wanglab/gogpt-training-data huggingface dataset:
Protein: Girdin, isoform E (M9PE55)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
Sequence:
MAGTATATPMEIDEFVNSSIISWLESCLPRAELLAGYTSLLDGHIIHSVWLQIDPEPQNNPSELNDLNGKSLSIARAKNFECVVRNLKSFFEEELGQTILVLPDAFTLGHHPESKNGLEQMKTLLTLLLGAAVQCPNKELFIARIKELDLETQHAIVGLIKQVTDSHSLVLTEDSLERLTPQSMYTHILRLTKERDVMYLKWIDLACVETEMTASDNLVECGQGVSVTRSPSNGTATSTPSSSSNSESNHLAVECADLRSKNRKLRQELEEKSENLLELREELDDKKARFDKLRQESQEWFTEAKRASAYRDEVDILRERAERADRLEVEVQKYREKLGDSDFYKSRVEELREDNRVLLESKEMLEEQLQRYRKRSEHAISLESEIIKYKQKINDMALERDVDRSKLEELLEENSQLQLVARNLNSTMDLDKSFSENEDDCNSGDNSLSEQLTNNAQTRALKLELENRRLTAALEQLKESSFHESTSKMLELEKEKKKLSLKIEQMQENINRLTQQNVELEGVFKNALEENKKLQDAVDNRQKSYDRQSLEREADRQKLSDAEQHVETLNKEKQRIQTLNESIQRRADDLERLAESKTKELEQYLEKSRQYELTKQKLYEIEARVSTYERENASLLKEVSKLKEGSEQKSVQLDDSINRLDVQSKELQKLGKALEDSEQVHQKLVELEKQNQELASQRIIDQEMISTLRNDLVTGTLVTKKVRNNLEKLGLADEEPGELNVEHVVEKLVRNPETFKTVREIMLNVTREQLEEEEREGGVKSDMCVLCHRQEIFTVEKNIELAATPAPAPAQPSSQELRFEHKVRLSPARESAELTRIKDSNTQLQTENARLSVDVAALGSQITSLNTQHVALQLANSQLAAEKDSLLKEIDSLQQEHKHALQDQVTLQCLHDQLSAEYESLNKDKEQLKAAVRDLRQELRDTREQQSALEQRIEELTIQNSNMKTCSEDLSILRTEHSKLTDDFRNLFATSDRFKNEYKNIQEQYKMVRMEHSSLKLQNTELSGELNAKSDQVRCLQMEYSKVQQRCEMLIQNNAELDSERKALMDNVSQLLSQYQELLAISLEDKKHFHEEEKNYTERVHSLKRQKEKLEEKIMEHYKKSETTVHKKKPFASMLVRRVKKASSDLMNKVPSRNRRSWVDDARTNSQFVIGSESGGNESDNSNEEPLSIASDTHLLQRNVPLRQSLQRSLEAPDVTGSSLTLGTAGSRRTVYLIDEHQKLPDGSTPGATQSQSVGGSGSVNAAPPTPAEPQTPQKSTENNAPVGPATFLMYNRINTTIGGASNSGDQSPLLQASGSVSGTTMQDDKSARKRTEDKSNSIWYEYGCV
Protein: Protein MMS22-like (Methyl methanesulfonate-sensitivity protein 22-like) (Q6ZRQ5)
Organism: Homo sapiens (Human)
Function: Component of the MMS22L-TONSL complex, a complex that promotes homologous recombination-mediated repair of double-strand breaks (DSBs) at stalled or collapsed replication forks. The MMS22L-TONSL complex is required to maintain genome integrity during DNA replication. It mediates the assembly of RAD51 filaments on single-stranded DNA (ssDNA): the MMS22L-TONSL complex is recruited to DSBs following histone replacement by histone chaperones and eviction of the replication protein A complex (RPA/RP-A) from DSBs. Following recruitment to DSBs, the TONSL-MMS22L complex promotes recruitment of RAD51 filaments and subsequent homologous recombination. Within the complex, MMS22L acts by binding ssDNA.
Subcellular location: Nucleus {ECO:0000269|PubMed:21055983, ECO:0000269|PubMed:21055984, ECO:0000269|PubMed:21113133}. Chromosome {ECO:0000269|PubMed:21055983, ECO:0000269|PubMed:21055984, ECO:0000269|PubMed:21113133, ECO:0000269|PubMed:27338793, ECO:0000269|PubMed:27797818}. Note=Localizes to DNA damage sites, accumulates at stressed replication forks (PubMed:21055983, PubMed:21055984, PubMed:27797818). Recruited to stalled or collapsed replication forks; directly binds replication protein A complex (RPA/RP-A)-coated single-stranded DNA (ssDNA) (PubMed:27797818). {ECO:0000269|PubMed:21055983, ECO:0000269|PubMed:21055984, ECO:0000269|PubMed:27797818}.
