wanglab/gogpt-training-data huggingface dataset:
Protein: Asp/Glu-specific dipeptidyl-peptidase (EC 3.4.14.-) (Dipeptidyl-peptidase 11) (DPP11) (A4Y3F4)
Organism: Shewanella putrefaciens (strain CN-32 / ATCC BAA-453)
Function: Catalyzes the removal of dipeptides from the N-terminus of oligopeptides. Shows a strict specificity for acidic residues (Asp or Glu) in the P1 position, and has probably a hydrophobic residue preference at the P2 position. Preferentially cleaves the synthetic substrate Leu-Glu-methylcoumaryl-7-amide (Leu-Glu-MCA) as compared to Leu-Asp-MCA.
Interaction partners:
- Peptidase S9, prolyl oligopeptidase active site domain protein
Sequence:
MRIALVATLVLTSGIANADEGQWQPYQMPSIADKLSERGIDIPAEKLADLTSYPMNAVVGLGYCTASFVSPQGLVVTNHHCAYKAIQYNTKQEHNYLEQGFLATSMDKEPSAGPNERLYITEAVTDVTKDVTKELSQDPLTRYEEIQNNSKALIKNCEVDDNYRCNVRSFHNGLEYYLIKQLMIRDVRLVYAPPESVGGYGGDIDNYEYPRHSGDFAFLRAYVGKDGKPAAYAEDNIPYKPKSYLKVNADGVKAGDGVFVAGYPGTTSRYNLTSELKFASDWLYPTQAKRYQLQIDTINAMGQEDADIAIKYAGNMASMANRMKKLNGLLAGFKATDIIGIKQSREDNFLAWLKQNPKLNQNLIAELEVLLAEQQQVFQSNYYFTNAQSSTLLTAANSLYRLAKEKQKSDAEREIGYQERDLAMFSSRLKRIDSSFHVDVDKTLWQQDLRAYLAQPNRIAALDDALDLNNKETNLEAKLDGLYSLTTLTDQAQRLAWMDADTTTFETSTDPFIRLAVALYDTNMAQEKAEKILDGKLSTARPDYMAAVIEYYKANNWPVYPDANGTLRISYGMVDGYQSRDALYKQPFTRLDGIVAKHTGAEPYNAPQKLLDAISEQRFGDHLVKSVYQDPRGWICRLFSCLDKPEEFNSVPVNFLSSVDTTGGNSGSPVFNGKGELVGLNFDSTYEAITKDWFFNPTITRAVHVDIRYILWMMDKVDHADNLIKELDLVRN
Protein: Contactin-associated protein-like 4 (Cell recognition molecule Caspr4) (Q99P47)
Organism: Mus musculus (Mouse)
Function: Presynaptic protein involved in both dopaminergic synaptic transmission and GABAergic system, thereby participating in the structural maturation of inhibitory interneuron synapses. Involved in the dopaminergic synaptic transmission by attenuating dopamine release through a presynaptic mechanism. Also participates in the GABAergic system.
Subcellular location: Presynaptic cell membrane {ECO:0000269|PubMed:24870235}; Single-pass type I membrane protein {ECO:0000269|PubMed:24870235}. Note=Specifically present within the presynaptic compartment of synapses. {ECO:0000269|PubMed:24870235}.
Interaction partners:
- Contactin-5
- Neuronal cell adhesion molecule
- Neural cell adhesion molecule L1-like protein
Sequence:
MNMGSVAGAVLKMLLLLSTQNWNRVEAGNSYDCDEPLVSALPQASFSSSSELSSSHGPGFARLNRRDGAGGWSPLVSNKYQWLQIDLGERMEVTSVATQGGYGSSNWVTSYLLMFSDSGRNWKQYRQEDSIWGFSGNANADSVVYYRLQPSIKARFLRFIPLEWNPKGRIGMRIEVFGCAYRSVVIDLDGKSSLLYRFDQNSLSPIRDIISLKFKTMESDGILLHRAGPAGDHITLELRRGKLFLLINSGDARLTSSSTLINLTLGSLLDDQHWHSVLIQRLGKQVNFTVDEHRRHFHAQGEFNYLDLDYEISFGGISAPAKSVSLPYKHFHGCLENLFYNGVDVIGLVKEHSPQIITMGNASFSCSQPQSMPLTFLSPRSYLVLPASTKEEAISASFQFRTWNKAGLLLFSELQLVSGSLLLLLSDGKLKLTLYQPGKSPSDITAGAGLGDGQWHSVSLSAKRNHLSVVVDGHISPASPWLGPEQVNSGGVFYFGGCPDKGFGSKCKSPLGGFQGCMRLISINNKMVDLIAVQQGALGNFSDLQIDSCGISDRCLPNSCEHGGECSQSWSTFHCNCTNTGYTGATCHSSVYEQSCEAYKHQGNASGFYYIDSDGSGPLQPFLLYCNMTETAWTVMQHNGSDLMRVRNTHSENAHTGVFEYTASMEQLQAAINRAEHCQQELVYYCKKSRLVNQQDGSPRSWWVGRTNETQTYWGGSLPVHQKCTCGLEGNCIDAQYHCNCDADLNEWTNDTGFLSYKEHLPVTKIVITDTGRPHSEAAYKLGPLLCRGDRPFWNAASFNTEASYLHFPTFHGELSADVSFFFKTTALSGVFLENLGITDFIRIELRSPTTVTFSFDVGNGPFELSVHSPTHFNDNQWHHVRVERNMKEASLRVDELPPKIQAAPTDGHVLLQLNSQLFVGGTATRQRGFLGCIRSLQLNGMALDLEERATVTPGVQPGCRGHCGSYGKLCRHGGKCREKPSGFFCDCSSSAYAGPFCSKEISAYFGSGSSVIYNFQENYSLSKNSSFHAASFHGDMKLSREMIKFSFRTTRAPSLLLHMSSFYKEYLSIIIAKNGSLQIRYKLNKYHEPDVISFDLKSMADGQLHHIKINREEGMVFVEIDENTRRQTYLSSGTEFSAVKSLVLGRMLEYSDVDQETALAAAHGFTGCLSAVQFSHIAPLKAALQPGPPAPVTVTGHVTESSCVAPSGTDATSRERTHSFADHSGTMDDREPLTHAIKSDSAVIGGLIAVVIFILLCVSAIAVRIYQQKRLYKRNEAKRSENVDSAEAVLKSELHIQNAVGENQKEYFF
Protein: Putative potassium channel regulatory protein unc-93 (Uncoordinated protein 93) (Q93380)
Organism: Caenorhabditis elegans
Function: May contribute to coordination of muscle contraction as regulatory subunit of a nonessential potassium channel complex. Plays a role in the formation of muscle connections, also called muscle arm extensions, between the body wall and the motor axons in the dorsal and ventral cord.
Subcellular location: Cell membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. Note=Associated with dense bodies. {ECO:0000269|PubMed:14534247}.
Interaction partners:
- Two pore potassium channel protein sup-9
- Putative potassium channel regulatory protein sup-10
- Iodotyrosine dehalogenase 1 homolog
Sequence:
MKFQKMGDSNTWDLVGEQQQRKKSRSPSRASRVDSELLVGVENAAELEALGLGKEQLEEEARRHKKQRSKSPALENIRKTSIHLLQKFGAIPKKKDDSVLLFRFHDIPDIPLESLCIRPKEFFEEPKVFSFRDMGREQQKAEVNEKCSYLFRGTSFDHDDHFELPTETGRVPEYDHFCPIHGSRRRLPRNKLVTMQTLMHSVDDEDNEDLAYIYGHDFLAKLVRKKKREMMSGTEKERANKIKRKIMSNLWILSVAFLFLFTAFNGLQNLQTSVNGDLGSDSLVALYLSLAISSLFVPSFMINRLGCKLTFLIAIFVYFLYIVINLRPTYSSMIPASIFCGIAASCIWGAKCAYITEMGIRYASLNFESQTTVIVRFFGYFFMIVHCGQVVGNMVSSYIFTLSYSQALRGPEDSIYDSCGYQFPKNLSDLTELAESNLARPPQKVYVAVCLAYLACVIISGMIMSMFLNALAKDARNRKMAQKFNSEIFYLMLKHLINIKFMLLVPLTIFNGLEQAFLVGVYTKAFVGCGLGIWQIGFVMACFGISDAVCSLVFGPLIKLFGRMPLFVFGAVVNLLMIVTLMVWPLNAADTQIFYVVAAMWGMADGVWNTQINGFWVALVGRQSLQFAFTKYRFWESLGIAIGFALIRHVTVEIYLLITFFMLLLGMCGFLAIENFDHIIKFWHHLIHTSCPEKEPLDDRNSDFE
Protein: Annexin A11 (Annexin XI) (Annexin-11) (Calcyclin-associated annexin 50) (CAP-50) (P33477)
Organism: Oryctolagus cuniculus (Rabbit)
Function: Required for midbody formation and completion of the terminal phase of cytokinesis (By similarity). Binds specifically to calcyclin in a calcium-dependent manner.
Subcellular location: Cytoplasm {ECO:0000250}. Melanosome {ECO:0000250}. Nucleus envelope {ECO:0000250}. Nucleus, nucleoplasm {ECO:0000250}. Cytoplasm, cytoskeleton, spindle {ECO:0000250}. Note=Found throughout the nucleoplasm at interphase and during mitosis concentrates around the mitotic apparatus. Elevation of intracellular calcium causes relocalization from the nucleoplasm to the nuclear envelope, with little effect on the cytoplasmic pool. Localization to the nuclear envelope is cell-cycle dependent. {ECO:0000250}.
