKEVRTVFPDAIIIRPSDMFGREDRFLNHFANYRWFLAVPLVSLGFKTVKQPVYVADVSKGIANATKNPDAIGKTFAFTGPNRYLLFHLVKYIFGMTHRTFIPYPLPRFVYSWIGRLFGLSPFEPWTTKDKVERIHISDVMATDLPGLEDLGVQPTPLELKSIEVLRRHRTYRWLSSEIEETKPAKTVNY
Protein: Taste receptor type 2 member 107 (T2R107) (mT2R43) (STC5-1) (T2R4) (Q7M725)
Organism: Mus musculus (Mouse)
Function: Putative taste receptor which may play a role in the perception of bitterness.
Subcellular location: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
- Guanine nucleotide-binding protein G
Sequence:
MLNSAEGILLCVVTSEAVLGVLGDTYIALFNCMDYAKNKKLSKIGFILIGLAISRIGVVWIIILQGYIQVFFPHMLTSGNITEYITYIWVFLNHLSVWFVTNLNILYFLKIANFSNSVFLWLKRRVNAVFIFLSGCLLTSWLLCFPQMTKILQNSKMHQRNTSWVHQRKNYFLINQSVTNLGIFFFIIVSLITCFLLIVFLWRHVRQMHSDVSGFRDHSTKVHVKAMKFLISFMVFFILHFVGLSIEVLCFILPQNKLLFITGLTATCLYPCGHSIIVILGNKQLKQASLKALQQLKCCETKGNFRVK
Protein: Uncharacterized protein (Q6TM97)
Organism: Pseudomonas phage D3112 (Bacteriophage D3112)
Interaction partners:
Sequence:
MSREKSLGLIDVDCSSANTTSDNASFISSSRPNDSVRSSSSSCNSRNSSSLIIPAPSKTADSIESIALGQAQLDAIHRPLLDDLRHATEFFNSVDGDLASVFNGSRQIAVEWLETAALALGNALIARHETTGGDHE
Protein: UDP-glycosyltransferase 73C6 (EC 2.4.1.-) (Flavonol-3-O-glycoside-7-O-glucosyltransferase 1) (Zeatin O-glucosyltransferase 2) (Q9ZQ95)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Acts as a UDP-glucose:flavonol-3-O-glycoside-7-O-glucosyltransferase. 6- and 7-hydroxyflavone, but not 3- or 5-hydroxyflavone are accepted as substrates. Possesses low quercetin 3-O-glucosyltransferase, 7-O-glucosyltransferase and 4'-O-glucosyltransferase activities in vitro.
Interaction partners:
- Flavonol-3-O-rhamnosyltransferase
- Probable long-chain-alcohol O-fatty-acyltransferase 3
- Cytosolic sulfotransferase 10
- BAHD acyltransferase BIA1
- Phenolic glucoside malonyltransferase 2
- Phenolic glucoside malonyltransferase 1
- Cytochrome P450 72C1
- Brassinosteroid-related acyltransferase 1
Sequence:
MAFEKNNEPFPLHFVLFPFMAQGHMIPMVDIARLLAQRGVLITIVTTPHNAARFKNVLNRAIESGLPINLVQVKFPYQEAGLQEGQENMDLLTTMEQITSFFKAVNLLKEPVQNLIEEMSPRPSCLISDMCLSYTSEIAKKFKIPKILFHGMGCFCLLCVNVLRKNREILDNLKSDKEYFIVPYFPDRVEFTRPQVPVETYVPAGWKEILEDMVEADKTSYGVIVNSFQELEPAYAKDFKEARSGKAWTIGPVSLCNKVGVDKAERGNKSDIDQDECLEWLDSKEPGSVLYVCLGSICNLPLSQLLELGLGLEESQRPFIWVIRGWEKYKELVEWFSESGFEDRIQDRGLLIKGWSPQMLILSHPSVGGFLTHCGWNSTLEGITAGLPMLTWPLFADQFCNEKLVVQILKVGVSAEVKEVMKWGEEEKIGVLVDKEGVKKAVEELMGESDDAKERRRRAKELGESAHKAVEEGGSSHSNITFLLQDIMQLAQSNN
Protein: Protein shisa-4 (Transmembrane protein 58) (Q96DD7)
Organism: Homo sapiens (Human)
Subcellular location: Membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}.
