wanglab/gogpt-training-data huggingface dataset:
Protein: Ethylene-responsive transcription factor ERF034 (Q8LBQ7)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Probably acts as a transcriptional activator. Binds to the GCC-box pathogenesis-related promoter element. May be involved in the regulation of gene expression by stress factors and by components of stress signal transduction pathways (By similarity).
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- Ankyrin repeat family protein
- AT3g45210/T14D3_150
- Cysteine/Histidine-rich C1 domain family protein
- Probable folate-biopterin transporter 8
- Protein kinase superfamily protein
- Spindle assembly abnormal protein
Sequence:
MARQINIESSVSQVTFISSAIPAVSSSSSITASASLSSSPTTSSSSSSSTNSNFIEEDNSKRKASRRSLSSLVSVEDDDDQNGGGGKRRKTNGGDKHPTYRGVRMRSWGKWVSEIREPRKKSRIWLGTYPTAEMAARAHDVAALAIKGTTAYLNFPKLAGELPRPVTNSPKDIQAAASLAAVNWQDSVNDVSNSEVAEIVEAEPSRAVVAQLFSSDTSTTTTTQSQEYSEASCASTSACTDKDSEEEKLFDLPDLFTDENEMMIRNDAFCYYSSTWQLCGADAGFRLEEPFFLSE
Protein: Syndecan-1 (SYND1) (CD antigen CD138) (P18827)
Organism: Homo sapiens (Human)
Function: Cell surface proteoglycan that bears both heparan sulfate and chondroitin sulfate and that links the cytoskeleton to the interstitial matrix. Regulates exosome biogenesis in concert with SDCBP and PDCD6IP.
Subcellular location: Membrane {ECO:0000255}; Single-pass type I membrane protein {ECO:0000255}. Secreted {ECO:0000269|PubMed:9169435}. Secreted, extracellular exosome {ECO:0000269|PubMed:22660413}. Note=Shedding of the ectodomain produces a soluble form. {ECO:0000269|PubMed:9169435}.
Interaction partners:
- Fibronectin
- Fibroblast growth factor 2
- Syntenin-1
- Glypican-1
- WD repeat-containing protein 82
- Thrombospondin-1
- Set1/Ash2 histone methyltransferase complex subunit ASH2
- Retinoblastoma-binding protein 5
- WD repeat-containing protein 5
- Syndecan-2
Sequence:
MRRAALWLWLCALALSLQPALPQIVATNLPPEDQDGSGDDSDNFSGSGAGALQDITLSQQTPSTWKDTQLLTAIPTSPEPTGLEATAASTSTLPAGEGPKEGEAVVLPEVEPGLTAREQEATPRPRETTQLPTTHLASTTTATTAQEPATSHPHRDMQPGHHETSTPAGPSQADLHTPHTEDGGPSATERAAEDGASSQLPAAEGSGEQDFTFETSGENTAVVAVEPDRRNQSPVDQGATGASQGLLDRKEVLGGVIAGGLVGLIFAVCLVGFMLYRMKKKDEGSYSLEEPKQANGGAYQKPTKQEEFYA
Protein: Pre-rRNA-processing protein TSR2 (20S rRNA accumulation protein 2) (Q06672)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Required for 20S pre-rRNA processing.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:14562095}. Nucleus {ECO:0000269|PubMed:14562095}.
Interaction partners:
- Small ribosomal subunit protein eS26A
- Small ribosomal subunit protein eS26B
- Ribosome assembly protein RRB1
- Ankyrin repeat-containing protein YAR1
- Ribosome biogenesis protein TSR1
- Assembly chaperone of RPL4
- Synchronized import protein 1
- Protein BCP1
- Serine/threonine-protein kinase RIO2
- U3 small nucleolar ribonucleoprotein protein LCP5
Sequence:
MSTQYIDETAFVQAEQGKTNLMFSDEKQQARFELGVSMVIYKWDALDVAVENSWGGPDSAEKRDWITGIVVDLFKNEKVVDAALIEETLLYAMIDEFETNVEDDSALPIAVEVINIYNDCFNLNYNKVEKLYLEWQEKQRTKKSKRVVHIEGDDDEDDEDVEDYDDEDEDEEMDEVVPDLVSSKPEPIVDEDGFELVQPKGRRKH
Protein: Paired box protein Pax-8 (F1Q9Q9)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- Forkhead box E1.
- LIM/homeobox protein Lhx1
- Thyrotropin receptor
- Thyroglobulin.
- Slc5a5 protein
- Forkhead box I1.
