wanglab/gogpt-training-data huggingface dataset:
Protein: ProSAAS (Proprotein convertase subtilisin/kexin type 1 inhibitor) (Proprotein convertase 1 inhibitor) (pro-SAAS) [Cleaved into: KEP; Big SAAS (b-SAAS); Little SAAS (l-SAAS) (N-proSAAS); Big PEN-LEN (b-PEN-LEN) (SAAS CT(1-49)); PEN; Little LEN (l-LEN); Big LEN (b-LEN) (SAAS CT(25-40))] (Q9UHG2)
Organism: Homo sapiens (Human)
Function: May function in the control of the neuroendocrine secretory pathway. Proposed be a specific endogenous inhibitor of PCSK1. ProSAAS and Big PEN-LEN, both containing the C-terminal inhibitory domain, but not the further processed peptides reduce PCSK1 activity in the endoplasmic reticulum and Golgi. It reduces the activity of the 84 kDa form but not the autocatalytically derived 66 kDa form of PCSK1. Subsequent processing of proSAAS may eliminate the inhibition. Slows down convertase-mediated processing of proopiomelanocortin and proenkephalin. May control the intracellular timing of PCSK1 rather than its total level of activity (By similarity).
Subcellular location: Secreted {ECO:0000250|UniProtKB:Q9QXV0}. Golgi apparatus, trans-Golgi network {ECO:0000250|UniProtKB:Q9QXV0}. Note=A N-terminal processed peptide, probably Big SAAS or Little SAAS, is accumulated in cytoplasmic protein tau deposits in frontotemporal dementia and parkinsonism linked to chromosome 17 (Pick disease), Alzheimer disease and amyotrophic lateral sclerosis-parkinsonism/dementia complex 1 (Guam disease). {ECO:0000269|PubMed:12914799, ECO:0000269|PubMed:14746899}.
Interaction partners:
- Carboxypeptidase E
- G-protein coupled receptor 171
- Neuroendocrine convertase 1
- Secretogranin-2
- Pro-opiomelanocortin
- Secretogranin-1
Sequence:
MAGSPLLWGPRAGGVGLLVLLLLGLFRPPPALCARPVKEPRGLSAASPPLAETGAPRRFRRSVPRGEAAGAVQELARALAHLLEAERQERARAEAQEAEDQQARVLAQLLRVWGAPRNSDPALGLDDDPDAPAAQLARALLRARLDPAALAAQLVPAPVPAAALRPRPPVYDDGPAGPDAEEAGDETPDVDPELLRYLLGRILAGSADSEGVAAPRRLRRAADHDVGSELPPEGVLGALLRVKRLETPAPQVPARRLLPP
Protein: Histone deacetylase 5 (EC 3.5.1.98) (Q8RX28)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Responsible for the deacetylation of lysine residues on the N-terminal part of the core histones (H2A, H2B, H3 and H4) (Probable). Histone deacetylation gives a tag for epigenetic repression and plays an important role in transcriptional regulation, cell cycle progression and developmental events (Probable). Histone deacetylases act via the formation of large multiprotein complexes. Involved in the regulation of flowering time by repressing FLC and AGL27/MAF1 expression. Forms a histone deacetylase complex with HDA6, FLD and MSI4/FVE that represses FLC gene expression to control flowering time. Unlike its tandem duplication HDA18, HDA5 does not seem to be required for the cellular patterning in the root epidermis.
Subcellular location: Nucleus {ECO:0000269|PubMed:22363501}. Cytoplasm {ECO:0000269|PubMed:22363501}.