Interaction partners:
- Tonsoku-like protein
- Histone chaperone ASF1B
- N-acetyltransferase ESCO2
- FACT complex subunit SSRP1
- DNA replication licensing factor MCM6
- Breast cancer type 1 susceptibility protein
- DNA repair protein RAD51 homolog 1
- Histone chaperone ASF1A
- DNA replication licensing factor MCM2
Sequence:
MENCSAASTFLTDSLELELGTEWCKPPYFSCAVDNRGGGKHFSGESYLCSGALKRLILNLDPLPTNFEEDTLEIFGIQWVTETALVNSSRELFHLFRQQLYNLETLLQSSCDFGKVSTLHCKADNIRQQCVLFLHYVKVFIFRYLKVQNAESHVPVHPYEALEAQLPSVLIDELHGLLLYIGHLSELPSVNIGAFVNQNQIKLFPPSWHLLHLHLDIHWLVLEILYMLGEKLKQVVYGHQFMNLASDNLTNISLFEEHCETLLCDLISLSLNRYDKVRSSESLMSDQCPCLCIKELWVLLIHLLDHRSKWFVSESFWNWLNKLLKTLLEKSSDRRRSSMPVIQSRDPLGFSWWIITHVASFYKFDRHGVPDEMRKVESNWNFVEELLKKSISVQGVILEEQLRMYLHCCLTLCDFWEPNIAIVTILWEYYSKNLNSSFSISWLPFKGLANTMKSPLSMLEMVKTCCCDKQDQELYKSSSSYTIFLCILAKVVKKAMKSNGPHPWKQVKGRIYSKFHQKRMEELTEVGLQNFFSLFLLLAAVAEVEDVASHVLDLLNFLKPAFVTSQRALIWKGHMAFLLMYAQKNLDIGVLAEKFSCAFREKAKEFLVSKNEEMVQRQTIWTLLSIYIDGVQEVFETSYCLYPSHEKLLNDGFSMLLRACRESELRTVLSFLQAVLARIRSMHQQLCQELQRDNVDLFVQSSLSAKERHLAAVASALWRHFFSFLKSQRMSQVVPFSQLADAAADFTLLAMDMPSTAPSDFQPQPVISIIQLFGWDDIICPQVVARYLSHVLQNSTLCEALSHSGYVSFQALTVRSWIRCVLQMYIKNLSGPDDLLIDKNLEEAVEKEYMKQLVKLTRLLFNLSEVKSIFSKAQVEYLSISEDPKKALVRFFEAVGVTYGNVQTLSDKSAMVTKSLEYLGEVLKYIKPYLGKKVFSAGLQLTYGMMGILVKSWAQIFATSKAQKLLFRIIDCLLLPHAVLQQEKELPAPMLSAIQKSLPLYLQGMCIVCCQSQNPNAYLNQLLGNVIEQYIGRFLPASPYVSDLGQHPVLLALRNTATIPPISSLKKCIVQVIRKSYLEYKGSSPPPRLASILAFILQLFKETNTDIYEVELLLPGILKCLVLVSEPQVKRLATENLQYMVKACQVGSEEEPSSQLTSVFRQFIQDYGMRYYYQVYSILETVATLDQQVVIHLISTLTQSLKDSEQKWGLGRNIAQREAYSKLLSHLGQMGQDEMQRLENDNT
Protein: Hypothetical second sulfur transcription regulator MetZ, bZIP transcription factor (Eurofung) (Q5B2L2)
Organism: Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- Cytochrome c oxidase subunit 6, mitochondrial
- Cytochrome c oxidase subunit 2
- Cytochrome c oxidase subunit 4, mitochondrial
- Probable E3 ubiquitin ligase complex SCF subunit sconB
- Cytochrome c oxidase subunit VIa, putative
- Cytochrome c oxidase polypeptide V
- Cytochrome c oxidase subunit 8
Sequence:
MSDEQIARQTAASSFDKLENFNFLLSRHDPEVAKHRQYSFDTDAAASLAHVPNLGMPYDPTEGMGGLSVSSYESIEDEHSPIDVRGYPYHAGDKTINYSVSDHMLSHSAYPLYPPISYGPDEVGHAPGAMTPSDVSSSISPPNGQIGNNKYSTQISGDHIASALNQEEHSRRAAEEDRRRRNTAASARFRMKKKQREQTLERTVRETTEKNASLEARVAQLEMENRWLKNLLTEKHEAASSRMPPPPATDVSLNHPSTTVTGSGQKHIQPKKKGVGTDN
Protein: Linear primary-alkylsulfatase (EC 3.1.6.21) (Sodium dodecyl sulfate hydrolase) (SDS hydrolase) (Type III linear primary-alkylsulfatase) (Q9I5I9)
Organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Function: Alkylsulfatase that cleaves both short and medium-length alkylsulfates, including the widely used detergent sodium dodecyl sulfate (SDS). Acts in vitro on primary alkylsulfates such as decyl sulfate, octyl sulfate and hexyl sulfate, but not on sulfated sugars and arylsulfates. The hydrolysis of SDS allows the bacterium to use SDS as a sole carbon or sulfur source. In addition, contributes to the in vivo virulence of P.aeruginosa by playing a central role in the degradation of mucin, a glycoprotein that is the primary component of the mucus overlaying the host epithelial tissues. Plays a role in the degradation of both protein and carbohydrate moieties in mucin via the release of sulfate from mucin, D-galactose 6-sulfate (Gal-6S) and N-acetyl-D-glucosamine 6-sulfate (GlcNAc-6S).