Interaction partners:
- Protein S100-A6
- Annexin
- Alpha-1,3/1,6-mannosyltransferase ALG2
Sequence:
MSYPGYPPPPGGYPPAPGGGAWGGAGYPPPSMPPIGLDNVANYAGQFNQDYLSGMAANMSGTFGGANVPPNLYPGAPGGGYPPVPPGGFGQPPPTQPSVPPYGVYPPPGGNPPSGVPSYPPFPGAPVPGQPMPPPGHQPPGPYPGQLPVTYPGQSPVPPPGQQPMPSYPGYPGSGTVTPAVPPVQFGNRGTITDASGFDPLRDAEVLRKAMKGFGTDEQAIIDCLGSRSNKQRQQILLSFKTAYGKDLIKDLKSELSGNFEKTILALMKTPILFDAYEIKEAIKGAGTDEACLIEILASRSNEHIRELNKAYKTEFKKTLEEAIRSDTSGHFQRLLISLSQGNRDESTNVDMSLVQRDVQELYAAGENRLGTDESKFNAVLCSRSRAHLVAVFNEYQRMTGRDIEKSICREMSGDLEQGMLAVVKCLKNTPAFFAERLNRAMRGAGTKDRTLIRIMVSRSEIDLLDIRAEYKRMYGKSLYHDISGDTSGDYRKILLKICGGND
Protein: Protein mitoshell (Q9VLP4)
Organism: Drosophila melanogaster (Fruit fly)
Function: Required for male meiotic cytokinesis through its involvement in the regulation of mitochondrial aggregation and fusion, astral spindle assembly and contractile ring formation.
Interaction partners:
- IP14417p1
Sequence:
MNIPIYQVPSVTMQSLHQQSLYQQTYLDRNRMVTDVFVQEHVSQSSWSMAGSSAVFIPGPIITGSAHGHCHHTATVSTVSPQLATFMPFPGMQYYAASSATMNAYGHNQMYSTRASASVGFYLPQYHASCSHEQPKKTFCAAQTQTQQTAKTSCDVGTQVDLDAEELRSEARKPRPESVVPEESSISSLESGAGDGFRVQKKLRNSEVKLLDQRLHDITRVSLHGSEIAERLANAHRNRPCFKKIDTLCARLKQDLLRPDGVLPNINSQGIAWAVKDFIFVFTRIVNAWVILKGYVYNTPDALNKIKDELPSGFMASFDSWQISTLSIVKMIVKSFVNLDELLQKQKNSFSGKDGAPINQSNSISLRSFIDSNDSSGLAQKYLGMTTGHGPSAFSTPNNQIRNNAASKGQEPTSSALYKPKCALNLNYLYTMIEDSEETQRHVDANGTYLKTGTYQPLQKESMQLEMPPAKPNDHYVERNANQQALPSQEIPNAPTPKSSPQSDRPRDVRSYTNPFSAIGKEVTRQLYEFSDRVMELKNLERFFKKQFTRNYYPNFYQHCQDDFIDVRAIILRCENSSYHHIYQAIHDLRRIIFTVRCYLQMYTDENLLYYIDLYERSVNDMLSKPPHYPNQFDHIMGRPGEKLFNYEI
Protein: COP9 signalosome complex subunit 2 (Signalosome subunit 2) (Q54HL6)
Organism: Dictyostelium discoideum (Social amoeba)
Function: Essential component of the COP9 signalosome complex (CSN), a complex involved in various cellular and developmental processes. The CSN complex is an essential regulator of the ubiquitin (Ubl) conjugation pathway by mediating the deneddylation of the cullin subunits of E3 ligase complexes, leading to modify the Ubl ligase activity.
Subcellular location: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
Interaction partners:
- COP9 signalosome complex subunit 3
- COP9 signalosome complex subunit 5
- COP9 signalosome complex subunit 4
- COP9 signalosome complex subunit 1
- COP9 signalosome complex subunit 6
- COP9 signalosome complex subunit 8