Interaction partners:
- WD-40 repeat-containing protein MSI4
- Histone deacetylase 17
- Putative histone deacetylase 10
- NAD-dependent protein deacylase SRT2
- Histone deacetylase 6
- NAD-dependent protein deacetylase SRT1
- Histone deacetylase HDT2
- High mobility group B protein 9
- WD-40 repeat-containing protein MSI5
- High mobility group B protein 15
Sequence:
MAMAGESSGKKIGDCDGKVAGNRQRKVGLIYDETMCKHDTPDGEDHPECPDRIRVIWEKLQLAGVSQRCVVLGSSKAEDKHLQLVHTKDHVNLVKSISTKQKDYRRNRIASQLNSIYLNGGSSEAAYLAAGSVVKLAEKVAEGELDCGFAIVRPPGHHAEADEAMGFCLFNNVAVAASFLLNERPDLGVKKILIVDWDVHHGNGTQKMFWKDPRVLFFSVHRHEYGGFYPAGDDGDYNMVGEGPGEGFNINVPWDQGRCGDADYLAAWDHILIPVAREFNPDVIFLSAGFDAAINDPLGGCCVTPYGYSVMLKKLMEFAQGKIVLALEGGYNLDSIAKSSLACVQVLLEDKQIQGPPEAYPFESTWRVIQAVRKRLCTYWPSLADELSWKLINQKTPTPIILISSSDSETEDNAQGLLDQMSKLSIENPQGTLLENHQVEPASTSWRADLAKVDVWYASFGSNMWKPRFLCYIQGGQVDGLKKVCVGSMDKSPPKETVWETFPHRLFFGRESSVGWGVGGVAFTNPLANLIDQTHMCLYRITLEQFNDVLSQENGLNVDSDSPVFDLAALQLVDNKGSILEAPLNSWYGNVVCLGKERDIPILTMTCTLSAVEKFKSGEIPIRPPAKAYANTLIRGLVEGGRLSKEEAEAYIDKAVSKPL
Protein: EG:BACN25G24.3 protein (Fbgn0004860;ph-d protein) (Polyhomeotic distal, isoform B) (Q9NF31)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MEVQQQLQLQQQLSEANGGGAASAGAGGAASPANSQQSQQQQHSTAISTMSPMQLAAATGGVGGDWTQGRTVQLMQPSTSFLYPQMIVSGNLLHPGGLGQQPIQVITAGKPFQGNGPQMLTTTTQNAKQMIGGQAGFAGGNYATCIPSNHNQSPQTVLISPVNVISHSPQQQQNLLQSMAAAAQQQQLTQQQQQQLNQQQQQLNQQQQQQQLTAALAKVGVDAQGKLAQKVVQKVTTTSSTVQAATGPGSTGSTQTQQVQQVQQQQQQTTQTTQQCVQVSQSTLPVGVGGQSVQTAQLLNAGQAQQMQIPWFWQNAAGLQPFGSNQIILRNQPDGTQGMFIQQQPATQTLQTQQNQIIQCNVTQTPTKARTQLDALAPKQQQQQQQVGTTNQTQQQQLAVATAQLQQQQQQLTAAALQRPGAPVMPHNGTQVRPASSVSTQTAQNQSLLKAKMRNKQQPVRPALATLKTEIGQVAGQNKVVGHLTTVQQQQQATNLQQVVNAAGNKMVVMSTTGTPITLQNGQTLHAATAAGVDKQQQQLQLFQKQHILQQQMLQQQIAAIQMQQQQAAVQAQQQQQQQVSQQQQVNAQQQQAVAQQQQAVAQAQQQQREQQQQVAQAQAQHQQALANATQQILQVAPNQFITSHQQQQQQQLHNQLIQQQLQQQAQAQVQAQVQAQAQQQQQQREQQQNIIQQIVVQQSTGATSQQQQQQPQQQSGQLQLSSVPFSVSPSMTAEDIAGITSSALQEALSVSGAIFQTTKPITCSSSTLPTSSVVTITSQSSTPLVTSSTVASMQQAQTQGTQIHQHQQLISATIAGGSQQQQQQQQLGLPSLTPTTPSPTTNPILAMTSMMNATVGHLSTAPPVSVSSTAVTPSSGQLVTLSSASSGGGAGFPATPTKETPSKGPTATLVPIDSPKTPVSGKDTCTTPKSSTPATVSASVEASSSTGEALSNGDASDRSSTPSKGATTPTSKQSNAAVQPPSSTIPNSVSGKEEPKLTTCGSLTSATSTSTTTTITNGIGVARTTASTAVSTASTTTTSSGTFTTSCTSTTTTTTSSISNGSKDLPKAMIKPNVLTHVIDGFIIQEANEPFPVTRQRYADKDVSDEPPKKKATMQEDIKLSGIASAPGSDMVACEQCGKMEHKAKLKRKRYCSPGCSRQAKNGIGGVGSGETNGLGTGGIVGVDAMALVDRLDEAMAEEKMQTESYQTVSDALPIQAATPEVPPISMPVLAAMSTSSPLSLPLTLPLPIAIAPTVSLPVVSAGVVAPVLAIPSSNINGSDRPPISSWSVEEVSNFIRELPGCQDYVDDFIQQEIDGQALLLLKENHLVNAMGMKLGPALKIVAKVESIKEVPPGDVKD