Subcellular location: Periplasm {ECO:0000305|PubMed:16684886}.
Interaction partners:
- Arylsulfatase
- Probable coniferyl aldehyde dehydrogenase
- Probable oxidoreductase
- Secretin/TonB short N-terminal domain-containing protein
- Choline sulfatase
- Probable transporter
Sequence:
MSRLLALLALAPLLAGAAETTAPKPPSAFTVEAQRRVEAELPFADRADFERADRGLIRRPERLLIRNPDGSVAWQLGGYDFLLDGKPRDSINPSLQRQALLNLKYGLFEVAEGIYQVRGFDLANITFIRGDSGWIVVDTLTTPATARAAYELVSRELGERPIRTVIYSHAHADHFGGVRGLVEPQQVASGAVQIIAPAGFMEAAIKENVLAGNAMMRRATYQYGTQLPKGPQGQVDMAIGKGLARGPLSLLAPTRLIEGEGEDLVLDGVPFTFQNTPGTESPAEMNIWLPRQKALLMAENVVGTLHNLYTLRGAEVRDALGWSKYINQALHRFGRQAEVMFAVHNWPRWGNAEIVEVLEKQRDLYGYLHDQTLHLANQGVTIGQVHNRLRLPPSLDQEWYDRGYHGSVSHNARAVLNRYLGYYDGNPATLDPLSPEDSAGRYVEYMGGAERLLEQARASYARGEYRWVVEVVNRLVFAEPDNRAARELQADALEQLGYQAENAGWRNSYLSAAYELRHGVPRDQPTMKAGSADALAAMDTGLLFDYLGVRLDAGAAEGKALSINLRLPDIGENYLLELKNSHLNNLRGVQSEDAGQTVSIDRADLNRLLLKEVSAVRLVFEGKLKSSGNPLLLGQLFGMLGDFDFWFDIVTPAAKSEG
Protein: Siderophore export accessory protein MmpS5 (P9WJS7)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: Part of an export system, which is required for biosynthesis and secretion of siderophores. Essential for virulence.
Subcellular location: Cell inner membrane {ECO:0000269|PubMed:23431276}; Single-pass membrane protein {ECO:0000255}.
Interaction partners:
- Siderophore exporter MmpL5
- HTH-type transcriptional regulator MmpR5
- Siderophore exporter MmpL4
- ATP synthase subunit c
- HTH-type transcriptional regulatory protein RaaS
Sequence:
MIGTLKRAWIPLLILVVVAIAGFTVQRIRTFFGSEGILVTPKVFADDPEPFDPKVVEYEVSGSGSYVNINYLDLDAKPQRIDGAALPWSLTLKTTAPSAAPNILAQGDGTSITCRITVDGEVKDERTATGVDALTYCFVKSA
Protein: Late embryogenesis abundant protein 37 (Q9M349)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Mitochondrion {ECO:0000269|PubMed:25005920}.
Interaction partners:
- Glycosyl hydrolase family protein with chitinase insertion domain-containing protein
- Cellulase
- Late embryogenesis abundant protein
- PB1 domain-containing protein tyrosine kinase
- Chalcone--flavanone isomerase 2
- Metal tolerance protein A1
- U-box domain-containing protein 35
- Late embryogenis abundant protein 41
Sequence:
MSQSLFNLKSLSRSINNTIRMRRYIVITKASQRAYTIGSSQEKPSWASDPDTGYFRPETAAKELDPYIAKTSQVQGKMMRGEELWWMPDPQTGYYRPDNFARELDAVELRSLHFNKNQKTYVVS
Protein: Interferon regulatory factor (B5XBW9)
Organism: Salmo salar (Atlantic salmon)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}. Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|PIRNR:PIRNR038196}.