- Iodothyronine deiodinase
- Eyes absent homolog
- NK2 homeobox 1a.
- NK2 homeobox 1b.
Sequence:
MSNSTGRGHGGLNQLGGMFVNGRPLPEVIRQRIVDMAHQGVRPCDISRQLRVSHGCVSKILGRYYETGSIKPGVIGGSKPKVATPKVVEKIAEYKRQNPTMFAWEIRDRLLAEGVCDGDTVPSVSSINRIIRTKVQQPFNLPLDTKGLSPGHTLIPSSAVTPPESPQSDSLGSTYSINGLLGITQTTADGKRGHDDSDQESCRHSVDSQGSGGGARKQLRTEHFPSAALDCGFERHYSSDSFSQSKAEQQLYPLALMNPGLDEGKGASSISRNLAAHQGYAVVTEALQPLPLCLKQEVSPEVNSLSPSPHIISGSAFLDLSAISSPSSAPVASSCGSAHLSHGFSSFSHHAPVHGQFSSPSLMAGREVASSMLPGYPPHIPTAQTGFSSSTIAGMVSAPEYTGQSYSHPAYSSYSEAWRFTNSSILGSPYYYSSATRPPPPAAAYDHL
Protein: Lipid droplet-regulating VLDL assembly factor AUP1 (Ancient ubiquitous protein 1) (Q9Y679)
Organism: Homo sapiens (Human)
Function: Plays a role in the translocation of terminally misfolded proteins from the endoplasmic reticulum lumen to the cytoplasm and their degradation by the proteasome. Plays a role in lipid droplet formation. Induces lipid droplet clustering. Recruits ubiquitin-conjugating enzyme UBE2G2 to lipid droplets which facilitates its interaction with ubiquitin ligases AMFR/gp78 and RNF139/TRC8, leading to sterol-induced ubiquitination of HMGCR and its subsequent proteasomal degradation. Also required for the degradation of INSIG1, SREBF1 and SREBF2. Plays a role in regulating assembly and secretion of very low density lipoprotein particles and stability of apolipoprotein APOB.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:12042322, ECO:0000269|PubMed:18711132, ECO:0000269|PubMed:21127063, ECO:0000269|PubMed:21857022, ECO:0000269|PubMed:23197321, ECO:0000269|PubMed:23223569}; Peripheral membrane protein {ECO:0000269|PubMed:21127063, ECO:0000269|PubMed:23197321}. Lipid droplet {ECO:0000269|PubMed:21127063, ECO:0000269|PubMed:21857022, ECO:0000269|PubMed:23197321, ECO:0000269|PubMed:23223569, ECO:0000269|PubMed:28183703, ECO:0000269|PubMed:29902443}.; SUBCELLULAR LOCATION: Cytoplasmic vesicle, autophagosome {ECO:0000269|PubMed:29902443}. Note=(Microbial infection) Upon Dengue virus infection, relocates from lipid droplets to autophagosomes. {ECO:0000269|PubMed:29902443}.
Interaction partners:
- Ubiquitin-conjugating enzyme E2 G2
- Protein sel-1 homolog 1
- FAS-associated factor 2
- Derlin-2
- E3 ubiquitin-protein ligase synoviolin
- Protein OS-9
- Ubiquitin-conjugating enzyme E2 J1
- Transitional endoplasmic reticulum ATPase
- Derlin-3
- Calnexin
Sequence:
MELPSGPGPERLFDSHRLPGDCFLLLVLLLYAPVGFCLLVLRLFLGIHVFLVSCALPDSVLRRFVVRTMCAVLGLVARQEDSGLRDHSVRVLISNHVTPFDHNIVNLLTTCSTPLLNSPPSFVCWSRGFMEMNGRGELVESLKRFCASTRLPPTPLLLFPEEEATNGREGLLRFSSWPFSIQDVVQPLTLQVQRPLVSVTVSDASWVSELLWSLFVPFTVYQVRWLRPVHRQLGEANEEFALRVQQLVAKELGQTGTRLTPADKAEHMKRQRHPRLRPQSAQSSFPPSPGPSPDVQLATLAQRVKEVLPHVPLGVIQRDLAKTGCVDLTITNLLEGAVAFMPEDITKGTQSLPTASASKFPSSGPVTPQPTALTFAKSSWARQESLQERKQALYEYARRRFTERRAQEAD
Protein: CTD small phosphatase-like protein 2 (CTDSP-like 2) (EC 3.1.3.-) (Q8BG15)
Organism: Mus musculus (Mouse)
Function: Probable phosphatase.
