wanglab/gogpt-training-data huggingface dataset:
Protein: Lysine-specific demethylase 4B (EC 1.14.11.66) (JmjC domain-containing histone demethylation protein 3B) (Jumonji domain-containing protein 2B) ([histone H3]-trimethyl-L-lysine(9) demethylase 4B) (Q91VY5)
Organism: Mus musculus (Mouse)
Function: Histone demethylase that specifically demethylates 'Lys-9' of histone H3, thereby playing a role in histone code. Does not demethylate histone H3 'Lys-4', H3 'Lys-27', H3 'Lys-36' nor H4 'Lys-20'. Only able to demethylate trimethylated H3 'Lys-9', with a weaker activity than KDM4A, KDM4C and KDM4D. Demethylation of Lys residue generates formaldehyde and succinate (By similarity). Plays a critical role in the development of the central nervous system (CNS).
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00537}.
Interaction partners:
- Lysine-specific demethylase 3A demethylase 3A)
- SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily A member 4
- Lysine-specific demethylase 2B
- Estrogen receptor
- Lysine-specific demethylase 6B demethylase 6B)
- Histone H3.2
- Histone H3.1
- Lysine-specific histone demethylase 1A
- Lysine-specific demethylase 3B demethylase 3B)
- TP53-binding protein 1
Sequence:
MGSEDHSAQNPSCKIMTFRPTMDEFRDFNRYVAYIESQGAHRAGLAKIIPPKEWKPRQTYDDIDDVVIPAPIQQVVTGQSGLFTQYNIQKKAMTVGEYRRLANSEKYCTPRHQDFDDLERKYWKNLTFVSPIYGADISGSLYDDDVAQWNIGNLRTILDMVERECGTIIEGVNTPYLYFGMWKTTFAWHTEDMDLYSINYLHFGEPKSWYAIPPEHGKRLERLAIGFFPGSSQGCDAFLRHKMTLISPIILKKYGIPFSRITQEAGEFMITFPYGYHAGFNHGFNCAESTNFATLRWIDYGKVATQCTCRKDMVKISMDVFVRILQPERYEQWKQGRDLTVLDHTRPTALSSPELSSWSASRTSIKAKLLRRQISVKESRPWRKAEEERRREPTRRPGPASHRRRSQPKKSKPEESRSPGEATAGVSTLDEARGCSRGEAMPEDEEEEELLPSQGHEAEGVEEDGRGKPRPTKARNKKKTPSPSSPPLLSAPPALFPTEEVLRPPPQPKSPGPAMGPMAAEGGPPPTPLNVVPPGAPVEEAEVRPRPIIPMLYVLPRTSSTDGDREHSAHAQLAPMELGPEEENQAQAGDSQGTTPFSKLKVEIKKSRRHPLGRPPTRSPLSVVKQEASSDEEAFLFSGEDDVTDPEALRSLLSLQWKNKAASFQAERKFNAAAALSEPYCAICTLFYPYSQSVQTERDSAVQPPSKSGQRTRPLIPEMCFTSSGENTEPLPANSYVGEDGTSPLISCAHCCLQVHASCYGVRPELAKEGWTCSRCAAHAWTAECCLCNLRGGALQRTTEHRWIHVICAIAVPEVRFLNVIERNPVDVSAIPEQRWKLKCIYCRKRMKRVSGACIQCSYEHCSTSFHVTCAHAAGVLMEPDDWPYVVSITCLKHRASGAGGQLLRTVSLGQIVITKNRNGLYYRCRVIGTTAQTFYEVNFDDGSYSDNLYPESITSRDCLRLGPPPEGELVELRWTDGNLYRARFISMATSLIYQVEFEDGSQLTVKRGDIFTLEEELPKRVRSRLSLSTGTPQEPSFSGDDVKAAKRPRVASVLATTTEDTGRSPEYLSFMESLLQAQGRPGAPF
Protein: Macrophage receptor MARCO isoform X3 (Macrophage receptor with collagenous structure) (F1QU19)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004606}; Single-pass type II membrane protein {ECO:0000256|ARBA:ARBA00004606}.
Interaction partners:
Sequence:
METEVDDFPGKASIFSQVNPLYSNNMKLCEAERYDFQHSEPKTMKSASKRHCVPVLILLFLLLIGLNSFLAYKVFTLEAWVHTHCTSAQNHELTSASSFQLGSSKNEVECFTDLCGTDGTLEHLRTQINQLNATAEKAIVCPPGPPGPPGSNGIPGFPGQKGIPGSPGRVGEPGAPGQKGQTGDPGIKGERGMVGFPGIPGAPGRKGDSGERGLQGLPGNDGSPGQDGRTGPQGMPGPSGSQGVKGDPGLKGERGDQGPPGPTGPQGSSGARGLQGIPGGKGSPGPKGDTGVGLRGLTGQQGQKGSQGLPGVPGARGANGEKGDRGLSGQKGDQGPKGEKGDAGAKGASGGSQVVRLVGSSTRGRVEVFYQNVWGTVCDDSFDNLDALVVCRMLGFQRSTQVYTDGSGSGRIWLDELRCTGTESSIFNCPHAGMGINNCGHGEDVGVSCA
Protein: dTDP-3-amino-3,4,6-trideoxy-alpha-D-glucose transaminase (EC 2.6.1.106) (Q9F837)
Organism: Micromonospora megalomicea subsp. nigra
Function: Involved in the biosynthesis of the amino sugar dTDP-L-megosamine which is found in the macrolide antibiotic and antiparasitic megalomicin A. Catalyzes the reversible transfer of the amino group from L-glutamate to the C-3 position of dTDP-3-keto-4,6-deoxyglucose to yield dTDP-3-amino-3,4,6-trideoxyglucose.