Interaction partners:
Sequence:
MPVSRMRMRPWLEEKIESNSISGLVWVDKDNKIFSVPWKHAARHGWDLNKDACLFKQWAMHTGKFIQGETKTDPKTWKANFRCAMNSLPDIEEVKDKSINRGSGAVRVYKMKNIYSKPNNKRSKANNVKKNKKGSQIKTGGMAYSETNCPENLNTNTHLQEDSMTQESIVDSTGNLGDFTFAPECSTNVEIGPDSTNNFYASFQVSPDHSTDYEDGHQETLIGMTHHWEQGSVNDKGFQSNEVGTAESFDTAESYHSQESQWSDNSETEIELRLYTELSSGLPIIDDILSCTDYWTLNNNTSSYPQQITCPL
Protein: Inactive pancreatic lipase-related protein 1 (PL-RP1) (P54316)
Organism: Rattus norvegicus (Rat)
Function: May function as inhibitor of dietary triglyceride digestion. Lacks detectable lipase activity (in vitro) (By similarity).
Subcellular location: Secreted {ECO:0000305}.
Interaction partners:
- Bile salt-activated lipase
- Pancreatic triacylglycerol lipase
- Colipase
- Pancreatic lipase-related protein 2
- Gastric triacylglycerol lipase
- Chymotrypsin-like elastase family member 2A
- Carboxypeptidase A1
- Diacylglycerol O-acyltransferase 1
- Hepatic triacylglycerol lipase
- Acylglycerol transacylase
Sequence:
MLTLWTVSLFLLGAAQGKEVCYDNLGCFSDAEPWAGTAIRPLKLLPWSPEKINTRFLLYTNENPTAFQTLQLSDPLTIGASNFQVARKTRFIIHGFIDKGEENWVVDMCKNMFQVEEVNCICVDWKKGSQTTYTQAANNVRVVGAQVAQMIDILVKNYSYSPSKVHLIGHSLGAHVAGEAGSRTPGLGRITGLDPVEANFEGTPEEVRLDPSDADFVDVIHTDAAPLIPFLGFGTNQMSGHLDFFPNGGQSMPGCKKNALSQIVDIDGIWSGTRDFVACNHLRSYKYYLESILNPDGFAAYPCASYKDFESNKCFPCPDQGCPQMGHYADKFAGKSGDEPQKFFLNTGEAKNFARWRYRVSLILSGRMVTGQVKVALFGSKGNTRQYDIFRGIIKPGATHSSEFDAKLDVGTIEKVKFLWNNQVINPSFPKVGAAKITVQKGEERTEYNFCSEETVREDTLLTLLPCETSDTV
Protein: 26S proteasome non-ATPase regulatory subunit 9 (26S proteasome regulatory subunit p27) (Transactivating protein Bridge-1) (Q9WTV5)
Organism: Rattus norvegicus (Rat)
Function: Acts as a chaperone during the assembly of the 26S proteasome, specifically of the base subcomplex of the PA700/19S regulatory complex (RC). During the base subcomplex assembly is part of an intermediate PSMD9:PSMC6:PSMC3 module, also known as modulator trimer complex; PSMD9 is released during the further base assembly process (By similarity).
Interaction partners:
- 26S proteasome regulatory subunit 6A
- 26S proteasome regulatory subunit 10B
- 26S proteasome regulatory subunit 8
- 26S proteasome non-ATPase regulatory subunit 1
- 26S proteasome regulatory subunit 6B
- 26S proteasome non-ATPase regulatory subunit 12
- 26S proteasome regulatory subunit 7
- 26S proteasome non-ATPase regulatory subunit 10
- Proteasome
- 26S proteasome non-ATPase regulatory subunit 8
Sequence:
MSSEEVRHRAESSEARAAAVSDIQELMRRKEEIEAQIKANYDVLESQKGIGMNEPLVDCEGYPRADVDLYQVRTARHNIICLQNDHKALMKQVEEALHQLHARDKEKQARDMAEAREEAMNRRLASDSPALPKAFARVNSISPGSPASIAGLQVDDEIVEFGSVNTQNFQSLQNVGTVVQHSEGKPLNVMVIRRGEKHQLRLTPTRWAGKGLLGCNITPLQR
Protein: D-beta-hydroxybutyrate dehydrogenase, mitochondrial (EC 1.1.1.30) (3-hydroxybutyrate dehydrogenase) (BDH) (Q02337)
Organism: Bos taurus (Bovine)
Subcellular location: Mitochondrion inner membrane {ECO:0000269|PubMed:718894}. Mitochondrion matrix {ECO:0000269|PubMed:718894}.
