wanglab/gogpt-training-data huggingface dataset:
Protein: Phosphatidylinositol N-acetylglucosaminyltransferase GPI2 subunit (EC 2.4.1.198) (O59802)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Part of the complex catalyzing the transfer of N-acetylglucosamine from UDP-N-acetylglucosamine to phosphatidylinositol, the first step of GPI biosynthesis.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:16823372}; Multi-pass membrane protein {ECO:0000269|PubMed:16823372}.
Interaction partners:
- Phosphatidylinositol N-acetylglucosaminyltransferase subunit gpi15
- Dolichol phosphate-mannose biosynthesis regulatory protein
- Phosphatidylinositol N-acetylglucosaminyltransferase gpi3 subunit
- Probable N-acetylglucosaminyl-phosphatidylinositol de-N-acetylase
- Meiotically up-regulated gene 84 protein
- N-acetylglucosaminyl-phosphatidylinositol biosynthetic protein gpi1
- GPI mannosyltransferase 2
- CDP-diacylglycerol--inositol 3-phosphatidyltransferase
Sequence:
MDEVCAAPAPKKMVAKSLVLNTFRKASVKEVVELKKPWKKVLWRKQDYPDNFIDESFLNGLQRNVNIQVTDFWSLVADSLPVSQHLSSVVIFASVFVSIYRNQLSCALVGFVSNVSAVAAFILWDFVLRKPCNNRTFPNYMGIVKSCILIVLTLAGLSPILMSLTKSTSPDSVWAIAVWLFLANVFFHEYTTETIRPHVRLHNSLSTNAALSASVVLASRLEKSINVFFFILFAVHWFALFPIFRKYIHVFSFYADMLMTLVLIISAYIALNAVASVVIAFVFLSLIFFISFICPIWFIKLQRFKNEIHGPWDIALPKLGPSKG
Protein: Cell division protein DivIB (Cell division and sporulation protein) (Division initiation protein DivIB) (P16655)
Organism: Bacillus subtilis (strain 168)
Function: Cell division protein that may be involved in stabilizing or promoting the assembly of the division complex. Plays an essential role in division at high temperatures, maybe by protecting FtsL from degradation or by promoting formation of the FtsL-DivIC complex. May modulate the transpeptidase activity of PBP-2B. Also required for efficient sporulation at all temperatures. Could be directly involved in the engulfment process or be required to form a sporulation septum competent for engulfment. Influences the Spo0J/Soj system of chromosome segregation.
Subcellular location: Cell membrane {ECO:0000255|HAMAP-Rule:MF_00912, ECO:0000269|PubMed:10852898, ECO:0000269|PubMed:18208530}; Single-pass type II membrane protein {ECO:0000255|HAMAP-Rule:MF_00912, ECO:0000269|PubMed:10852898, ECO:0000269|PubMed:18208530}. Note=Localizes to the division septum. Localization requires FtsZ and DivIC. Localization of DivIB and DivIC is codependent at high temperatures.
Interaction partners:
- Penicillin-binding protein 2B
- Cell division protein DivIC
- Cell division protein FtsA
- Cell division protein FtsL
- Cell division protein FtsZ
- Probable peptidoglycan glycosyltransferase FtsW
- Septation ring formation regulator EzrA
- UDP-N-acetylglucosamine--N-acetylmuramyl-
- Cell cycle protein GpsB
- Cell division protein ZapA
Sequence:
MNPGQDREKIVNIEERIPKIKEQRKQKANRRLISFIMLFFIMVLIIVYLQTPISKVSTISVTGNENVSKKEIIDLSDINSGDTEFWSLDKQKTEKKIQQNKLVKKAEISKSLPNKINIAIEEYKAIAYLEKDDVYYEVLENGSVLPNEVTPDDAGPILVNWTNAKKRSQMAKQLDALSNSLKQSISEIYYTPVKMDENRIKLYMNDGYVVTASIKTFADRMKTYPSIISQLSSNKKGIIHLEVATYFEEFGKNDKAAKKEDEN