Interaction partners:
Sequence:
MTTYVWSYLLEYERERADILDAVQKVFASGSLILGQSVENFETEYARYHGIAHCVGVDNGTNAVKLALESVGVGRDDEVVTVSNTAAPTVLAIDEIGARPVFVDVRDEDYLMDTDLVEAAVTPRTKAIVPVHLYGQCVDMTALRELADRRGLKLVEDCAQAHGARRDGRLAGTMSDAAAFSFYPTKVLGAYGDGGAVVTNDDETARALRRLRYYGMEEVYYVTRTPGHNSRLDEVQAEILRRKLTRLDAYVAGRRAVAQRYVDGLADLQDSHGLELPVVTDGNEHVFYVYVVRHPRRDEIIKRLRDGYDISLNISYPWPVHTMTGFAHLGVASGSLPVTERLAGEIFSLPMYPSLPHDLQDRVIEAVREVITGL
Protein: Decidual PRL-related protein (Growth hormone d11) (Prolactin family 8, subfamily a, member 2) (O54832)
Organism: Mus musculus (Mouse)
Subcellular location: Secreted {ECO:0000256|ARBA:ARBA00004613}.
Interaction partners:
- Prolactin-3C1
- Prolactin-4A1
Sequence:
MLPLSQPHFSGALLLLVVSNLLLWEKAASIPECQTGENGCSDPLVITFKNALQRAEVINILADKMHEEFYHNPFSAGQFETLVSRMYRRDEEVLRARNHCHSNVTNPPAHGPEHENLKTKRYLKTMINFMGAWITPVYYLVEVLSDMQNVPESIYSKAQEIELKFREIHDDLTWVLKKVYPKVTFWEKSIIWEYLPGLRSTDTSKKFLAMFNLSHCLRVDIFFIKYHLSALMCRITGQDC
Protein: Transcription intermediary factor 1-alpha (TIF1-alpha) (EC 2.3.2.27) (E3 ubiquitin-protein ligase Trim24) (RING-type E3 ubiquitin transferase TIF1-alpha) (Tripartite motif-containing protein 24) (Q64127)
Organism: Mus musculus (Mouse)
Function: Transcriptional coactivator that interacts with numerous nuclear receptors and coactivators and modulates the transcription of target genes. Interacts with chromatin depending on histone H3 modifications, having the highest affinity for histone H3 that is both unmodified at 'Lys-4' (H3K4me0) and acetylated at 'Lys-23' (H3K23ac) (By similarity). Has E3 protein-ubiquitin ligase activity. Promotes ubiquitination and proteasomal degradation of p53/TP53. Plays a role in the regulation of cell proliferation and apoptosis via its effects on p53/TP53 levels. Up-regulates ligand-dependent transcription activation by AR, GCR/NR3C1, thyroid hormone receptor (TR) and ESR1. Modulates transcription activation by retinoic acid (RA) receptors, such as RARA. Plays a role in regulating retinoic acid-dependent proliferation of hepatocytes. Required for normal transition from proliferating neonatal hepatocytes to quiescent adult hepatocytes.
Subcellular location: Nucleus {ECO:0000269|PubMed:10610177, ECO:0000269|PubMed:11313457, ECO:0000269|PubMed:16880268, ECO:0000269|PubMed:19909775, ECO:0000269|PubMed:7744009}. Cytoplasm {ECO:0000269|PubMed:16880268}. Note=Detected in the cytoplasm of the zygote (PubMed:16880268). Translocates into the pronucleus at the time of genome activation (PubMed:16880268). Colocalizes with sites of active transcription (PubMed:10610177). Localizes to sites of DNA damage (By similarity). {ECO:0000250|UniProtKB:O15164, ECO:0000269|PubMed:10610177, ECO:0000269|PubMed:16880268}.