- COP9 signalosome complex subunit 7
- Cullin-4
- RING-box protein 1
- Cullin-5
Sequence:
MSDDEDMMYDDDEYFDDDEDQDQNDSESEGVEIENQYYNSKGLIDESIPDAIKSYEKVVDLENGEKGEWGFKALKKITKLYFRIGDFDNMLESFKKFLPYTKSSASSNYIEKGINSVLDMVSSSNTIELDMIQKVFDLTLKSLLDTKNERVWFRTNLKLAKLLFEKAEYGRLAKILRDLHKSCELEDGTDDQKKGSQLVDIYALEIQMYTETKNNKKLKDLYKKALEIKSAIPHPRIMGIIRECGGKMHMAEKEWEKAHTDFFEAFKNYDEAGNSRRIQCLKYLVLACMLMLSTINPFDSTEAKPYKNDPDILAMTNLVMAYEKNDIYAFEKILKDNRKTIMDDPFIRMYIEDLLRNIRTQVLLKLLKPYTRIRISFISKELNIPSSDVESLLVSLILDNKIRGSIDQVNQQLELDTAKSSAYWKYTSIHKWANQIGQLNGGINNKLVS
Protein: Rap guanine nucleotide exchange factor 2 (G5EEE0)
Organism: Caenorhabditis elegans
Interaction partners:
Sequence:
MSVDSIAMPPPPVPPRPLRLPQTAAKGPAPLPPRGLPRTYPLDFPVDIPTTSSSSSNTSYNDQHRSQVYLNGLSADEDTLVRVKHRREKSNSVGGQAQNGISTARRLRGRSTASSTTTEGETASNEGADSDEDEGSMPSQESSSGGFMDLRDSVRECLEKEPSERNSEDLAVLLDFMQHMSAFAALPMSIKRQLCLKMVFAVVNDAGTVVLAHNEKLDSWSVIVNGCVEVVKPSGERVEYKLGDSFGAEPTPATQIHIGEMRTMVDDCEFVLVEHRDFCSIMSTIGDHIEKDRDGLTGEVVSEVERRTVGTHCGQVLIKGKPDKLIHHLVDERDHNVDPHYVDDFLLTYRVFIRDPTTIFEKLMLWFADSIYRDKVARLVLLWVNNHFNDFETNDEMWNLLERFEGALERDGMHSQLSLLNIACSVKAKPRQVILTRRKDDKMMMRLVGGQESGNSVYVAEVFPDTSAAREGVKRADEMLEVNQQSAKYLSAKKAEDLLTGSLSLTLMLKNNVLGYKETIGKIEHNKPKNGTSRSGAGIPMVIPVHKTSITGKKSSTTSSKSGMMEKLMTILKSSKEDSMDFTDEAKISSADLRPSRSNPDITSISQYYGPVRSECPEHVLKIYRNDQTFKYLPVYKETSAQNVVQLALQEFNMTAEGSPEWSLCECTVTIDGVIKQRRLPPQMENLAERIALNSRYYLKNNSRSEPLVPDELAPELLKEAQTQLLSLNAQVVAAQLTLQDFSVFSAIEPTEFLDNLFKLDSKYGSPKLEEFEQLFNREMWWVATEICTERHVQKRAKLIKKFIKVARYCRDLRNFNSMFAIMSGLDKPAVRRLHSSWERVSSKYIRMLDEIHQLVDPSRNMSKYRQHLAEVAQEPPVVPIYPVIKKDLTFAHDGNATYSEKLINFEKLRLIAKSIRGVMKLSSAPYEIASMAERSGGVVMDALLHMNSFENSNVATMRKGMSGKQNQPRKKVYEQALMVRKVKSYLEGLHVVDNEMELDSMSYDIEPQVQTAHRGANSSSTANIRRVPSPTPSSLSSQSAGSADQSSRHRLLFNGTGSISSAGGGSKFGVESPQAVQKMLSLVQNSKVKGAPPQITSPSTSARSSLQRNMPRVTGRQATSSAQGPVQLNEETSTVTTYYQSDNGRRQRSGSEGRFDNIPPSTFYLTSDGLTVSPRQSLSVVIPTHPHGHSPTSPRCRSRSPASSGCSSFSTIASIAATSMAAAPSAFVSNPYQHHQTVRGHVIGHRPMPIVTSGSATLPNHVSPRGLPPKSRPTILPGSHTNSSSRMGTIKEATFLTSEQVSRV
Protein: cGMP-specific 3',5'-cyclic phosphodiesterase (EC 3.1.4.35) (cGMP-binding cGMP-specific phosphodiesterase) (CGB-PDE) (O76074)
Organism: Homo sapiens (Human)
Function: Plays a role in signal transduction by regulating the intracellular concentration of cyclic nucleotides. This phosphodiesterase catalyzes the specific hydrolysis of cGMP to 5'-GMP. Specifically regulates nitric-oxide-generated cGMP.