Protein: Cytochrome P450 - like protein (Cytochrome P450, family 706, subfamily A, polypeptide 2) (Cytochrome P450-like protein) (O49652)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- NAD
- UDP-glycosyltransferase 91B1
Sequence:
MGTASSKSNINLSQVLNTEEPYSSVMLAVAALLAVVCYLWIQGKSKSKKEPPLPPGPWPLPIVGNLPFLNSDVLHTQFQALTLKYGPLMKIHLGSKLAIVVSSPDMAREVLKTHDITFANHDLPEVGKINTYGGEDILWSPYGTHWRRLRKLCVMKMFTTPSLEASYSTRREETRQTIVHMSEMAREGSPVNLGEQIFLSIFNVVTRMMWGATVEGDERTSLGNELKTLISDISDIEGIQNYSDFFPLFSRFDFQGLVKQMKGHVKKLDLLFDRVMESHVKMVGKKSEEEEDFLQYLLRVKDDDEKAPLSMTHVKSLLMDMVLGGVDTSVNASEFAMAEIVSRPEVLNKIRLELDQVVGKDNIVEESHLPKLPYLQAVMKETLRLHPTLPLLVPHRNSETSVVAGYTVPKDSKIFINVWAIHRDPKNWDEPNEFKPERFLENSLDFNGGDFKYLPFGSGRRICAAINMAERLVLFNIASLLHSFDWKAPQGQKFEVEEKFGLVLKLKSPLVAIPVPRLSDPKLYTA
Protein: Actin-like protein (Q584P9)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MLSGTTFGASPLARNIADDPEGWPVVVVVGELATYMCRSGDIRPFAQEKPISADVLGKPPPTATESDNDATNSSREEAHSFLLSRLRRHLSHRNIILVAPVRSTLEWHEKLVVFCFEKLQVRTLVMLSDFVADAFAVGCRNALVLHASPSAISIGRVEAGVTVKQATMSYGQLSPLMCETTGDIKHNVLTQQHANAGTNCREGDNQTRESVSSGTAVIPGKLPSDDSVFSSVFSAASPKVVDLLDEVHHDALASLVGENVYNRVVSSMREGRPNQRKLRATKRDRASNSGGRRSSRNGRVNAAANVSENSSKRSLIDISSSGGDEGGESEEDDGEGPLIRLILSVAGREPVPVIIAGEALRVAPSLQKFLEEAVRACGTSHMKRACNDDSNSSSSSSTASSSSSSGGASSFSSSLSTPSDGQEVLKIQPLPIGELPWELSLLGGSLVSQLPMLELCKLYISREDALSSKGSIIRWRSVI
Protein: Probable GTP cyclohydrolase-2 (EC 3.5.4.25) (GTP cyclohydrolase II) (Q9P7M9)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus {ECO:0000269|PubMed:16823372}.
Interaction partners:
- Riboflavin synthase
- 6,7-dimethyl-8-ribityllumazine synthase
- 2,5-diamino-6-ribosylamino-4
- 3,4-dihydroxy-2-butanone 4-phosphate synthase
- GTP cyclohydrolase 1
- Diaminohydroxyphosphoribosylamino-pyrimidine deaminase
- Nucleoside diphosphate kinase
- Inosine triphosphate pyrophosphatase
- Adenylate cyclase
- Golgi apyrase
Sequence:
MDKKEGDQVHHDKTLLQDLSLPENVASEKRLPIDDVQCVNSPMLSPALDIEPKPNVVGTAERLPKVRCVVRARIPTVKGTEIFLHLYKNDFDNKEHLAIVFGQQIRSDSLDAVQEGETEMDRMVRGAYVGTLYPGRKSSYIDVNSSKTTEEQKEEARKTNFVPLVRIHSECYTGETAWSARCDCGEQLDEAARLISEEGNGVIIYLRQEGRGIGLSEKLKAYNLQDLGNDTVQANLLLQHPADGRSYAVATAMLMDLGQRDIRLLTNNPEKVNSIEGPNKEVRVVERISMIPKSWRGEKGIESAEVVLYLKTKIEKMGHLLDLPDS
Protein: Guanylate cyclase (EC 4.6.1.2) (F1QWF7)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Photoreceptor outer segment membrane {ECO:0000256|ARBA:ARBA00004451}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004451}.