Interaction partners:
Sequence:
MPPAGLRRAAPLTAIALLVLGAPLVLAGEDCLWYLDRNGSWHPGFNCEFFTFCCGTCYHRYCCRDLTLLITERQQKHCLAFSPKTIAGIASAVILFVAVVATTICCFLCSCCYLYRRRQQLQSPFEGQEIPMTGIPVQPVYPYPQDPKAGPAPPQPGFIYPPSGPAPQYPLYPAGPPVYNPAAPPPYMPPQPSYPGA
Protein: Catalase-peroxidase (CP) (EC 1.11.1.21) (Peroxidase/catalase) (P9WIE5)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: Bifunctional enzyme with both catalase and broad-spectrum peroxidase activity, oxidizing various electron donors including NADP(H). Protects M.tuberculosis against toxic reactive oxygen species (ROS) including hydrogen peroxide as well as organic peroxides and thus contributes to its survival within host macrophages by countering the phagocyte oxidative burst. Also displays efficient peroxynitritase activity, which may help the bacterium to persist in macrophages.
Interaction partners:
- Transcriptional regulator FurA
- Superoxide dismutase
- Alkyl hydroperoxide reductase C
- Nicotinamidase/pyrazinamidase
- Probable arabinosyltransferase B
- DUF4262 domain-containing protein
- Superoxide dismutase
- Type II NADH:quinone oxidoreductase Ndh
- 3-oxoacyl-[acyl-carrier-protein] synthase 1
- DNA-directed RNA polymerase subunit beta
Sequence:
MPEQHPPITETTTGAASNGCPVVGHMKYPVEGGGNQDWWPNRLNLKVLHQNPAVADPMGAAFDYAAEVATIDVDALTRDIEEVMTTSQPWWPADYGHYGPLFIRMAWHAAGTYRIHDGRGGAGGGMQRFAPLNSWPDNASLDKARRLLWPVKKKYGKKLSWADLIVFAGNCALESMGFKTFGFGFGRVDQWEPDEVYWGKEATWLGDERYSGKRDLENPLAAVQMGLIYVNPEGPNGNPDPMAAAVDIRETFRRMAMNDVETAALIVGGHTFGKTHGAGPADLVGPEPEAAPLEQMGLGWKSSYGTGTGKDAITSGIEVVWTNTPTKWDNSFLEILYGYEWELTKSPAGAWQYTAKDGAGAGTIPDPFGGPGRSPTMLATDLSLRVDPIYERITRRWLEHPEELADEFAKAWYKLIHRDMGPVARYLGPLVPKQTLLWQDPVPAVSHDLVGEAEIASLKSQIRASGLTVSQLVSTAWAAASSFRGSDKRGGANGGRIRLQPQVGWEVNDPDGDLRKVIRTLEEIQESFNSAAPGNIKVSFADLVVLGGCAAIEKAAKAAGHNITVPFTPGRTDASQEQTDVESFAVLEPKADGFRNYLGKGNPLPAEYMLLDKANLLTLSAPEMTVLVGGLRVLGANYKRLPLGVFTEASESLTNDFFVNLLDMGITWEPSPADDGTYQGKDGSGKVKWTGSRVDLVFGSNSELRALVEVYGADDAQPKFVQDFVAAWDKVMNLDRFDVR
Protein: Mannosyltransferase (EC 2.4.1.-) (Q8IDS3)
Organism: Plasmodium falciparum (isolate 3D7)
Subcellular location: Endoplasmic reticulum membrane {ECO:0000256|ARBA:ARBA00004477, ECO:0000256|RuleBase:RU363075}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004477, ECO:0000256|RuleBase:RU363075}.
