wanglab/gogpt-training-data huggingface dataset:
Protein: Glutamate decarboxylase 1 (Glutamic acid decarboxylase) (G5EDB7)
Organism: Caenorhabditis elegans
Interaction partners:
- Vesicular GABA transporter
- Probable 4-aminobutyrate aminotransferase, mitochondrial
- Cysteine dioxygenase 1
- Glutamate dehydrogenase
- Alanine--glyoxylate aminotransferase 2, mitochondrial
- Aldehyde dehydrogenase
- Aldehyde dehydrogenase
- Aldehyde dehydrogenase domain-containing protein
- Aldehyde dehydrogenase domain-containing protein
- Multifunctional fusion protein
Sequence:
MSSAAADESDAVLENLIAKEILPQTGNWEGTEEFLNRIVQVLLKYIKDQNDRDQKILEFHHPDKMQMLMDLSIPEKPESLLKLVKSCEDVLRLGVRTGHPRFFNQISCGLDLVSMAGEWLTATANTNMFTYEIAPVFILMEKSVMARMWEAVGWDPEKADGIFAPGGAIANLYAMNAARHQLWPRSKHLGMKDIPTLCCFTSEDSHYSIKSASAVLGIGADYCFNIPTDKNGKMIPEALEAKIIECKKEGLTPFFACCTAGSTVYGAFDPLERVANICERHKLWFHVDAAWGGGMLLSPEHRYKLAGIERANSVTWNPHKLMGALLQCSACLFRQDGLLFQCNQMSADYLFQQDKPYDVSFDTGDKAIQCGRHNDVFKLWLMWKSKGMEGYRQQINKLMDLANYFTRRIKETEGFELIIENPEFLNICFWYVPSKIRNLEPAEMRARLEKIAPKIKAGMMQRGTTMVGYQPDKQRPNFFRMIISNQAITREDLDFLIKEIVDIGESLE
Protein: Secretagogin (Q5XJX1)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Cytoplasm {ECO:0000250}.
Interaction partners:
- Synaptosomal-associated protein 25-A
- Calcium-binding protein 1b
- Myeloid leukemia factor 2
- Ciliary rootlet coiled-coil, rootletin family member 2
- Dimethylarginine dimethylaminohydrolase 2
- ADP-ribosylation factor GTPase-activating protein 2.
Sequence:
MDSAFANLDAAGFLQIWQHFDADDNGYIEGKELDDFFRHMLKKLQPKDKITDERVQQIKKSFMSAYDATFDGRLQIEELANMILPQEENFLLIFRREAPLDNSVEFMKIWRKYDADSSGYISAAELKNFLKDLFLQHKKKIPPNKLDEYTDAMMKIFDKNKDGRLDLNDLARILALQENFLLQFKMDASSQVERKRDFEKIFAHYDVSRTGALEGPEVDGFVKDMMELVRPSISGGDLDKFRECLLTHCDMNKDGKIQKSELALCLGLKHKP
Protein: Protein DEFECTIVE IN EXINE FORMATION 1 (F4IYM4)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Required for exine pattern formation during pollen development, especially for primexine deposition.
Subcellular location: Cell membrane {ECO:0000255}; Single-pass type I membrane protein {ECO:0000255}.
Interaction partners:
- No exine formation 1
- ATP-dependent helicase/deoxyribonuclease subunit B
- Cytochrome P450 703A2
- Bidirectional sugar transporter SWEET8
- ABC transporter G family member 26
- Callose synthase 5
- Transcription factor DYT1
- Cytochrome P450 704B1
- Transcription factor MYB80
- Short-chain dehydrogenase reductase ATA1
Sequence:
MKSRARQCLLVCLLCLSLTNLSYGENKFRERKATDDELGYPDIDEDALLNTQCPKKLELRWQTEVTSSVYATPLIADINSDGKLDIVVPSFVHYLEVLEGADGDKMPGWPAFHQSNVHSSPLLFDIDKDGVREIALATYNAEVLFFRVSGFLMSDKLEVPRRKVHKNWHVGLNPDPVDRSHPDVHDDVLEEEAMAMKSSTTQTNATTTTPNVTVSMTKEVHGANSYVSTQEDQKRPENNQTEAIVKPTPELHNSSMDAGANNLAANATTAGSRENLNRNVTTNEVDQSKISGDKNETVIKLNTSTGNSSETLGTSGNSSTAETVTKSGRRLLEEDGSKESVDSHSDSKDNSEGVRMATVENDGGLEADADSSFELLRENDELADEYSYDYDDYVDEKMWGDEEWVEGQHENSEDYVNIDAHILCTPVIADIDKDGVQEMIVAVSYFFDPEYYDNPEHLKELGGIDIKNYIASSIVVFNLDTKQVKWIKELDLSTDKANFRAYIYSSPTVVDLDGDGYLDILVGTSFGLFYAMDHRGNIREKFPLEMAEIQGAVVAADINDDGKIELVTTDSHGNIAAWTTQGVEIWEAHLKSLVPQGPSIGDVDGDGHTEVVVPTSSGNIYVLSGKDGSIVRPYPYRTHGRVMNQLLLVDLNKRGEKKKGLTIVTTSFDGYLYLIDGPTSCTDVVDIGETSYSMVLADNVDGGDDLDLIVSTMNGNVFCFSTPSPHHPLKAWRSSDQGRNNKANRYDREGVFVTHSTRGFRDEEGKNFWAEIEIVDKYRYPSGSQAPYNVTTTLLVPGNYQGERRITQSQIYDRPGKYRIKLPTVGVRTTGTVMVEMADKNGLHFSDEFSLTFHMYYYKLLKWLLVLPMLGMFGLLVILRPQEAVPLPSFSRNTDL
Protein: HTH-type transcriptional regulator PecS (P42195)
Organism: Dickeya dadantii (strain 3937) (Erwinia chrysanthemi (strain 3937))
Function: Negative regulator of pectinase, cellulase, blue pigment production and virulence genes. Also binds to promoter sites in the pecS-pecM intergenic region and negatively autoregulate its expression as well as that of pecM.
