wanglab/gogpt-training-data huggingface dataset:
Protein: Transcription factor HES-1 (C-HAIRY1) (Hairy and enhancer of split 1) (O57337)
Organism: Gallus gallus (Chicken)
Function: Transcriptional repressor of genes that require a bHLH protein for their transcription. May act as a negative regulator of myogenesis by inhibiting the functions of MYOD1 and ASH1 (By similarity).
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- E3 ubiquitin-protein ligase FANCL
- Fanconi anemia group F protein
- Uncharacterized protein.
- Fanconi_A_N domain-containing protein.
- Fanconi anemia group C protein homolog
- Hes family bHLH transcription factor 1
- Uncharacterized protein.
- Uncharacterized protein.
- FA_FANCE domain-containing protein.
- Fanconi anemia group M protein
Sequence:
MPADTGMEKPTASPIAGAPASASHTPDKPRSASEHRKSSKPIMEKRRRARINESLGQLKMLILDALKKDSSRHSKLEKADILEMTVKHLRNLQRAQMAAALSADPSVLGKYRAGFNECMNEVTRFLSTCEGVNADVRARLLGHLSACLGQIVAMNYLPPPPAGQPAHLAQPLHVQLPPTTTGAVPVPCKLEPTEALSPKVYGGFQLVPATDGQFAFLIPNPAFPPGSGPVIPLYANANVPVSTAWRSSERVHPPAGIPGAGLDIIWARVVPASQAGSPIAERREAVWRPW
Protein: Oligopeptide transporter 8 (AtOPT8) (Q9FJD1)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: May be involved in the translocation of tetra- and pentapeptides across the cellular membrane in an energy-dependent manner.
Subcellular location: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
- Probable metal-nicotianamine transporter YSL8
- Probable metal-nicotianamine transporter YSL6
- Probable metal-nicotianamine transporter YSL5
- Probable metal-nicotianamine transporter YSL7
- Probable metal-nicotianamine transporter YSL4
- Metal-nicotianamine transporter YSL1
- Metal-nicotianamine transporter YSL3
- Metal-nicotianamine transporter YSL2
- Protein DMP9
- Armadillo repeat only 3
Sequence:
MKDFTDTISESECDDEISIVPQVELTVPKTDDPTSPTVTFRMWVLGITACVLLSFLNQFFWYRTNPLTISSVSAQIAVVPIGHLMAKVLPTRRFFEGTRWSFTMNPGPFSTKEHVLITVFANSGSGAVYATHILSAVKLYYKRRLDFLPALLVMITTQVLGFGWAGLYRKHLVEPGEMWWPSNLVQVSLFRALHEKENKSKWGISRNQFFVITLITSFSYYLLPGYLFTVLTTVSWLCWISPKSILVNQLGSGSAGLGIGSFGLDWSTIASYLGSPLASPFFASANIAAGFFLVMYVITPLCYYLDLYNAKTFPIYSGKLFVASGKEYKVTSIIDANFRLDRQAYAETGPVHMSTFFAVTYGLGFATLSASIFHVLIFNGKDLWTQTRGAFGKNKKMDIHTKIMKRNYKEVPLWWFLSIFAVNLAVIVFICIYYKTQIQLPWWGAFLACLIAIFFTPLVGVIMATTNQAPGLNIITEYIIGYAYPERPVANICFKTYGYISMSQSLTFLSDLKLGTYMKIPPRTMFMAQVVGTLVAVIAYAGTAWWLMAEIPNLCDTNLLPPGSQWTCPSDRVFFDASVIWGLVGPRRMFGDLGEYSNINWFFVGGAIAPALVYLASRLFPNKKWISDIHIPVLIGATAIMPPASAVNFTSWLVMAFVFGHFVFKYRREWWQRYNYVLSGGMDAGTGFMSVLLFLALQRSEIAIDWWGNSGEGCPVAKCPTAKGVVVHGCPVF
Protein: Small GTPase, putative (Q381R1)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Geranylgeranyl transferase type-2 subunit beta
- Golgi reassembly stacking protein
Sequence:
MQQHHYVFKYIIIGDSGVGKSCLLLQFTDKRFEPLHDLTIGVEFGARVVTIKEKNIKLQIWDTAGQESFRSITRSYYRGACGALLVYDVTRRDTFTHLQTWLEDARSNANTAIVIMLIGNKCDLEKKREVSREEGEAFARKHNLVFMETSAKTAQNVDDAFLKTAAMIYDNVESGVLDAGAVSGKQGTGPGVARVSRTGGKKSEDSESGCFC
Protein: RNA demethylase ALKBH5 (EC 1.14.11.53) (Alkylated DNA repair protein alkB homolog 5) (Alpha-ketoglutarate-dependent dioxygenase alkB homolog 5) (Q3TSG4)
Organism: Mus musculus (Mouse)
Function: Dioxygenase that demethylates RNA by oxidative demethylation: specifically demethylates N(6)-methyladenosine (m6A) RNA, the most prevalent internal modification of messenger RNA (mRNA) in higher eukaryotes. Can also demethylate N(6)-methyladenosine in single-stranded DNA (in vitro) (By similarity). Requires molecular oxygen, alpha-ketoglutarate and iron (By similarity). Demethylation of m6A mRNA affects mRNA processing and export (By similarity). Required for the late meiotic and haploid phases of spermatogenesis by mediating m6A demethylation in spermatocytes and round spermatids: m6A demethylation of target transcripts is required for correct splicing and the production of longer 3'-UTR mRNAs in male germ cells.