Interaction partners:
- Serine/threonine-protein kinase PDIK1L
Sequence:
MKLRTRKASQQSSPIQTQRTARAKRKYSEVDDSLPSGGEKPSKNETGLLSSIKKFIKGSTPKEERENPSKRSRIERDIDNNLITSTPRTGEKPDKQLSRVRRKSPVNGEAGSYEMTNQHIKQNGKLEDNPCSGSPPRTTLLGTIFSPVFNFFSPANKNGTSGSDSPGQAVEAEEIVKQLDMEQVDEITTSTTSANGAAYSNQAVQVRPSLNNGLEEAEETVTRDIPPLTAPVTPESGYSSAHAEATYEEDWEVFDPYYFIKHVPPLTEEQLNRKPALPLKTRSTPEFSLVLDLDETLVHCSLNELEDAALTFPVLFQDVIYQVYVRLRPFFREFLERMSQMYEIILFTASKKVYADKLLNILDPKKQLVRHRLFREHCVCVQGNYIKDLNILGRDLSKTIIIDNSPQAFAYQLSNGIPIESWFMDKNDNELLKLIPFLEKLVELNEDVRPHIRDRFRLHDLLPPD
Protein: PR domain containing 2, with ZNF domain (A2A7B7)
Organism: Mus musculus (Mouse)
Interaction partners:
Sequence:
MHQNTESVAVTETLAEVPEHVLRGLPEEVRLLPSAVDKTRIGVWATKPILKGKKFGPFVGDKKKRSQVRNNVYMWEVYYPNLGWMCIDATDPEKGNWLRYVNWACSGEEQNLFPLEINRAIYYKTLKPIAPGEELLVWYNGEDNPEIAAAIEEERASARSKRSSPKSRR
Protein: Cyclin-dependent kinase 17 (EC 2.7.11.22) (Cell division protein kinase 17) (PCTAIRE-motif protein kinase 2) (Serine/threonine-protein kinase PCTAIRE-2) (Q00537)
Organism: Homo sapiens (Human)
Function: May play a role in terminally differentiated neurons. Has a Ser/Thr-phosphorylating activity for histone H1 (By similarity).
Interaction partners:
- Tudor domain-containing protein 7
- CDK5 and ABL1 enzyme substrate 1
- Coiled-coil domain-containing protein 180
- Cyclin-dependent kinase 14
Sequence:
MKKFKRRLSLTLRGSQTIDESLSELAEQMTIEENSSKDNEPIVKNGRPPTSHSMHSFLHQYTGSFKKPPLRRPHSVIGGSLGSFMAMPRNGSRLDIVHENLKMGSDGESDQASGTSSDEVQSPTGVCLRNRIHRRISMEDLNKRLSLPADIRIPDGYLEKLQINSPPFDQPMSRRSRRASLSEIGFGKMETYIKLEKLGEGTYATVYKGRSKLTENLVALKEIRLEHEEGAPCTAIREVSLLKDLKHANIVTLHDIVHTDKSLTLVFEYLDKDLKQYMDDCGNIMSMHNVKLFLYQILRGLAYCHRRKVLHRDLKPQNLLINEKGELKLADFGLARAKSVPTKTYSNEVVTLWYRPPDVLLGSSEYSTQIDMWGVGCIFFEMASGRPLFPGSTVEDELHLIFRLLGTPSQETWPGISSNEEFKNYNFPKYKPQPLINHAPRLDSEGIELITKFLQYESKKRVSAEEAMKHVYFRSLGPRIHALPESVSIFSLKEIQLQKDPGFRNSSYPETGHGKNRRQSMLF
Protein: Stage II sporulation protein M (P37873)
Organism: Bacillus subtilis (strain 168)
Function: Required for complete septum migration and engulfment of the forespore compartment during sporulation. Required for stabilizing and recruiting of SpoIIP to the septal membrane.
Subcellular location: Cell membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. Note=Localizes to the sporulation septum and to the second division site within the mother cell. Before the start of engulfment localizes to the septal midpoint, then spreads throughout the septum prior to becoming enriched at the leading edge of the engulfing membrane, where it remains until the completion of membrane migration. Some remain partially trapped at the septum during engulfment and upon completion of engulfment become dispersed in the outer forespore membrane. Localization of the MPD complex to the septal membrane is dependent on SpoIIB. {ECO:0000269|PubMed:12502745, ECO:0000269|PubMed:17376078}.