Subcellular location: Cytoplasm {ECO:0000305|PubMed:9194707}.
Interaction partners:
- Protein PecM
- Uncharacterized protein
Sequence:
MARYLEVSDIVQQWRNERPDLDVEPMLVIGTLSRVSLLIDRALDKVFSKYKLSAREFDILATLRRRGAPYAISPSQIVNALMINNSTLTSRLDRLEQAGWLRRMPIEGDRRSVNIQLTDEGFALINRVVEEHVENERDILSPFSEEEKTHLRALLGRVEKHLVNNR
Protein: PABC domain-containing protein (Q3TUS5)
Organism: Mus musculus (Mouse)
Interaction partners:
Sequence:
MRPNPRWQQGGRPQGFQGMPSALRQSGPRPALRHLAPTGNAPASRGLPTTAQRVGSECPDRLAMDFGGAGAAQQGLTDSCQSGGVPTAVPNLAPRAAVAAAAPRAVAPYKYASSVRSPHPAIQPLQAPQPAVHVQGQEPLTASMLAAAPPQEQKQMLGERLFPLIQTMHSNLAGKITGMLLEIDNSELLHMLESPESLRSKVDEAVAVLQAHHAKKEAAQKVGHCCCCYLLDKKKSRKPNNPSWHPAKV
Protein: Small conductance calcium-activated potassium channel protein 3 (SK3) (SKCa 3) (SKCa3) (KCa2.3) (P58391)
Organism: Mus musculus (Mouse)
Function: Forms a voltage-independent potassium channel activated by intracellular calcium. Activation is followed by membrane hyperpolarization (By similarity). Thought to regulate neuronal excitability by contributing to the slow component of synaptic afterhyperpolarization (By similarity).
Subcellular location: Cell membrane {ECO:0000269|PubMed:11557517}; Multi-pass membrane protein {ECO:0000255}. Cytoplasm, myofibril, sarcomere, Z line {ECO:0000269|PubMed:20689065}.
Interaction partners:
- Calcium-activated potassium channel subunit beta-4
- Calcium-activated potassium channel subunit beta-1
- Calcium-activated potassium channel subunit beta-2
- Small conductance calcium-activated potassium channel protein 2
- Intermediate conductance calcium-activated potassium channel protein 4
- Potassium channel subfamily U member 1 current)
- Protein kinase C beta type
- Protein kinase C gamma type
- Protein kinase C alpha type
- Calcium-activated potassium channel subunit beta
Sequence:
MDTSGHFHDSGVGDLDEDPKCPCPSSGDEQQQQQQPPPPPAPPAVPQQPPGPLLQPQPPQPQQQQSQQQQQQQSQQQQQQAPLHPLPQLAQLQSQLVHPGLLHSSPTAFRAPTSANSTAILHPSSRQGSQLNLNDHLLGHSPSSTATSGPGGGSRHRQASPLVHRRDSNPFTEIAMSSCKYSGGVMKPLSRLSASRRNLIEAEPEGQPLQLFSPSNPPEIIISSREDNHAHQTLLHHPNATHNHQHAGTTAGSTTFPKANKRKNQNIGYKLGHRRALFEKRKRLSDYALIFGMFGIVVMVIETELSWGLYSKDSMFSLALKCLISLSTVILLGLIIAYHTREVQLFVIDNGADDWRIAMTYERILYISLEMLVCAIHPIPGEYKFFWTARLAFSYTPSRAEADVDIILSIPMFLRLYLIARVMLLHSKLFTDASSRSIGALNKINFNTRFVMKTLMTICPGTVLLVFSISLWIIAAWTVRVCERYHDQQDVTSNFLGAMWLISITFLSIGYGDMVPHTYCGKGVCLLTGIMGAGCTALVVAVVARKLELTKAEKHVHNFMMDTQLTKRIKNAAANVLRETWLIYKHTKLLKKIDHAKVRKHQRKFLQAIHQLRGVKMEQRKLSDQANTLVDLSKMQNVMYDLITELNDRSEDLEKQIGSLESKLEHLTASFNSLPLLIADTLRQQQQQLLTAFVEARGISVAVGTSHAPPSDSPIGISSTSFPTPYTSSSSC
Protein: Tachykinin-related peptide 6 (TKRP-6) (P86568)
Organism: Banasa dimiata (Banasa stink bug) (Pentatoma dimiata)
Subcellular location: Secreted {ECO:0000269|PubMed:19084564, ECO:0000305}.