Subcellular location: Nucleus speckle {ECO:0000269|PubMed:29279410}. Note=Promotes formation and localizes to paraspeckles, a nuclear membraneless organelle. {ECO:0000250|UniProtKB:Q6P6C2}.
Interaction partners:
- Alpha-ketoglutarate-dependent dioxygenase FTO
- Probable ATP-dependent RNA helicase DDX46
- N
- YTH domain-containing family protein 1
- Pre-mRNA-splicing regulator WTAP
- Nucleic acid dioxygenase ALKBH1
- N
- 3'-5' RNA helicase YTHDC2
- YTH domain-containing family protein 2
- YTH domain-containing protein 1
Sequence:
MAAASGYTDLREKLKSMTSRDNYKAGSREAAAAAAAAVAAAAAAAAAAEPYPASGTTKRKYQEDSDPERSDYEEHQLQKEEEARKVKSGIRQIRLFSQDECSKIEARIDEVVSRAEKGLYNEHTVDRAPLRNKYFFGEGYTYGAQLQKRGPGQERLYPPGDVDEIPDWVHQLVIQKLVEHRVIPEGFVNSAVINDYQPGGCIVSHVDPIHIFERPIVSVSFFSDSALCFGCKFQFKPIRVSEPVLSLPVRRGSVTVLSGYAADEITHCIRPQDIKERRAVIILRKTRLDAPRLETKSLSSSTLPPSYASDRLSGNTRDPALKPKRSHRKADPDAAHRPRILEMDKEENRRSVLLPTHRRRGSFSSENYWRKSYESSEDCPEAASSPTRKVKMRRH
Protein: Uroplakin-2 (UP2) (Uroplakin II) (UPII) (O00526)
Organism: Homo sapiens (Human)
Function: Component of the asymmetric unit membrane (AUM); a highly specialized biomembrane elaborated by terminally differentiated urothelial cells. May play an important role in regulating the assembly of the AUM (By similarity).
Subcellular location: Cell membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. Note=Heterodimer formation with UPK1A is a prerequisite to exit out of the endoplasmic reticulum (ER). {ECO:0000250}.
Interaction partners:
- Uroplakin-3a
- Uroplakin-1b
- Uroplakin-1a
- Putative postmeiotic segregation increased 2-like protein 11
- Keratin, type I cytoskeletal 20
Sequence:
MAPLLPIRTLPLILILLALLSPGAADFNISSLSGLLSPALTESLLVALPPCHLTGGNATLMVRRANDSKVVTSSFVVPPCRGRRELVSVVDSGAGFTVTRLSAYQVTNLVPGTKFYISYLVKKGTATESSREIPMSTLPRRNMESIGLGMARTGGMVVITVLLSVAMFLLVLGFIIALALGSRK
Protein: Deubiquitinase SseL (Deubiquitinating enzyme) (Deubiquitinating protease) (Salmonella secreted effector L) (A0A0H3NDL6)
Organism: Salmonella typhimurium (strain SL1344)
Subcellular location: Host cytoplasm {ECO:0000256|ARBA:ARBA00004192}. Secreted {ECO:0000256|ARBA:ARBA00004613}.
Interaction partners:
Sequence:
MSDEALTLLFSAVENGDQNCIDLLCNLALRNDDLGHRVEKFLFDLFSGKRTGSSDIDKKINQACLVLHQIANNDITKDNTEWKKLHAPSRLLYMAGSATTDLSKKIGIAHKIMGDQFAQTDQEQVGVENLWCGARMLSSDELAAATQGLVQESPLLSVNYPIGLIHPTTKENILSTQLLEKIAQSGLSHNEVFLVNTGDHWLLCLFYKLAEKIKCLIFNTYYDLNENTKQEIIEAAKIAGISESDEVNFIEMNLQNNVPNGCGLFCYHTIQLLSNAGQNDPATTLREFAENFLTLSVEEQALFNTQTRRQIYEYSLQ
Protein: Magnetosome protein MamF (Q6NE74)
Organism: Magnetospirillum gryphiswaldense (strain DSM 6361 / JCM 21280 / NBRC 15271 / MSR-1)
Function: Plays a role in regulating magnetite crystal size; partially redundant function with MmsF.