Protein: Mature parasite-infected erythrocyte surface antigen (Q8I492)
Organism: Plasmodium falciparum (isolate 3D7)
Interaction partners:
- Gametocyte-specific protein
- Knob-associated histidine-rich protein
Sequence:
MEVICRNLCYDKKNNMMENEGNKVKKVYNNSSLKKYMKFCLCTIICVFLLDIYTNCESPTYSYSSIKNNNDRYVRILSETEPPMSLEEIMRTFDEDHLYSIRNYIECLRNAPYIDDPLWGSVVTDKRNNCLQHIKLLEMQESERRKQQEEENAKDIEEIRKKEKEYLMKELEEMDESDVEKAFRELQFIKLRDRTRPRKHVNVMGESKETDESKETDESKETGESKETGESKETGESKETGESKETGESKETGESKETGESKETGESKETGESKETGESKETGESKETGESKETGESKETGESKETRIYEETKYNKITSEFRETENVKITEESKDREGNKVSGPYENSENSNVTSESEETKKLAEKEENEGEKLGENVNDGASENSEDPKKLTEQEENGTKESSEETKDDKPEENEKKADNKKKSKKKKKSFFQMLGCNFLCNKNIETDDEEETLVVKDDAKKKHKFLREANTEKNDNEKKDKLLGEGDKEDVKEKNDEQKDKVLGEGDKEDVKEKNDEQKDKVLGEGDKEDVKEKNDGKKDKVIGSEKTQKEIKEKVEKRVKKKCKKKVKKGIKENDTEGNDKVKGPEIIIEEVKEEIKKQVEDGIKENDTEGNDKVKGPEIITEEVKEEIKKQVEEGIKENDTEGNDKVKGPEIITEEVKEEIKKQVEEGIKENDTESKDKLIGQEIITEEVKEGIKENDTENKDKVIGQEIITEEVKEGIKENDTENKDKVIGQEIITEEVKKEIEKQEEKGNKENILEIKDIVIGQEVIIEEVKKVIKKKVEKGIKENHTESKDKVIGQEIIVEEVKEEIEKQVEEGIKENDTESKDKVIGQEVIKGDVNEEGPENKDKVTKQEKVKEVKKEVKKKVKKRVKKRNNKNERKDNVIGKEIMKEDVNEKDTANKDKEIEQEKEKEEVKEKEEVKEKEEVKEKEEVKEKEEVKEKEEVKEKEEVKEKEEVKEKDTESKDKEIEQEKEKEEVKEVKEKDTENKDKVIGQEIIIEEIKKEVKKRVKKRNNKNENKDNVIVQEIMNEDVNEKDTANKDKVIEQEKEKEEVKEKEEVKEKEEVKEKEEVKEKEEVKEKEEVKEKDTESKDNVIVQEIMNEDVNEKDTESKDKMIGKEVIIEEVKEEVKKRVNKEVNKRVNRRNRKNERKDVIEQEIVSEEVNEKDTKNNDKKIGKRVKKPIDDCKKEREVQEESEEESEEESEEESEEESEEESEEESEEESEEESEEESEEESEEESEEESEEESEEESEEESEEESEEESDEEKNTSGLVHRRNCKKEKKYNNGELEEYYKEKQNEEYFDEEYIIQSKEHNTLNTFPNMALNEDFRREFHNILSIHEDTDLMELKRILYNLFLEYNPHMNNKQKAELDKKFSEMNVVHQILNYEERIRMYEENAARGRLNTVILDPIITFNVIFGDDTMFKFIDE
Protein: Meiotic driver wtf23 (O94409)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Promotes unequal transmission of alleles from the parental zygote to progeny spores by acting as poison/antidote system where the poison and antidote proteins are produced from the same locus; the poison component is trans-acting and targets all spores within an ascus whereas the antidote component is spore-specific, leading to poisoning of all progeny that do not inherit the allele.
Subcellular location: [Isoform 1]: Spore membrane {ECO:0000250|UniProtKB:A0A218N034, ECO:0000255}; Multi-pass membrane protein {ECO:0000255}. Vacuole membrane {ECO:0000250|UniProtKB:A0A218N034, ECO:0000255}; Multi-pass membrane protein {ECO:0000255}. Note=Contained within spores expressing the isoform and localizes isoform 2 to the vacuole. {ECO:0000250|UniProtKB:A0A218N034}.; SUBCELLULAR LOCATION: [Isoform 2]: Ascus epiplasm {ECO:0000250|UniProtKB:A0A218N034}. Cytoplasm {ECO:0000250|UniProtKB:A0A218N034}. Spore membrane {ECO:0000250|UniProtKB:A0A218N034, ECO:0000255}; Multi-pass membrane protein {ECO:0000255}. Vacuole membrane {ECO:0000250|UniProtKB:A0A218N034, ECO:0000255}; Multi-pass membrane protein {ECO:0000255}. Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:A0A218N034, ECO:0000255}; Multi-pass membrane protein {ECO:0000255}. Note=Localizes in trans to all spores within an ascus. Localization to the spore vacuole is dependent on isoform 1. {ECO:0000250|UniProtKB:A0A218N034}.