Interaction partners:
Sequence:
APSMGFMGMR
Protein: 3',5'-cyclic-AMP phosphodiesterase, isoform I (EC 3.1.4.53) (Learning/memory process protein) (Protein dunce) (cAMP-specific phosphodiesterase, isoform I) (Q9W4T4)
Organism: Drosophila melanogaster (Fruit fly)
Function: Hydrolyzes the second messenger cAMP, which is a key regulator of many important physiological processes (By similarity). Vital for female fertility. Required for learning/memory.
Interaction partners:
- Adenylate cyclase 1
- Adenylate kinase 2
- Adenosine kinase
- Adenosine kinase
- Adenosine kinase
- AMP deaminase
- GTP:AMP phosphotransferase, mitochondrial
- Adenine phosphoribosyltransferase
- Uncharacterized protein, isoform C
- 5'-nucleotidase
Sequence:
MMRLARFTQGFSFNKNVAKHRGSGSSNGTGNGSGTGNGQGLGGSCSANGLAATGGVGGGGGSGSGGGGCGSGSGSGSGKRKSKARTKCFGGTVFRCCLPCRGGGSAAPATSPPQTPAQTPDELKVIPEDCNLEKSAEQKRDLLERNNKEDDLLNRTVSGSELDLYGGAGGGTKKHSLADTIDTSVTTPISLKTLINDVDEELDQQLSAADIAAASLASGLVARRAEPETLSDASVSPTAVVQQQQQQQQQLQQPLLQSQPHFVPSSGNILSQVTLYSGSNPSTNPCQSAVQNQGQNSNPNPNQNPNTNPNQNQQRCSCQPQTSPLPHIKEEEESDQANFKHQTSLKEHQPLPPPITIATGYCGSCESVHHSSATSSSAGTVPPGGQQTQEYIAGTSSTPSPRIKLKFRKPHKSCWSRIVLAPIGSAGGSSSATTVIGSNSNETLASSSTTGGTATTTQNSSSVSVAAHHRLTSSSASALATSHPSNSQLLPTSKMQAEQGSIGDLQKYHSRYLKNRRHTLANVRFDVENGQGARSPLEGGSPSAGLVLQNLPQRRESFLYRSDSDFEMSPKSMSRNSSIASERFKEQEASILVDRSHGEDLIVTPFAQILASLRSVRNNLLSLTNVPASNKSRRPNQSSSASRSGNPPGAPLSQGEEAYTRLATDTIEELDWCLDQLETIQTHRSVSDMASLKFKRMLNKELSHFSESSRSGNQISEYICSTFLDKQQEFDLPSLRVEDNPELVAANAAAGQQSAGQYARSRSPRGPPMSQISGVKRPLSHTNSFTGERLPTFGVETPRENELGTLLGELDTWGIQIFSIGEFSVNRPLTCVAYTIFQSRELLTSLMIPPKTFLNFMSTLEDHYVKDNPFHNSLHAADVTQSTNVLLNTPALEGVFTPLEVGGALFAACIHDVDHPGLTNQFLVNSSSELALMYNDESVLENHHLAVAFKLLQNQGCDIFCNMQKKQRQTLRKMVIDIVLSTDMSKHMSLLADLKTMVETKKVAGSGVLLLDNYTDRIQVLENLVHCADLSNPTKPLPLYKRWVALLMEEFFLQGDKERESGMDISPMCDRHNATIEKSQVGFIDYIVHPLWETWADLVHPDAQDILDTLEENRDYYQSMIPPSPPPSGVDENPQEDRIRFQVTLEESDQENLAELEEGDESGGESTTTGTTGTTAASALSGAGGGGGGGGGMAPRTGGCQNQPQHGGM
Protein: DnaJ protein homolog xdj1 (O94657)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Endoplasmic reticulum membrane {ECO:0000305}; Lipid-anchor {ECO:0000305}.