Subcellular location: Magnetosome membrane {ECO:0000269|PubMed:14766587, ECO:0000269|PubMed:18539817}; Multi-pass membrane protein {ECO:0000255}. Note=Resistant to trypsin digestion in isolated magnetosomes (PubMed:14766587). Localizes as a filament-like structure in a straight line running through the center of the cell, in a position that corresponds to magnetosomes (PubMed:18539817). Requires MamE for correct localization (By similarity). {ECO:0000250|UniProtKB:Q2W8R8, ECO:0000269|PubMed:14766587, ECO:0000269|PubMed:18539817}.
Interaction partners:
- Magnetosome formation protease MamE
- Magnetosome protein MamD
- Magnetosome protein MamC
- Magnetosome protein MamW
- Probable membrane transporter protein MamO
- Magnetite biomineralization protein Mms6
- Magnetosome protein MamH
- Actin-like protein MamK
- Magnetosome protein MamZ
- Endonuclease/exonuclease/phosphatase domain-containing protein
Sequence:
MAETILIETKTAGGNCRSYLMAGASYLGILCFVPLLMSRDDEYVYFHAKQGLVLWMWSILAMFALHLPGIGKWLFGFSSMGVLMLSVVGLVSVALRRTWRLPLISHVVALI
Protein: RRM domain-containing protein (Q386H7)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MSKLFISKLPKTVSAEEVKEFLENLMPEATRIQLLLGSQHHEHKGYAYAHFAGEEAATEALQRLCGDEPPSLHGVAITAKRASRVSDAVESDVTPLPAALAHFSHSQCVTVAPPSLVDELNGVVARCSVNDNLEAVAFATGAEAAACVASSGGRVVKCTPPRLPELLASREATKRRREEPPVVKSGEAATEGSAGDIVTAYERLGYTALSPSQLLQLVEDFLEGRGRVAVQDREGHVALLNLPAYISALE
Protein: Ribosome biogenesis protein MAK21 (Maintenance of killer protein 21) (Nucleolar complex protein 1) (Q12176)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Required for 60S ribosomal subunit synthesis.
Subcellular location: Nucleus, nucleolus {ECO:0000269|PubMed:11371346}.
Interaction partners:
- rRNA biogenesis protein RRP5
- Ribosome biogenesis protein ERB1
- Nucleolar complex-associated protein 3
- Nucleolar GTP-binding protein 1
- Pescadillo homolog
- 25S rRNA
- Nucleolar complex protein 2
- ATP-dependent RNA helicase HAS1
- U3 small nucleolar RNA-associated protein 20
- Ribosome biogenesis protein SSF1
Sequence:
MSENNGNPLDLSSLRNKISSKLRDNNSKKAKKTHKGKDVKASSNSKKVNEDIRREALALGASEEDLKLIQGLSDDDDAKSEQEFDAVADEDADDKGFKNDLQNFMKNVGFDQHKLEDVDDDDIEEESTSSKESKIPAQEKEHAQSNIASSTIEKTSQESIDNGSEQEENTVEEANLSSDQEPESESAEKEKKEEKDGGLITQTTIISSDKLIIPYDKPWYEIPLDPQVGQNDDVEELSKEQIEKLFERGKQTLEADNQTYYEEFTKDSSQAKFMSQILSDGTLNDKISAVTLLIQDSPLHNTKSLETLVSYCGKKSRNSALQSLNALKDLFLNGLLPNRKLRYFKNQPGLSMMLNKKTLAIFYFEDYLKKLFFRVLEVLEVLSHDPIIHVRLQILNHVFDLLTNQPEQEFNLLRLGVNKIGDIDSKVSSKASYLLLKLEQAHPNMKSIVIDAIVDIALRPNADYHTTYYSVITLNQTILKRSEDSVANKLVKTYFTLFEKFLINTDKDNTNGVVKSNSKSYEEKRKKNFKKGKHGGKSVKIEKTENEVLDEKNSKLFSALLTGINRAFPFAQIPASVYEVHMETLFKITHSSNFNTSIQALVLINQVTVKAKLNSDRYYRTLYESLFDPRLVNSSKQGIYLNLLYKSLKQDALNVERVEAFVKRILQVCSHWLNVGTITGFFFLLIQLAKTVPQIKNLLTNTPVDYEYESDAEEEQGDKDIKRKEYDGRKRDPKFANAEKSSLWEINNFINHFHPTVKTYANAYVTGETEQIAKPDLGLFTLSHFLDRFVYRSAKQTNTARGTSIMQPLFSGSRVNDSVLVKASDIMHDQGPVNTEDWLTKKVEDIKPEDKFFYQYFTTKKTADGKGKKSNKASNFDSDDEMDENEIWSALVKSRPDVEDDSDDSELDFAEDDFSDSTSDDEPKLDAIDDEDAKSEGSQESDQEEGLDEDIFYSFDGEQDNSDKKRSFAESSEEDESSEEEKEEEENKEVSAKRAKKKQRKNMLKSLPVFASADDYAQYLDQDSD
Protein: A disintegrin and metalloproteinase with thrombospondin motifs 7 (ADAM-TS 7) (ADAM-TS7) (ADAMTS-7) (EC 3.4.24.-) (COMPase) (Q9UKP4)
Organism: Homo sapiens (Human)
Function: Metalloprotease that may play a role in the degradation of COMP.