Interaction partners:
- Wtf element wtf14
Sequence:
MKNKYYPLRSSMDELSAKNDNEIDLEKGPLPEYNSEDGSTLPPYSENINLKDPKQMGANNPNLFNTDESTTPPDYGEDSLSITHRENHSSGTADNSSTSPLKKAFLSFISIFVLNVPAVCYLTYKDALFKDYGKDEWVYFGVWCAICLMIFISLWYFYETWIKAVKVTVIFLAQCIKVTVVFLAQCVKVISIGLFNIRREMMIIIWLLWLIICCILFGCVKSGDLNLNKALIYSTCTISAVLLLIVSSVCIPFWTFERTLAKLAKVFLLQSGIVLVLNGTMFLRGKHFEWTGCEIEASVLFIMGNVLFLCEMECPGALIRTRNSIRNGIAFILGGIGNAMMGLANAFRGGNDNNNNIPLGEMDVEGEV
Protein: Uncharacterized protein (Q38ET5)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MIAAGNESAMPETAEERVVEAVRAFHSDLCSGLTARAIHESSSNATVALQQLTELHSRTVEDLNDQIDRLQKQLFEAVEVIEKLGAQFARNEDEKSTDDQRSFTVDVLSISHGLETEVEVGQQNTEHACERGREYRPSREELSSDAFATAKSGSSLRDTGVMDDETADPSLLRDLWRGRRTLQQQQQQTWLVDQIKDLTSLLEKVVKENAVYRRELKLLHATSVPLEEHKKLLEERDRLLHDCSSMRIELQRLHEEVEATFDSAHGAHRRQRDFVSSCATASSLSEYKGEGSFPLQMREPEGLVHSLTTPLEGGESNDPDAQFAGGCHSGFDDGALLHTGLWKTAMRELEQQAALAASQLSAAGRLRELDDRVAELTRELDELRASYKELAAEDKCVREDCEQLTFRNAVLSQQVASLLVRVERQCRSIHRLSRQHDEQKEEIETLSESEELTDRGRDVGKVRHRADRGRTAAAARALLERRSAVMGQSPLPSTPTAGRGTGCGVSHVLDVMLPQLEPLQVEGGLRSAVGVFARGPRRSVHLRNLGSPPVTLENTQPPRLPPCEELSGVALGRPSGYATVYPSQLKGQTGPSSVNSKGSFYSETSAASGLVVSEDEEENKRFVELLREDENLERFSINSVKDLLKRNQELLKQLYIMTQRADSVPKQNSSEVAAEEGEKSRSTSDTEAAVPLQRSNRKRRRESTSFSGEEVREQSGKLQRSCEEVGSPDQAVSDSYVQLERHVHEHIDAVLRSHEAQLTLTDKGLASSLIHVIELGREFNTSAGNKHFENWVDVTAKDNIITSLVRLCLQQGIRAADQAIALAAAQQSIDIPSMKDCWCEAQRVLKQSARELQSAASQLQRDNPAITVVEGISSASVSASEKEADEAQLLQSITQLLRTASLREHTVQRVLRLAARRMRATRRACDVSKSAPLQPCEDTQEQCDQPARDKTNETHDVPFGDTDDDWDSDSDGDDGPRQLRLQVDAAHAQYQKLLAAHHEERKQHTVLLDRMWRLEEEMVAARRQREEALESMATMMKREDYEATVAALDNANATVEMLEERVKQQSAVQGLQQQELERCKQEREEDVRRHAEEAAQRAAQFAHKDEIIAHYASQQQQLEQRISDLQTANHQLEAQVQQGQCVINAKEEEVTELQKKLCRAELALLEQECTQGLLLTMFPGDEFLEKNSNLIHEQRREKEDLTQQVALLKVELDTARQDMTEQRLQLQQAVQMRQEAELLLQELVLGHKRTVEDPLDASSTQTSCAAMASETYRAELESLRRANALLLVEKQGWEEREELLRRQLDALGRNPVSETARRYGLQGTQSFEEQLEQMQVRCAELQQKLEEAEALRITLKELTEEKVHLASQLDELQTVLSEQRETNKALEREIKKVHERLVEKEESHDAVKITLAEKEEMINNISDAIRSLEAQIKNLDRSVSETEKERDKLLQDNVKLIESVKALTEAVKKKEAERKAAQAALAQGLASASASSQRRRGRTSGGAGGPTPVSITGSLGLKPS
Protein: PHD finger protein 11 (BRCA1 C-terminus-associated protein) (Renal carcinoma antigen NY-REN-34) (Q9UIL8)
Organism: Homo sapiens (Human)
Function: Positive regulator of Th1-type cytokine gene expression.
Subcellular location: Nucleus {ECO:0000269|PubMed:18405956}.