Interaction partners:
- Succinyl-CoA:3-ketoacid-coenzyme A transferase
- Hydroxymethylglutaryl-CoA lyase, mitochondrial
- Dehydrogenase/reductase SDR family member 6
- hydroxymethylglutaryl-CoA lyase
- Acetoacetyl-CoA synthetase
- Hydroxymethylglutaryl-CoA synthase, mitochondrial
- Acetyl-CoA acetyltransferase, mitochondrial
Sequence:
MLTARLSRPLSQLPRKTLNFSDRENGTRGSLLLYSAPFVPVGRRTYAASVDPVGSKAVLITGCDSGFGFSLAKHLHSEGFLVFAGCLMKDKGSDGVKELDSMKSDRLRTVQLNVCKSEEVDKAAEVIRSSLEDPEKGLWGLVNNAGISTFGDVEFTSMETYKEVAEVNLWGTVRVTKAFLPLIRRAKGRVVNISSMMGRMANVARSPYCITKFGVEAFSDCLRYEMHPLGVKVSVVEPGNFIAATSLYGGTERIQAIANKMWEELPEVVRQDYGRKYFDEKVARMESYCTSGSTDTSPVIKAVTHALTATTPYTRYHPMDYYWWLRMQIMTHFPGAISDRIYIH
Protein: Valine--tRNA ligase, mitochondrial (EC 6.1.1.9) (Valyl-tRNA synthetase) (ValRS) (O14160)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Mitochondrion {ECO:0000269|PubMed:16823372}.
Interaction partners:
- Putative glycine--tRNA ligase
- Putative leucine--tRNA ligase, cytoplasmic
- Elongation factor 1-gamma
- Valine--tRNA ligase
- Probable arginine--tRNA ligase, cytoplasmic
- Tyrosine--tRNA ligase, cytoplasmic
- Histidine--tRNA ligase, mitochondrial
- Probable proline--tRNA ligase, mitochondrial
- Tyrosine--tRNA ligase, mitochondrial
- Putative proline--tRNA ligase C19C7.06
Sequence:
MFHFQRSFSSRKAHGLLSFKNRNYIHIEAPFDIAAIQDGWNIIRKHIHYPKPKSIEAPMFPILLPPPNITGKLHIGHALTITIQDALARFYAMHGYKVSFRPGTDHAGIATQSVVEKYLQKKGVYRNQLSKDELLSSIHSWQVKYQKSIINQLKSFEAIFDWDNIFYTMDQNRSEAVNEAFISLFNAGLIYRANRFVNWCPKLESAVSDIEVESQQINKPVTKYVDNTPVEFGWLYEISYQLEGSDNEQLNVSTTRPETIFGDRAIAVSPHDERYKKYVGRFVKHPLIDDLLIPVICDNAVDRHFGTGVLKITPMHSIVDYEIAKRHNIDCVSIMDKSGNLINCSKEVNGMNRLKARSKIVRLLQQRNRLVEQVPHSLILSVCSRTGDVIEPVMVPQWYLSVDSLKKEVLKSSNKLKLVPSLARKEWDSWFKKMGDWCISRQIWWGHQIPVWKILEEDKWIAAPNYEKALQLSVGKSVSQDSDVLDTWFSSALLPLSAFGWPKSKDIQPLPFIESGQDILFFWIARMALLCKYFSNELPFKEIILHPLVRDSEGRKMSKSLGNVIDPMDIINGVTLENMKKALLEGNLPISEVHKSSKQMEKAFPNGIPAQGIDIFRYGLFLCLHHEQRILLDMNSFSDAHRFVSKLWNLARYFNQYKDKENPLKLTDSQRQRISLLKMATYSKLHHAVEGVKESFEQRKFFNAADIMKNFLLNDLSSVYVELTRFDVKDSKSSAYEVYRVFSDILHIFLKLIHPIVPCISGVMLHSKIIPERKNSEFLSFPTSQQECLLVHDNQAEVVVQNAYDVLIQLRKLESPLNKSPSREHTVYISTSLEPLKYFYDAIEQSTNLKLKSISQEDTIDLMRNQTFILSRISSDTILLVPKKLYPSKRKKLRKNLDDLQKKLDKIQHTTSSSGYEKAPSYIKLKNCELQKDILVKIQDIKQALLNTEI
Protein: Iron-sulfur cluster assembly scaffold protein IscU (Sulfur acceptor protein IscU) (P0ACD4)
Organism: Escherichia coli (strain K12)
Function: A scaffold on which IscS assembles Fe-S clusters. Exists as 2 interconverting forms, a structured (S) and disordered (D) form. The D-state is the preferred substrate for IscS. Converts to the S-state when an Fe-S cluster is assembled, which helps it dissociate from IscS to transfer the Fe-S to an acceptor. It is likely that Fe-S cluster coordination is flexible as the role of this complex is to build and then hand off Fe-S clusters.