Subcellular location: Secreted, extracellular space, extracellular matrix {ECO:0000250}. Note=Also found associated with the external cell surface. {ECO:0000250}.
Interaction partners:
- Cartilage oligomeric matrix protein
- Furin
- Phosphatase and actin regulator 1
Sequence:
MPGGPSPRSPAPLLRPLLLLLCALAPGAPGPAPGRATEGRAALDIVHPVRVDAGGSFLSYELWPRALRKRDVSVRRDAPAFYELQYRGRELRFNLTANQHLLAPGFVSETRRRGGLGRAHIRAHTPACHLLGEVQDPELEGGLAAISACDGLKGVFQLSNEDYFIEPLDSAPARPGHAQPHVVYKRQAPERLAQRGDSSAPSTCGVQVYPELESRRERWEQRQQWRRPRLRRLHQRSVSKEKWVETLVVADAKMVEYHGQPQVESYVLTIMNMVAGLFHDPSIGNPIHITIVRLVLLEDEEEDLKITHHADNTLKSFCKWQKSINMKGDAHPLHHDTAILLTRKDLCAAMNRPCETLGLSHVAGMCQPHRSCSINEDTGLPLAFTVAHELGHSFGIQHDGSGNDCEPVGKRPFIMSPQLLYDAAPLTWSRCSRQYITRFLDRGWGLCLDDPPAKDIIDFPSVPPGVLYDVSHQCRLQYGAYSAFCEDMDNVCHTLWCSVGTTCHSKLDAAVDGTRCGENKWCLSGECVPVGFRPEAVDGGWSGWSAWSICSRSCGMGVQSAERQCTQPTPKYKGRYCVGERKRFRLCNLQACPAGRPSFRHVQCSHFDAMLYKGQLHTWVPVVNDVNPCELHCRPANEYFAEKLRDAVVDGTPCYQVRASRDLCINGICKNVGCDFEIDSGAMEDRCGVCHGNGSTCHTVSGTFEEAEGLGYVDVGLIPAGAREIRIQEVAEAANFLALRSEDPEKYFLNGGWTIQWNGDYQVAGTTFTYARRGNWENLTSPGPTKEPVWIQLLFQESNPGVHYEYTIHREAGGHDEVPPPVFSWHYGPWTKCTVTCGRGVQRQNVYCLERQAGPVDEEHCDPLGRPDDQQRKCSEQPCPARWWAGEWQLCSSSCGPGGLSRRAVLCIRSVGLDEQSALEPPACEHLPRPPTETPCNRHVPCPATWAVGNWSQCSVTCGEGTQRRNVLCTNDTGVPCDEAQQPASEVTCSLPLCRWPLGTLGPEGSGSGSSSHELFNEADFIPHHLAPRPSPASSPKPGTMGNAIEEEAPELDLPGPVFVDDFYYDYNFINFHEDLSYGPSEEPDLDLAGTGDRTPPPHSHPAAPSTGSPVPATEPPAAKEEGVLGPWSPSPWPSQAGRSPPPPSEQTPGNPLINFLPEEDTPIGAPDLGLPSLSWPRVSTDGLQTPATPESQNDFPVGKDSQSQLPPPWRDRTNEVFKDDEEPKGRGAPHLPPRPSSTLPPLSPVGSTHSSPSPDVAELWTGGTVAWEPALEGGLGPVDSELWPTVGVASLLPPPIAPLPEMKVRDSSLEPGTPSFPTPGPGSWDLQTVAVWGTFLPTTLTGLGHMPEPALNPGPKGQPESLSPEVPLSSRLLSTPAWDSPANSHRVPETQPLAPSLAEAGPPADPLVVRNAGWQAGNWSECSTTCGLGAVWRPVRCSSGRDEDCAPAGRPQPARRCHLRPCATWHSGNWSKCSRSCGGGSSVRDVQCVDTRDLRPLRPFHCQPGPAKPPAHRPCGAQPCLSWYTSSWRECSEACGGGEQQRLVTCPEPGLCEEALRPNTTRPCNTHPCTQWVVGPWGQCSGPCGGGVQRRLVKCVNTQTGLPEEDSDQCGHEAWPESSRPCGTEDCEPVEPPRCERDRLSFGFCETLRLLGRCQLPTIRTQCCRSCSPPSHGAPSRGHQRVARR
Protein: Slr1270 protein (P74182)
Organism: Synechocystis sp. (strain ATCC 27184 / PCC 6803 / Kazusa)
Subcellular location: Cell outer membrane {ECO:0000256|ARBA:ARBA00004442}.