Interaction partners:
- cGMP-dependent 3',5'-cyclic phosphodiesterase
- Alpha-aminoadipic semialdehyde dehydrogenase
- Retinal rod rhodopsin-sensitive cGMP 3',5'-cyclic phosphodiesterase subunit gamma
- Adenine phosphoribosyltransferase
- GMP reductase 1
- Guanylate kinase
- Inosine triphosphate pyrophosphatase
- Hypoxanthine-guanine phosphoribosyltransferase
- GMP synthase
- Guanylate cyclase soluble subunit beta-1
Sequence:
MERAGPSFGQQRQQQQPQQQKQQQRDQDSVEAWLDDHWDFTFSYFVRKATREMVNAWFAERVHTIPVCKEGIRGHTESCSCPLQQSPRADNSAPGTPTRKISASEFDRPLRPIVVKDSEGTVSFLSDSEKKEQMPLTPPRFDHDEGDQCSRLLELVKDISSHLDVTALCHKIFLHIHGLISADRYSLFLVCEDSSNDKFLISRLFDVAEGSTLEEVSNNCIRLEWNKGIVGHVAALGEPLNIKDAYEDPRFNAEVDQITGYKTQSILCMPIKNHREEVVGVAQAINKKSGNGGTFTEKDEKDFAAYLAFCGIVLHNAQLYETSLLENKRNQVLLDLASLIFEEQQSLEVILKKIAATIISFMQVQKCTIFIVDEDCSDSFSSVFHMECEELEKSSDTLTREHDANKINYMYAQYVKNTMEPLNIPDVSKDKRFPWTTENTGNVNQQCIRSLLCTPIKNGKKNKVIGVCQLVNKMEENTGKVKPFNRNDEQFLEAFVIFCGLGIQNTQMYEAVERAMAKQMVTLEVLSYHASAAEEETRELQSLAAAVVPSAQTLKITDFSFSDFELSDLETALCTIRMFTDLNLVQNFQMKHEVLCRWILSVKKNYRKNVAYHNWRHAFNTAQCMFAALKAGKIQNKLTDLEILALLIAALSHDLDHRGVNNSYIQRSEHPLAQLYCHSIMEHHHFDQCLMILNSPGNQILSGLSIEEYKTTLKIIKQAILATDLALYIKRRGEFFELIRKNQFNLEDPHQKELFLAMLMTACDLSAITKPWPIQQRIAELVATEFFDQGDRERKELNIEPTDLMNREKKNKIPSMQVGFIDAICLQLYEALTHVSEDCFPLLDGCRKNRQKWQALAEQQEKMLINGESGQAKRN
Protein: Kv channel interacting protein 3, calsenilin (Kv channel-interacting protein 3b, calsenilin) (Q6PBP8)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
Sequence:
MQADGQKGVDGGLLPDANGRDGDSSGQKESDGKWQKPRITRKSLMKCCLVKWIIASAAPQGSNDSTDSELELSAVRHQPEGLEQLQAQTQFTRKELQSLYRGFKNECPSGLVDEETFKSIYSQFFPQGDATTYAHFLFNAFDMDRNGSIRFEDFVIGLSVLLRGSVTEKLRWAFNLYDINKDGYITKEEMLAIMKSIYDMMGRYTSPCVKDDAAFEHVEKFFQKMDRNRDGVVTLEEFIETCQKDENIMSSMQLFENVI
Protein: AT3g59470/T16L24_20 (Far-red impaired responsive (FAR1) family protein) (Q93Z68)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
Sequence:
MMMGIPVELEVTTVENHNEMGESSGQAMIEQDDDNHNELGENSGEQDEKVDLDSIPLAVADMTEAQGDEPYVGQEFESEAAAHGFYNAYATKVGFVIRVSKLSRSRHDGSPIGRQLVCNKEGYRLPSKRDKVIRQRAETRVGCKAMILIRKENSGKWVITKFVKEHNHSLMPGRVRRGCIYDQYPNEHDKIQELMQQLAAEKKRAATYKRHLEMLFEQIEQHNESLSKRIQHIVDNVRNLEQRDHQQNHQV
Protein: Aspartate--tRNA ligase, chloroplastic/mitochondrial (EC 6.1.1.12) (Aspartyl-tRNA synthetase) (AspRS) (F4JJT9)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Catalyzes the specific attachment of an amino acid to its cognate tRNA in a 2 step reaction: the amino acid (AA) is first activated by ATP to form AA-AMP and then transferred to the acceptor end of the tRNA.
Subcellular location: Plastid, chloroplast {ECO:0000269|PubMed:16251277}. Mitochondrion {ECO:0000269|PubMed:16251277}.
Interaction partners:
- Glutamyl-tRNA
- Aspartate--tRNA ligase 1, cytoplasmic
- Aspartate--tRNA ligase 2, cytoplasmic
- Histidine--tRNA ligase, chloroplastic/mitochondrial
- Outer envelope protein 64, chloroplastic
- GMP synthase
- eIF-2-alpha kinase GCN2
- histidine--tRNA ligase
- Histidine--tRNA ligase, cytoplasmic
- Outer envelope protein 64, mitochondrial
Sequence:
MSLLLRTLPLRPTRFLSATAISISNATNFFVVPKRTNPLPGTRRTFSSSPVAAASGDVVVKPVPSPPSVLRWVSRTELCGELSVNDVGKRVHLCGWVALHRVHGGLTFLNLRDHTGIVQVRTLPDEFPEAHGLINDMRLEYVVLVEGTVRSRPNESVNKKMKTGFVEVVAEHVEILNPVRTKLPFLVTTADENKDLIKEEIRLRFRCLDLRRQQMKNNIVLRHNVVKLIRRYLEDRHGFIEIETPILSRSTPEGARDYLVPSRIQSGTFYALPQSPQLFKQMLMVSGFDKYYQIARCFRDEDLRADRQPEFTQLDMEMAFMPMEDMLKLNEDLIRKVFSEIKGIQLPDPFPRLTYADAMDRYGSDRPDTRFDLELKDVSNVFTESSFRVFTEALESGGIIKVLCVPLGAKKYSNSALKKGDIYNEAMKSGAKGLPFLKVLDNGEIEGIAALVSSLDSAGKINFVKQCGAAPGDLILFGVGPVTSVNKTLDRLRLFVAHDMDLIDHSKHSILWVTDFPMFEWNEPEQRLEALHHPFTAPKPEDMDDLPSARALAYDMVYNGVEIGGGSLRIYKRDVQEKVLEIIGISPEEAESKFGYLLEALDMGAPPHGGIAYGLDRMVMMLGGASSIRDVIAFPKTTTAQCALTRTPSEVDPKQLQDLSIRTK