Interaction partners:
- GPI mannosyltransferase 2
- GPI mannosyltransferase 1
- Dolichol-phosphate mannosyltransferase subunit 1
Sequence:
MIYNDILTLCANKLRGLIDSKIFIWLLIFFRIFNCLFVVTSFYPDEYFQSVEIAHFWAYGYGHMSWEWEPCVALRSVITPFIYYVLFLFLKLINIDHPVCVLYIPKLCHGICAALCDLGIYKLLIYWYVELYNDAWINEDNIKRNEKDENNGNNNNNNNNNNNNNNNNNNYYYHNNILYNTNDIISTILCCHFFCWFYFYSICRTSSHSFECLFNIWGVYFLSQNYYPLKNQSNKIEKIDLLLQNDVIIQKGKKHLNEWTNLKERRNDHHFDTYENNFIYHKGTQNCKQYDKNMVDQNVCGQNMVDHIIQNRNNLCRTHFYSSKFNKIQEAKNLLFSLFFSSLSVIFRPNALVFWLSLYILYIIKNIFEKQNKINYKEIFKIGITYTFFFLTIIIIIDSYYFGHITFPFWNFFVYNFLSGNNKYFGGHSFFFYFVCVIPSIYLTLTPFLFYGYYIIYNNILNKVKYKTINIYMYILKRIDWIVYLVTHLEILSLSFSKHKEHKIVIGYIPFLTIFVGYALYIIKLHYKKYNGKNGKNIYNNNKIQYGNITIKGRNKYIFLISSSLFTNISFLLQFLCILFFCLIHNRSPEHVASYFRNLETKDDQNIYIFITNCYDIPLYSHIHRKFNIGFLDCSPYDTSNDEATKNWRKRIYEDKFKEQFFNIFQEKKNNNHHINSTYGDTITPYIIPDKSFYWFGHHHFNKKNNFQYIYQNINLSCLNYRFHIPLQGQLPTYIVTTTIELTHLQLFLSTYNYKLETKPFFSYFMISEAKGIVPVYHYIFKRVPS
Protein: GH13040p (Mulet, isoform A) (Mulet, isoform B) (Mulet, isoform C) (Q7K549)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- GEO09046p1
Sequence:
MPSLLEALERKYFAECEFENAHQPELHKRSDLPNDFTVTKCGGRMEFSIFIPRLSPLTSVPALLVLNDCDIDSAGDFDSIREKCQRVRELDLAQNKLSDWSEVFSILEHMPRIEFLNLSKNQLASPIGTLPTAPTINLKSLVLNGTYLDWACVDTLLKNLPVLQELHLSLNNYRQVLIDAEEAEQRLQETETPEETERRITKAHPALKTLHFTGNPVEHWQEICRLGRLFPNLEALVLADCPIKSLQAEESSETHRYFPSLRLLNLSSAQLDSWAAIDELAKFSELRNLRVKHWPLWESLECTEHERRQLLIARLPNVEMLNGGGKISSDERVDSERAFVRYYMDKPEEERPARYQELLQIHGKLDPLVNVSLKPDKRVKVLFTYNDVSESRFVDIYLTVNDLKVKLEKLVGLAPNKMRLYYLDQDYKEFGPEEMRYPNKQLYSYNIQSGDEIIIDAKK
Protein: Double-Strand Break factor (D4PH99)
Organism: Caenorhabditis elegans
Interaction partners:
Sequence:
MEVNSRKLTVIHGVEPIETVYCNMEVSRYPSLKMKNTNLFVIVNNQAQGFRLTLRGEDRENFLSTVRKFAYISETPVKDHLNRSSTNTDVWYNSVEKRKGGSSSQPTSFSQPCDIDIGGSVKKSAARNLSHTYSTNIGESSRMPALTANEFFSQPVYNPYNRPASSASTVSSSIGSAYSVLHDDSPFSGFSPNSNHSLQFPCPSPSHSSSFSGFSQSSSHSSQLSSSPANAPSFPDFHSPPSANDIQIDQLNPVTVAPQIKQTADKCVQTDKQYVDERFDDPAFLRRYIKRVMSDSKMARLVGMMRSEIRKLPNDEFDAFYKKVKDHQRTAPSSSSKIGPPAIVQQTSDMEF
Protein: Linoleate 9S-lipoxygenase 2 (EC 1.13.11.58) (Lipoxygenase 1-2) (O24379)
Organism: Solanum tuberosum (Potato)
Function: Plant lipoxygenases may be involved in a number of diverse aspects of plant physiology including growth and development, pest resistance, and senescence or responses to wounding. Catalyzes the hydroperoxidation of lipids containing a cis,cis-1,4-pentadiene structure. Linoleic acid is the preferred substrate, but is also active with linolenic and arachidonic acids.
