wanglab/gogpt-training-data huggingface dataset:
Protein: Elastin (Tropoelastin) (Q99372)
Organism: Rattus norvegicus (Rat)
Function: Major structural protein of tissues such as aorta and nuchal ligament, which must expand rapidly and recover completely. Molecular determinant of the late arterial morphogenesis, stabilizing arterial structure by regulating proliferation and organization of vascular smooth muscle (By similarity).
Subcellular location: Secreted, extracellular space, extracellular matrix {ECO:0000250|UniProtKB:P15502}. Note=Extracellular matrix of elastic fibers. {ECO:0000250|UniProtKB:P15502}.
Interaction partners:
- Fibronectin
- Protein-lysine 6-oxidase
- Fibulin-5
Sequence:
MAGLTAAVPQPGVLLILLLNLLHPAQPGGVPGAVPGGVPGGLPGGVPGGVYYPGAGIGGGLGGGALGPGGKPPKPGAGLLGAFGAGPGGLGGAGPGAGLSYASRPGGVLVPGGGAGAAAAYKAAAKAGAGLGGIGGVPGGVGVGGVPGAVGVGGVPGAVGGIGGIGGLGVSTGAVVPQLGAGVGAGGKPGKVPGVGLPGVYPGGVLPGTGARFPGVGVLPGVPTGTGVKAKVPGGGGGAFSGIPGVGPFGGQQPGVPLGYPIKAPKLPGGYGLPYTNGKLPYGVAGAGGKAGYPTGTGVGSQAAVAAAKAAKYAGAGGGGVLPGVGGGGIPGGAGAIPGIGGITGAGTPAAAAAAKAAAKAAKYGAAGGLVPGGPGVRVPGAGIPGVGIPGVGGIPGVGGIPGVGGIPGVGGPGIGGPGIVGGPGAVSPAAAAKAAAKAAKYGARGGVGIPTYGVGAGGFPGYGVGAGAGLGGASQAAAAAAAAKAAKYGAGGAGTLGGLVPGAVPGALPGAVPGALPGAVPGALPGAVPGVPGTGGVPGAGTPAAAAAAAAAKAAAKAGQYGLGPGVGGVPGGVGVGGLPGGVGPGGVTGIGTGPGTGLVPGDLGGAGTPAAAKSAAKAAAKAQYRAAAGLGAGVPGLGVGAGVPGFGAGAGGFGAGAGVPGFGAGAVPGSLAASKAAKYGAAGGLGGPGGLGGPGGLGGPGGFGGPGGLGGVPGGVAGGAPAAAAAAKAAAKAAQYGLGGAGGLGAGGLGAGGLGAGGLGAGGLGAGGLGAGGVIPGAVGLGGVSPAAAAKAAKYGAAGLGGVLGARPFPGGGVAARPGFGLSPIYPGGGAGGLGVGGKPPKPYGGALGALGYQGGGCFGKSCGRKRK
Protein: TBP-associated factor 3 (Q9V4D4)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- Transcription initiation factor TFIID subunit 13
- Transcription initiation factor TFIID subunit 1
- Transcription initiation factor TFIID subunit 11
- Transcription initiation factor TFIID subunit 2
- Transcription initiation factor TFIID subunit 10
- Transcription initiation factor TFIID subunit 6
- Transcription initiation factor TFIID subunit 12
- Transcription initiation factor TFIID subunit 5
- Transcription initiation factor TFIID subunit 7
- Transcription initiation factor TFIID subunit 8
Sequence:
MMADRYASDLALVVVAQITQTIGYSCTLSAPLELLQDILQKFVQEFARDMHRHMEHANRIEPNLKDARLSIKNLSINVQELLDYIGNVEPVGFIRDVPQFPIGKSVNMNFLKPGSAETLTRPVYIFEYLPPMQDPELREIPADVQKEFSEKQEFCSKAEYSSTNAADKLGAKHIDSISPNTVINFRSNAFELDVGSSVREMSSVVMTTGGFISPAIEGKLPEDIIPDIVEKFLGLDAPFSPTIIVNSLQKSPQLALSDRDKTVNPRKIIPSETKIFKQNAALLTSGHSESSIIYASNNHTMLTVTTPKKNRKQKHDLICEPGQSELLTNPFEKAQEKSQRKALKMYKQTSKNQRDSSINQIQNMKKLKKKFNRGSFDPNKKHLEKIFKKQSKLKQNDLQLDIDEKHFLQNSQTTSGLAIKANSNENALQADIPSQPPTVTSQIENNFRNSIYPVQPSVIQQTQVLLAEKKSGSEPERSKLDIFKKISKPRTPRPDIGATLVPPGTGVSVFGSTMTPSALISLPSGTTITPTPSLGLNSENKNVPSMKINPCNIFDGTIPLTKAGVEMSIIDSPKPKKRGRKPGGKNVIKQTNVVSQPLINKVERKKSSQAITLPLSSSPMIITQSSLNVSPPTEPLNLCNTEQPSNNFLSNLYAKEKKDRKKYKSLPENVMQLDKSCSPEKASTLHNSIRPTKQNNDVQCSDKFVTISNALSNASIYPGIQTGMVPLLPLLQFPPRPGLIPTGPGLFPAVTGLVGFGNHGNRIPISPFIDYPGPEESVADTVRCPPIKDSPVTDSDQFLSRSSTQTDLQMDRNYCNVAPLVPDSMKFAECKSVSCASTILENPSAQATSKINTKPLLEASGNPDDPIEVSDDSDESMHNRQMVQRKTPISSPTYVKTSFAELNPSSFTSAASNGEEKSKMDLRNIVSLSSNEPLKKFKKLVKQSFPDVKSVPHTPASHSSFPQFNLPNFMGGDKFSLAGGADLIPLSRVSDSEYSSKIVPFSSLGGTIPNQIKISEEHNIFSTFSNYEDITITPTGLTSLEPKMRKHHKKLKKVKEGKNKKKKEKKDKSKKADQIGLPSFKSDRKIKANDKRQKKEKKKDKDKQILVHIPDDTEEFDKVPLANNDEPVLKSSSMTINPSLGAATSGISPNQIPKLTLKLSGKSTLFSSSEKEMTDAGKLKQTTILSSENKKRERDNSPELARFSPLVTGPPKNKQSETLHLGNSSTAVLPVPSPVAVRAVQLPVSQTSSNSAGWLSNPNNSNTASSTLSASSVLLPQQLMLAPHTIMNNFVPAMCNSTGTVSKSGLCSSPPNTSEENANAMQIAESSRPSSYVDAEGNRIWICPACGKVDDGSAMIGCDGCDAWYHWICVGITFAPKDNDDWFCRVCVTKKRIHGSEKKKRRNKKK
Protein: Carnitine O-palmitoyltransferase 1, liver isoform (CPT1-L) (EC 2.3.1.21) (Carnitine O-palmitoyltransferase I, liver isoform) (CPT I) (CPTI-L) (Carnitine palmitoyltransferase 1A) (Succinyltransferase CPT1A) (EC 2.3.1.-) (P32198)
Organism: Rattus norvegicus (Rat)
Function: Catalyzes the transfer of the acyl group of long-chain fatty acid-CoA conjugates onto carnitine, an essential step for the mitochondrial uptake of long-chain fatty acids and their subsequent beta-oxidation in the mitochondrion. Plays an important role in hepatic triglyceride metabolism.
Subcellular location: Mitochondrion outer membrane {ECO:0000269|PubMed:16908527, ECO:0000269|PubMed:18192268, ECO:0000269|PubMed:19136561, ECO:0000269|PubMed:21622568}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Long-chain-fatty-acid--CoA ligase 1
- Carnitine O-palmitoyltransferase 2, mitochondrial
- Fatty acid CoA ligase Acsl3
- Long-chain-fatty-acid--CoA ligase 5
- Long-chain-fatty-acid--CoA ligase 4
- Long-chain-fatty-acid--CoA ligase 6
- Carnitine O-palmitoyltransferase 1, muscle isoform
- Palmitoyl thioesterase CPT1C
- Peroxisome proliferator-activated receptor alpha
- Peroxisomal acyl-coenzyme A oxidase 1
Sequence:
MAEAHQAVAFQFTVTPDGIDLRLSHEALKQICLSGLHSWKKKFIRFKNGIITGVFPANPSSWLIVVVGVISSMHAKVDPSLGMIAKISRTLDTTGRMSSQTKNIVSGVLFGTGLWVAVIMTMRYSLKVLLSYHGWMFAEHGKMSRSTKIWMAMVKVLSGRKPMLYSFQTSLPRLPVPAVKDTVSRYLESVRPLMKEEDFQRMTALAQDFAVNLGPKLQWYLKLKSWWATNYVSDWWEEYIYLRGRGPLMVNSNYYAMEMLYITPTHIQAARAGNTIHAILLYRRTLDREELKPIRLLGSTIPLCSAQWERLFNTSRIPGEETDTIQHIKDSRHIVVYHRGRYFKVWLYHDGRLLRPRELEQQMQQILDDPSEPQPGEAKLAALTAADRVPWAKCRQTYFARGKNKQSLDAVEKAAFFVTLDESEQGYREEDPEASIDSYAKSLLHGRCFDRWFDKSITFVVFKNSKIGINAEHSWADAPVVGHLWEYVMATDVFQLGYSEDGHCKGDTNPNIPKPTRLQWDIPGECQEVIDASLSSASLLANDVDLHSFPFDSFGKGLIKKCRTSPDAFIQLALQLAHYKDMGKFCLTYEASMTRLFREGRTETVRSCTMESCNFVQAMMDPKSTAEQRLKLFKIACEKHQHLYRLAMTGAGIDRHLFCLYVVSKYLAVDSPFLKEVLSEPWRLSTSQTPQQQVELFDFEKNPDYVSCGGGFGPVADDGYGVSYIIVGENFIHFHISSKFSSPETDSHRFGKHLRQAMMDIITLFGLTINSKK
Protein: Glycerol dehydrogenase (GDH) (GLDH) (EC 1.1.1.6) ((R)-aminopropanol dehydrogenase) (EC 1.1.1.75) (1,2-propanediol dehydrogenase) (D-1-amino-2-propanol oxidoreductase) (P0A9S5)