Interaction partners:
- Uncharacterized J domain-containing protein C17A3.05c
- Presequence translocated-associated motor subunit pam17
- Mitochondrial protein import protein mas5
- Probable heat shock protein ssa2
- Probable heat shock protein ssa1
- Protein psi1
- Endoplasmic reticulum chaperone BiP
- Heat shock protein homolog pss1
- Oxidation resistance protein 1
- Heat shock protein 70 homolog C57A7.12
Sequence:
MVVDTKLYDILEVHFEASAEEIKKSYKRLALLHHPDKAPIHEKEEAAERFRGVQEAYDILKDPESREMYDMYGMNSDSNSQFDGGVNLDDVLAQMFGMNFEAGGPGKNVPRDRKRRGSDVIHDYEISLEDMFKGKEVKLRATRNTLCPRCQGRGGKRFAKEKPCLSCDGKGVKQHLKHVGPHHVTNSQVICDTCNGKGVSFRGKDRCKHCKGSGTVPEQRMLSFFVNRSAKENDKIIQRGMADEAYGITPGDVILQLHQKPHPVFERLGDDLKAKLKISLAEALTGFNRVILTTLDGRGLEYVQPIGKILHPGDCLIIPGEGMYKDSKTDLRGDLYLEVDIEFPKDGLIGTTEIEILRDILPSIPKVSVMDDTLIDSVRGVPGDISHFGGDARYANEDYGDETYEGVPECQAQ
Protein: Plasmolipin (Plasma membrane proteolipid) (A3KQ86)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:Q9Y342}; Multi-pass membrane protein {ECO:0000255}. Myelin membrane {ECO:0000250|UniProtKB:P47987}; Multi-pass membrane protein {ECO:0000255}. Apical cell membrane {ECO:0000269|PubMed:25706235}; Multi-pass membrane protein {ECO:0000255}. Recycling endosome membrane {ECO:0000269|PubMed:25706235}; Multi-pass membrane protein {ECO:0000255}. Vesicle {ECO:0000269|PubMed:25706235}. Note=In polarized cells, localized predominantly in the apical membrane (PubMed:25706235). Located in lipid raft (By similarity). Recycled between the plasma membrane and the Golgi complex (By similarity). PLLP is continuously recirculating in the cell (By similarity). {ECO:0000250|UniProtKB:P47987, ECO:0000250|UniProtKB:Q9Y342, ECO:0000269|PubMed:25706235}.
Interaction partners:
- Neuromast-expressed gpi-anchored lymphocyte antigen 6
- Calcium/calmodulin-dependent protein kinase kinase 1, alpha b
Sequence:
MADFPGKVSTQTSSQEPQRSFAISSSVDMGFIKSIPGILLIAEIVVGLLVWTLIASTPHYLIPALGWVLFVSITLWLLSIALLVILLLSLHQRLPSVPWPLVLLVFYSVAALLYLTAFLANAATVPGGYYQGHLGASAFFGIVETLLYTASSYFAYLGWRGEGQNAAGSTVPV
Protein: B-related factor 1 (F1R9S3)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- TATA-box-binding protein
- General transcription factor 3C polypeptide 3
- Zgc:162472.
- DNA-directed RNA polymerase III subunit RPC6
- Transcription factor IIIB 50 kDa subunit
- DNA-directed RNA polymerase subunit
- DNA-directed RNA polymerase subunit beta
- DNA-directed RNA polymerases I, II, and III subunit RPABC4
- DNA-directed RNA polymerase III subunit RPC3
- RNA polymerase I and III subunit C.