Interaction partners:
- HlyD family of secretion proteins
- Sll0180 protein
- Slr1908 protein
- S-layer protein
- Slr1841 protein
- HlyB family
- Haemolysin secretion ATP-binding protein
- Slr1506 protein
- Cation or drug efflux system protein
- Sll1835 protein
Sequence:
MKSIHPLKFWSSSTLLLLLSTSVGVFLPGFSGGQGAIAVAQSVSPPDNAPSAETGNNADDSGFPLPQLPDTAPNERLNPSGNPLMFPTKPDEVDTTVRQAITLDEAIDLALRNNEQLQQAKLSLEQQEAGLMAARAALFPSLDTDFTFSRDSSAAAEATNALIANQNQTTTVNPELRSETSTNAVGNINLTYSIYAGGERSAQIAKAEQLVQNSRLQVEVVAEQTRFEATDRYYALQGADAQVAIAQASVEDASQSLRDARLLEQAGLGTRFDVLRAEGDLATANEALTRSIADQRNARRRLAQLLSVGQRVELTAADEIVEAGDWSLPLDESIVQAYKNRAELEQQLVQIEVSEQDRYIALAAIKPRVDFLANYTYQNNFDSSAGLVDGYAFAARVRWNFFDGGRAFAEARRADRQMDIAKTAFSEQRNQIRLEVEESYYTLISNKENIGSTRTNVIRFEEALRLARLRFQAGVGTQTDVINAQRDLANARGRFLQAIIGYNQSLNQLQRSISNLPNNHLFDIQP
Protein: WEB family protein At3g56270 (Q9LYL6)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
Sequence:
MAERQQSPAAETIPGTPVIREVRTGTGSENFNPENTRRGCLRAEIDISPQLYGGRGFWVPFNLEDNYDCVGEFDIKRMEEQTVELEKDLIMKELETLDLLEALGSTKRIFEDLKWQLQQQALRCKETPQHLRSHSKEMVDEHCHRNPLKSPDLMTMEMKQAGMNLCKTMDDLALIHSYAESLNMKTKEEKDVLGVASLAEELNSLKFKPAGPDQVERFNTENLPVNPQCEQIKMVVETYDTAFHKQSKTCPRTADMRLVAARKMEEAARAAEALALAEMTILSSRRNQDALCFPKTPCFPLTLKAQMNKELSTNVSRIEILRKLEEANEEVKQSKQALEVALNRVEIASVKQLEAEEAFRQWNIESWKDQKAVGAKRSMKRESFPQRSFLSHINQHEPLIDLPEPMLKRNVSMGNALNRKDEKQLVTPRRKFRFIQTHQASIRKTE
Protein: D-2-hydroxyglutarate--pyruvate transhydrogenase DLD3 (D-2HG--pyruvate transhydrogenase DLD3) (EC 1.1.99.40) ((R)-2-hydroxyglutarate--pyruvate transhydrogenase) (D-lactate dehydrogenase [cytochrome] 3) (EC 1.1.2.4) (D-lactate ferricytochrome C oxidoreductase) (D-LCR) (P39976)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Catalyzes the reversible oxidation of (R)-2-hydroxyglutarate to 2-oxoglutarate coupled to reduction of pyruvate to (R)-lactate. Can also use oxaloacetate as electron acceptor instead of pyruvate producing (R)-malate.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:10509019}.