Interaction partners:
- Histone-lysine N-methyltransferase SETDB2
- Disintegrin and metalloproteinase domain-containing protein 33
- Inactive dipeptidyl peptidase 10
- Serine protease inhibitor Kazal-type 5
- Neuropeptide S receptor
Sequence:
MAQASPPRPERVLGASSPEARPAQEALLLPTGVFQVAEKMEKRTCALCPKDVEYNVLYFAQSENIAAHENCLLYSSGLVECEDQDPLNPDRSFDVESVKKEIQRGRKLKCKFCHKRGATVGCDLKNCNKNYHFFCAKKDDAVPQSDGVRGIYKLLCQQHAQFPIIAQSAKFSGVKRKRGRKKPLSGNHVQPPETMKCNTFIRQVKEEHGRHTDATVKVPFLKKCKEAGLLNYLLEEILDKVHSIPEKLMDETTSESDYEEIGSALFDCRLFEDTFVNFQAAIEKKIHASQQRWQQLKEEIELLQDLKQTLCSFQENRDLMSSSTSISSLSY
Protein: Pogo transposable element with ZNF domain (Suppressor of hairy wing homolog 5) (Zinc finger protein 280E) (Zinc finger protein 635) (Q7Z3K3)
Organism: Homo sapiens (Human)
Function: Plays a role in mitotic cell cycle progression and is involved in kinetochore assembly and mitotic sister chromatid cohesion. Probably through its association with CBX5 plays a role in mitotic chromosome segregation by regulating aurora kinase B/AURKB activation and AURKB and CBX5 dissociation from chromosome arms. Promotes the repair of DNA double-strand breaks through the homologous recombination pathway.
Subcellular location: Nucleus {ECO:0000269|PubMed:26721387}. Chromosome. Cytoplasm. Note=According to some authors, it is not localized to mitotic chromatin (PubMed:19244240). Recruited to trimethylated 'Lys-9' of histone H3 (H3K9me3). {ECO:0000269|PubMed:19244240}.
Interaction partners:
- PC4 and SFRS1-interacting protein
- Chromosome alignment-maintaining phosphoprotein 1
- Chromobox protein homolog 1
- Chromobox protein homolog 5
- Chromobox protein homolog 3
- Mitotic spindle assembly checkpoint protein MAD2B
- Chromodomain-helicase-DNA-binding protein 4
- Hepatoma-derived growth factor-related protein 2
- Activity-dependent neuroprotector homeobox protein
Sequence:
MADTDLFMECEEEELEPWQKISDVIEDSVVEDYNSVDKTTTVSVSQQPVSAPVPIAAHASVAGHLSTSTTVSSSGAQNSDSTKKTLVTLIANNNAGNPLVQQGGQPLILTQNPAPGLGTMVTQPVLRPVQVMQNANHVTSSPVASQPIFITTQGFPVRNVRPVQNAMNQVGIVLNVQQGQTVRPITLVPAPGTQFVKPTVGVPQVFSQMTPVRPGSTMPVRPTTNTFTTVIPATLTIRSTVPQSQSQQTKSTPSTSTTPTATQPTSLGQLAVQSPGQSNQTTNPKLAPSFPSPPAVSIASFVTVKRPGVTGENSNEVAKLVNTLNTIPSLGQSPGPVVVSNNSSAHGSQRTSGPESSMKVTSSIPVFDLQDGGRKICPRCNAQFRVTEALRGHMCYCCPEMVEYQKKGKSLDSEPSVPSAAKPPSPEKTAPVASTPSSTPIPALSPPTKVPEPNENVGDAVQTKLIMLVDDFYYGRDGGKVAQLTNFPKVATSFRCPHCTKRLKNNIRFMNHMKHHVELDQQNGEVDGHTICQHCYRQFSTPFQLQCHLENVHSPYESTTKCKICEWAFESEPLFLQHMKDTHKPGEMPYVCQVCQYRSSLYSEVDVHFRMIHEDTRHLLCPYCLKVFKNGNAFQQHYMRHQKRNVYHCNKCRLQFLFAKDKIEHKLQHHKTFRKPKQLEGLKPGTKVTIRASRGQPRTVPVSSNDTPPSALQEAAPLTSSMDPLPVFLYPPVQRSIQKRAVRKMSVMGRQTCLECSFEIPDFPNHFPTYVHCSLCRYSTCCSRAYANHMINNHVPRKSPKYLALFKNSVSGIKLACTSCTFVTSVGDAMAKHLVFNPSHRSSSILPRGLTWIAHSRHGQTRDRVHDRNVKNMYPPPSFPTNKAATVKSAGATPAEPEELLTPLAPALPSPASTATPPPTPTHPQALALPPLATEGAECLNVDDQDEGSPVTQEPELASGGGGSGGVGKKEQLSVKKLRVVLFALCCNTEQAAEHFRNPQRRIRRWLRRFQASQGENLEGKYLSFEAEEKLAEWVLTQREQQLPVNEETLFQKATKIGRSLEGGFKISYEWAVRFMLRHHLTPHARRAVAHTLPKDVAENAGLFIDFVQRQIHNQDLPLSMIVAIDEISLFLDTEVLSSDDRKENALQTVGTGEPWCDVVLAILADGTVLPTLVFYRGQMDQPANMPDSILLEAKESGYSDDEIMELWSTRVWQKHTACQRSKGMLVMDCHRTHLSEEVLAMLSASSTLPAVVPAGCSSKIQPLDVCIKRTVKNFLHKKWKEQAREMADTACDSDVLLQLVLVWLGEVLGVIGDCPELVQRSFLVASVLPGPDGNINSPTRNADMQEELIASLEEQLKLSGEHSESSTPRPRSSPEETIEPESLHQLFEGESETESFYGFEEADLDLMEI
Protein: Probable 26S proteasome regulatory subunit 4 (O16368)
Organism: Caenorhabditis elegans
Function: The 26S proteasome is involved in the ATP-dependent degradation of ubiquitinated proteins. The regulatory (or ATPase) complex confers ATP dependency and substrate specificity to the 26S complex (By similarity). May play a role in the degradation of microtubule severing protein mei-1.