Interaction partners:
- Transcription intermediary factor 1-beta
- E3 ubiquitin-protein ligase TRIM33
- Estrogen receptor
- Retinoic acid receptor RXR-alpha
- Cellular tumor antigen p53
- Speckle-type POZ protein
- Retinoic acid receptor alpha
- Histone H3.1
- Histone H3.2
- Nuclear receptor-interacting protein 1
Sequence:
MEVAVEKAAAAAAPAGGPAAAAPSGENEAESRQGPDSESGGEASRLNLLDTCAVCHQNIQSRVPKLLPCLHSFCQRCLPAPQRYLMLTAPALGSAETPPPAPAPAPAPGSPAGGPSPFATQVGVIRCPVCSQECAERHIIDNFFVKDTTEVPSSTVEKSNQVCTSCEDNAEANGFCVECVEWLCKTCIRAHQRVKFTKDHTVRQKEEVSPEAVGVTSQRPVFCPFHKKEQLKLYCETCDKLTCRDCQLLEHKEHRYQFIEEAFQNQKVIIDTLITKLMEKTKYIKYTGNQIQNRIIEINQNQKQVEQDIKVAIFTLMVEINKKGKALLHQLESLAKDHRMKLMQQQQEVAGLSKQLEHVMHFSKWAVSSGSSTALLYSKRLITYRLRHLLRARCDASPVTNTTIQFHCDPSFWAQNIINLGSLVIEDKESQPQMPKQNPVVEQSSQPPGGLPSNQLSKFPTQISLAQLRLQHIQQQVMAQRQQVQRRPAPVGLPNPRMQGPIQQPSISHQHPPPRLINFQNHSPKPNGPVLPPYPQQLRYSPSQNVPRQTTIKPNPLQMAFLAQQAIKQWQISSVQAPPTTASSSSSTPSSPTITSAAGYDGKAFSSPMIDLSAPVGGSYNLPSLPDIDCSSTIMLDNIARKDTGVDHAQPRPPSNRTVQSPNSSVPSPGLAGPVTMTSVHPPIRSPSASSVGSRGSSGSSSKPAGADSTHKVPVVMLEPIRIKQENSGPPENYDFPVVIVKQESDEESRPQNTNYPRSILTSLLLNSSQSSASEETVLRSDAPDSTGDQPGLHQENSSNGKSEWSDASQKSPVHVGETRKEDDPNEDWCAVCQNGGELLCCEKCPKVFHLTCHVPTLTNFPSGEWICTFCRDLSKPEVDYDCDVPSHHSEKRKSEGLTKLTPIDKRKCERLLLFLYCHEMSLAFQDPVPLTVPDYYKIIKNPMDLSTIKKRLQEDYCMYTKPEDFVADFRLIFQNCAEFNEPDSEVANAGIKLESYFEELLKNLYPEKRFPKVEFRHEAEDCKFSDDSDDDFVQPRKKRLKSTEDRQLLK
Protein: Nuclear pore complex protein Nup75 (Nucleoporin Nup85) (A1YK01)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Nucleus, nuclear pore complex {ECO:0000256|ARBA:ARBA00004567, ECO:0000256|RuleBase:RU365073}.
Interaction partners:
Sequence:
MSDSGVFAFELGDDLATRCGNTLTGVFVPGSRIALSAYRHVTHSSRDEPTENAGQVPVLIYMAQESTLFDEPVLRSVLAEANATFATLQQLGSRATRAEYVNISRAYRSIVRSCLEKLEQAKKSPEVQTDEARLQRLCDAIVVFYAAECLWHLFEILYIQSNQLVVPQLLDWARFHSPHAEDRATDLLLMGEEASESDDYWSIVKSLIMLGEIDVTRAVLSQNRKAGQTSFKAAEQILKSMPVYQEGYALQKFHSQWEFWHVDTERKIQSGLFATEPELEQLIRLVAGDSEQWDAGIKESQDFYEYLPGYLLFTKPTCKPFELKIAAAKWLNRWCLLRPEREQCSMNRMVSQLMDHDLRLFIYDAQKLNDTHWFSTHLIDLIHHCGQLKSYFDQNNIDLPALRHSMIYEYGSYLMTSHNMWQLGIDYLDCCKQEGQAAIELLLPRITLRSERQATKLINLARQRGLISVEREICKVLSKRSYDNERYGNALEWAIRSKDVLLVTAVADFILKHYSKTGCMLCPDTIANVGGRMFASPRLVFLSKYFEFYEFYRTRDFLSASELLVNLLESKITPDYFWPSLLIDSMPLLESKDPKIFAKETVAILHHIETDLVPIIERDVSKYGKHHTETVFKDYRVENVDEIMNLMRLACARNLARALIIENTLPVV
Protein: Type-1 angiotensin II receptor (Q6NUP5)
Organism: Homo sapiens (Human)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004651, ECO:0000256|RuleBase:RU368058}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651, ECO:0000256|RuleBase:RU368058}.