Interaction partners:
- L-lactate dehydrogenase
- Hydroxyacylglutathione hydrolase, mitochondrial
- Hydroxyacylglutathione hydrolase, cytoplasmic isozyme
- Pyruvate carboxylase 1
- NAD-dependent malic enzyme, mitochondrial
- Pyruvate dehydrogenase E1 component subunit beta, mitochondrial
- D-lactate dehydrogenase [cytochrome] 1, mitochondrial
- Pyruvate dehydrogenase E1 component subunit alpha, mitochondrial
- Probable glutathione-independent glyoxalase SNO4
- Probable glutathione-independent glyoxalase HSP33
Sequence:
MTAAHPVAQLTAEAYPKVKRNPNFKVLDSEDLAYFRSILSNDEILNSQAPEELASFNQDWMKKYRGQSNLILLPNSTDKVSKIMKYCNDKKLAVVPQGGNTDLVGASVPVFDEIVLSLRNMNKVRDFDPVSGTFKCDAGVVMRDAHQFLHDHDHIFPLDLPSRNNCQVGGVVSTNAGGLNFLRYGSLHGNVLGLEVVLPNGEIISNINALRKDNTGYDLKQLFIGAEGTIGVVTGVSIVAAAKPKALNAVFFGIENFDTVQKLFVKAKSELSEILSAFEFMDRGSIECTIEYLKDLPFPLENQHNFYVLIETSGSNKRHDDEKLTAFLKDTTDSKLISEGMMAKDKADFDRLWTWRKSVPTACNSYGGMYKYDMSLQLKDLYSVSAAVTERLNAAGLIGDAPKPVVKSCGYGHVGDGNIHLNIAVREFTKQIEDLLEPFVYEYIASKKGSISAEHGIGFHKKGKLHYTRSDIEIRFMKDIKNHYDPNGILNPYKYI
Protein: Matrix protein (gp18) (p16) (P0C795)
Organism: Borna disease virus (strain V) (BDV)
Function: Plays a crucial role in virion assembly and budding.
Subcellular location: Virion {ECO:0000305}. Host cytoplasm {ECO:0000269|PubMed:17079312}. Host cell membrane; Peripheral membrane protein {ECO:0000250|UniProtKB:P0C794}. Host nucleus {ECO:0000269|PubMed:17079312}. Note=During viral budding, associates with the inner side of the plasma membrane of infected cells (By similarity). Found in nuclear punctate structures that have been proposed to be the sites of viral replication and transcription, also termed viral speckles of transcripts (vSPOTs). {ECO:0000250|UniProtKB:P0C794, ECO:0000269|PubMed:17079312}.
Interaction partners:
Sequence:
MNSKHSYVELKDKVIVPGWPTLMLEIDFVGGTSRNQFLNIPFLSVKEPLQLPREKKLTDYFTIDVEPAGHSLVNIYFQIDDFLLLTLNSLSVYKDPIRKYMFLRLNKDQSKHAINAAFNVFSYRLRNIGVGPLGPDIRSSGP
Protein: FGGY carbohydrate kinase domain-containing protein (D-ribulokinase FGGY) (EC 2.7.1.47) (Q96C11)
Organism: Homo sapiens (Human)
Function: Catalyzes ATP-dependent phosphorylation of D-ribulose at C-5 to form D-ribulose 5-phosphate. Postulated to function in a metabolite repair mechanism by preventing toxic accumulation of free D-ribulose formed by non-specific phosphatase activities. Alternatively, may play a role in regulating D-ribulose 5-phosphate recycling in the pentose phosphate pathway. Can phosphorylate ribitol with low efficiency.
Interaction partners:
- Sedoheptulokinase
- Glycerol-3-phosphate dehydrogenase, mitochondrial
- Cystinosin
- Elongator complex protein 3
Sequence:
MSGGEQKPERYYVGVDVGTGSVRAALVDQSGVLLAFADQPIKNWEPQFNHHEQSSEDIWAACCVVTKKVVQGIDLNQIRGLGFDATCSLVVLDKQFHPLPVNQEGDSHRNVIMWLDHRAVSQVNRINETKHSVLQYVGGVMSVEMQAPKLLWLKENLREICWDKAGHFFDLPDFLSWKATGVTARSLCSLVCKWTYSAEKGWDDSFWKMIGLEDFVADNYSKIGNQVLPPGASLGNGLTPEAARDLGLLPGIAVAASLIDAHAGGLGVIGADVRGHGLICEGQPVTSRLAVICGTSSCHMGISKDPIFVPGVWGPYFSAMVPGFWLNEGGQSVTGKLIDHMVQGHAAFPELQVKATARCQSIYAYLNSHLDLIKKAQPVGFLTVDLHVWPDFHGNRSPLADLTLKGMVTGLKLSQDLDDLAILYLATVQAIALGTRFIIEAMEAAGHSISTLFLCGGLSKNPLFVQMHADITGMPVVLSQEVESVLVGAAVLGACASGDFASVQEAMAKMSKVGKVVFPRLQDKKYYDKKYQVFLKLVEHQKEYLAIMNDD
Protein: 5-hydroxymethyl-dUMP N-hydrolase (EC 3.2.2.-) (2'-deoxynucleoside 5'-phosphate N-hydrolase 1) (Deoxyribonucleoside 5'-monophosphate N-glycosidase) (c-Myc-responsive protein Rcl) (O35820)
Organism: Rattus norvegicus (Rat)
Function: Catalyzes the cleavage of the N-glycosidic bond of deoxyribonucleoside 5'-monophosphates to yield deoxyribose 5-phosphate and a purine or pyrimidine base. Deoxyribonucleoside 5'-monophosphates containing purine bases are preferred to those containing pyrimidine bases.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:O43598}. Nucleus {ECO:0000269|PubMed:9271375}.