Subcellular location: Cytoplasm {ECO:0000255|PROSITE-ProRule:PRU00726}.
Interaction partners:
- Fatty acid hydroperoxide lyase
- allene-oxide cyclase
Sequence:
MIGQITSGLFGGPDDSKKLKGTVVMMNKNALDFTDLAGSLTDKAFEFLGQTVSFQLISSVQGDPTNGLQGKHSNPAYLENSLFTLTPLTAGSETAFGVTFDWNEEFGVPGAFIIKNTHINEFFLKSLTLEDVPNHGKVHFVCNSWVYPSFRYKSDRIFFVNQPYLPSKTPELLRKYRENELLTLRGDGTGKREAWDRIYDYDIYNDLGNPDEGKENVRTTLGGSAEYPYPRRGRTGRPPTRTDPKSESRIPLILSLDIYVPRDERFGHLKMSDFLTYALKSIVQFILPELHALFDGTPNEFDSFEDVLRLYEGGIKLPQGPLFKALTAAIPLEMIRELLRTDGEGILRFPTPLVIKDSKTAWRTDEEFAREMLAGVNPVIISRLQEFPPKSKLDPEAYGNQNSTITAEHIEDKLDGLTVDEAMNNNKLFILNHHDVLIPYLRRINTTTTKTYASRTLLFLQDNGSLKPLAIELSLPHPDGDQFGVTSKVYTPSDQGVESSIWQLAKAYVAVNDSGVHQLISHWLNTHAVIEPFVIATNRQLSVLHPIHKLLYPHFRDTMNINAMARQILINAGGVLESTVFQSKFAMEMSAVVYKDWVFPDQALPADLVKRGVAVEDSSSPHGVRLLIEDYPYAVDGLEIWSAIKSWVSDYCSFYYGSDEEILKDNELQAWWKELREVGHGDKKNEPWWPEMERPQELIDSCTTIIWIASALHAAVNFGQYPYAGYLPNRPTVSRRFMPEPGTPEYEELKKNPDKAFLKTITAQLQTLLGVSLIEILSRHTTDEIYLGQRESPEWTKDKEPLAAFDKFGKKLTDIEKQIIQRNGDNILTNRSGPVNAPYTLLFPTSEGGLTGKGIPNSVSI
Protein: Nucleophosmin (NPM) (Nucleolar phosphoprotein B23) (Nucleolar protein NO38) (Numatrin) (Q61937)
Organism: Mus musculus (Mouse)
Function: Involved in diverse cellular processes such as ribosome biogenesis, centrosome duplication, protein chaperoning, histone assembly, cell proliferation, and regulation of tumor suppressors p53/TP53 and ARF. Binds ribosome presumably to drive ribosome nuclear export. Associated with nucleolar ribonucleoprotein structures and bind single-stranded nucleic acids. Acts as a chaperonin for the core histones H3, H2B and H4. Stimulates APEX1 endonuclease activity on apurinic/apyrimidinic (AP) double-stranded DNA but inhibits APEX1 endonuclease activity on AP single-stranded RNA. May exert a control of APEX1 endonuclease activity within nucleoli devoted to repair AP on rDNA and the removal of oxidized rRNA molecules. In concert with BRCA2, regulates centrosome duplication. Regulates centriole duplication: phosphorylation by PLK2 is able to trigger centriole replication. Negatively regulates the activation of EIF2AK2/PKR and suppresses apoptosis through inhibition of EIF2AK2/PKR autophosphorylation. Antagonizes the inhibitory effect of ATF5 on cell proliferation and relieves ATF5-induced G2/M blockade. In complex with MYC enhances the transcription of MYC target genes. May act as chaperonin or cotransporter in the nucleolar localization of transcription termination factor TTF1.
Subcellular location: Nucleus, nucleolus {ECO:0000250|UniProtKB:P06748}. Nucleus, nucleoplasm {ECO:0000250|UniProtKB:P06748}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250|UniProtKB:P06748}. Note=Generally nucleolar, but is translocated to the nucleoplasm in case of serum starvation or treatment with anticancer drugs. Has been found in the cytoplasm in patients with primary acute myelogenous leukemia (AML), but not with secondary AML. Co-localizes with the methylated form of RPS10 in the granular component (GC) region of the nucleolus. Colocalized with nucleolin and APEX1 in nucleoli. Isoform 1 of NEK2 is required for its localization to the centrosome during mitosis. Can shuttle between cytoplasm and nucleus. {ECO:0000250|UniProtKB:P06748}.