Interaction partners:
- Stage II sporulation protein P
- Stage II sporulation protein D
- Stage III sporulation protein AH
- Stage IV sporulation protein FA
- Stage III sporulation protein AB
- Stage II sporulation protein B
- Stage II sporulation protein Q
- Stage III sporulation protein AA
- Sporulation sigma-E factor-processing peptidase
- Stage IV sporulation protein FB
Sequence:
MRKISYKDMFLRHVKDHLSLYIFVSVLFFMGVIFGAIIVNSMTISQKEDLYYYLSQFFGQLSDGKQASSADMFGQSIFHNAKYLGLMWILGISVIGMPIIFIMIFLKGIVVGFTVGFLVNQMGVSGFFLSFVSVLPQNVLLIPAYLIMGTCAIAFSLKLIRQLFVKRSLHDAPIQWFGRYAFVLLVILFLALISSLFEAYLSPVLMEKLTSRLF
Protein: Voltage dependent anion channel 2 (F4K3R8)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
Sequence:
MSKGPGLFTDIGKKAKDLLTRDYNSDQKFSISTYSASGVGTERENEYQDDIYFCLRTRCLIMSENEALTSTALKKGGVHAADVATQYKYKNALFDVKIDTDSSVLTTVTLTEILPSTKAIASFKVPDYNSAKLEVQYFHDHATVTAAAALKQNPLIDITATLGSPVISFGAEAGYDTTSKTFTKYNAGISVTKPDACLSIILGDKGDSLKASYLHHFDEFKRTAAVGEVYRKFSTNENTITVGGLYAIDHSTAVKAKLNNHGTLGALLQHEVLPRSLVTVSSEIDTKALEKHPRFGLSLALKP
Protein: 6,7-dimethyl-8-ribityllumazine synthase (DMRL synthase) (LS) (Lumazine synthase) (EC 2.5.1.78) (P61940)
Organism: Nitratidesulfovibrio vulgaris (strain ATCC 29579 / DSM 644 / CCUG 34227 / NCIMB 8303 / VKM B-1760 / Hildenborough) (Desulfovibrio vulgaris)
Function: Catalyzes the formation of 6,7-dimethyl-8-ribityllumazine by condensation of 5-amino-6-(D-ribitylamino)uracil with 3,4-dihydroxy-2-butanone 4-phosphate. This is the penultimate step in the biosynthesis of riboflavin.
Interaction partners:
- Riboflavin synthase
- Riboflavin biosynthesis protein RibD
- Riboflavin biosynthesis protein RibBA
- 3,4-dihydroxy-2-butanone 4-phosphate synthase
- Transcription antitermination protein NusB
- Riboflavin biosynthesis protein
- S-adenosylmethionine synthase
- Inosine-5'-monophosphate dehydrogenase
- Aspartate carbamoyltransferase catalytic subunit
- Large ribosomal subunit protein bL21
Sequence:
MLHIKTIEGQLDAKGLKFAIVATRFNDFIVDRLIGGACDYLQRHGCDRENLTIVRIPGAFEMPLVAKKLAHSGKYDGIIALGAVIRGATPHFDFVSNEASKGLAQACLESGVPLGFGLLTTDNIEQAIERAGSKAGNKGAEAAAAVLETVRVMEQL
Protein: Plexin-B1 (Q8CJH3)
Organism: Mus musculus (Mouse)
Function: Receptor for SEMA4D. Plays a role in GABAergic synapse development. Mediates SEMA4A- and SEMA4D-dependent inhibitory synapse development. Plays a role in RHOA activation and subsequent changes of the actin cytoskeleton (By similarity). Plays a role in axon guidance, invasive growth and cell migration (By similarity).
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:O43157}; Single-pass type I membrane protein {ECO:0000255}.