Sequence:
MGRCKTCGGTDIDVDQARGVAVCMGCGSVLEDNIIVSEVTFVESGGGGSSAVGQFVAGDASGNVPSLGGNFQTSVGRESRAATLQNAKRQINHLGHQLQMNQHCLDTAFNFYKMALSKHLTKGRKSTHVIAACLYLVCRTEGTPHMLLDLSDLLQVNVYVLGKTFLVLARELCINAPAIDPCLYIPRFAQLLEFGEKSHEVSMTALRLLQRMKRDWMHTGRRPSGLCGAALLVAARMHEFRRTIKEVISVVKVCEATLRKRLYEFEDTPTSELTIEEFMKTDLEQECDPPSFTAGLRKQKLKQIEQELAKKVDDIEGEICGYQDEIEVELESCRPKARGIYASCSREDDVVSLASSSHLDGEDDELRAAASHLCGENEEQEQDGERVSLTKRPSLSLLLGALPTSASLGLSESITKMGEEKENDVEAEGGELDLSGIDEDEIDRYILNDKEVKVKTELWMIQNADYLKEQKEKEERIAKEKEEGTYKERKPRKSTRRREPINANTADEAIEKMLEQKRISTKINYDVLKDLNKSSPKSPTRQPEEASAGAKRTPAARQRKPQLTSPDIGKTVSSFGKRLQPLVRAQPSKKLALDQIGSSVPVATPAVSAQTAVVVESGPVAYEEHADEEEEDEEDEHCVSAMQLMGGTSDYGYELDDDDGF
Protein: Caspase 2 L homeolog (EC 3.4.22.55) (Caspase-2) (Q9IB67)
Organism: Xenopus laevis (African clawed frog)
Interaction partners:
Sequence:
MLGGMQQHHRKALQRLRVSLASEMIIEELLDHLVSSEILTNNMHSNIMAYRSDYAQNVALLNLLPKRGPRAFSAFCNALHSTNQEHLAQQVEKEALLQEEFITSKVHHGSFPLPVQESTLSRPGRQICREYREESIDDGDGPVTVQLCSVNFYITHCQQAYKMHSCPRGRALLISNVKFETPDLDYRCGGEVDLASLEKLFSSLGYQVDVRCNLNAQSMMSQLGAFSALPVHSALDSCVVAILSHGLDGAVYGTDGKLVQLQEVFTALDNAHCPQLQNKPKMFFIQACRGEETDRGVDQRDGREQSGSPGCEQSDAGREDIKVRLPTQSDMICAYACLKGTVSLRNTKRGSWFVQDLVSVFSQHSKDTHVADMLVKVNALIKEREGHAPGTEFHRCKEMSEYCSTLCRDLYLFPGSPSNGLPK
Protein: F-actin-capping protein subunit alpha-1 (Beta-actinin subunit I) (CapZ 36/32) (P13127)
Organism: Gallus gallus (Chicken)
Function: F-actin-capping proteins bind in a Ca(2+)-independent manner to the fast growing ends of actin filaments (barbed end) thereby blocking the exchange of subunits at these ends. Unlike other capping proteins (such as gelsolin and severin), these proteins do not sever actin filaments. May play a role in the formation of epithelial cell junctions (By similarity). Forms, with CAPZB, the barbed end of the fast growing ends of actin filaments in the dynactin complex and stabilizes dynactin structure. The dynactin multiprotein complex activates the molecular motor dynein for ultra-processive transport along microtubules (By similarity).
Subcellular location: Cytoplasm, myofibril, sarcomere, Z line {ECO:0000269|PubMed:2762296}. Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:A0PFK5}. Note=CapZ is located at the Z line in muscle. {ECO:0000269|PubMed:2762296}.
Interaction partners:
- F-actin-capping protein subunit beta isoforms 1 and 2
- Protein S100-B
- Dynactin subunit 2
- F-actin-capping protein subunit alpha-2
- F-actin-capping protein subunit alpha
- Dynactin subunit 1
- Uncharacterized protein.
- ARP1 actin-related A, centractin alpha
- Dynactin subunit 4
- Dynactin subunit 5
Sequence:
MADFEDRVSDEEKVRIAAKFITHAPPGEFNEVFNDVRLLLNNDNLLREGAAHAFAQYNMDQFTPVKIEGYDDQVLITEHGDLGNGRFLDPRNKISFKFDHLRKEASDPQPEDTESALKQWRDACDSALRAYVKDHYPNGFCTVYGKSIDGQQTIIACIESHQFQPKNFWNGRWRSEWKFTITPPTAQVAAVLKIQVHYYEDGNVQLVSHKDIQDSVQVSSDVQTAKEFIKIIENAENEYQTAISENYQTMSDTTFKALRRQLPVTRTKIDWNKILSYKIGKEMQNA
Protein: Zinc-regulated GTPase metalloprotein activator 1 (EC 3.6.5.-) (Cobalamin synthase W domain-containing protein 1) (COBW domain-containing protein 1) (Q8VEH6)
Organism: Mus musculus (Mouse)
Function: Zinc chaperone that directly transfers zinc cofactor to target metalloproteins, thereby activating them. Catalyzes zinc insertion into the active site of methionine aminopeptidase METAP1, which function to cleave the initiator methionine from polypeptides during or after protein translation. Mechanistically, the N-terminal psi-PxLVp motif binds to the C6H2-type zinc finger of inactive form of METAP1. After formation of the docked complex, zinc is transferred from the CXCC motif in the GTPase domain of ZNG1 to the zinc binding site in the peptidase domain of METAP1 in a process requiring GTP hydrolysis. GTP/GDP exchange is required for release of active METAP1.
Subcellular location: Nucleus {ECO:0000269|PubMed:31862704}.