Interaction partners:
- Nucleolin
- Tumor suppressor ARF
- Protein argonaute-2
- Large ribosomal subunit protein uL18
- ALK tyrosine kinase receptor
- Cellular tumor antigen p53
- Holliday junction recognition protein
- Histone-binding protein RBBP4
- E3 ubiquitin-protein ligase Mdm2
- Histone H4
Sequence:
MEDSMDMDMSPLRPQNYLFGCELKADKDYHFKVDNDENEHQLSLRTVSLGAGAKDELHIVEAEAMNYEGSPIKVTLATLKMSVQPTVSLGGFEITPPVVLRLKCGSGPVHISGQHLVAVEEDAESEDEDEEDVKLLGMSGKRSAPGGGNKVPQKKVKLDEDDEDDDEDDEDDEDDDDDDFDEEETEEKVPVKKSVRDTPAKNAQKSNQNGKDLKPSTPRSKGQESFKKQEKTPKTPKGPSSVEDIKAKMQASIEKGGSLPKVEAKFINYVKNCFRMTDQEAIQDLWQWRKSL
Protein: Polyadenylate-binding protein RBP47A (Poly(A)-binding protein RBP47A) (RNA-binding protein 47A) (AtRBP47A) (F4I3B3)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Heterogeneous nuclear ribonucleoprotein (hnRNP)-protein binding the poly(A) tail of mRNA and probably involved in some steps of pre-mRNA maturation.
Subcellular location: Nucleus {ECO:0000250}. Cytoplasmic granule {ECO:0000250}.
Interaction partners:
- Eukaryotic translation initiation factor 2 subunit alpha homolog
- T-complex protein 1 subunit beta
- protein-synthesizing GTPase
- Gb|AAD20086.1 family protein with RNA binding
- Protein BTR1
- Sister chromatid cohesion protein PDS5 homolog C
- DEAD-box ATP-dependent RNA helicase 37
- Nuclear transport factor 2A
- Serine/arginine-rich SC35-like splicing factor SCL30
- T-complex protein 1 subunit epsilon
Sequence:
MQTPNNNGSTDSVLPPTSAGTTPPPPLQQSTPPPQQQQQQQWQQQQQWMAAMQQYPAAAMAMMQQQQMMMYPHPQYAPYNQAAYQQHPQFQYAAYQQQQQQHHQSQQQPRGGSGGDDVKTLWVGDLLHWMDETYLHTCFSHTNEVSSVKVIRNKQTCQSEGYGFVEFLSRSAAEEALQSFSGVTMPNAEQPFRLNWASFSTGEKRASENGPDLSIFVGDLAPDVSDAVLLETFAGRYPSVKGAKVVIDSNTGRSKGYGFVRFGDENERSRAMTEMNGAFCSSRQMRVGIATPKRAAAYGQQNGSQALTLAGGHGGNGSMSDGESNNSTIFVGGLDADVTEEDLMQPFSDFGEVVSVKIPVGKGCGFVQFANRQSAEEAIGNLNGTVIGKNTVRLSWGRSPNKQWRSDSGNQWNGGYSRGQGYNNGYANQDSNMYATAAAAVPGAS
Protein: Chlorophyll a-b binding protein (LHCII type II CAB) (LHCP) (Q9T2K9)
Organism: Spinacia oleracea (Spinach)
Function: The light-harvesting complex (LHC) functions as a light receptor, it captures and delivers excitation energy to photosystems with which it is closely associated.
Subcellular location: Plastid, chloroplast thylakoid membrane {ECO:0000269|PubMed:1894641}; Multi-pass membrane protein {ECO:0000269|PubMed:1894641}.