Interaction partners:
Sequence:
MILNSSTEDGIKRIQDDCPKAGRHNYIFVMIPTLYSIIFVVGIFGNSLVVIVIYFYMKLKTVASVFLLNLALADLCFLLTLPLWAVYTAMEYRWPFGNYLCKIASASVSFNLYASVFLLTCLSIDRYLAIVHPMKSRLRRTMLVAKVTCIIIWLLAGLASLPAIIHRNVFFIENTNITVCAFHYESQNSTLPIGLGLTKNILGFLFPFLIILTSYTLIWKALKRAYEIQKNKPRNDDIFKIIMAIVLFFFFSWIPHQIFTFLDVLIQLGIIRDCRIADIVDTAMPITICIAYFNNCLNPLFYGFLGKKFKRYFLQLLKYIPPKAKSHSNLSTKMSTLSYRPSDNVSSSTKKPAPCFEVE
Protein: ORF46 (Q9AZ58)
Organism: Lactococcus phage TP901-1
Interaction partners:
Sequence:
MYKFRDTTKQKHYRNLPFIPTSAMSYDGAWLEELIEGYQTLAVEGREMYSLSFETQDMQVGGVITNVKYPPRELTIKYKLEDRDPRVLQEKFDTLKAFLIRQEDVPIIFNDDLEYTFYGRFKTADNVAGDTNSIISSFTVLCSDPFKHGKIQSVKNKVIEVLPYPVKPDKLSFKLLTEGLLATDGNYRLKSSQAKKGDFLEFDFQTGDTFLNGKVNNNLLDLDSDFKNIRLTTGTDFSSSNYELTIQYRKAVL
Protein: Leucine-rich repeat protein SHOC-2 (Protein soc-2 homolog) (Protein sur-8 homolog) (Q9UQ13)
Organism: Homo sapiens (Human)
Function: Regulatory subunit of protein phosphatase 1 (PP1c) that acts as a M-Ras/MRAS effector and participates in MAPK pathway activation. Upon M-Ras/MRAS activation, targets PP1c to specifically dephosphorylate the 'Ser-259' inhibitory site of RAF1 kinase and stimulate RAF1 activity at specialized signaling complexes.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:19684605, ECO:0000269|PubMed:25137548}. Nucleus {ECO:0000269|PubMed:19684605, ECO:0000269|PubMed:25137548}. Note=Translocates from cytoplasm to nucleus upon growth factor stimulation. {ECO:0000269|PubMed:19684605}.
Interaction partners:
- Ras-related protein M-Ras
- Serine/threonine-protein phosphatase PP1-gamma catalytic subunit
- GTPase HRas
- GTPase KRas
- GTPase NRas
- RAF proto-oncogene serine/threonine-protein kinase
- Serine/threonine-protein phosphatase PP1-beta catalytic subunit
- Ras-related protein R-Ras
- Serine/threonine-protein phosphatase PP1-alpha catalytic subunit
- Ras-related protein R-Ras2
Sequence:
MSSSLGKEKDSKEKDPKVPSAKEREKEAKASGGFGKESKEKEPKTKGKDAKDGKKDSSAAQPGVAFSVDNTIKRPNPAPGTRKKSSNAEVIKELNKCREENSMRLDLSKRSIHILPSSIKELTQLTELYLYSNKLQSLPAEVGCLVNLMTLALSENSLTSLPDSLDNLKKLRMLDLRHNKLREIPSVVYRLDSLTTLYLRFNRITTVEKDIKNLSKLSMLSIRENKIKQLPAEIGELCNLITLDVAHNQLEHLPKEIGNCTQITNLDLQHNELLDLPDTIGNLSSLSRLGLRYNRLSAIPRSLAKCSALEELNLENNNISTLPESLLSSLVKLNSLTLARNCFQLYPVGGPSQFSTIYSLNMEHNRINKIPFGIFSRAKVLSKLNMKDNQLTSLPLDFGTWTSMVELNLATNQLTKIPEDVSGLVSLEVLILSNNLLKKLPHGLGNLRKLRELDLEENKLESLPNEIAYLKDLQKLVLTNNQLTTLPRGIGHLTNLTHLGLGENLLTHLPEEIGTLENLEELYLNDNPNLHSLPFELALCSKLSIMSIENCPLSHLPPQIVAGGPSFIIQFLKMQGPYRAMV
Protein: TA01656p1 (Uncharacterized protein, isoform A) (Uncharacterized protein, isoform B (EC 1.3.1.24, EC 1.5.1.30)) (Q9VH72)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- NADH dehydrogenase iron-sulfur protein 3, mitochondrial
- Cytochrome b-c1 complex subunit Rieske, mitochondrial
- NADH dehydrogenase 1 alpha subcomplex subunit 8
- NADH dehydrogenase 1 alpha subcomplex subunit 12
- NADH dehydrogenase 13 kDa B subunit
- NADH dehydrogenase iron-sulfur protein 4
- NADH dehydrogenase 23 kDa subunit
- NADH dehydrogenase 1 beta subcomplex subunit 8, mitochondrial
- NADH dehydrogenase 1 alpha subcomplex subunit 2
- NADH dehydrogenase 1 alpha subcomplex subunit 6
Sequence:
MQRIAIIGGTGMTGECAVDHALQKGLSVKLLYRSEKTVPERFKSKVELVKGDVTNYEDVQRVIEGVDAVAVILGTRNKLEATTELSRGTENLIKAMKEAKLTKFSIVMSSFLLRPLNEVPTVFHRLNEEHQRMLDLTKACDLDWIAILPPHIADEPATAYTVLHDEAPGRLVSKYDLGKFIIDSLEQPEHYRKVCGIGKSPKSA
Protein: Potassium channel subfamily K member 9 (Acid-sensitive potassium channel protein TASK-3) (TWIK-related acid-sensitive K(+) channel 3) (Two pore potassium channel KT3.2) (Two pore K(+) channel KT3.2) (Q9ES08)
Organism: Rattus norvegicus (Rat)
Function: pH-dependent, voltage-insensitive, background potassium channel protein.