Interaction partners:
- Semaphorin-4D
- Rho-related GTP-binding protein Rho6
- Rho guanine nucleotide exchange factor 12
- Receptor tyrosine-protein kinase erbB-2
- Semaphorin-4A
- Ras-related protein R-Ras
- Hepatocyte growth factor receptor
- Semaphorin-4C
- Ras-related C3 botulinum toxin substrate 2
- Rho guanine nucleotide exchange factor 11
Sequence:
MSVLGPVLLQVFWAGCVVTLRSPLPAAFTANGTHLQHLARDPTTGTLYVGATNFLFQLSPGLQLEAVVSTGPVNDSRDCLPPVIPDECPQAQPTNNPNQLLLVSPEALVVCGSVHQGICELRSLGQIRQLLLRPERPGDTQYVAANDPAVSTVGLVAQGLVGEPLLFVGRGYTSRGVGGGIPPITTRALRPPDPQAAFSYEETAKLAVGRLSEYSHHFVSAFVRGASAYFLFLRRDLKAPSRAFRAYVSRVCLQDQHYYSYVELPLACQGGRYGLIQAAAVATSKEVARGDVLFAAFSSVAPPTVDWPLSASTGASGTSVLCAFPLDEVDQLANYTRDACYTREGRAENGTKVADIAYDVLSDCAQLPVDTPDAFPCGSDHTPSPMVSCVPLEATPILELPGVQLTAVAVTMEDGHTIAFLGDSQGQLHRVYLGPGRSAAPYSKQSIQPGSPVNRDLTFDGTFEHLYVATQTTLVKVPVAPCAQHLDCDSCLAHRDPYCGWCVLLGRCSRRSECSRDQGPEQWLWSFQPELGCLRVVAVSPANISREERREVFLSVPGLPSLWPGESYFCYFGDQQSPALLTSSGVMCPSPDPSEAPVLQRGADHISVNVELRFGAVVIASTSLSFYDCVAVTASSPSAPCRACVSSRWGCNWCVWQQLCTHKASCDAGPMVASQQSPLLPLIPPARDELTPFPPTVPQTTVTPTPNSFPIEPRAPSTASDVLPGAKPSRLSLWGPWAGPGPILSPTSTESPLHEKPLPPDPPTIPGTTVPAPTGLGPSTTPEDLLASYPFPSDAAAVSPAEPGPEALPSMVALDQPPGTVPDTTFPGAPGSMKPVLDWLTKGGGELPEADEWMGGDTPAFSTSTLLSGDGDSAEHEGPPAPLILLSSLDYQYDTPGLWELGEVNQRVSSCPCVETVQGSLLIPVHVEREVQLRGRNLWLFQDGPRSSECVLELGSREVAVEAQVECAPPPDVWCHIKCQQHQFSYEALKPELQVGLFLRWAGGLRVDSADGLHVVLYDCSVGHGDCSRCQTAMPQYDCVWCEGERPRCVAREACNEAETVATQCPAPLIHSVDPLTGPIDGGTRVTIRGSNLGQHVQDVLDMVRVAGVPCAVDAGEYDVSSSLVCITGASGEEVTGTVAVEVPGRGHGVSEFSFAYQDPKVHSIFPARGPRAGGTRLTLHGSKLLTGRLEDIRVVVGDQPCHLLLEQQSEQLHCETGPYPVPAELPVTVLFGATERRLQHGQFKYTSDPNVTSVGPSKSFFSGGREIWVRGQDLDVVQRPRIRVTVVPRQHGQGLAQKQHVVPEKFEEPCLVNSSHLLMCRTPALPGPPWDSGVQVEFILDNMVFDFAALSPTPFSYEADPTLRSLNPEDPSTPFRHKPGSVFSVEGENLDLAMSKEEVVAMIGDGPCVVKTLTRNHLYCEPPVEQPLPHPHALREAPDALPEFTVQMGNLRFSLGHVQYDGESPVAFPVAAQVGLGVGTSLLALGVIIIVLIYRRKSKQALRDYKKVQIQLENLESSVRDRCKKEFTDLMTEMTDLTSDLLGSGIPFLDYKVYAERVFFPGYRESPLHRDLGVPDSRRPTVEQGLGQLSNLLNSKLFLTKFIHTLESQRTFSARDRAYVASLLTVALHGKLEYFTDILRTLLSDLVAQYVAKNPKLMLRRTETVVEKLLTNWMSICLYTFVRDSVGEPLYMLFRGIKHQVDKGPVDSVTGKAKYTLNDNRLLREDVEYRPLTLNALLAVGPGAGEAQCVPVKVLDCDTISQAKEKMLDQLYKGVPLAQRPDSCTLDVEWRSGVAGHLILSDEDVTSELQGLWRRLNTLQHYKVPDGATVALVPCLTKHILRENQDYVPGERTPMLEDVDEGGIRPWHLVKPSDEPEPPRPRRGSLRGGERERAKAIPEIYLTRLLSMKGTLQKFVDDLFQVILSTSRPVPLAVKYFFDLLDEQAQQHGISDQDTIHIWKTNSLPLRFWINIIKNPQFVFDVQTSDNMDAVLLVIAQTFMDACTLADHKLGRDSPINKLLYARDIPRYKQMVERYYADIRQTVPASDQEMNSVLAELSRNCSADLGARVALHELYKYINKYYDQIITALEEDGTAQKMQLGYRLQQIAAAVENKVTDL
Protein: Forkhead protein sep1 (O43058)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Required for promoter sequence element PCB-driven, M-phase-specific transcription. Acts as a transcriptional activator with a role in the regulation of mitosis. Regulates septation and the periodic transcription of cdc15.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00089, ECO:0000269|PubMed:9427538}.