Protein: Master replication protein (M-Rep) (EC 2.7.7.-) (EC 3.1.21.-) (EC 3.6.1.-) (Q86567)
Organism: Banana bunchy top virus (isolate Autralia) (BBTV)
Function: Essential for the replication of all genomic viral ssDNA (trans-replication). The closed circular ssDNA genome is first converted to a superhelical dsDNA. Rep binds a specific hairpin at the genome origin of replication. Introduces an endonucleolytic nick within the conserved sequence 5'-A[GT]TATTAC-3' in the intergenic region of the genome, thereby initiating the rolling circle replication (RCR). Following cleavage, binds covalently to the 5'-phosphate of DNA as a tyrosyl ester. The cleavage gives rise to a free 3'-OH that serves as a primer for the cellular DNA polymerase. The polymerase synthesizes the (+) strand DNA by rolling circle mechanism. After one round of replication, a Rep-catalyzed nucleotidyl transfer reaction releases a circular single-stranded virus genome, thereby terminating the replication. Displays origin-specific DNA cleavage, nucleotidyl transferase, ATPase and helicase activities (By similarity).
Subcellular location: Host nucleus {ECO:0000305}.
Interaction partners:
Sequence:
MARYVVCWMFTINNPTTLPVMRDEIKYMVYQVERGQEGTRHVQGYVEMKRRSSLKQMRGFFPGAHLEKRKGSQEEARSYCMKEDTRIEGPFEFGSFKLSCNDNLFDVIQDMRETHKRPLEYLYDCPNTFDRSKDTLYRVQAEMNKTKAMNSWRTSFSAWTSEVENIMAQPCHRRIIWVYGPNGGEGKTTYAKHLMKTRNAFYSPGGKSLDICRLYNYEDIVIFDIPRCKEDYLNYGLLEEFKNGIIQSGKYEPVLKIVEYVEVIVMANFLPKEGIFSEDRIKLVSC
Protein: Heterogeneous nuclear ribonucleoprotein M (hnRNP M) (M4 protein) (Q62826)
Organism: Rattus norvegicus (Rat)
Function: Pre-mRNA binding protein, binds avidly to poly(G) and poly(U) RNA homopolymers. Involved in splicing. Acts as a receptor for carcinoembryonic antigen in Kupffer cells, may initiate a series of signaling events leading to tyrosine phosphorylation of proteins and induction of IL-1 alpha, IL-6, IL-10 and tumor necrosis factor alpha cytokines.
Subcellular location: Nucleus matrix {ECO:0000269|PubMed:16128803}.
Interaction partners:
- Heterogeneous nuclear ribonucleoprotein U
- Heterogeneous nuclear ribonucleoproteins A2/B1
- Heterogeneous nuclear ribonucleoprotein Q
- Heterogeneous nuclear ribonucleoprotein K
- Heterogeneous nuclear ribonucleoprotein A1
- Heterogeneous nuclear ribonucleoprotein F
- Heterogeneous nuclear ribonucleoproteins C1/C2-like
- Heterogeneous nuclear ribonucleoprotein H3
- Heterogeneous nuclear ribonucleoprotein H
- KH domain-containing, RNA-binding, signal transduction-associated protein 1
Sequence:
MAAGVEAAAEVAATEPKMEEESGAPCVPSGNGAPVPKGEERPTQNEKRKEKNIKRGGNRFEPYANPTKRYRAFITNIPFDVKWQSLKDLVKEKVGEVTYVELLMDAEGKSRGCAVVEFKMEESMKKAAEVLNKHSLSGRPLKVKEDPDGEHARRAMQKAGRLGSTVFVANLDYKVGWKKLKEVFSMAGVVVRADILEDKDGKSRGIGTVTFEQSIEAVQAISMFNGQLLFDRPMHVKMDERALPKGDFFPPERPQQLPHGLGGIGMGLGPGGQPIDANHLNKGIGMGNLGPAGMGMEGIGFGINKIGGMEGPFGGGMENMGRFGSGMNMGRINEILSNALKRGEIIAKQGGSGAGGSVPGIERMGPGIDRISGAGMERMGAGLGHGMDRVGSEIERMGLVMDRMGSVERMGSGIERMGPLGLDHMASSIERMGQTMERIGSGVERMGAGMGFGLERMAAPIDRVGQTIERMGSGVERMGPAIERMGLSMDRMVPTGMGAGLERMGPVMDRMATGLERMGANNLERMGLERMGANSLERMGLERMGANSLERMGPAMGPALGAGIERMGLAMGGAGGASFDRTIEMERGNFGGSFAGSFGGAGGHAPGVARKACQIFVRNLPFDFTWKMLKDKFNECGHVLYADIKMENGKSKGCGVVKFESPEVAERACRMMNGMKLSGREIDVRIDRNA
Protein: Uncharacterized fimbrial chaperone YbgP (P75749)
Organism: Escherichia coli (strain K12)
Function: Could be required for the biogenesis of the putative YbgD fimbria.