Interaction partners:
- Co-chaperone protein HscB
- 2Fe-2S ferredoxin
- Chaperone protein HscA
- Cysteine desulfurase IscS
- HTH-type transcriptional regulator IscR
- Iron-binding protein IscA
- Iron-sulfur cluster assembly protein CyaY
- Protein IscX
- Cysteine desulfurase CsdA
- Fe/S biogenesis protein NfuA
Sequence:
MAYSEKVIDHYENPRNVGSFDNNDENVGSGMVGAPACGDVMKLQIKVNDEGIIEDARFKTYGCGSAIASSSLVTEWVKGKSLDEAQAIKNTDIAEELELPPVKIHCSILAEDAIKAAIADYKSKREAK
Protein: Uncharacterized protein ycf68 (P0C305)
Organism: Oryza sativa subsp. indica (Rice)
Subcellular location: Plastid, chloroplast.
Interaction partners:
Sequence:
MAYSSCLNRSLKPNKLLLRRIDGAIQVRSHVDLTFYSLVGSGRSGGGTTAPLFSRIHTSLISVWRAISRAQVEVRPQWENGAPNNASSQTKNYEITLSFWGDGGIVPFEPFFHAFPGGLEKAAINRTSLILPS
Protein: RH19679p (Q9VVG5)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- GEO11443p1
- Cyclope, isoform A
- GEO13367p1
- Cytochrome c oxidase subunit 5B, isoform A
- ATP synthase F
- Cytochrome b-c1 complex subunit 7
- Cytochrome c oxidase subunit 8, isoform A
- NADH dehydrogenase 1 beta subcomplex subunit 4
- Cytochrome b-c1 complex subunit 8
- Levy, isoform A
Sequence:
MLVKHIVKQGLLLKNAGALSRAAYHGGHGPHSTMNDLPVPAGDWKEQHSQKNAKYNAALITGILVLAGTIGFVKSSGIIHFNYYAPKSLD
Protein: Glutathione transport system permease protein GsiD (P75799)
Organism: Escherichia coli (strain K12)
Function: Part of the ABC transporter complex GsiABCD involved in glutathione import. Probably responsible for the translocation of the substrate across the membrane.
Subcellular location: Cell inner membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Glutathione transport system permease protein GsiC
- Glutathione-binding protein GsiB
- Glutathione import ATP-binding protein GsiA
- Probable D,D-dipeptide transport ATP-binding protein DdpD
- Dipeptide transport ATP-binding protein DppD
- Oligopeptide transport ATP-binding protein OppD
- Oligopeptide transport ATP-binding protein OppF
- Probable D,D-dipeptide transport ATP-binding protein DdpF
- Nickel import ATP-binding protein NikD
- Putrescine export system ATP-binding protein SapD
Sequence:
MRLFNWRRQAVLNAMPLVKPDQVRTPWHEFWRRFRRQHMAMTAALFVILLIVVAIFARWIAPYDAENYFDYDNLNNGPSLQHWFGVDSLGRDIFSRVLVGAQISLAAGVFAVFIGAAIGTLLGLLAGYYEGWWDRLIMRICDVLFAFPGILLAIAVVAVLGSGIANVIIAVAIFSIPAFARLVRGNTLVLKQQTFIESARSIGASDMTVLLRHILPGTVSSIVVFFTMRIGTSIISAASLSFLGLGAQPPTPEWGAMLNEARADMVIAPHVAVFPALAIFLTVLAFNLLGDGLRDALDPKIKG
Protein: Endo/exonuclease Mre11 (Q586P4)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- DNA repair protein RAD50
- Exonuclease, putative
- Recombination initiation protein NBS1, putative
- non-specific serine/threonine protein kinase
- Protein artemis
- KU70 protein
- Flap endonuclease 1
- KU80 protein
- BRCT domain-containing protein
- BRCT domain-containing protein
Sequence:
MGSRVTVLHIIMAERASTQSHALPTSTQADPSLAASTFKFLVTSDNHLGYQERDSRRGDDSFTTFEECLRAARLEHEVDAILLAGDFFHDNKPSLGCLARTSSLLRSYVLGDKPISFTLLSDPKRNFPTHPVPLANFQDPNINVALPIFMIHGNHDDPVGGTSSIDILSTAGLVNYFGHTSSLDDIVVEPVLLKKGDTYIALYGLGNVRDDRLHRCFRMKKLHFVQPKTEPGKDWFKILLFHQNRGVRSGGNMKCGIYETMLAGHGMDLVIWGNEHEQQMEPSPSEGFDIIQPGSTILTSLSEHECNPKKYGVLEVRGGSYRVTGFPLRSIRPVVRRTVELWRDNPGCRTLDAVEDFLRSVVEQMIEEAEEQVSRIPDDVLKFHPNIKFPIMRLAVDFTDPDSTTFPQPNINRFGQQYMDIVVNPSELLRPIKPKQVPRVASSASATGGEAPVVPVPRLNTSDIRTKVAEVFNANARDACSLLSESEVSAAVYAFAEKGERDAIDERICELLSKCQKSVWVSMRRGESESILKPESIYEEVVRHKKEANKRYEELSRAAEEALQRSTQGNELTERLRADTELAASMDSGNFPRVGGELADGAALGLLSATAPRRAGGSGATNNGEGANDALSQVGFTFPDFSNSLSPPDASGGAATRGKRSRDELNVFDVATERDTNEVNSHPNASTVKGGGKAVKSETSAPKPARGRKPKRPVDGGVSGLPLFPSLELTRDPVPDENFLLPPVVGGGVKGASTSSSGMPDNY
Protein: Nucleoporin-62 C-terminal-like protein (Q9H1M0)
Organism: Homo sapiens (Human)
Interaction partners:
- Nucleoporin p54
- Nuclear pore complex protein Nup93
- Nuclear pore complex protein Nup205
- Nuclear pore complex protein Nup155
- Nuclear pore complex protein Nup214
- Nuclear pore complex protein Nup107
- Nuclear pore complex protein Nup133
- Nuclear pore complex protein Nup88
- Nuclear pore complex protein Nup98-Nup96
- Nucleoporin NUP35
Sequence:
MQFTSISNSLTSTAAIGLSFTTSTTTTATFTTNTTTTITSGFTVNQNQLLSRGFENLVPYTSTVSVVATPVMTYGHLEGLINEWNLELEDQEKYFLLQATQVNAWDHTLIENGEMIRILHGEVNKVKLDQKRLEQELDFILSQQQELEFLLTYLEESTRDQSGLHYLQDADEEHVEISTRSAEF
Protein: Uncharacterized transcriptional regulatory protein C1773.16c (O94573)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Nucleus membrane {ECO:0000255|PROSITE-ProRule:PRU00227, ECO:0000269|PubMed:16823372}; Single-pass membrane protein {ECO:0000269|PubMed:16823372}.
Interaction partners:
Sequence:
MKRIRNACELCRRKKLRCNGELTCQNCMVYGEECRYVKRVKHDNRAAVQENERYPILYTPLSTSDHDNDEENEINELKNAVKALDKRFDNFELKLEALFSLLRSQQDSERKVKPGGFPSLVSQILSAGALVDSKLQAYTMRTNFFSNGFSSNDLFPHSFPTWKSAFRDVPDKDWAKTCLDWYFRFINCNWPIFYKKQYMESFEKLYIDKNLVKGAWIVSFYAILALAVSRDKRVDNSKLAESFFATSWFLIQRPGFFLTPQLEKIQALVIMIQFASHLSLYNLCKKLCGQVCLMVKDLNLHKESTDKDLDQDMAELHRRIFWVCYIFETTTSLIFGTPPVLGDLEIECKYPDINYAHCFAENVQGDLIFTCEISLTVLKHEIRTKLYNSNNVFLDKGQKGVISNIQTKILNFERAIPSEMKHYFEILKAGNGLPEELDIIKQHFFTACVEIYLSYCNTLIYLYLADDSIEGSKICLSTARAAIDVIKGFLVVLDPISKNICYLWLFLYCPFTPFLTVFSHLLEDDDLDADICVKDVDRLYSIHAFFLKMKDISGEFAERLSVITENFIQSAEQYLALQNTSVFGTFDALSESFSI
Protein: Colicin-E2 immunity protein (ImmE2) (Microcin-E2 immunity protein) (P04482)
Organism: Escherichia coli
Function: This protein is able to protect a cell, which harbors the plasmid ColE2 encoding colicin E2, against colicin E2.
Interaction partners:
Sequence:
MELKHSISDYTEAEFLEFVKKICRAEGATEEDDNKLVREFERLTEHPDGSDLIYYPRDDREDSPEGIVKEIKEWRAANGKSGFKQG
Protein: Intermediate cleaving peptidase 55 (EC 3.4.11.26) (Intermediate cleaving peptidase of 55 kDa) (P40051)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Aminopeptidase which cleaves preprotein intermediates that carry destabilizing N-ter amino acid residues after the mitochondrial processing peptidase (MPP) cleavage site and is thus critical for stabilization of the mitochondrial proteome.
Subcellular location: Nucleus {ECO:0000269|PubMed:19720832}. Mitochondrion inner membrane {ECO:0000269|PubMed:16823961, ECO:0000269|PubMed:19720832}; Peripheral membrane protein {ECO:0000269|PubMed:19720832}; Matrix side {ECO:0000269|PubMed:19720832}. Note=Has the same dual localization (mitochondrion and nucleus) as one of its substrate, NFS1. {ECO:0000269|PubMed:19720832}.