Interaction partners:
Sequence:
MRHIHLPFGGALWQFSSYPCCPVLRSRRSLSTLPFYSITLWIILGVLTFPRCVQCLVFKVGIIGPWNCDPNYAKSLPAIASRLAVGRINNDFSLDLGCTMDFVILQEACETSKALTSFVQYENVADAFVGPTNPGYCNAAALMSKNWDKSLFSWACVNHELDRVQGYPTFARTLPSPLRVLFNVLKFFRWANIGIVSSNEDIWIDTAAKLASALRNRGLPVGIVTSMGNNDTMLENTLMSIKNAGDIKVIIMCMHSVLIGGEQQATFLTKAYDMGLASGRYVFIPYDTLLYSLPYINITYYPLQNNSKLSKAYDAVLTITLDSDIMTFNEAFNAAKQLGELMVTQEPEQVSPLFGTIYNSLYLLAKSMHNARRAGRWLSGTNLAYFTRNITFTGFNQDIQTDEQGNGQTNYVILDTEAWGTQLYRCFLVDMTSDLVLFAGRFIHFPGESPPPSDSRCWFEDNAICTGGVDIIYVIIAFVIVLIIVLGSIGLSLFIRRRIQQIQLIKGPNRILLTLEDLTFINPQLSKRKITLEDLSDSKSYIEEKSTGDRSRSVNSMATATHETSNVAVYEGDWVWLKKFTEGHFKEVKQSTTKIFTKMKDLRNENVNPFLGFFTDCEMFAIVTEHCSRGSLHDLLRNDDVKLDWMFKSSLVLDLIKGMKYLHHREFPHGRLKSRNCVVDGRFVLKITDYGYNEILETQKAPKETLPPEDLFWTAPEHLRDPESPRKGTYKGDVYSFAIILQEVVVRGAPYCMLGLSPEEIIRKVKKPPPMCRPTVAPDQAPLECIQLMKQCWSEQPDRRPPFDQIFDQFKLINKGKKTNIIDSMLRMLEQYSSNLEDLIRERTEELEVEKQRTEKLLSEMLPPSVAEALKTGASVEPEYFDQVTIYFSDIVGFTTISSLSDPIEVVDLLNDLYSLFDAVLGSHDVYKVETIGDAYMVASGLPKKNGNKHAAEIANMSLNILSSVGSFKMRHMPEVPVRIRIGIHSGPCVAGVVGLTMPRYCLFGDTVNTASRMESTGLPYRIHVNISTVQILRSLNDGYKIDVRGKTELKGKGIEETYWLVGKANFTKPLPNPPEIKPGEDNHGLKPEDIEAYKRRKAEKKA
Protein: General odorant-binding protein 1 (GOBP 1) (Q95VP3)
Organism: Epiphyas postvittana (Light brown apple moth)
Function: Present in the aqueous fluid surrounding olfactory sensory dendrites and are thought to aid in the capture and transport of hydrophobic odorants into and through this fluid.
Interaction partners:
Sequence:
MATVSKWRMLVLTLCLTGVWQVESSADVMKKLTTGFATALEKCRDELNLPDAVMQDFFNFWREDYELVNRDMGCAIMCMATKFDLVTEEQKLHHGNAHEFAKSHGADDSMAKQLVTMLHECETQTASISDDCGRTLEIAKCFRTKIHGLKWAPSMETILEEVMTEV
Protein: cAMP-dependent protein kinase catalytic subunit (EC 2.7.11.11) (Dd GPK2) (DdPK3) (P34099)
Organism: Dictyostelium discoideum (Social amoeba)
Function: Essential for differentiation and fruit morphogenesis.