Subcellular location: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
Interaction partners:
- Ubiquitin carboxyl-terminal hydrolase 14
- 26S protease regulatory subunit 6A
- Probable 26S proteasome regulatory subunit 10B
- 26S proteasome non-ATPase regulatory subunit 2
- 26S proteasome non-ATPase regulatory subunit 7
- 26S proteasome non-ATPase regulatory subunit 6
- Proteasome subunit beta type-2
- 26S proteasome non-ATPase regulatory subunit 14
- 26S proteasome non-ATPase regulatory subunit 4
- PCI domain-containing protein
Sequence:
MGQQQSGFGGRGNDRGAGDGEKKEKKKYEAPIPSRIGKKKKGSKGPDAASKLPAVTPHARCRLKLLKSERIKDYLLMEQEFIQNQERLKPQEERQEEERAKVDELRGTPMAVGSLEEIIDDQHAIVSTNVGSEHYVNIMSFVDKEQLEPGCSVLLNHKNHAVIGVLSDDTDPMVSVMKLEKAPQETYADVGGLDQQIQEIKEAVELPLTHPEYYEEMGIRPPKGVILYGCPGTGKTLLAKAVANQTSATFLRIVGSELIQKYLGDGPKMVRELFRVAEENAPSIVFIDEIDAVGTKRYDSNSGGEREIQRTMLELLNQLDGFDSRGDVKVLMATNRIESLDPALIRPGRIDRKIEFPLPDEKTKRRIFQIHTSRMTLGKEVNLEEFITAKDELSGADIKAMCTEAGLLALRERRMRVTMEDFQKSKENVLYRKKEGAPEELYL
Protein: Small nuclear ribonucleoprotein Sm D2 (Sm-D2) (snRNP core protein D2) (Q06217)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
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.
Subcellular location: Nucleus {ECO:0000250|UniProtKB:P62316}. Cytoplasm, cytosol {ECO:0000250|UniProtKB:P62316}.
Interaction partners:
- Pre-mRNA-splicing factor SYF1
- Splicing factor MUD2
- Pre-mRNA-splicing factor CWC2
- LSM complex subunit LSM4
- Cold sensitive U2 snRNA suppressor 1
- Small nuclear ribonucleoprotein Sm D3
- U2 small nuclear ribonucleoprotein A'
- Pre-mRNA-splicing factor SNU114
- Protein LUC7
- LSM2-LSM8 complex subunit LSM8
Sequence:
MSSQIIDRPKHELSRAELEELEEFEFKHGPMSLINDAMVTRTPVIISLRNNHKIIARVKAFDRHCNMVLENVKELWTEKKGKNVINRERFISKLFLRGDSVIVVLKTPVE
Protein: O-glycosylated covalently-bound cell wall protein, putative (B9WFE5)
Organism: Candida dubliniensis (strain CD36 / ATCC MYA-646 / CBS 7987 / NCPF 3949 / NRRL Y-17841) (Yeast)
Subcellular location: Secreted, cell wall {ECO:0000256|ARBA:ARBA00004191}.
Interaction partners:
Sequence:
MKFSTAALTLSLFAIVNSSVTTYGAGFSGDDDDNSKHHKYDCEIDTFDWKFALAVKEWKHCQDKKFCQDTDLDLVYEGDDGQLYHGCDGTYPYSKCKHCTNVFTGDDDDDANCDDDCKKKKKKVYYAKRGDDDDDDNCDDDCKYPYCEIHNTDCDLLITLCGGVLKDEKHATGEIVANHQFQFDKPPQKDALHKEGFSIVHTEGTYYLALDHKIDFWHCKVDDKGLYKIYDKSIGEQCSKIKLIVLKSDERATFSDDNDDCDDDCKNKKKQHD
Protein: Mitotic checkpoint serine/threonine-protein kinase BUB1 beta (EC 2.7.11.1) (MAD3/BUB1-related protein kinase) (hBUBR1) (Mitotic checkpoint kinase MAD3L) (Protein SSK1) (O60566)
Organism: Homo sapiens (Human)
Function: Essential component of the mitotic checkpoint. Required for normal mitosis progression. The mitotic checkpoint delays anaphase until all chromosomes are properly attached to the mitotic spindle. One of its checkpoint functions is to inhibit the activity of the anaphase-promoting complex/cyclosome (APC/C) by blocking the binding of CDC20 to APC/C, independently of its kinase activity. The other is to monitor kinetochore activities that depend on the kinetochore motor CENPE. Required for kinetochore localization of CENPE. Negatively regulates PLK1 activity in interphase cells and suppresses centrosome amplification. Also implicated in triggering apoptosis in polyploid cells that exit aberrantly from mitotic arrest. May play a role for tumor suppression.