Interaction partners:
- MADS-box transcription factor 1
- Fork head protein homolog 2
- Metallothionein expression activator
- Primary septum glucan endo-1,3-beta-D-glucosidase
- Glucan endo-1,3-alpha-glucosidase agn1
- Mediator of RNA polymerase II transcription subunit 8
Sequence:
MNFNSTNPYYFTHEKNLNNASKYSELPIAYQEIPLQSLPPYPKVASKLKGVVAGGKENNIASFQKPSSKATRPYIPSYTRLTYSVPPLPIPPPSEQSLDTIIYRNPSVSSSQSQEPEEFFLPLDDGKKPPYSYAMLIGMSIIRSPDRRLTLSAIYDWISNTFSFYNKSNNGWQNSIRHNLSLNKAFMKIERPRNLPGKGHFWSIRPGHEEQFLKLKLRKPGVNSRPAPPVQDVTSSTKYGSSTGSSGFNTFNTSPHIFNQRHQYLQNYYTASLTNIPTISNVNATNFHPLHSQQPYVDTPGIDAPSDLEAKFSDLGVSSVVSVTSPLQSCTNSPSPPLSSPASSASPSESLRNESLGIKSAKSLGLNKDDAPVEGPPVSHLEKDVETPSVHDSVLGFNDTVTNLGKKGLKDGTTNTLQIPAVRLPSLPSSPTIKNPSGLLLKRSNSIDFPTPPKALCPKLFCFRDDIVADDYTKFSLLSPIRSDMSGISASPNTNLKEHRTRILQMLATPDAKQLSSLTSSDAEFWSVTPLKSSILRNGDASKQVTLSESPKGDSLLDGGSLSYFTNNISSVAGLETPSKLPMSKSFDTFEDDFLDPMDMLSFENHFSDFNSNRKVSPVKREVRRKYISSATTIHSSAAQDDTYLPSPTKRKMPLLRQTSTLF
Protein: Copper amine oxidase 1 (EC 1.4.3.21) (Q9P7F2)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Copper amine oxidase involved in the metabolism of xenobiotic and biogenic amines. Capable of catalyzing the oxidative deamination of primary amines such as ethylamine as alternate sources of nitrogen to support growth.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16823372, ECO:0000269|PubMed:18723604}.
Interaction partners:
- Putative aldehyde dehydrogenase-like protein C922.07c
- Putative aldehyde dehydrogenase-like protein C9E9.09c
- Copper amine oxidase-like protein cao2
- Metal homeostasis factor atx1
- Probable catechol O-methyltransferase 2
- Probable catechol O-methyltransferase 1
- Uncharacterized transporter mfc1
- Uncharacterized mitochondrial carrier C27B12.09c
- Lactoylglutathione lyase
- Glutathione-independent glyoxalase hsp3101
Sequence:
MAYYPHLPYHHHHHTSVPGERLSDPLDPLSADELKLAVEIIRHEYPSKHFAFNVVTLEEPPKAKYLHWKYSKEDAHKPERIALAVLLEKGVPGILEARVNLTKAEVIQIEHITGVCPILTADMLVNTEQIVRKDPAVIEQCILSGVPPDQMDHVYCDPWTIGYDERYGNTRRMQQAMMYYRSNEDDSQYSHPLDFCPIIDTEDQKVVAIDIPPVRRPLSKHKHSNFNKKDIEAELGKMREVKPISVTQPEGVNFRMKGRYIEWQNFRMHIGFNYREGIVLSDISYNDNGHIRPLFYRMSIAEMVVPYGNPEHPHQRKHAFDLGEYGAGYLTNPLALGCDCKGVIHYLDAHFVNNTGEVETVKNAICIHEEDDGVLFKHSDFRDKFRTTISARGIRLVISQIFTAANYEYMVYWIFHMDGVIECELKLTGILNTYAMNEGEDLKGWGTQVYPQVNAHNHQHLFCLRLNPMLDGYSNSVAVVDGVSGPGEPGSKENYYGNAFTTERTVPKTVKEAICDYNSDTSRTWDICNPNKLHPYSGKPVSYKLVSRETPRLMARPGSLVSNRAGFARHHIHVTPYKDGQIYPAGDYVPQTSGEPTKGLPEWIAEEPDASVDNTDIVVWHTFGITHFPAPEDFPLMPAEPIRLLLRPRNFFLRNPALDVPPSKNVTTSEVKQAHHHGNLHMMDMMKSLTDATSEFAFGEKFCEKHKGDHFF
Protein: DNA repair and transcription factor protein, putative (Q57TV9)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- DNA 5'-3' helicase
- General transcription factor IIH subunit 4
- [RNA-polymerase]-subunit kinase
- DNA-direcetd RNA polymerase II, subunit 9, putative
- DNA-directed RNA polymerases I, II, and III subunit RPABC3