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:Q3LS21}; Multi-pass membrane protein {ECO:0000255}. Mitochondrion inner membrane {ECO:0000250|UniProtKB:Q3LS21}; Multi-pass membrane protein {ECO:0000255}. Cell projection, dendrite {ECO:0000250|UniProtKB:Q3LS21}. Note=Colocalizes with MAP2 in the soma and proximal dendrites of dentate gyrus granule cells. {ECO:0000250|UniProtKB:Q3LS21}.
Interaction partners:
- Potassium channel subfamily K member 3 channel 1)
- Potassium two pore domain channel subfamily K member 5
- Potassium channel subfamily K member 10
- Potassium channel subfamily K member 18
- Transient receptor potential cation channel subfamily M member 8
- Potassium channel subfamily K member 4
Sequence:
MKRQNVRTLSLIACTFTYLLVGAAVFDALESDHEMREEEKLKAEEVRLRGKYNISSDDYQQLELVILQSEPHRAGVQWKFAGSFYFAITVITTIGYGHAAPGTDAGKAFCMFYAVLGIPLTLVMFQSLGERMNTFVRYLLKRIKKCCGMRNTEVSMENMVTVGFFSCMGTLCLGAAAFSQCEDWSFFHAYYYCFITLTTIGFGDFVALQSKGALQRKPFYVAFSFMYILVGLTVIGAFLNLVVLRFLTMNTDEDLLEGEVAQILAGNPRRVVVRVPQSRKRHHPMYFLRKYGRTLCYLCFPGANWGDDDDDDDDAVENVVVTTPVPPAVAAAAAAATPGPSTRNVRATVHSVSCRVEEIPPDVLRNTYFRSPFGAIPPGMHTCGENHRLHIRRKSI
Protein: FiLamiN (Actin binding protein) homolog (D0IMZ6)
Organism: Caenorhabditis elegans
Interaction partners:
Sequence:
MPPTQKKEVAEIIDNLDGTILVKYTPKVHGSHELSILQNGAQLQGTPIKFYVDAYGDGWATVYGPGLQNAVVGEPATFTVCAKGSQAKELSVSIEGPAKSQIKIHDNKDGTCSAAWVPPVPGEYKVHVKLGGKAVKDSPFRVLVMGEGQKRSHLSVGSTSEVALPITQQELKGISASIKSPGGIEEPCFVRLLDGGRLGVSFTPREAGEHLITVKRDGKLVPKAPFKIKVDKTQVGDASKVEVSGSGKAKGITLQANELLVDTSKAGYGGLSVSVQGPSKAELTCKEVKSGLIKVLYTPTEPGVYAIAIKFADHHVKDSPLTVQCTGKSAGRVIQTIQKDVEQHGICLPDQESHLFLKLLNTSPMDITARLMDPKGHTDDIEMRDLGQQYYQLKFTPKMEGIHTLSVMYKDAHVNGSPFQFTVGSFSEGGAHKVRAAGQGVVRGETGTFNAFNIYHREAGVGAVAVTIEGPSKATLEFKDHNDGNCHVDYKVATPGEYVVAVKFNDQHIPDSPFKVYIAPATGEVRKLELAQFHGQGIPAGKAFTFTVLTHRAKGHLEAKVVTPNNEVDTIDIVPIEDGESYAMRFVPKETGNHFIHVTLDGAPMRESPFRLRVGGKDLCDPTAISASGDGLVKGTTGQKCEFVINTANAGAGILTVQMDGPSKATLDAYELEKGYKVRYTPLAPGSYFASVKYNGIHAPGSPFKIPVEGKELGGNGYNETSHVKIDAVAKTSKGTVAVVPEYQGDAAKVTAKGAGLNKFFPGRPAAFQIDTGLAGTNLLMVGVVTTKGPCEEVVVRHQGSGHYVCSYRIPDRVKGFVFIKYGDKEIPGSPFAIEP
Protein: NAD(P)-binding Rossmann-fold superfamily protein (Q9LDY7)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
Sequence:
MWPFWWKGASGFSARSTAEEVTHGIDGTGLTAIVTGASSGIGEETTRVLALRGVHVVMAVRNTDSGNQVRDKILKEIPQAKIDVMKLDLSSMASVRSFASEYQSLDLPLNLLINNAGIMACPFLLSSDNIELQFATNHLGHFLLTNLLLERMKKTASESNREGRIVIVSSEGHRFAYREGVQFDKINDEARYNTLQAYGQSKLGNILHATELARLFKEQGVNITANSLHPGSIMTNLLRYHSFINTIGNAVGKYVLKSIPQGAATTCYAALHPQAKGVSGEYLMDNNISDPNSQGKDKDLAKKLWEFSLRLTGEEES
Protein: Endoplasmic reticulum chaperone BiP (EC 3.6.4.10) (78 kDa glucose-regulated protein homolog) (GRP-78) (Immunoglobulin heavy chain-binding protein homolog) (BiP) (P16474)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Probably plays a role in facilitating the assembly of multimeric protein complexes inside the ER. Is required for secretory polypeptide translocation. May physically associate with SEC63 protein in the endoplasmic reticulum and this interaction may be regulated by ATP hydrolysis.