Organism: Escherichia coli (strain K12)
Function: Catalyzes the NAD-dependent oxidation of glycerol to dihydroxyacetone (glycerone). Allows microorganisms to utilize glycerol as a source of carbon under anaerobic conditions. In E.coli, an important role of GldA is also likely to regulate the intracellular level of dihydroxyacetone by catalyzing the reverse reaction, i.e. the conversion of dihydroxyacetone into glycerol. Possesses a broad substrate specificity, since it is also able to oxidize 1,2-propanediol and several of its analogs, DL-2,3-butanediol and D-1-amino-2-propanol, and to reduce dihydroxyacetone, hydroxyacetone, glycolaldehyde and methylglyoxal into glycerol, 1,2-propanediol, ethylene glycol and lactaldehyde, respectively.
Interaction partners:
- Methylglyoxal synthase
- Glycerol kinase
- Lactaldehyde reductase
- NADPH-dependent aldehyde reductase YqhD
- PEP-dependent dihydroxyacetone kinase, phosphoryl donor subunit DhaM
- PEP-dependent dihydroxyacetone kinase, ADP-binding subunit DhaL
- PEP-dependent dihydroxyacetone kinase, dihydroxyacetone-binding subunit DhaK
- Aldehyde reductase YahK
- NADH-specific methylglyoxal reductase
- Bifunctional aldehyde-alcohol dehydrogenase AdhE
Sequence:
MDRIIQSPGKYIQGADVINRLGEYLKPLAERWLVVGDKFVLGFAQSTVEKSFKDAGLVVEIAPFGGECSQNEIDRLRGIAETAQCGAILGIGGGKTLDTAKALAHFMGVPVAIAPTIASTDAPCSALSVIYTDEGEFDRYLLLPNNPNMVIVDTKIVAGAPARLLAAGIGDALATWFEARACSRSGATTMAGGKCTQAALALAELCYNTLLEEGEKAMLAAEQHVVTPALERVIEANTYLSGVGFESGGLAAAHAVHNGLTAIPDAHHYYHGEKVAFGTLTQLVLENAPVEEIETVAALSHAVGLPITLAQLDIKEDVPAKMRIVAEAACAEGETIHNMPGGATPDQVYAALLVADQYGQRFLQEWE
Protein: Centrosomal protein of 164 kDa (Cep164) (Q9UPV0)
Organism: Homo sapiens (Human)
Function: Plays a role in microtubule organization and/or maintenance for the formation of primary cilia (PC), a microtubule-based structure that protrudes from the surface of epithelial cells. Plays a critical role in G2/M checkpoint and nuclear divisions. A key player in the DNA damage-activated ATR/ATM signaling cascade since it is required for the proper phosphorylation of H2AX, RPA, CHEK2 and CHEK1. Plays a critical role in chromosome segregation, acting as a mediator required for the maintenance of genomic stability through modulation of MDC1, RPA and CHEK1.
Subcellular location: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole {ECO:0000269|PubMed:26337392}. Nucleus. Note=Localizes specifically to very distally located appendage structures on the mature centriole from which initiate PC formation (PubMed:26337392). Persisted at centrioles throughout mitosis. Expressed in chromatin-enriched nuclear fraction of HeLa cells. In response to DNA damage, it translocates to nuclear foci that contain the DNA damage response proteins KAT5/TIP60 and CHEK1. {ECO:0000269|PubMed:26337392}.