- DNA-directed RNA polymerase subunit beta
- Plastid-encoded RNA polymerase subunit alpha
- DNA-directed RNA polymerase II, putative
- RNA polymerase-like protein
- DNA-directed RNA polymerases I, II, and III subunit RPABC5
Sequence:
MLKTVLLLDGSEAVNCSLDYLPTRLIALRPQLNKFVHTYLDANPLASLGVVVMRDGVAQRLIPCTTNATDIVQTLELKYFRFGGSGAMSLENGLRMALSELVDLRRIAKRLRENNSGSTGSDVQEDVTSRLRIVLASSSVTIVDPLDVFAVQKIVAQLRVRVDVISFCGAVHVLQEAAVLTGGSLHTPMNYEHLTEILRHLASPEGGSARHVDVQPALIQIGFPMYVGDEAEGKRYLTCPQCGLIQTSIPSTCSLCKLLLFSVPLIHVTFITRNELCAPSQKVEHVTKKKTTAAAGGAADTARCSLCQRKLAGEDGGGYWCCGCCLCERCEACETYIRENLGLCPTCVATS
Protein: Secreted chorismate mutase (CM) (EC 5.4.99.5) (*MtCM) (P9WIB9)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: Catalyzes the Claisen rearrangement of chorismate to prephenate. May play some role in the pathogenicity.
Subcellular location: Secreted {ECO:0000269|PubMed:15654876, ECO:0000269|PubMed:15737998, ECO:0000269|PubMed:17146044}.
Interaction partners:
- Intracellular chorismate mutase
- Chorismate synthase
- Diacylglycerol acyltransferase/mycolyltransferase Ag85B
- Prephenate dehydrogenase
- Prephenate dehydratase
- Anthranilate synthase component 1
- Putative isochorismate synthase MenF
- Anthranilate synthase component 2
- Resuscitation-promoting factor RpfC
- 3-dehydroquinate dehydratase
Sequence:
MLTRPREIYLATAVSIGILLSLIAPLGPPLARADGTSQLAELVDAAAERLEVADPVAAFKWRAQLPIEDSGRVEQQLAKLGEDARSQHIDPDYVTRVFDDQIRATEAIEYSRFSDWKLNPASAPPEPPDLSASRSAIDSLNNRMLSQIWSHWSLLSAPSCAAQLDRAKRDIVRSRHLDSLYQRALTTATQSYCQALPPA
Protein: 3-epi-6-deoxocathasterone 23-monooxygenase CYP90C1 (3-dehydro-6-deoxoteasterone) (EC 1.14.14.147) ((22R,23R)-22,23-dihydroxy-campest-4-en-3-one synthase) (EC 1.14.14.-) ((22R,23R)-22,23-dihydroxycampesterol synthase) (EC 1.14.14.-) (6-deoxoteasterone synthase) (EC 1.14.14.-) (Cytochrome P450 90C1) (Protein ROTUNDIFOLIA 3) (Teasterone synthase) (EC 1.14.14.-) (Q9M066)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Involved in brassinosteroid (BR) biosynthesis. Converts typhasterol (TY) to cathasterone (CS) and 6-deoxotyphasterol (6-deoxoTY) to 6-deoxocathasterone (6-deoxoCT). C-23 hydroxylase that converts directly (22S,24R)-22-hydroxy-5-alpha-ergostan-3-one and 3-epi-6-deoxocathasterone to 3-dehydro-6-deoxoteasterone (6-deoxo3DT, 6-deoxo3DHT) and 6-deoxotyphasterol (6-deoxoTY), respectively. These C-23 hydroxylation shortcuts bypass campestanol, 6-deoxocathasterone, and 6-deoxoteasterone (6-deoxoTE). Catalyzes also the conversion of cathasterone to teasterone (TE), (22S,24R)-22-hydroxyergost-4-en-3-one (22-OH-4-en-3-one) to (22R,23R)-22,23-dihydroxy-campest-4-en-3-one (22,23-diOH-4-en-3-one) and (22S)-22-hydroxycampesterol (22-OHCR) to (22R,23R)-22,23-dihydroxycampesterol (22,23-diOHCR). Required for the regulation of polar elongation of leaf cells. Required for the longitudinal elongation of floral organs.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}.