Interaction partners:
Sequence:
RRTVKSAPQ
Protein: Protein FAM107B (Q3TGF2)
Organism: Mus musculus (Mouse)
Interaction partners:
Sequence:
MAEPDYIEDDNPELIRPQKLINPVKSSRNHQDLHRELLMNQKRGLAPQNKPELQKVMEKRRRDQVIKQKEEEAQKKKSDLEIELLKRQQKLEQLELEKQKLQEEQENAPEFVKVKGNLRRTGQEVAQAQES
Protein: Gamma-adducin (Adducin-like protein 70) (Q9UEY8)
Organism: Homo sapiens (Human)
Function: Membrane-cytoskeleton-associated protein that promotes the assembly of the spectrin-actin network. Plays a role in actin filament capping. Binds to calmodulin (Probable). Involved in myogenic reactivity of the renal afferent arteriole (Af-art), renal interlobular arteries and middle cerebral artery (MCA) to increased perfusion pressure. Involved in regulation of potassium channels in the vascular smooth muscle cells (VSMCs) of the Af-art and MCA ex vivo. Involved in regulation of glomerular capillary pressure, glomerular filtration rate (GFR) and glomerular nephrin expression in response to hypertension. Involved in renal blood flow (RBF) autoregulation. Plays a role in podocyte structure and function. Regulates globular monomer actin (G-actin) and filamentous polymer actin (F-actin) ratios in the primary podocytes affecting actin cytoskeleton organization. Regulates expression of synaptopodin, RhoA, Rac1 and CDC42 in the renal cortex and the primary podocytes. Regulates expression of nephrin in the glomeruli and in the primary podocytes, expression of nephrin and podocinin in the renal cortex, and expression of focal adhesion proteins integrin alpha-3 and integrin beta-1 in the glomeruli. Involved in cell migration and cell adhesion of podocytes, and in podocyte foot process effacement. Regulates expression of profibrotics markers MMP2, MMP9, TGF beta-1, tubular tight junction protein E-cadherin, and mesenchymal markers vimentin and alpha-SMA (By similarity). Promotes the growth of neurites (By similarity).
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:Q62847}. Cell membrane {ECO:0000250|UniProtKB:Q62847}; Peripheral membrane protein; Cytoplasmic side. Cytoplasm {ECO:0000250|UniProtKB:Q9QYB5}. Note=Full-length protein and the cleavage fragment 358-706 localize mainly to the cytoplasm, while cleavage fragment 1-357 translocates from the cytoplasm to the nucleus. {ECO:0000250|UniProtKB:Q9QYB5}.
Interaction partners:
- Protein 4.1
- Dematin
- Ankyrin-2
- Ankyrin-1
- Alpha-adducin
- Ankyrin-3
- Tropomodulin-4
- Tropomodulin-1
- Tropomodulin-3
- Tropomodulin-2
Sequence:
MSSDASQGVITTPPPPSMPHKERYFDRINENDPEYIRERNMSPDLRQDFNMMEQRKRVTQILQSPAFREDLECLIQEQMKKGHNPTGLLALQQIADYIMANSFSGFSSPPLSLGMVTPINDLPGADTSSYVKGEKLTRCKLASLYRLVDLFGWAHLANTYISVRISKEQDHIIIIPRGLSFSEATASNLVKVNIIGEVVDQGSTNLKIDHTGFSPHAAIYSTRPDVKCVIHIHTLATAAVSSMKCGILPISQESLLLGDVAYYDYQGSLEEQEERIQLQKVLGPSCKVLVLRNHGVVALGETLEEAFHYIFNVQLACEIQVQALAGAGGVDNLHVLDFQKYKAFTYTVAASGGGGVNMGSHQKWKVGEIEFEGLMRTLDNLGYRTGYAYRHPLIREKPRHKSDVEIPATVTAFSFEDDTVPLSPLKYMAQRQQREKTRWLNSPNTYMKVNVPEESRNGETSPRTKITWMKAEDSSKVSGGTPIKIEDPNQFVPLNTNPNEVLEKRNKIREQNRYDLKTAGPQSQLLAGIVVDKPPSTMQFEDDDHGPPAPPNPFSHLTEGELEEYKRTIERKQQGLEDAEQELLSDDASSVSQIQSQTQSPQNVPEKLEENHELFSKSFISMEVPVMVVNGKDDMHDVEDELAKRVSRLSTSTTIENIEITIKSPEKIEEVLSPEGSPSKSPSKKKKKFRTPSFLKKNKKKEKVEA
Protein: 26S proteasome non-ATPase regulatory subunit 5 (26S protease subunit S5 basic) (26S proteasome subunit S5B) (Q8BJY1)
Organism: Mus musculus (Mouse)
Function: Acts as a chaperone during the assembly of the 26S proteasome, specifically of the base subcomplex of the PA700/19S regulatory complex (RC). In the initial step of the base subcomplex assembly is part of an intermediate PSMD5:PSMC2:PSMC1:PSMD2 module which probably assembles with a PSMD10:PSMC4:PSMC5:PAAF1 module followed by dissociation of PSMD5 (By similarity).