Subcellular location: Endoplasmic reticulum lumen {ECO:0000255|PROSITE-ProRule:PRU10138, ECO:0000269|PubMed:2661018}.
Interaction partners:
- Protein OS-9 homolog
- Serine/threonine-protein kinase/endoribonuclease IRE1
- Nucleotide exchange factor SIL1
- Heat shock protein 70 homolog LHS1
- Protein translocation protein SEC63
- DER1-like family member protein 1
- ERAD-associated E3 ubiquitin-protein ligase component HRD3
- DnaJ-related protein SCJ1
- Calnexin homolog
- Protein disulfide-isomerase
Sequence:
MFFNRLSAGKLLVPLSVVLYALFVVILPLQNSFHSSNVLVRGADDVENYGTVIGIDLGTTYSCVAVMKNGKTEILANEQGNRITPSYVAFTDDERLIGDAAKNQVAANPQNTIFDIKRLIGLKYNDRSVQKDIKHLPFNVVNKDGKPAVEVSVKGEKKVFTPEEISGMILGKMKQIAEDYLGTKVTHAVVTVPAYFNDAQRQATKDAGTIAGLNVLRIVNEPTAAAIAYGLDKSDKEHQIIVYDLGGGTFDVSLLSIENGVFEVQATSGDTHLGGEDFDYKIVRQLIKAFKKKHGIDVSDNNKALAKLKREAEKAKRALSSQMSTRIEIDSFVDGIDLSETLTRAKFEELNLDLFKKTLKPVEKVLQDSGLEKKDVDDIVLVGGSTRIPKVQQLLESYFDGKKASKGINPDEAVAYGAAVQAGVLSGEEGVEDIVLLDVNALTLGIETTGGVMTPLIKRNTAIPTKKSQIFSTAVDNQPTVMIKVYEGERAMSKDNNLLGKFELTGIPPAPRGVPQIEVTFALDANGILKVSATDKGTGKSESITITNDKGRLTQEEIDRMVEEAEKFASEDASIKAKVESRNKLENYAHSLKNQVNGDLGEKLEEEDKETLLDAANDVLEWLDDNFETAIAEDFDEKFESLSKVAYPITSKLYGGADGSGAADYDDEDEDDDGDYFEHDEL
Protein: GrpE protein homolog 1, mitochondrial (Q9FLP3)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Essential component of the PAM complex, a complex required for the translocation of transit peptide-containing proteins from the inner membrane into the mitochondrial matrix in an ATP-dependent manner (By similarity). Seems to control the nucleotide-dependent binding of mitochondrial HSP70 to substrate proteins (By similarity). Binds ATP. Interacts with copper ions Cu(2+).
Subcellular location: Mitochondrion matrix {ECO:0000269|PubMed:17137349}.
Interaction partners:
- Mitochondrial import inner membrane translocase subunit TIM50
- Mitochondrial import inner membrane translocase subunit PAM16 like 2
- Mitochondrial import inner membrane translocase subunit TIM44-1
- Probable mitochondrial import inner membrane translocase subunit TIM21
- Heat shock 70 kDa protein 4
- Mitochondrial import inner membrane translocase subunit PAM16 like 1
- Mitochondrial import inner membrane translocase subunit TIM44-2
- Mitochondrial import inner membrane translocase subunit TIM17-1
- Mitochondrial import inner membrane translocase subunit TIM10
- Mitochondrial import inner membrane translocase subunit TIM14-3
Sequence:
MLVSRVLSRVSRSAGLRSSFSSVVTPKRNQIPIVASRFHSLVHGTPNKLVAVPVSLRNHGTLDLNVLQRFGFFSSSSAEPKGNESNTEVPKTGETSENVEVGKATDAEIDFDDLSRDDLVKLVSEKEDLLKVQQKDIMEMKDKFLRTYAEQQNLMDRTNRNAESAKKFAVQNFATSLLDVADNLERASSVVKESFSKIDTSKDLAGATPLLKNLLEGVEMTEKQLAEVFRKAGLVKEDPLNEPFNPNRHNAVFQVPDASKPKGTIAHVLKSGYSLYDRVIRPAEVGVTCAVENQEGGKESAA
Protein: Sterol 12alpha-hydroxylase P450 (Q9WVT5)
Organism: Rattus norvegicus (Rat)
Subcellular location: Endoplasmic reticulum membrane {ECO:0000256|ARBA:ARBA00004389}; Single-pass membrane protein {ECO:0000256|ARBA:ARBA00004389}.