Interaction partners:
- Steroid 5-alpha-reductase DET2
- Cytochrome P450 85A2
- Cytochrome P450 85A1
- Steroid
- 3beta,22alpha-dihydroxysteroid 3-dehydrogenase
- 3-epi-6-deoxocathasterone 23-monooxygenase CYP90D1
- 7-dehydrocholesterol reductase
- Delta
- Small polypeptide DEVIL 16
- Delta
Sequence:
MQPPASAGLFRSPENLPWPYNYMDYLVAGFLVLTAGILLRPWLWLRLRNSKTKDGDEEEDNEEKKKGMIPNGSLGWPVIGETLNFIACGYSSRPVTFMDKRKSLYGKVFKTNIIGTPIIISTDAEVNKVVLQNHGNTFVPAYPKSITELLGENSILSINGPHQKRLHTLIGAFLRSPHLKDRITRDIEASVVLTLASWAQLPLVHVQDEIKKMTFEILVKVLMSTSPGEDMNILKLEFEEFIKGLICIPIKFPGTRLYKSLKAKERLIKMVKKVVEERQVAMTTTSPANDVVDVLLRDGGDSEKQSQPSDFVSGKIVEMMIPGEETMPTAMTLAVKFLSDNPVALAKLVEENMEMKRRKLELGEEYKWTDYMSLSFTQNVINETLRMANIINGVWRKALKDVEIKGYLIPKGWCVLASFISVHMDEDIYDNPYQFDPWRWDRINGSANSSICFTPFGGGQRLCPGLELSKLEISIFLHHLVTRYSWTAEEDEIVSFPTVKMKRRLPIRVATVDDSASPISLEDH
Protein: Solute carrier family 15 member 3 (Osteoclast transporter) (Peptide transporter 3) (Peptide/histidine transporter 2) (hPHT2) (Q8IY34)
Organism: Homo sapiens (Human)
Function: Proton-coupled amino-acid transporter that transports free histidine and certain di- and tripeptides, and is involved in innate immune response (By similarity). Also able to transport carnosine. Involved in the detection of microbial pathogens by toll-like receptors (TLRs) and NOD-like receptors (NLRs), probably by mediating transport of bacterial peptidoglycans across the endolysosomal membrane: catalyzes the transport of certain bacterial peptidoglycans, such as muramyl dipeptide (MDP), the NOD2 ligand (By similarity).
Subcellular location: Lysosome membrane {ECO:0000269|PubMed:17897319}; Multi-pass membrane protein {ECO:0000255}. Endosome membrane {ECO:0000250|UniProtKB:Q8BPX9}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- T-cell differentiation antigen CD6
Sequence:
MPAPRAREQPRVPGERQPLLPRGARGPRRWRRAAGAAVLLVEMLERAAFFGVTANLVLYLNSTNFNWTGEQATRAALVFLGASYLLAPVGGWLADVYLGRYRAVALSLLLYLAASGLLPATAFPDGRSSFCGEMPASPLGPACPSAGCPRSSPSPYCAPVLYAGLLLLGLAASSVRSNLTSFGADQVMDLGRDATRRFFNWFYWSINLGAVLSLLVVAFIQQNISFLLGYSIPVGCVGLAFFIFLFATPVFITKPPMGSQVSSMLKLALQNCCPQLWQRHSARDRQCARVLADERSPQPGASPQEDIANFQVLVKILPVMVTLVPYWMVYFQMQSTYVLQGLHLHIPNIFPANPANISVALRAQGSSYTIPEAWLLLANVVVVLILVPLKDRLIDPLLLRCKLLPSALQKMALGMFFGFTSVIVAGVLEMERLHYIHHNETVSQQIGEVLYNAAPLSIWWQIPQYLLIGISEIFASIPGLEFAYSEAPRSMQGAIMGIFFCLSGVGSLLGSSLVALLSLPGGWLHCPKDFGNINNCRMDLYFFLLAGIQAVTALLFVWIAGRYERASQGPASHSRFSRDRG