Interaction partners:
- Methionine aminopeptidase 1
- Large ribosomal subunit protein bL33m
- Radical S-adenosyl methionine domain-containing protein 1, mitochondrial
- Small ribosomal subunit protein uS14
- Small ribosomal subunit protein uS14m
Sequence:
MLPAVKTVEAEEEYAEDCPELVPIETKNQEEENLDFITKIPVTIVTGYLGAGKTTLLNYILTEQHNRKIAVILNEFGEGSAVEKSLAVSQGGELYEEWLELRNGCLCCSVKDSGLRAIENLMQKKGKFDYILLETTGLADPGAVASMFWVDAELGSDIYLDGIITVVDSKYGLKHLTEEKPDGLVNEATRQVALADMILINKTDLVSEEELNNLRTTIRSINGLGKVLETQRSRVHLSNILDLHAYDILSGISLQKKLQHVSTAPHLDQSIVTVTFEVPGSAKEECLNVFIQNLLWEKNVKNKDGHCMEVIRLKGLVSIKDKPQQMIVQGIHELYDLEESLVNWKDDAERACQLVFIGRNLDKDVLQQLFLTAVAEAEEQRTAPGRDGVCPSH
Protein: Uncharacterized protein (Q386G8)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MKPEGAKGAVVSDDVGGDSANLAYCSDRITLLSRADIEAFTCCSNGAGGGGASNSENHNGGCGGLASEAQSVDPCSTLDTCIAALPMFLQSEALVLRRHEQQFRHHMKELVELTECITLLCDGSLRQHAAAVAGQPAEQSADAQRAESAALHRMLHRAEELERYVRAAAVERLRSAQRMVLAASTTKRREKVGRKSAVRPPKATK
Protein: Glutamine-dependent NAD(+) synthetase (EC 6.3.5.1) (NAD(+) synthase [glutamine-hydrolyzing]) (P9WJJ3)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: Catalyzes the ATP-dependent amidation of deamido-NAD to form NAD. Uses L-glutamine as a nitrogen source. In vitro, can also use ammonia with comparable specific activity.
Interaction partners:
- Probable nicotinate-nucleotide adenylyltransferase
- Possible transcriptional regulatory protein NadR
- NAD-dependent protein deacylase
- NAD kinase
- NAD-capped RNA hydrolase NudC
- Probable soluble pyridine nucleotide transhydrogenase
- GMP synthase
- NAD
- proton-translocating NAD
- NAD
Sequence:
MNFYSAYQHGFVRVAACTHHTTIGDPAANAASVLDMARACHDDGAALAVFPELTLSGYSIEDVLLQDSLLDAVEDALLDLVTESADLLPVLVVGAPLRHRHRIYNTAVVIHRGAVLGVVPKSYLPTYREFYERRQMAPGDGERGTIRIGGADVAFGTDLLFAASDLPGFVLHVEICEDMFVPMPPSAEAALAGATVLANLSGSPITIGRAEDRRLLARSASARCLAAYVYAAAGEGESTTDLAWDGQTMIWENGALLAESERFPKGVRRSVADVDTELLRSERLRMGTFDDNRRHHRELTESFRRIDFALDPPAGDIGLLREVERFPFVPADPQRLQQDCYEAYNIQVSGLEQRLRALDYPKVVIGVSGGLDSTHALIVATHAMDREGRPRSDILAFALPGFATGEHTKNNAIKLARALGVTFSEIDIGDTARLMLHTIGHPYSVGEKVYDVTFENVQAGLRTDYLFRIANQRGGIVLGTGDLSELALGWSTYGVGDQMSHYNVNAGVPKTLIQHLIRWVISAGEFGEKVGEVLQSVLDTEITPELIPTGEEELQSSEAKVGPFALQDFSLFQVLRYGFRPSKIAFLAWHAWNDAERGNWPPGFPKSERPSYSLAEIRHWLQIFVQRFYSFSQFKRSALPNGPKVSHGGALSPRGDWRAPSDMSARIWLDQIDREVPKG
Protein: Dicarboxylate transporter 1, chloroplastic (2-oxoglutarate/malate translocator 1) (AtpOMT1) (Q9LXV3)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: 2-oxoglutarate/malate translocator involved with DIT2-1 in primary ammonia assimilation and in the re-assimilation of ammonia generated by the photorespiratory pathway. Imports 2-oxoglutarate into plastids as precursor for ammonia assimilation. 2-oxoglutarate is converted to glutamate, the end product of ammonia assimilation, which is exported to the cytosol by DIT2-1.