Interaction partners:
- Centrosomal protein of 83 kDa
- Sodium channel and clathrin linker 1
- Tau-tubulin kinase 2
- Fas-binding factor 1
- Centrosomal protein of 89 kDa
- Ninein
- Rab-3A-interacting protein
- Serine/threonine-protein kinase PLK1
- Ras-related protein Rab-8A
- ADP-ribosylation factor-like protein 13B
Sequence:
MAGRPLRIGDQLVLEEDYDETYIPSEQEILEFAREIGIDPIKEPELMWLAREGIVAPLPGEWKPCQDITGDIYYFNFANGQSMWDHPCDEHYRSLVIQERAKLSTSGAIKKKKKKKEKKDKKDRDPPKSSLALGSSLAPVHVPLGGLAPLRGLVDTPPSALRGSQSVSLGSSVESGRQLGELMLPSQGLKTSAYTKGLLGSIYEDKTALSLLGLGEETNEEDEEESDNQSVHSSSEPLRNLHLDIGALGGDFEYEESLRTSQPEEKKDVSLDSDAAGPPTPCKPSSPGADSSLSSAVGKGRQGSGARPGLPEKEENEKSEPKICRNLVTPKADPTGSEPAKASEKEAPEDTVDAGEEGSRREEAAKEPKKKASALEEGSSDASQELEISEHMKEPQLSDSIASDPKSFHGLDFGFRSRISEHLLDVDVLSPVLGGACRQAQQPLGIEDKDDSQSSQDELQSKQSKGLEERLSPPLPHEERAQSPPRSLATEEEPPQGPEGQPEWKEAEELGEDSAASLSLQLSLQREQAPSPPAACEKGKEQHSQAEELGPGQEEAEDPEEKVAVSPTPPVSPEVRSTEPVAPPEQLSEAALKAMEEAVAQVLEQDQRHLLESKQEKMQQLREKLCQEEEEEILRLHQQKEQSLSSLRERLQKAIEEEEARMREEESQRLSWLRAQVQSSTQADEDQIRAEQEASLQKLREELESQQKAERASLEQKNRQMLEQLKEEIEASEKSEQAALNAAKEKALQQLREQLEGERKEAVATLEKEHSAELERLCSSLEAKHREVVSSLQKKIQEAQQKEEAQLQKCLGQVEHRVHQKSYHVAGYEHELSSLLREKRQEVEGEHERRLDKMKEEHQQVMAKAREQYEAEERKQRAELLGHLTGELERLQRAHERELETVRQEQHKRLEDLRRRHREQERKLQDLELDLETRAKDVKARLALLEVQEETARREKQQLLDVQRQVALKSEEATATHQQLEEAQKEHTHLLQSNQQLREILDELQARKLKLESQVDLLQAQSQQLQKHFSSLEAEAQKKQHLLREVTVEENNASPHFEPDLHIEDLRKSLGTNQTKEVSSSLSQSKEDLYLDSLSSHNVWHLLSAEGVALRSAKEFLVQQTRSMRRRQTALKAAQQHWRHELASAQEVAKDPPGIKALEDMRKNLEKETRHLDEMKSAMRKGHNLLKKKEEKLNQLESSLWEEASDEGTLGGSPTKKAVTFDLSDMDSLSSESSESFSPPHREWWRQQRIDSTPSLTSRKIHGLSHSLRQISSQLSSVLSILDSLNPQSPPPLLASMPAQLPPRDPKSTPTPTYYGSLARFSALSSATPTSTQWAWDSGQGPRLPSSVAQTVDDFLLEKWRKYFPSGIPLLSNSPTPLESRLGYMSASEQLRLLQHSHSQVPEAGSTTFQGIIEANRRWLERVKNDPRLPLFSSTPKPKATLSLLQLGLDEHNRVKVYRF
Protein: Peptidyl-prolyl cis-trans isomerase FKBP42 (PPIase FKBP42) (EC 5.2.1.8) (42 kDa peptidyl-prolyl isomerase) (FK506-binding protein 42) (AtFKBP42) (Immunophilin FKBP42) (Protein TWISTED DWARF 1) (Protein ULTRACURVATA 2) (Rotamase) (Q9LDC0)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides (By similarity). Modulates the uptake of MRP substrates into the vacuole; reduces metolachlor-GS (MOC-GS) and enhances 17-beta-estradiol 17-(beta-D-glucuronide) (E(2)17betaG) uptake. Regulates cell elongation and orientation. Functions as a positive regulator of PGP1-mediated auxin transport. Confers drug modulation of PGP1 efflux activity as interaction with NPA or flavonol quercetin prevents its physical and functional interaction with PGP1. Required for the proper localization of auxin-related ABCB transporters. Plays a role in brassinosteroid (BR) signaling pathway.