Subcellular location: Cytoplasm. Nucleus. Chromosome, centromere, kinetochore. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome. Note=Cytoplasmic in interphase cells. Associates with the kinetochores in early prophase. Kinetochore localization requires BUB1, PLK1 and KNL1.
Interaction partners:
- Serine/threonine-protein kinase Nek2
- Serine/threonine-protein kinase PLK1
- Anaphase-promoting complex subunit 2
- Aurora kinase B
- Cell division cycle protein 23 homolog
- Anaphase-promoting complex subunit 4
- Mitotic checkpoint serine/threonine-protein kinase BUB1
- Cell division cycle protein 20 homolog
- Centromere protein F
- Cell division cycle protein 16 homolog
Sequence:
MAAVKKEGGALSEAMSLEGDEWELSKENVQPLRQGRIMSTLQGALAQESACNNTLQQQKRAFEYEIRFYTGNDPLDVWDRYISWTEQNYPQGGKESNMSTLLERAVEALQGEKRYYSDPRFLNLWLKLGRLCNEPLDMYSYLHNQGIGVSLAQFYISWAEEYEARENFRKADAIFQEGIQQKAEPLERLQSQHRQFQARVSRQTLLALEKEEEEEVFESSVPQRSTLAELKSKGKKTARAPIIRVGGALKAPSQNRGLQNPFPQQMQNNSRITVFDENADEASTAELSKPTVQPWIAPPMPRAKENELQAGPWNTGRSLEHRPRGNTASLIAVPAVLPSFTPYVEETARQPVMTPCKIEPSINHILSTRKPGKEEGDPLQRVQSHQQASEEKKEKMMYCKEKIYAGVGEFSFEEIRAEVFRKKLKEQREAELLTSAEKRAEMQKQIEEMEKKLKEIQTTQQERTGDQQEETMPTKETTKLQIASESQKIPGMTLSSSVCQVNCCARETSLAENIWQEQPHSKGPSVPFSIFDEFLLSEKKNKSPPADPPRVLAQRRPLAVLKTSESITSNEDVSPDVCDEFTGIEPLSEDAIITGFRNVTICPNPEDTCDFARAARFVSTPFHEIMSLKDLPSDPERLLPEEDLDVKTSEDQQTACGTIYSQTLSIKKLSPIIEDSREATHSSGFSGSSASVASTSSIKCLQIPEKLELTNETSENPTQSPWCSQYRRQLLKSLPELSASAELCIEDRPMPKLEIEKEIELGNEDYCIKREYLICEDYKLFWVAPRNSAELTVIKVSSQPVPWDFYINLKLKERLNEDFDHFCSCYQYQDGCIVWHQYINCFTLQDLLQHSEYITHEITVLIIYNLLTIVEMLHKAEIVHGDLSPRCLILRNRIHDPYDCNKNNQALKIVDFSYSVDLRVQLDVFTLSGFRTVQILEGQKILANCSSPYQVDLFGIADLAHLLLFKEHLQVFWDGSFWKLSQNISELKDGELWNKFFVRILNANDEATVSVLGELAAEMNGVFDTTFQSHLNKALWKVGKLTSPGALLFQ
Protein: Neurexin-3-beta (H2FLH5)
Organism: Caenorhabditis elegans
Interaction partners:
Sequence:
MVFLEHLRGGTPRGTTTVSPILCLMNWNDEQCRQQLKSYIPKFASNFDAPRHVPQPPSSPSYDYEGDEDEEKKEEKDHGIADRSMNDVSGETTGFFSPVLPTVANFPTTRQTERPAWRTNKSLTTTATTEASSTKSNRKTTTTTTTSATTTIRIQQRPNYDIDNEVTALITSSLAPQKTRPKSTPHFTVYPVRPTTPMGDTITTTMQAATVTDFPRTPLIMCSSLAVIIAIAAVVFFVFKCRQNPPNSEHYTMAMKSQSGYTAIAPELSPPMNHDRSNDSCTQPLLAKPHINGNGYEPLKGAVIANGNGATATMMRNGNGNGVAKKKDFKEWYV
Protein: Uncharacterized protein (Q383S1)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Uncharacterized protein
- 50S ribosomal protein L17, putative
- Mitochondrial RNA binding complex 1 subunit
- 50S ribosomal protein L16, putative
- Uncharacterized protein
- Large ribosomal subunit protein uL3m