Subcellular location: Periplasm {ECO:0000250}.
Interaction partners:
- Uncharacterized outer membrane usher protein YbgQ
- Uncharacterized fimbrial-like protein YbgD
- Cell division protein YtfB
- Uncharacterized protein YbgO
- Outer membrane usher protein SfmD
- Outer membrane usher protein HtrE
- Uncharacterized outer membrane usher protein YhcD
- Outer membrane usher protein YraJ
- Outer membrane usher protein FimD
- Probable outer membrane usher protein ElfC
Sequence:
MTFIKGLPLMLLTISLGCNAAVQPDRTRIVFNANDKATSLRIENQSDKLPYLAYSWIENEKGEKSDALLVALPPIQRLEPKATSQVRVVKQASTTQLPGDRETLFFYNMREIPPAPDKSSDHAILQVAIQSRIKLFWRPAALRKKAGEKVELQLQVSQQGNQLTLKNPTAYYLTIAYLGRNEKGVLPGFKTVMVAPFSTVNTNTGSYSGSQFYLGYMDDYGALRMTTLNCSGQCRLQAVEAK
Protein: TLE family member 5 (Amino-terminal enhancer of split) (Amino enhancer of split) (Gp130-associated protein GAM) (Grg-5) (Groucho-related protein 5) (Protein ESP1) (Protein GRG) (TLE family member 5, transcriptional modulator) (Q08117)
Organism: Homo sapiens (Human)
Function: Transcriptional corepressor. Acts as dominant repressor towards other family members. Inhibits NF-kappa-B-regulated gene expression. May be required for the initiation and maintenance of the differentiated state. Essential for the transcriptional repressor activity of SIX3 during retina and lens development.
Subcellular location: Nucleus {ECO:0000250}.
Interaction partners:
- Transducin-like enhancer protein 3
- Transducin-like enhancer protein 1
- Transducin-like enhancer protein 4
- Peptidyl-tRNA hydrolase 2, mitochondrial
- Transducin-like enhancer protein 2
- Protein ripply1
- Transducin-like enhancer protein 7
- Homeobox protein VENTX
- Transducin-like enhancer protein 6
- Homeobox protein SIX6
Sequence:
MMFPQSRHSGSSHLPQQLKFTTSDSCDRIKDEFQLLQAQYHSLKLECDKLASEKSEMQRHYVMYYEMSYGLNIEMHKQAEIVKRLNGICAQVLPYLSQEHQQQVLGAIERAKQVTAPELNSIIRQQLQAHQLSQLQALALPLTPLPVGLQPPSLPAVSAGTGLLSLSALGSQAHLSKEDKNGHDGDTHQEDDGEKSD
Protein: ADP,ATP carrier protein (ADP/ATP translocase) (Adenine nucleotide translocator) (ANT) (Stress-sensitive protein B) (Q26365)
Organism: Drosophila melanogaster (Fruit fly)
Function: ADP:ATP antiporter that mediates import of ADP into the mitochondrial matrix for ATP synthesis, and export of ATP out to fuel the cell (By similarity). Cycles between the cytoplasmic-open state (c-state) and the matrix-open state (m-state): operates by the alternating access mechanism with a single substrate-binding site intermittently exposed to either the cytosolic (c-state) or matrix (m-state) side of the inner mitochondrial membrane (By similarity).
Subcellular location: Mitochondrion inner membrane {ECO:0000269|PubMed:7520869}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Cytochrome c-2
- ATP synthase subunit alpha, mitochondrial
- GH02075p
- Voltage-dependent anion-selective channel
- Cytochrome b-c1 complex subunit Rieske, mitochondrial
- Probable citrate synthase, mitochondrial
- Mitochondrial-processing peptidase subunit beta
- Citrate transport protein
- Small ribosomal subunit protein uS12m
- Cytochrome c-1
Sequence:
MGNISASITSQSKMGKDFDAVGFVKDFAAGGISAAVSKTAVAPIERVKLLLQVQHISKQISPDKQYKGMVDCFIRIPKEQGFSSFWRGNLANVIRYFPTQALNFAFKDKYKQVFLGGVDKNTQFWRYFAGNLASGGAAGATSLCFVYPLDFARTRLAADTGKGGQREFTGLGNCLTKIFKSDGIVGLYRGFGVSVQGIIIYRAAYFGFYDTARGMLPDPKNTPIYISWAIAQVVTTVAGIVSYPFDTVRRRMMMQSGRKATEVIYKNTLHCWATIAKQEGTGAFFKGAFSNILRGTGGAFVLVLYDEIKKVL
Protein: Mannan endo-1,4-beta-mannosidase 6 (EC 3.2.1.78) (Beta-mannanase 6) (Endo-beta-1,4-mannanase 6) (AtMAN6) (Q9LZV3)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Secreted {ECO:0000305}.