Subcellular location: Cell membrane {ECO:0000269|PubMed:12410806, ECO:0000269|PubMed:14517332, ECO:0000269|PubMed:15133126}; Single-pass type IV membrane protein. Vacuole membrane {ECO:0000269|PubMed:12410806, ECO:0000269|PubMed:15133126}; Single-pass type IV membrane protein. Endoplasmic reticulum {ECO:0000269|PubMed:20971896}.
Interaction partners:
- ABC transporter B family member 1
- ABC transporter B family member 19
- Co-chaperone protein p23-2
- Co-chaperone protein p23-1
- Peptidyl-prolyl cis-trans isomerase Pin1
- ABC transporter B family member 4
- Peptidyl-prolyl cis-trans isomerase FKBP13, chloroplastic
- Peptidyl-prolyl cis-trans isomerase FKBP20-1
- Serine/threonine-protein kinase D6PK
- Heat shock protein 90-1
Sequence:
MDESLEHQTQTHDQESEIVTEGSAVVHSEPSQEGNVPPKVDSEAEVLDEKVSKQIIKEGHGSKPSKYSTCFLHYRAWTKNSQHKFEDTWHEQQPIELVLGKEKKELAGLAIGVASMKSGERALVHVGWELAYGKEGNFSFPNVPPMADLLYEVEVIGFDETKEGKARSDMTVEERIGAADRRKMDGNSLFKEEKLEEAMQQYEMAIAYMGDDFMFQLYGKYQDMALAVKNPCHLNIAACLIKLKRYDEAIGHCNIVLTEEEKNPKALFRRGKAKAELGQMDSARDDFRKAQKYAPDDKAIRRELRALAEQEKALYQKQKEMYKGIFKGKDEGGAKSKSLFWLIVLWQWFVSLFSRIFRRHRVKAD
Protein: Plant intracellular Ras-group-related LRR protein 5 (Q5G5E0)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Leucine-rich repeat protein that likely mediates protein interactions, possibly in the context of signal transduction.
Interaction partners:
- AT3g47210/F13I12_260
- F-box protein At3g17710
- Immune-associated nucleotide-binding protein 4
- Serine/threonine-protein phosphatase PP1 isozyme 8
- non-specific serine/threonine protein kinase
- Zinc finger CCCH domain-containing protein 26
- Polyadenylate-binding protein 3
- Aldehyde oxidase GLOX1
- Cytochrome P450, family 721, subfamily A, polypeptide 1
- Shaggy-related protein kinase theta
Sequence:
MDSKEMVVEEIMRIHRSLPLRPEIDDVETATSLIQNVEKEDRNRLEAIDKLVKTSSSEVPLELFNVFKEMKKSLVRFQSTEQTREATKILDLESVHVVFDELIQRASFCIASPNSTTALPRSVPVPAPVVSSDEIPFKSKEIISRDDTFVKKAKSSFYSDGLLAPSKPQVLDSTLHQAKNVAGNDGEKLSLIKLASLIEVSAKKATQELNLQHRLMDQLEWLPDSLGKLSSLVRLDLSENCIMVLPATIGGLISLTRLDLHSNRIGQLPESIGDLLNLVNLNLSGNQLSSLPSSFNRLIHLEELDLSSNSLSILPESIGSLVSLKKLDVETNNIEEIPHSISGCSSMEELRADYNRLKALPEAVGKLSTLEILTVRYNNIRQLPTTMSSMANLKELDVSFNELESVPESLCYAKTLVKLNIGNNFANLRSLPGLIGNLEKLEELDMSNNQIRFLPYSFKTLSNLRVLQTEQNPLEELPRDITEKGAQAVVQYMNDLVEARNTKSQRTKPKKSWVNSICFFCKSSTN
Protein: UDP-galactopyranose mutase (UGM) (EC 5.4.99.9) (UDP-GALP mutase) (Uridine 5-diphosphate galactopyranose mutase) (P9WIQ1)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: Catalyzes the interconversion through a 2-keto intermediate of uridine diphosphogalactopyranose (UDP-GalP) into uridine diphosphogalactofuranose (UDP-GalF) which is a key building block for cell wall construction in Mycobacterium tuberculosis.