- Rhodanese domain-containing protein
- Uncharacterized protein
- Uncharacterized protein
- Ribosomal protein L11, putative
Sequence:
MLRLCRVSLRVQSHQKKRAQHPNAGTRFGRVYNRGFIRYGFGGFGMSVYTPKKDRRFRVQPLPSLHANSLADDTPLVTTTRTLSPNFRAFALQDGGVFFTHPSHEQVMRVGQNILAEETKATGMTSMDTYVNSRIQSIIAENTVENVALSHWRRRHMWNLVRTHGKLQRHWGVSDATKGARSNIYGRPS
Protein: Kelch like family member 12 (J3QSX3)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MDVNKFEASVGFLDVKKFLSTWKLQNPRTHFVLSPHCFMGGIMAPKDIMTNTHAKSILNSMNSLRKSNTLCDVTLRVEQKDFPAHRIVLAACSDYFCAMFTSELSEKGKPYVDIQGLTASTMEILLDFVYTETVHVTVENVQELLPAACLLQLKGVKQACCEFLESQLDPSNCLGIRDFAETHNCVDLMQAAEVFSQKHFPEVVQHEEFILLSQGEVEKLIKCDEIQVDSEEPVFEAVINWVKHAKKEREESLPNLLQYVRMPLLTPRYITDVIDAEPFIRCSLQCRDLVDEAKKFHLRPELRSQMQGPRTRARL
Protein: Heat shock protein 16 (16 kDa heat shock protein) (O14368)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Cytoplasm {ECO:0000269|PubMed:11452028}. Nucleus {ECO:0000269|PubMed:11452028}.
Interaction partners:
- Heat shock protein 104
- Heat shock protein homolog C338.06c
- Probable heat shock protein ssa1
- Probable heat shock protein ssa2
- Heat shock protein hsp9
- Heat shock protein 78
- Protein psi1
- Small ribosomal subunit protein uS17A
- Heat shock protein 90 homolog
Sequence:
MSLQPFFGFPPTVNDLFSDFVSYSPRLNNQIPGELSPSIDVHEGKDTVSVDVELPGVKKEDVQVHYDSGKLTISGEVVNERKNESTEGNQRWSERRFGSFSRTITIPAKIDADRIEANFSNGLLTVTLPKVEKSQTKKQIAIK
Protein: Mobilization protein MbeC (Conjugative accessory protein MbeC) (P13657)
Organism: Escherichia coli
Function: Required for efficient mobilization of ColE1 plasmid and is thus essential to promote the specific transfer of the plasmid during conjugation. Probably functions by inducing DNA bending, helping the MbeA relaxase to melt the DNA around the nic site and cleave the phosphodiester bond. Binds specifically double-stranded DNA (dsDNA) containing the ColE1 oriT but does not recognize the inverted repeat (IR).
Interaction partners:
Sequence:
MIPMKRERMLTIRVTDDEHARLLERCEGKQLAVWMRRVCLGEPVARSGKLPTLAPPLLRQLAAIGNNLNQTARKVNSGQWSSGDRVQVVAALMAIGDELRRLRLAVREQGARDDS
Protein: Cullin-4 (CUL-4) (Cullin-D) (Q54CS2)
Organism: Dictyostelium discoideum (Social amoeba)
Function: Probable core component of cullin-based SCF-like E3 ubiquitin-protein ligase complexes which mediate the ubiquitination and subsequent proteasomal degradation of target proteins. The E3 ubiquitin-protein ligase activity of the complex is dependent on the neddylation of the cullin subunit (By similarity).