Interaction partners:
- 26S proteasome regulatory subunit 7
- 26S proteasome regulatory subunit 4
- 26S proteasome non-ATPase regulatory subunit 2
- 26S proteasome non-ATPase regulatory subunit 7
- 26S proteasome non-ATPase regulatory subunit 6
- 26S proteasome non-ATPase regulatory subunit 4
- 26S proteasome regulatory subunit 6A
- 26S proteasome regulatory subunit 6B
- 26S proteasome non-ATPase regulatory subunit 14
- 26S proteasome regulatory subunit 10B
Sequence:
MAAQAVSLLREVARLEAPLEELRALQSVVQAVPLHELREQAAELRLRPLFSLLNQNNREQTALCVSILERLLQAVEPIHLARNLRLDLQRGLTHPDDSVKTLTLSQIGRIVENSEAVTEILNNAELLKQIVYCIGGENLSVAKAAIKSLSRISLTQAGLEALFESNLLDDLKNVMKTNDVVRYRVYELIIDISSVSSESLNYCTTSGLVTQLLKELTGEDVLVRATCIEMVTSLAYTHHGRQYLAQEGVIDQISNIIVGADSDPFSGFYLPGFVKFFGNLAVMDSPQQICERYPVFLEKVFEMADSQDPTMIGVAVDTVGILGSSVEGKQVLQKTGTRFERVLMRVGYQAKNASTELKIRCLDAVSSLLYLSPEQQTDDFLGMTESWFSSMSRDSLELFRGISNQPFPELHCAALKVFTAIADQPWAQRLMFNSPGFVEFVMDRSVEHDKASKDAKYELVKALANSKTVAEIFGNSNYLRLRAYLSEGPYYVKPVATTAVEGAD
Protein: Vacuolar-sorting protein SNF8 (ESCRT-II complex subunit VPS22) (Vacuolar protein-sorting-associated protein 22) (Q12483)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Component of the endosomal sorting complex required for transport II (ESCRT-II), which is required for multivesicular body (MVB) formation and sorting of endosomal cargo proteins into MVBs. The MVB pathway mediates delivery of transmembrane proteins into the lumen of the lysosome for degradation. The ESCRT-II complex is probably involved in the recruitment of the ESCRT-III complex.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:12194858}. Endosome membrane {ECO:0000269|PubMed:12194858}; Peripheral membrane protein {ECO:0000269|PubMed:12194858}.
Interaction partners:
- Vacuolar protein-sorting-associated protein 36
- Vacuolar protein sorting-associated protein 28
- Vacuolar protein sorting-associated protein 20
- Vacuolar protein-sorting-associated protein 25
- Vacuolar-sorting protein SNF7
- Vacuolar protein-sorting-associated protein 24
- DOA4-independent degradation protein 4
- Suppressor protein STP22 of temperature-sensitive alpha-factor receptor and arginine permease
- Protein SRN2
- Multivesicular body sorting factor 12
Sequence:
MKQFGLAAFDELKDGKYNDVNKTILEKQSVELRDQLMVFQERLVEFAKKHNSELQASPEFRSKFMHMCSSIGIDPLSLFDRDKHLFTVNDFYYEVCLKVIEICRQTKDMNGGVISFQELEKVHFRKLNVGLDDLEKSIDMLKSLECFEIFQIRGKKFLRSVPNELTSDQTKILEICSILGYSSISLLKANLGWEAVRSKSALDEMVANGLLWIDYQGGAEALYWDPSWITRQL
Protein: cDNA FLJ51864, highly similar to Syntaxin-17 (B4DJ69)
Organism: Homo sapiens (Human)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004370}.