Subcellular location: Plastid, chloroplast inner membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
- Plastidal glycolate/glycerate translocator 1, chloroplastic
- Malate dehydrogenase, chloroplastic
- Sodium/pyruvate cotransporter BASS2, chloroplastic
- D-glycerate 3-kinase, chloroplastic
- AT5g24690/MXC17_8)
- Mitochondrial succinate-fumarate transporter 1
- Mitochondrial carnitine/acylcarnitine carrier-like protein
- S-adenosylmethionine carrier 1, chloroplastic/mitochondrial
- ADP,ATP carrier protein 2, chloroplastic
- Pyruvate, phosphate dikinase 1, chloroplastic
Sequence:
MASLALSGSCSLAFPLKSRSLSLPRPPSSSLNLTKPLRSLDSRFSLLKSPLPVSLRRRSSTLVKASSTVASASSSPTPPLVPAPVPWQGAAIKPLLASIATGLILWFVPVPEGVTRNAWQLLAIFLATIVGIITQPLPLGAVALMGLGASVLTKTLTFAAAFSAFGDPIPWLIALAFFFARGFIKTGLGNRVAYQFVRLFGSSSLGLGYSLVFSEALLAPAIPSVSARAGGIFLPLVKSLCVACGSNVGDGTEHRLGSWLMLTCFQTSVISSSMFLTAMAANPLSANLAFNTIKQTIGWTDWAKAAIVPGLVSLIVVPFLLYLIYPPTVKSSPDAPKLAQEKLDKMGPMSKNELIMAATLFLTVGLWIFGAKLGVDAVTAAILGLSVLLVTGVVTWKECLAESVAWDTLTWFAALIAMAGYLNKYGLIEWFSQTVVKFVGGLGLSWQLSFGILVLLYFYTHYFFASGAAHIGAMFTAFLSVSTALGTPPYFAALVLAFLSNLMGGLTHYGIGSAPIFYGANYVPLAKWWGYGFLISIVNILIWLGVGGAWWKFIGLW
Protein: F420-dependent methylenetetrahydromethanopterin dehydrogenase (MTD) (EC 1.5.98.1) (Coenzyme F420-dependent N5,N10-methylenetetrahydromethanopterin dehydrogenase) (P55300)
Organism: Methanothermobacter marburgensis (strain ATCC BAA-927 / DSM 2133 / JCM 14651 / NBRC 100331 / OCM 82 / Marburg) (Methanobacterium thermoautotrophicum)
Function: Catalyzes the reversible reduction of methenyl-H(4)MPT(+) to methylene-H(4)MPT.
Interaction partners:
- 5,10-methenyltetrahydromethanopterin hydrogenase
- 5,10-methylenetetrahydromethanopterin reductase
- Coenzyme F420 hydrogenase subunit alpha
- Methenyltetrahydromethanopterin cyclohydrolase
- Coenzyme F420 hydrogenase subunit beta
- F420-dependent glutamate synthase
- Formylmethanofuran--tetrahydromethanopterin formyltransferase
- Probable [NiFe]-hydrogenase-type-3 Eha complex membrane subunit A
- Bifunctional enzyme Fae/Hps
- F420-non-reducing hydrogenase subunit A
Sequence:
MVVKIGIIKCGNIGTSPVLDLLLDERADRPNIDVCVVGSGAKMNPDEIERAVPTMLEMERDFVIFISPNPGAPGPAKARELLSAADVPAMIIGDAPGLRVKDEIEEQGLGYIIVKADPMIGARREFLDPTEMASFNSDVIKVLAFTGAYRVVQNTIDAMIADVEAGKAPELPQVVIDTDKAVEAAGYTNPYAKAKAMAAYEIATKVADIDVRGCFMVQDPDQYIPIVASAHEMLSAAAKLAIEAREIEKANDTVLRTPHGKEGKTLSKKDLLAKPE
Protein: E3 ubiquitin-protein ligase Praja-1 (Praja1) (EC 2.3.2.27) (RING finger protein 70) (RING-type E3 ubiquitin transferase Praja-1) (Q8NG27)
Organism: Homo sapiens (Human)
Function: Has E2-dependent E3 ubiquitin-protein ligase activity. Ubiquitinates MAGED1 antigen leading to its subsequent degradation by proteasome (By similarity). May be involved in protein sorting.