Interaction partners:
- Galactofuranosyltransferase GlfT2
- Possible dTDP-glucose 4,6-dehydratase
- Uncharacterized protein Rv0501
- UDP-glucose 4-epimerase
- Galactofuranosyltransferase GlfT1
- dTDP-4-dehydrorhamnose 3,5-epimerase
- Glucose-1-phosphate thymidylyltransferase
- Galactose-1-phosphate uridylyltransferase
- Probable O-antigen/lipopolysaccharide transport integral membrane protein ABC transporter RfbD
- Uncharacterized protein Rv1510
Sequence:
MQPMTARFDLFVVGSGFFGLTIAERVATQLDKRVLVLERRPHIGGNAYSEAEPQTGIEVHKYGAHLFHTSNKRVWDYVRQFTDFTDYRHRVFAMHNGQAYQFPMGLGLVSQFFGKYFTPEQARQLIAEQAAEIDTADAQNLEEKAISLIGRPLYEAFVKGYTAKQWQTDPKELPAANITRLPVRYTFDNRYFSDTYEGLPTDGYTAWLQNMAADHRIEVRLNTDWFDVRGQLRPGSPAAPVVYTGPLDRYFDYAEGRLGWRTLDFEVEVLPIGDFQGTAVMNYNDLDVPYTRIHEFRHFHPERDYPTDKTVIMREYSRFAEDDDEPYYPINTEADRALLATYRARAKSETASSKVLFGGRLGTYQYLDMHMAIASALNMYDNVLAPHLRDGVPLLQDGA
Protein: Peptidyl-prolyl cis-trans isomerase (EC 5.2.1.8) (Q59KZ2)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Interaction partners:
- 1-phosphatidylinositol-4-phosphate 5-kinase
- DNA-directed RNA polymerase subunit
- Large ribosomal subunit protein uL14m
- GSKIP domain-containing protein
- Multifunctional tryptophan biosynthesis protein
- rRNA adenine N
Sequence:
MASTSTGLPPNWTIRVSRSHNKEYFLNQSTNESSWDPPYGTDKEVLNAYIAKFKNNGYKPLVNEDGQVRVSHLLIKNNQSRKPKSWKSPDGISRTRDESIQILKKHLERILSGEVKLSELANTESDCSSHDRGGDLGFFSKGQMQPPFEEAAFNLHVGEVSNIIETNSGVHILQRTG
Protein: UV excision repair protein RAD23 homolog A (HR23A) (mHR23A) (P54726)
Organism: Mus musculus (Mouse)
Function: Multiubiquitin chain receptor involved in modulation of proteasomal degradation. Binds to 'Lys-48'-linked polyubiquitin chains in a length-dependent manner and with a lower affinity to 'Lys-63'-linked polyubiquitin chains. Proposed to be capable to bind simultaneously to the 26S proteasome and to polyubiquitinated substrates and to deliver ubiquitinated proteins to the proteasome (By similarity).
Subcellular location: Nucleus {ECO:0000250}.
Interaction partners:
- DNA repair protein complementing XP-C cells homolog
- 26S proteasome non-ATPase regulatory subunit 4
- Centrin-2
- Ataxin-3
- UV excision repair protein RAD23 homolog B
- Ubiquitin-ribosomal protein eS31 fusion protein
- Polyubiquitin-B
- Ubiquitin-ribosomal protein eL40 fusion protein
- 26S proteasome non-ATPase regulatory subunit 2
- Peptide-N
Sequence:
MAVTITLKTLQQQTFKIRMEPDETVKVLKEKIEAEKGRDAFPVAGQKLIYAGKILSDDVPIKEYHIDEKNFVVVMVTKAKAGQGIPAPPEASPTAVPEPSTPFPPVLASGMSHPPPTSREDKSPSEESTTTTSPESISGSVPSSGSSGREEDAASTLVTGSEYETMLTEIMSMGYERERVVAALRASYNNPHRAVEYLLTGIPGSPEPEHGSVQESQAPEQPATEAAGENPLEFLRDQPQFQNMRQVIQQNPALLPALLQQLGQENPQLLQQISRHQEQFIQMLNEPPGELADISDVEGEVGAIGEEAPQMNYIQVTPQEKEAIERLKALGFPESLVIQAYFACEKNENLAANFLLSQNFDDE
Protein: Signal peptidase I (SPase I) (EC 3.4.21.89) (Leader peptidase I) (P00803)
Organism: Escherichia coli (strain K12)
Subcellular location: Cell inner membrane {ECO:0000269|PubMed:21778229}; Multi-pass membrane protein {ECO:0000269|PubMed:21778229}.