Interaction partners:
Sequence:
MLWGSVLGALLMAVGCLCLSLLPRHRRPWEPPLDKGFVPWLGHTMAFRKNMFEFLKGMRAKHGDVFTLQLGGQYFTFVMDPLSFGPIIKSTQKVLDFVTYARELVFKVFGYQSMDEDHQMLHVASTKHLMGQGLEDLNRAMLDSLSLVMLGPKGRSLGARSWCEDGLFHFCYSILFKAGFLSLFGCTKDKEQDLDEADELFRKFRRFDLLFPRFVYSLLGPLEWVEVSQLQRLFHQRLSVEQNLEKDGISNWLGFMLRFLRERGMASSMQDKFNFMMLWASQGNTGPTCFWALLFLLKHQDAMKAVREEATRVLGEARLEAETSFAFTLSALKCTPVLDSVMEETLRLCATPTLLGVVQEDYVLKMASGQEYQIRRGDKVALFPYLSVHMDPDIHPEPTTFKYNRFLNPDGTRKVDFYKSGKKIHHYNMPWGSGVSICPGRFFAPSEMKTFVLLMVMYFDFELVDPDMPVPPIDPRRWGFGTSQPSHEVRFRYRLKPMQ
Protein: Calcium-binding protein M (Q54LX0)
Organism: Dictyostelium discoideum (Social amoeba)
Interaction partners:
- Probable serine/threonine-protein kinase roco6
- Probable serine/threonine-protein kinase roco8
- Probable serine/threonine-protein kinase qkgA
- Probable serine/threonine-protein kinase roco5
- Probable serine/threonine-protein kinase roco11
Sequence:
MGQQNSKLTKSDIEFIGKNSNFSKEEVANIYGEFKKFDKDGNGSFDRKEFVLFFKSKLPNYPEDNLNKLFDAFDSDKSNTIDFKELTVALSIIGKGSAEDKLKVLFDIYDKDKSGILEKKEVDEMIALMKNVGVSLGKSPGDIELFIVKLFEKIDKDKNNLISREEFLTEGARSPSLLTLLGI
Protein: Amyloid-beta A4 precursor protein-binding family B member 3 (Protein Fe65-like 2) (Fe65L2) (Q8R1C9)
Organism: Mus musculus (Mouse)
Function: May modulate the internalization of amyloid-beta precursor protein.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:O95704}. Nucleus {ECO:0000250|UniProtKB:O95704}.
Interaction partners:
- Amyloid-beta precursor protein
Sequence:
MLGKDYMLAIILVNCDDDLWGDQNLEGETGLPPGWRKIRDAAGTYYWHVPSGSTQWQRPTWELPGAEDPGRGTEGIWELRPPKGRSFSSLDSSLNRSNSLTWYSEDSYVRSLEPGAKCFAVRSLGWVEVPEEDLAPGKSSIAVNNCIQQLAQTRNRSQPHDGTWGEGQNMLMILKKDAMSLLNPLDHSLIHCQPLVHIRVWGVGSSKGRDRDFAFVAGDKDSCMLKCHVFHCDVPAKAIASALQGLCAQILSERVGVSGEAACCSPDPISPEDLPRQVELLDAVSQAAQKYEALYMGILPVTKAMGMDVLNEAIGTLTARGDRKTWVPAMLSVSDSLMTAHAIQAEAGAEEEPLWQCPVRLVTFIGVGRDPHTFGLIADLGCQSFQCAAFWCEPHAGGLSEAVQAACMVQYQKCLVASAARGKAWGAQARARLRLKRTSSMDSPGGPLPPPLLKGGAGGAGAAPRKRGVFSFLDAFRLKPSLLHMS
Protein: L-seryl-tRNA(Sec) selenium transferase (EC 2.9.1.1) (Selenocysteine synthase) (Sec synthase) (Selenocysteinyl-tRNA(Sec) synthase) (O67140)
Organism: Aquifex aeolicus (strain VF5)
Function: Converts seryl-tRNA(Sec) to selenocysteinyl-tRNA(Sec) required for selenoprotein biosynthesis.
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00423}.
Interaction partners:
- Selenide, water dikinase
- Selenocysteine-specific elongation factor
- Serine--tRNA ligase
- Shikimate kinase
Sequence:
MKSLLRQIPQISKVVEIFKKKYPEIYVVKAAREVAEKYRKEIIEGKRKDLNGFLEDVERKIKSLMKPNIKRVINATGVVINTNLGRAPLSKDVINFISEIANGYSNLEYNLEEGKRGSRIAHIEKYLNELTGAESSFVVNNNAGAVFLVLNTLAEGKEVIISRGELVEIGGSFRIPDIMKKSGAILREVGTTNKTKVSDYEGAINQNTALLMKVHKSNFYMEGFVEEVKLEDLVKLGHKYGIPTYYDAGSGLLINLKEFGISVDEPNFRDCISLGIDLVSGSGDKLLGGPQAGIIVGKKNLIEKIKKNPIARALRIDKLTLSGLEMTLKLYFEKRYEDIPVIRMLTQDEKALRQKAKRLEKLLKDIPGLKISVIKDKAKPGGGSLPELELPTYCVAIRHDRLSSQELSRRLRLAEPPIVCRIREDQLLFDMRTVFHEDLKTIKKTLQELLSI
Protein: Autophagy-related protein 18g (AtATG18g) (Q8GUL1)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: The PI(3,5)P2 regulatory complex regulates both the synthesis and turnover of phosphatidylinositol 3,5-bisphosphate (PtdIns(3,5)P2). Required for autophagy (By similarity).