Interaction partners:
- Bifunctional fucokinase/GDP-fucose pyrophosphorylase
- Uncharacterized GPI-anchored protein At1g61900
- Mannosyl-oligosaccharide 1,2-alpha-mannosidase MNS3
- Mannosyl-oligosaccharide 1,2-alpha-mannosidase MNS2
- Berberine bridge enzyme-like 11
- Hexokinase-4
- Hexokinase-like 1 protein
- Probable hexokinase-like 2 protein
- Hexokinase-3
- Hexokinase-1
Sequence:
MKDQLGFRIVLCSAVFIILTQNRALADLDSESHEVNSESVGEEQWEMVQRKGMQFTLNGQPFYVNGFNTYWMMTLAADNSTRGKVTEVFQQASAVGMTVGRTWAFNDGQWRALQKSPSVYDEEVFKALDFVLSEARKYKIRLILSLVNNWDAYGGKAQYVKWGNASGLNLTSDDDFFTNPTLRNFYQSHVRTVLNRVNTFTNITYKNDPTIFAWELMNEPRCPSDPSGDKLQSWIQEMAVFVKSLDAKHLVEIGLEGFYGPSAPARTRFNPNPYAAQVGTDFIRNNQVLGIDFASVHVYPDSWISPAVSNSFLEFTSSWMQAHVEDAEMYLGMPVLFTEFGVSAHDPGFNTSFRDMMLNTVYKMTLNSTRKGGAGAGSLVWQVFPQGAEFMDDGYAVYLTRAHTASKIISLQSKRLAIFNSLCSWRCRWGCKKKNQTALDALLSHDEL
Protein: S-adenosylmethionine-dependent methyltransferase UmaA (SAM-dependent methyltransferase UmaA) (EC 2.1.1.-) (Q6MX39)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: Methyltransferase that modifies short-chain fatty acids. In vitro, catalyzes the transfer of the methyl group from S-adenosyl-L-methionine (SAM) to the double bond of phospholipid-linked oleic acid to produce tuberculostearic acid (10-methylstearic-acid or TSA).
Subcellular location: Cytoplasm {ECO:0000269|PubMed:23435098}.
Interaction partners:
Sequence:
MTELRPFYEESQSIYDVSDEFFSLFLDPTMAYTCAYFEREDMTLEEAQNAKFDLALDKLHLEPGMTLLDIGCGWGGGLQRAIENYDVNVIGITLSRNQFEYSKAKLAKIPTERSVQVRLQGWDEFTDKVDRIVSIGAFEAFKMERYAAFFERSYDILPDDGRMLLHTILTYTQKQMHEMGVKVTMSDVRFMKFIGEEIFPGGQLPAQEDIFKFAQAADFSVEKVQLLQQHYARTLNIWAANLEANKDRAIALQSEEIYNKYMHYLTGCEHFFRKGISNVGQFTLTK
Protein: Receptor activity-modifying protein 1 (Calcitonin-receptor-like receptor activity-modifying protein 1) (CRLR activity-modifying protein 1) (O60894)
Organism: Homo sapiens (Human)
Function: Transports the calcitonin gene-related peptide type 1 receptor (CALCRL) to the plasma membrane. Acts as a receptor for calcitonin-gene-related peptide (CGRP) together with CALCRL.
Subcellular location: Cell membrane {ECO:0000269|PubMed:33602864}; Single-pass type I membrane protein {ECO:0000269|PubMed:33602864}.
Interaction partners:
- Calcitonin receptor
- Calcitonin gene-related peptide type 1 receptor
- Calcitonin gene-related peptide 2
- Pro-adrenomedullin
- Islet amyloid polypeptide
- Calcitonin
- DNA-directed RNA polymerase III subunit RPC9
- Guanine nucleotide-binding protein G
- Receptor activity-modifying protein 3
- Receptor activity-modifying protein 2
Sequence:
MARALCRLPRRGLWLLLAHHLFMTTACQEANYGALLRELCLTQFQVDMEAVGETLWCDWGRTIRSYRELADCTWHMAEKLGCFWPNAEVDRFFLAVHGRYFRSCPISGRAVRDPPGSILYPFIVVPITVTLLVTALVVWQSKRTEGIV
Protein: N-terminal Xaa-Pro-Lys N-methyltransferase 1 (EC 2.1.1.244) (Alpha N-terminal protein methyltransferase 1A) (Methyltransferase-like protein 11A) (X-Pro-Lys N-terminal protein methyltransferase 1A) (S4R3J7)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MTSEVIEDEKQFYSKAKTYWKQIPPTVDGMLGGYGHISSIDINSSRKFLQRFLRVGRSGVLSRRGCGSGGTAESMWGATFYTCNTAGLLAISWYLPQSLEELGWVGTVG