Interaction partners:
Sequence:
MSEDEEKVKLRRLEPAIQKFIKIVIPTDLERLRKHQINIEKYQRCRIWDKLHEEHINAGRTVQQLRSNIREIEKLCLKVRKDDLVLLKRMIDPVKEEASAATAEFLQLHLESVEELKKQFNDEETLLQPPLTRSMTVGGNVLY
Protein: 26S proteasome complex subunit SEM1 (F4I886)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Nucleus {ECO:0000256|RuleBase:RU369057}.
Interaction partners:
Sequence:
MAAEPKAATAEVVKMDLFEDDDEFEEFEINEVDSSDLTSSCIERIDKDGLVYELSRSDMKTNLFDVNFRCEIDWLEKEEVKEVSQQWEDDWDDDDVNDDFSRQLRKELENGTDKK
Protein: RNA polymerase II-associated factor 1 homolog (Q8K2T8)
Organism: Mus musculus (Mouse)
Function: Component of the PAF1 complex (PAF1C) which has multiple functions during transcription by RNA polymerase II and is implicated in regulation of development and maintenance of embryonic stem cell pluripotency. PAF1C associates with RNA polymerase II through interaction with POLR2A CTD non-phosphorylated and 'Ser-2'- and 'Ser-5'-phosphorylated forms and is involved in transcriptional elongation, acting both independently and synergistically with TCEA1 and in cooperation with the DSIF complex and HTATSF1. PAF1C is required for transcription of Hox and Wnt target genes. PAF1C is involved in hematopoiesis and stimulates transcriptional activity of KMT2A/MLL1. PAF1C is involved in histone modifications such as ubiquitination of histone H2B and methylation on histone H3 'Lys-4' (H3K4me3). PAF1C recruits the RNF20/40 E3 ubiquitin-protein ligase complex and the E2 enzyme UBE2A or UBE2B to chromatin which mediate monoubiquitination of 'Lys-120' of histone H2B (H2BK120ub1); UB2A/B-mediated H2B ubiquitination is proposed to be coupled to transcription. PAF1C is involved in mRNA 3' end formation probably through association with cleavage and poly(A) factors. Connects PAF1C with the RNF20/40 E3 ubiquitin-protein ligase complex. Involved in polyadenylation of mRNA precursors (By similarity).
Subcellular location: Nucleus. Note=Punctuate distribution throughout the nucleus except in nucleoli and the perinuclear chromatin. {ECO:0000250}.
Interaction partners:
- RNA polymerase-associated protein LEO1
- RNA polymerase-associated protein CTR9 homolog
- Parafibromin
- RNA polymerase-associated protein RTF1 homolog
- FACT complex subunit SPT16
- Transcription elongation factor SPT5
- Superkiller complex protein 8
- DNA-directed RNA polymerase II subunit RPB1
- Transcription elongation factor SPT4-A
- FACT complex subunit SSRP1
Sequence:
MAPTIQTQAQREDGHRPNSHRTLPERSGVVCRVKYCNSLPDIPFDPKFITYPFDQNRFVQYKATSLEKQHKHDLLTEPDLGVTIDLINPDTYRIDPNVLLDPADEKLLEEEIQAPTSSKRSQQHAKVVPWMRKTEYISTEFNRYGISNEKPEVKIGVSVKQQFTEEEIYKDRDSQITAIEKTFEDAQKSISQHYSKPRVTPVEVMPVFPDFKMWINPCAQVIFDSDPAPKDTSGAAALEMMSQAMIRGMMDEEGNQFVAYFLPVEETLKKRKRDQEEEMDYAPDDVYDYKIAREYNWNVKNKASKGYEENYFFIFREGDGVYYNELETRVRLSKRRAKAGVQSGTNALLVVKHRDMNEKELEAQEARKAQLENHEPEEEEEEEMEAEEKEAGGSDEEQEKGSSSEKEGSEDEHSGSESDREEGDRDEASDKSGSGEDESSEDEARAARDKEEIFGSDADSEDDADSDDEDRGQAHRGSDNDSDSGSDGGGQRSRSQSRSRSRSASPFPSGSEHSAQEDGSEAAASDSSEADSDSD