Interaction partners:
- Dipeptidyl aminopeptidase A
- Kexin
- Mitochondrial intermediate peptidase
- Vacuolar aminopeptidase 1
- Aspartyl aminopeptidase 4
- Mitochondrial-processing peptidase subunit alpha
- Alpha-mannosidase
- Aminopeptidase 2, mitochondrial
- Mitochondrial-processing peptidase subunit beta
Sequence:
MLHRINPVRFSMQSCQRYFSKLVSPLEQHKSNTFTNRVRIPIEAGQPLHETRPFLIKSGELTPGISALEYYERRIRLAETLPPKSCVILAGNDIQFASGAVFYPFQQENDLFYLSGWNEPNSVMILEKPTDSLSDTIFHMLVPPKDAFAEKWEGFRSGVYGVQEIFNADESASINDLSKYLPKIINRNDFIYFDMLSTSNPSSSNFKHIKSLLDGSGNSNRSLNSIANKTIKPISKRIAEFRKIKSPQELRIMRRAGQISGRSFNQAFAKRFRNERTLDSFLHYKFISGGCDKDAYIPVVATGSNSLCIHYTRNDDVMFDDEMVLVDAAGSLGGYCADISRTWPNSGKFTDAQRDLYEAVLNVQRDCIKLCKASNNYSLHDIHEKSITLMKQELKNLGIDKVSGWNVEKLYPHYIGHNLGLDVHDVPKVSRYEPLKVGQVITIEPGLYIPNEESFPSYFRNVGIRIEDDIAIGEDTYTNLTVEAVKEIDDLENVMQNGLSTKFEEDQVAPL
Protein: Inosine-5'-monophosphate dehydrogenase 2 (IMP dehydrogenase 2) (IMPD 2) (IMPDH 2) (EC 1.1.1.205) (Q9SA34)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Catalyzes the conversion of inosine 5'-phosphate (IMP) to xanthosine 5'-phosphate (XMP), the first committed and rate-limiting step in the de novo synthesis of guanine nucleotides, and therefore plays an important role in the regulation of cell growth.
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03156}.
Interaction partners:
- GMP synthase
- Adenylosuccinate synthetase, chloroplastic
- AMP deaminase
- AICARFT/IMPCHase bienzyme family protein
- Hypoxanthine phosphoribosyltransferase
- Inosine triphosphate pyrophosphatase
- Inosine-5'-monophosphate dehydrogenase 1
- Apyrase 2
- Apyrase 1
- 5'-nucleotidase
Sequence:
MSGFEDGFSAEKLFSQGYSYTYDDVIFLPHFIDFSTDAVSLSTRLSKRVPLSIPCVASPMDTVSESHMAAAMAALGGIGIVHYNCDIDTQASVIRHAKSLQVPIASDAVFKCPEHQIGSVDDFGPSSFVFVSQTGTLTPKLLGYVSKSEWSSMKDDQKEVKIYDYMKSCENKDYYVPWDIDLDKIEAVLEDKQKGFVVLEKEGETVNVVTKDDVERVKGYPKLGSGTVGADKKWMVGAAIGTRESDKERLEHLVKAGANVVVLDSSQGNSIYQLEMIKYVKNTYPELDVVGGNVVTMYQAENLIKAGVDGLRVGMGSGSICTTQEVCAVGRGQATAVYKVSTLAAQHGVPVIADGGISNSGHIVKALVLGASTVMMGSFLAGSTEAPGAYEYRNGRRVKKYRGMGSLEAMTKGSDQRYLGDTAKLKIAQGVVGAVADKGSVLKFIPYTMHAVKQGFQDLGASSLQSAHELLRDNTLRLEARTGAAQIEGGIHGLVSYEKKSF
Protein: UPF0522 protein C (Q55BA2)
Organism: Dictyostelium discoideum (Social amoeba)
Subcellular location: Secreted {ECO:0000305}.
Interaction partners:
- UPF0522 protein A
- UPF0522 protein B
Sequence:
MKLFILIILSICLALVNSQQGVYPDSGVYVSLNSNFLATFGNEFTQTIQNQINSYPVANVDGKTGKVSYSVTNIQQSVQLGDFFFQQTGVNTYNIGWNSVTFTITTDYQGCYKIGGLKKLSICEKGDIKINSQATLSLSIAMTIDFTQSTPTISCSSTTLNVPANGINYNVHCSSKVCDKTHDITNEIASKFVPSVESGMTTEINNNVGKYLSLFPSLRDMNMEYNGNEFYLDSRGTIVESSQGGVLTPTMVLAMNGGIVVKNSAGQFIYPTQSPSSLPSEEAVEDFQTDIAVTLTPYLFESLVDAMFESALPMTITPSEVPSESPVHLNTSDPFFNQTAPGLTGKYPNSPIDVEIISPSSSSQTMVSINSTGVLVGLHSIPVNFIVNDETVFQILFNFNIELTPALSQSSNGISVTGTLDKLDALVTVGSTSVGDIDVSGFVQLIELAQGLVKIPTITIQNPLTTYSLSDLSLSIGDQYIQILGNLQQQQQQQQKQKQILIK