Interaction partners:
- Melanoma-associated antigen D1
- Non-structural maintenance of chromosomes element 3 homolog
- Oligophrenin-1
- Ubiquitin-conjugating enzyme E2 D2
- Non-structural maintenance of chromosomes element 4 homolog A
- Melanoma-associated antigen D4
- Necdin
- Structural maintenance of chromosomes protein 6
- Structural maintenance of chromosomes protein 5
- Ephrin-B1
Sequence:
MGQESSKPVWPNPTGGYQSNTGRRYGRRHAYVSFRPPTSQRERIASQRKTNSEVPMHRSAPSQTTKRSRSPFSTTRRSWDDSESSGTNLNIDNEDYSRYPPREYRASGSRRGMAYGHIDSYGADDSEEEGAGPVERPPVRGKTGKFKDDKLYDPEKGARSLAGPPPHFSSFSRDVREERDKLDPVPAARCSASRADFLPQSSVASQSSSEGKLATKGDSSERERREQNLPARPSRAPVSICGGGENTSKSAEEPVVRPKIRNLASPNCVKPKIFFDTDDDDDMPHSTSRWRDTANDNEGHSDGLARRGRGESSSGYPEPKYPEDKREARSDQVKPEKVPRRRRTMADPDFWTHSDDYYKYCDEDSDSDKEWIAALRRKYRSREQTLSSSGESWETLPGKEEREPPQAKVSASTGTSPGPGASASAGAGAGASAGSNGSNYLEEVREPSLQEEQASLEEGEIPWLQYHENDSSSEGDNDSGHELMQPGVFMLDGNNNLEDDSSVSEDLEVDWSLFDGFADGLGVAEAISYVDPQFLTYMALEERLAQAMETALAHLESLAVDVEVANPPASKESIDALPEILVTEDHGAVGQEMCCPICCSEYVKGEVATELPCHHYFHKPCVSIWLQKSGTCPVCRCMFPPPL
Protein: DNA repair protein RAD52 homolog (RAD52 homolog, DNA repair protein) (Rad52 short isoform) (Q4U0V2)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
Sequence:
MDYSSGRQEERKPHTTNTCFGQYSYSAEEYQAVQNALRQKLGPEYISTRQAGGGQKVCYIEGHKVISLANEMFGYNGWSHSISQQNVDFVDLINGKFYVGVSAFIKVQLKDGSFHEDVGYGVSEGLKSKALSLEKARKEAVTDGLKRALKCFGNALGNCILNKEYLIAINKIPKQPPPPLDADKTKRSDLEPSVEKARFDSLAQTNSRQFTKLENPANIPIEQMGNLPVREGHESATGPRTSLTNTTALLGNTTTHQDTENRPSNTSRSASDTTELSSSDPLLDSKQQRKLRQQQLQQKFRQEMEAKKLLQEKKDQQPTLHIKQDDPELWDFTLDGIDMLDDPSTRSTDPPRPSTPNQHTMTTRSKTPQRPQCLRPPAQPQGHFRSSTAGGPSSPYRHGQMMKKRRLDT
Protein: RISC-loading complex subunit TARBP2 (Protamine-1 RNA-binding protein) (PRM-1 RNA-binding protein) (TAR RNA-binding protein 2) (P97473)
Organism: Mus musculus (Mouse)
Function: Required for formation of the RNA induced silencing complex (RISC). Component of the RISC loading complex (RLC), also known as the micro-RNA (miRNA) loading complex (miRLC), which is composed of DICER1, AGO2 and TARBP2. Within the RLC/miRLC, DICER1 and TARBP2 are required to process precursor miRNAs (pre-miRNAs) to mature miRNAs and then load them onto AGO2. AGO2 bound to the mature miRNA constitutes the minimal RISC and may subsequently dissociate from DICER1 and TARBP2. May also play a role in the production of short interfering RNAs (siRNAs) from double-stranded RNA (dsRNA) by DICER1 (By similarity). Binds in vitro to the PRM1 3'-UTR. Seems to act as a repressor of translation.
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03034, ECO:0000269|PubMed:8649414}. Cytoplasm, perinuclear region {ECO:0000255|HAMAP-Rule:MF_03034}. Nucleus {ECO:0000255|HAMAP-Rule:MF_03034, ECO:0000269|PubMed:8649414}.
Interaction partners:
- Endoribonuclease Dicer
- Protein argonaute-2
- Protein argonaute-1
- Ribonuclease 3
- Protein argonaute-4
- Protein argonaute-3
- Microprocessor complex subunit DGCR8
- Interferon-inducible double-stranded RNA-dependent protein kinase activator A
- Trinucleotide repeat-containing gene 6A protein
- Exportin-5
Sequence:
MSEEDQGSGTTTGCGLPSIEQMLAANPGKTPISLLQEYGTRIGKTPVYDLLKAEGQAHQPNFTFRVTVGDTSCTGQGPSKKAAKHKAAEVALKHLKGGSMLEPALEDSSSFSLLDSSPPEDTPVVAAEAAAPVPSAVLTRSPPMEMQPPVSPQQSECNPVGALQELVVQKGWRLPEYMVTQESGPAHRKEFTMTCRVERFIEIGSGTSKKLAKRNAAAKMLLRVHTVPLDARDGNEAEPDDDHFSIGVSSRLDGLRNRGPGCTWDSLRNSVGEKILSLRSCSVGSLGALGSACCSVLSELSEEQAFHVSYLDIEELSLSGLCQCLVELSTQPATVCYGSATTREAARGDAAHRALQYLRIMAGSK