Interaction partners:
- RWD domain-containing protein 1
Sequence:
MAASGEQAPCSVYFCGSIRGGREDQALYARIVSRLRRYGKVLTEHVADAELEPLGEEAAGGDQFIHEQDLNWLQQADVVVAEVTQPSLGVGYELGRAVALGKPILCLFRPQSGRVLSAMIRGAADGSRFQVWDYAEGEVETMLDRYFEAYLPQKTASSSHPSA
Protein: Uncharacterized transcriptional regulatory protein C530.05 (O59741)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00227, ECO:0000269|PubMed:10759889}.
Interaction partners:
- Transporter mfs1
- Probable transcriptional regulatory protein C8D2.12c
- Uncharacterized transporter C36.03c
- Brefeldin A resistance protein
- ATP-binding cassette transporter pdr1
- Caffeine resistance protein 5
Sequence:
MENLKSASPEEDSPRHGDNMGKPKRIPRACDMCRKRKIRCDGKQPACSNCVSHGIPCVFTARPKRRTGQRQMYIKSLVSRLEQMESTLRSVIPNYDQQPDIIHPSSTPKNYHDLNCTKGETSSDDSTDDIAFLNEKMGTLVTTPIGSQKYFGSSSTFSIIQHAAKFASGVESDKVLEHLSMAKSGCLFDPDESFDGSKAELPSSEIANIYIDAYFKSYNPLFPVFTRENFYQKFGSPNCFKKPDGSIDLVNYASYVVVLSLGCLAIADTEEQVSRANALFKNTLGISIEVTKDMSFRTLVFNFLTSVYYCAVSKPNAVWLNVGVVVRVAQTLGLHRNSAMWSIGKEDAEEKARLFWYIYYLDRVSSMMTGKPVAFQDDDIDQMVPFYSIYCYYGLKPPEGDPLGTFNFLEAEVQLTRIVGQVLKELYSVSGMKSNSSQVMEKILEFDLLLNNWYNSLPDCMQPRNRFKIPKFCSSNLILTSAIYYSCLILIHRHSLTKNLQVNCVHRGTGSITDSQALCIAAARSITNLFVESVDLQPLIMKIIMYHAFTSSIIIFISILKRPLASICSEDLNCLISVKNRLISFETHGFVRLNVVMDALESMISTAQAAMQKAKQIAINFSSNLATNEDVTNSGMPDIADVSLKSQSHVPPRISSNHSDTSVKSNSPSSIFDNSGYLNSLNNSILQMHQNLQNSSNTNDQYKFDSVQENELHANITPVLDQTMSMFPFKDQLDLNFAAANVYNPNVFDDMGLDCSFYGNGL
Protein: IST1 homolog (Charged multivesicular body protein 8) (CHMP8) (Q9CX00)
Organism: Mus musculus (Mouse)
Function: ESCRT-III-like protein involved in cytokinesis, nuclear envelope reassembly and endosomal tubulation (By similarity). Is required for efficient abscission during cytokinesis (By similarity). Involved in recruiting VPS4A and/or VPS4B to the midbody of dividing cells (By similarity). During late anaphase, involved in nuclear envelope reassembly and mitotic spindle disassembly together with the ESCRT-III complex: IST1 acts by mediating the recruitment of SPAST to the nuclear membrane, leading to microtubule severing (By similarity). Recruited to the reforming nuclear envelope (NE) during anaphase by LEMD2 (By similarity). Regulates early endosomal tubulation together with the ESCRT-III complex by mediating the recruitment of SPAST (By similarity).
Subcellular location: Cytoplasmic vesicle {ECO:0000250|UniProtKB:P53990}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250|UniProtKB:P53990}. Midbody {ECO:0000250|UniProtKB:P53990}. Nucleus envelope {ECO:0000250|UniProtKB:P53990}. Note=Localizes to centrosome and midbody of dividing cells. Colocalized with SPART to the ends of Flemming bodies during cytokinesis. Localizes to the reforming nuclear envelope on chromatin disks during late anaphase. {ECO:0000250|UniProtKB:P53990}.