Subcellular location: Preautophagosomal structure membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Vacuole membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Note=Peripheral membrane protein of pre-autophagosomal structure (PAS) and vacuole. {ECO:0000250}.
Interaction partners:
- Autophagy-related protein 18c
- Autophagy-related protein 18e
- Autophagy-related protein 18b
- Autophagy-related protein 9
- Serine/threonine-protein kinase ATG1c
- Autophagy-related protein 11
- Autophagy-related protein 13b
- Autophagy-related protein 2
- Ubiquitin-like protein ATG12A
- Autophagy-related protein 8b
Sequence:
MMKKGKGKNSGLLPNSFKIISSCLKTVSANATNVASSVRSAGASVAASISAAEDDKDQVTWAGFGILELGQHVTRHVLLLGYQNGFQVFDVEDASNFNELVSKRGGPVSFLQMQPLPARSGDHEGFWNSHPLLLVVAGDETNGTGLGHSFSQNGSLARDGSSDSKAGDAINYPTTVRFYSLRSHSYVYVLRFRSSVCMIRCSSRVVAVGLANQIYCVDALTLENKFSVLTYPVPQPVRQGTTRVNVGYGPMAVGPRWLAYASKSSMTMKTGRLSPQTFTSSPSLSPSSSSGGSSFMARYAMESSKQLANGLINLGDMGYKTLSKYCQDMLPDGSTSPASPNAIWKVGGVSGSDAENAGMVAVKDLVSGALVSQFKAHTSPISALCFDPSGTLLVTASVCGNNINVFQIMPSRSHNAPGDLSYEWESSHVHLFKLHRGITSAIVQDICFSQQSQWVAIISSKGTCHIFVLNSSGSDAAFQPCEGEEPTRLPASSLPWWFTQSLSSNQQSLSPPTAVALSVVSRIKYSSFGWLNTVSNATTAATGKVFVPSGAVAAVFHKSVTHDLQLNSRTNALEHILVYTPSGHVVQHELLPSVCTESPENGLRVQKTSHVQVQEDDLRVKVEPIQWWDVCRRSDWLETEERLPKSITEKQYDLETVSNHLTSHEDACLSLDMNSHFSEDKYLKSCSEKPPERSHCYLSNFEVKVTSGMLPVWQNSKISFHVMDSPRDSSSTGGEFEIEKVPAHELEIKQKKLLPVFDHFHSTKATLEDRFSMKCYHTSATGSHQVNGKICQDIINCHSKPGSIESAESSEEGSTKQMENLHDSDHMSNSIKSSLPLYPTVNGIYKEIEKNNANGWMEKPVTAKLSTLKETRITNGFTTPPILTDSVNEQMLSTGKPPMGFGFALHEEHCKAVADPKEEHLKKKLDEVTNVHHLNVNNNNTEKLQGDKMVHGMVSFVGD
Protein: LEE-encoded effector Map (B7UMA0)
Organism: Escherichia coli O127:H6 (strain E2348/69 / EPEC)
Interaction partners:
Sequence:
MFSPTAMVGRALAQAVTQTLRPAVTKAATQAGMAASGMRFTPMQSNLMINHGKLTTQLLQAVAKQTGSSDTQQWFKQEQITFLSRAVNKTVDDYCMSNNSAISKETKCRIFKEVESAIQQPLDMNCAQSSISHFLQSNKYFNQKVDEQCGKGVDPITRFNTQTKLIEQVSREIFEQNFSTAKISDIKALTEKAIADNVQDTRL
Protein: Glutathione S transferase E10, isoform A (EC 2.5.1.18) (Glutathione S transferase E10, isoform B) (IP08242p) (Q4V6J1)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Bifunctional glutamate/proline--tRNA ligase
- Uncharacterized protein, isoform C
- folate gamma-glutamyl hydrolase
- folate gamma-glutamyl hydrolase
- Glutathione peroxidase
Sequence:
MANLILYGTESSPPVRAVLLTLRALQLDHEFHTLDMQAGDHLKPDMLRKNPQHTVPMLEDGESCIWDSHAIIGYLVNKYAQSDELYPKDPLKRAVVDQRLHFETGVLFHGIFKQLQRALFKENATEVPKDRLAELKDAYALLEQFLAENPYVAGPQLTIADFSIVATVSTLHLSYCPVDATKYPKLSAWLARISALPFYEEDNLRGARLLADKIRSKLPKQFDKLWQKAFEDIKSGAGKQ