Interaction partners:
- Elongation factor 4
- Ribonuclease 3
- Membrane protein insertase YidC
- Protein translocase subunit SecY
- Lipoprotein signal peptidase
- Outer membrane protein A
- Protein translocase subunit SecA
- Prepilin leader peptidase/N-methyltransferase
- Elongation factor Tu 1
- Elongation factor Tu 2
Sequence:
MANMFALILVIATLVTGILWCVDKFFFAPKRRERQAAAQAAAGDSLDKATLKKVAPKPGWLETGASVFPVLAIVLIVRSFIYEPFQIPSGSMMPTLLIGDFILVEKFAYGIKDPIYQKTLIETGHPKRGDIVVFKYPEDPKLDYIKRAVGLPGDKVTYDPVSKELTIQPGCSSGQACENALPVTYSNVEPSDFVQTFSRRNGGEATSGFFEVPKNETKENGIRLSERKETLGDVTHRILTVPIAQDQVGMYYQQPGQQLATWIVPPGQYFMMGDNRDNSADSRYWGFVPEANLVGRATAIWMSFDKQEGEWPTGLRLSRIGGIH
Protein: Cytochrome c isoform 2 (Iso-2-cytochrome c) (Cytochrome c hypoxic isoform) (P00045)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Electron carrier protein. The oxidized form of the cytochrome c heme group can accept an electron from the heme group of the cytochrome c1 subunit of ubiquinol-cytochrome c oxidoreductase. Cytochrome c then transfers this electron to the dinuclear copper A center (CU(A)) of the COX2 subunit of cytochrome oxidase, the final protein carrier in the mitochondrial electron-transport chain. Isoform 2 (CYC7) is the predominant cytochrome c under anaerobic/hypoxic conditions.
Subcellular location: Mitochondrion intermembrane space {ECO:0000269|PubMed:22984289, ECO:0000269|PubMed:8636074}.
Interaction partners:
- Cytochrome c1, heme protein, mitochondrial
- Cytochrome b-c1 complex subunit Rieske, mitochondrial
- Cytochrome b
- Cytochrome b-c1 complex subunit 7, mitochondrial
- Holocytochrome-c synthase
- Cytochrome b-c1 complex subunit 8, mitochondrial
- Cytochrome b-c1 complex subunit 9, mitochondrial
- Cytochrome b-c1 complex subunit 1, mitochondrial
- Cytochrome b-c1 complex subunit 2, mitochondrial
- Cytochrome c oxidase subunit 5B, mitochondrial
Sequence:
MAKESTGFKPGSAKKGATLFKTRCQQCHTIEEGGPNKVGPNLHGIFGRHSGQVKGYSYTDANINKNVKWDEDSMSEYLTNPKKYIPGTKMAFAGLKKEKDRNDLITYMTKAAK
Protein: Ethanolamine ammonia-lyase small subunit (EAL small subunit) (EC 4.3.1.7) (Ethanolamine ammonia-lyase beta subunit) (P19265)
Organism: Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Function: Catalyzes the deamination of various vicinal amino-alcohols to oxo compounds (Probable). It is spontaneously inactivated by its substrate and reactivated by EutA (By similarity). May play a role in bacterial microcompartment (BMC) assembly or maintenance (Probable). Directly targeted to the BMC.
Subcellular location: Bacterial microcompartment {ECO:0000255|HAMAP-Rule:MF_00601, ECO:0000269|PubMed:22428024, ECO:0000269|PubMed:27063436, ECO:0000269|PubMed:27450681}. Note=Probably located inside the BMC (Probable). Has been suggested to be on the BMC exterior. {ECO:0000269|PubMed:23585538, ECO:0000305|PubMed:22428024, ECO:0000305|PubMed:23585538, ECO:0000305|PubMed:27063436, ECO:0000305|PubMed:27450681}.