Interaction partners:
- DNA damage-binding protein 1
- RING-box protein 1
- COP9 signalosome complex subunit 5
- WD40 repeat-containing protein
- Cullin-associated NEDD8-dissociated protein 1
- COP9 signalosome complex subunit 4
- DDB1- and CUL4-associated factor 7 homolog
- COP9 signalosome complex subunit 6
- Uncharacterized protein
- COP9 signalosome complex subunit 2
Sequence:
MNFNNNNNNNNNNNNNNNLNNNNNNVNNINNNNKKPLTNSLAGTPPAKKILVIKNLKQIPKTPDNYEDSSWNKLSSAITSINMKQATTLTQEELYKMVENLCFDKILASNLYNKISVQIEKHITLTIKHLVLTMSSDPIIFLKSINSIWKDHTNQMIMIRSIFLYLDRTYVIQNSNTVKSIWDLGLFYFGNNLSQQSNLERKTIDSLLYSIRCEREGDEIDRDLIHSLVKMLSSLNIYTKFEIEFIKETNRFYDMEGNSKINEIETPMYLKYVCERLNQEGERLMRYLEQSTKKQLMAVLDRQLIERHVDVILEKGFNAMVNGDRLEDLGKLYQLLNSVGEIKKIKESWQSYIKQTGIQMLNDKEKEATLIQDLLDYKDRLDRILSQSFSKNELLTYALKESFEYFINTKQNKPAELVARFIDSKLKVGGKRMSEEELETVLNKSLILFRYIQGKDVFEAFYKQDLSKRLLLDKSTSIDAEKSMISKLKTECGTTFTAKLEEMFKDIELSNDIMNSFRDSPMTQNFKSIEMNIYVLTSGNWPIQPPIEATLPKEFLEYQEVFNKFYLSKHNGKTLKWQNALSYCVLKANFIQGKKELSVSLFQTIILYLFNDVIDGGELSFRDIQANTGLAIPELKKNLLSLCSSKSDILIQKKSSTSSNTSSNTSSNTSSSASGSASGGASGGATKTKVIDETDTFLFNSKFSSKLFKIKVNSIQIQETVEENQKTNENIISDRQYQVDAAIVRIMKTRKTLAHNLLISELVSLLKFQPKPVDLKKRIEILIEKEYLCRDPENAMIYNYMA
Protein: LicD/FKTN/FKRP nucleotidyltransferase domain-containing protein (A0A1D8PGW8)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004167}; Single-pass membrane protein {ECO:0000256|ARBA:ARBA00004167}.
Interaction partners:
Sequence:
MPRLKRALLSPKLFVKSILLFTIVYTIYLSTSTTTSVYLSTTQSKLNIYTNQLYQKINLQFNQWYYNILVYDYNLFSDSNFQQQLTIIKSEKLQDENHKIDLWNLDDSFNLPVSVKVPNYLLSPSSSSSSSTDKKPLIQPFDPRLTLSVYYNYIETNKDNGNDLKLPFHWSDWVDFSKLHKYILNPSKTDLCSSLFDISNNDKLNKDSEIKSVDQYCQFIGNANNGNENKATNMLGYKIFAPAQAQTGANHELIGKSYLYTQAPSPKRLIFLTNTNGNYQFDVDNYNVNNISNSILYNEKLTSNLASKVNKENEQSSTLNVLSSYISLIKNSPPSLLPTKQQNNPKDNEIDSHIIEIPEEYFINDPQSIINQLESSNSQLSNSEKDFLSSIKYSVDCKDPPKYFYEAKYVKAMKENWSGEHYDWRFYNGLTIHNAQQQSIILHRLLKNYLKFTQSNNLITWIAHGSLLSWYWNGINFPWDTDIDVQMPIHELYQLARFYNQSLVVENAGTKRLGNSDKTEEFEFDGMGRYFIDVGSSVTHRTKGNGNNNIDARFIDIDTGLYIDITGLALTNEESPDRYNDFLTIDQNTDAGKQKFDQLKQNQKDGDKNNNYSLKNQQLKLYNCRNNHFSSYNELSPLIQTVVENQPGYIPKNFMYILNDEYNLKSLAKKNHRDFTYFNNFNLWLNTKDVSKYLAHKHSPNENSPDGSNQAYSLIKFNKLSKSDHINLLKYNPIMMKEYLETMNFTNYHNLELSQLLKISNYNHNHNNAQTNVSNIGIYRESYDLFNHYRNNYKLGYSLRPDHFINFIIHDNSRWDYQLQVDDLIKLQKQLENDSQQQQEQHHEQQQG
Protein: Succinate dehydrogenase assembly factor 4, mitochondrial (SDH assembly factor 4) (SDHAF4) (Q8BTE0)
Organism: Mus musculus (Mouse)
Function: Plays an essential role in the assembly of succinate dehydrogenase (SDH), an enzyme complex (also referred to as respiratory complex II) that is a component of both the tricarboxylic acid (TCA) cycle and the mitochondrial electron transport chain, and which couples the oxidation of succinate to fumarate with the reduction of ubiquinone (coenzyme Q) to ubiquinol. Binds to the flavoprotein subunit Sdha in its FAD-bound form, blocking the generation of excess reactive oxigen species (ROS) and facilitating its assembly with the iron-sulfur protein subunit Sdhb into the SDH catalytic dimer (By similarity).
Subcellular location: Mitochondrion matrix {ECO:0000250|UniProtKB:P38345}.
Interaction partners:
- Succinate dehydrogenase assembly factor 3, mitochondrial
- Succinate dehydrogenase assembly factor 2, mitochondrial
- Succinate dehydrogenase flavoprotein subunit, mitochondrial
- Succinate dehydrogenase assembly factor 1, mitochondrial
- Cytochrome c oxidase assembly factor 4 homolog, mitochondrial
Sequence:
MVSTTLSVSRMTFVWRAARPSLLNHSLRKMSYQEGKPEPAKQALKKSKLPLGRFDSLEDSPEEREPLQKFPDDVNPVTKEKGGPKGPEPTRYGDWERKGRCIDF