Interaction partners:
- Spastin
- Charged multivesicular body protein 1B1
- Vacuolar protein sorting-associated protein VTA1 homolog
- Charged multivesicular body protein 1a
- Charged multivesicular body protein 5
- Charged multivesicular body protein 3
- Charged multivesicular body protein 2a
- Vacuolar protein sorting-associated protein 4B
- Charged multivesicular body protein 6
- Vacuolar protein sorting-associated protein 4A
Sequence:
MLGSGFKAERLRVNLRLVINRLKLLEKKKTELAQKARKEIADYLAAGKDERARIRVEHIIREDYLVEAMEILELYCDLLLARFGLIQSMKELDSGLAESVSTLIWAAPRLQSEVAELKIVADQLCAKYSKEYGKLCRTNQIGTVNDRLMHKLSVEAPPKILVERYLIEIAKNYNVPYEPDSVVMAEAPVGVETDLIDVGFTDDVKKGGPGRGGGGGFTAPVGGPDGIVPMPMPMPMPSPNAPFAYPLPKGPSDFSGLPVGTYQAFPNIHPPQIPATPPSYESVDDINGDKTVSSAQIVGPKPEAPAKPPSRPVDNYNTFVLPELPSVPDTLPTASAGASTSASEDIDFDDLSRRFEELKKKT
Protein: Ataxin-7 (Spinocerebellar ataxia type 7 protein homolog) (Q8R4I1)
Organism: Mus musculus (Mouse)
Function: Involved in neurodegeneration. Acts as component of the STAGA transcription coactivator-HAT complex. Mediates the interaction of STAGA complex with the CRX and is involved in CRX-dependent gene activation (By similarity). Necessary for microtubule cytoskeleton stabilization (By similarity).
Subcellular location: Nucleus {ECO:0000250|UniProtKB:O15265}. Nucleus, nucleolus {ECO:0000250|UniProtKB:O15265}. Nucleus matrix {ECO:0000250|UniProtKB:O15265}. Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:O15265}. Note=In addition to a diffuse distribution throughout the nucleus, it is associated with the nuclear matrix and the nucleolus. It is able to shuttle between the nucleus and cytoplasm (By similarity). {ECO:0000250|UniProtKB:O15265}.
Interaction partners:
- Transcription and mRNA export factor ENY2
- Ataxin-7-like protein 3
- Histone acetyltransferase KAT2A
- Ubiquitin carboxyl-terminal hydrolase 22
- Transcription initiation factor TFIID subunit 10
- Transformation/transcription domain-associated protein
- Transcriptional adapter 3
- Transcription initiation factor TFIID subunit 12
- TAF6-like RNA polymerase II p300/CBP-associated factor-associated factor 65 kDa subunit 6L
- Transcription initiation factor TFIID subunit 9B
Sequence:
MSERAADDVRGEPRRAAGGAAAARQQQQQPQPLQPQRQHPPLRRPRAEDGGTGDTTTSAAAMATVGERRPLPSPEAMLGQSWNLWVEASKLPGKDGTELDESFKEFGKNREVMGLCREDMPIFGLCPAHDDFYLVVCNDCNQVVKPQAFQSHYERRHSSSSKPALAVPHTSVFSLLPSLSKSKGSGAGGSSRPPSGGVLCASSSSKLLRLPKEKLPLRGNMKPMHPVQQIKVPHGRVMTPSVKVEKMHPKMDGTLLKSTVGPACPATMSSAVKPGLNCPSIPKPTLPSPGQILNGKGLPAMPTLEKKSEDSSNNRKFLNKRLSEREFDPDIHCGVIDLDTKKPCTRSLTCKTHSLTQRRAVQGRRKRFDVLLAEHKNKAREKELIRHDSQQVPHPLRDPHPTPPRTPQEPQLPAESKPFLASKPKPQTPSLPRPPGCPAQQGGSTPIDPPPGQESPHPPLPATEPASRLSSEEGEGDDREESVEKLDCHYSGRHPQPASFCTFGSRQIGRGYYVFDSRWNRLRCALNLMVEKHLNAQLWKKIPPVPCTTSPVSARVPHRTNSVPTSQGGISYLAATTVSAPPVLLSSTCISPNSKSVPAHGTTLNAQPAGSGAMDPVCSVQSRQVSASSSPPSTPSGLSSVPSSPLSRKPQKWKPSKSIRPKESSALSTNCHNASSSTSGGSGKKRKNSSPLLVPSSSSSSSSSSSSSHSVNSFRKNCVAHSGTPYLSTAPSSHSIGLNCVTNKTHSVSLRHEQAGRGPAGVSSAEPIKRMSVMVNSSDSTLSLGPFIHQASELPVNPHSHTPLDKLIGKKRKCSPGSSTVGNSGSKPTKVAKLPAMNNVHMKHTGNISGAQGLTNNSLLHQPKARP