Interaction partners:
- Ethanolamine ammonia-lyase large subunit
- Ethanolamine ammonia-lyase reactivase EutA
- Probable ethanolamine permease EutH
- Bacterial microcompartment shell protein EutL
- Acetate kinase EutQ
- Acetaldehyde dehydrogenase
- Bacterial microcompartment shell protein EutS
- Corrinoid adenosyltransferase EutT
- Bacterial microcompartment shell protein EutK
- HTH-type DNA-binding transcriptional activator EutR
Sequence:
MDQKQIEEIVRSVMASMGQDVPQPAAPSTQEGAKPQCAAPTVTESCALDLGSAEAKAWIGVENPHRADVLTELRRSTAARVCTGRAGPRPRTQALLRFLADHSRSKDTVLKEVPEEWVKAQGLLEVRSEISDKNLYLTRPDMGRRLSPEAIDALKSQCVMNPDVQVVVSDGLSTDAITANYEEILPPLLAGLKQAGLNVGTPFFVRYGRVKIEDQIGEILGAKVVILLVGERPGLGQSESLSCYAVYSPRVATTVEADRTCISNIHQGGTPPVEAAAVIVDLAKRMLEQKASGINMTR
Protein: Protein JTB (Jumping translocation breakpoint protein) (Prostate androgen-regulated protein) (PAR protein) (O76095)
Organism: Homo sapiens (Human)
Function: Required for normal cytokinesis during mitosis. Plays a role in the regulation of cell proliferation. May be a component of the chromosomal passenger complex (CPC), a complex that acts as a key regulator of mitosis. The CPC complex has essential functions at the centromere in ensuring correct chromosome alignment and segregation and is required for chromatin-induced microtubule stabilization and spindle assembly. Increases AURKB activity. Inhibits apoptosis induced by TGFB1 (By similarity). Overexpression induces swelling of mitochondria and reduces mitochondrial membrane potential (By similarity).
Subcellular location: Membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. Mitochondrion {ECO:0000250}. Cytoplasm. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome. Cytoplasm, cytoskeleton, spindle. Note=Detected at the centrosome and along spindle fibers during prophase and metaphase. Detected at the midbody during telophase.
Interaction partners:
Sequence:
MLAGAGRPGLPQGRHLCWLLCAFTLKLCQAEAPVQEEKLSASTSNLPCWLVEEFVVAEECSPCSNFRAKTTPECGPTGYVEKITCSSSKRNEFKSCRSALMEQRLFWKFEGAVVCVALIFACLVIIRQRQLDRKALEKVRKQIESI
Protein: NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 13 (Q8VXK6)
Organism: Gossypium hirsutum (Upland cotton) (Gossypium mexicanum)
Subcellular location: Mitochondrion inner membrane {ECO:0000256|ARBA:ARBA00004298, ECO:0000256|RuleBase:RU368034}; Single-pass membrane protein {ECO:0000256|ARBA:ARBA00004298, ECO:0000256|RuleBase:RU368034}; Matrix side {ECO:0000256|ARBA:ARBA00004298, ECO:0000256|RuleBase:RU368034}.
Interaction partners:
Sequence:
MTEAVIREKPGMASVKDMPLLQDGPPPGGFAPVRYARRIPNKGPSAMAIFLAAFGAFSYGMYQIGQGNKIRRALKEEKFAARRAVLPVLQAEEDERFVKEWRKYLEYEAEVMKDVPGWKVGENVYNSGRWMPPATGELRLKFGDTFFF
Protein: Casein kinase II subunit alpha (CK II subunit alpha) (EC 2.7.11.1) (P40231)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Catalytic subunit of a constitutively active serine/threonine-protein kinase complex that phosphorylates a large number of substrates containing acidic residues C-terminal to the phosphorylated serine or threonine.
Interaction partners:
- Casein kinase II subunit beta
- Casein kinase II subunit beta-2
- Ribosomal RNA-processing protein 7
- U3 small nucleolar RNA-associated protein 22
- FACT complex subunit pob3
- FACT complex subunit spt16
- U3 small nucleolar ribonucleoprotein protein imp3
- Probable U3 small nucleolar RNA-associated protein 18
- rRNA biogenesis protein rrp36
- Pre-rRNA-processing protein esf1
Sequence:
MNQTEAAPVVSVSRVYAHVNEEMPREYWDYENMQEVFGYQDNYEIIRKVGRGKYSEVFEGLNVLNNSKCIIKVLKPVKYKKIKREIKILQNLAGGPNIISLLDIVRDPESKTPSLIFEFVDNIDFRTLYPTLSDYDIRYYSYELLKALDFCHSRGIMHRDVKPHNVMIDHKKRKLRLIDWGLAEFYHAGMEYNVRVASRYFKGPELLVDFREYDYSLDIWSFGVMFAALIFKKDTFFRGRDNYDQLVKIAKVLGTDELFAYVQKYQIVLDRQYDNILGQYPKRDWYSFVNRDNRSLANDEAIDLLNRLLRYDHQERLTCQEAMAHPYFQVLK