Interaction partners:
- cAMP-dependent protein kinase regulatory subunit
- cAMP/cGMP-dependent 3',5'-cAMP/cGMP phosphodiesterase B
- Adenylate cyclase, aggregation specific
- 3',5'-cyclic-nucleotide phosphodiesterase regA
- cGMP-dependent 3',5'-cGMP phosphodiesterase A
Sequence:
MSNSNNNSSSGNHNSTTINNPKVNVYSNIPNSTTYTYGSGGGGTLSGNNTNNNNTNNNNNNNNNSSGDNKNHSPVTSATDRLTKMDIEEKWDNKNYEKDEREKSPLFHILASNLNSFGNFKVPSTFSLTPPEPNKQQQPQQQPQQQQPQQQQPQQQQPQQQQQQQPQQQQQPQQQLQQNNQQQQQQLQQQQLQQQLQQQQQQQQQQQQQQQQKQQKQQQQQQQHLHQDGIVNTPSTTQTSTTTTTTTTTTNPHTSGLSLQHAHSSYTPSNVLHSPTHFQSSLPTRLDTNPITTPIRQQQQSQQQLQQQQLQQIPPPTVNSFFLPPPVNARERLKEFKQIRVIGTGTFGKVYLIQNTKDGCYYAMKCLNKAYVVQLKQVEHLNSEKSILSSIHHPFIVNLYQAFQDEKKLYLLFEYVAGGEVFTHLRKSMKFSNSTAKFYAAEIVLALEFLHKQNIVYRDLKPENLLIDNQGHIKITDFGFAKRVEDRTFTLCGTPEYLAPEIIQSKGHGKAVDWWALGILIFEMLAGYPPFYDDDTFAIYNKILAGRITFPLGFDVDAKDLIKRLLTADRTRRLGALKDGALDVKNHRWFSDINWERLYQRRDNGPFIPKIQHQGDSSNFEMYDEEEMVEEPPSSNYVDPYAHLFKDF
Protein: Zuotin (DnaJ-related protein ZUO1) (J protein ZUO1) (Heat shock protein 40 homolog ZUO1) (Ribosome-associated complex subunit ZUO1) (P32527)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Component of the ribosome-associated complex (RAC), a heterodimeric chaperone complex involved in regulation of accurate translation termination and in folding or maintaining nascent polypeptides in a folding-competent state. RAC stimulates the ATPase activity of the ribosome-associated pool of Hsp70-type chaperones SSB1/SSB2 that bind to the nascent polypeptide chain. ZUO1 can act as a J-protein for SSB1/SSB2 only when associated with SSZ1.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:14562095}.
Interaction partners:
- Ribosome-associated complex subunit SSZ1
- Mitochondrial protein import protein MAS5
- Ribosome-associated molecular chaperone SSB2
- Protein SIS1
- Auxilin-like clathrin uncoating factor SWA2
- DnaJ protein homolog XDJ1
- Large ribosomal subunit protein eL31A
- J protein JJJ2
- Ribosome-associated molecular chaperone SSB1
- Pre-mRNA-splicing factor CWC23
Sequence:
MFSLPTLTSDITVEVNSSATKTPFVRRPVEPVGKFFLQHAQRTLRNHTWSEFERIEAEKNVKTVDESNVDPDELLFDTELADEDLLTHDARDWKTADLYAAMGLSKLRFRATESQIIKAHRKQVVKYHPDKQSAAGGSLDQDGFFKIIQKAFETLTDSNKRAQYDSCDFVADVPPPKKGTDYDFYEAWGPVFEAEARFSKKTPIPSLGNKDSSKKEVEQFYAFWHRFDSWRTFEFLDEDVPDDSSNRDHKRYIERKNKAARDKKKTADNARLVKLVERAVSEDPRIKMFKEEEKKEKERRKWEREAGARAEAEAKAKAEAEAKAKAESEAKANASAKADKKKAKEAAKAAKKKNKRAIRNSAKEADYFGDADKATTIDEQVGLIVDSLNDEELVSTADKIKANAAGAKEVLKESAKTIVDSGKLPSSLLSYFV
Protein: Alpha-1-antiproteinase-like protein (Q7ZZW1)
Organism: Oncorhynchus mykiss (Rainbow trout) (Salmo gairdneri)
Interaction partners:
- Prothrombin
- Prothrombin
- Vitamin K-dependent protein C
- EGF-like domain-containing protein
- Uncharacterized protein
- EGF-like domain-containing protein
- Fibrinogen C-terminal domain-containing protein
- Antithrombin-III
- Antithrombin-III
- Serpin domain-containing protein
Sequence:
MWGISYCTIVAVLLCVALAAPHDGDHAGHTEDHHHHLHHIAGEAHPQHSHGDEESCHKLAPHNADFAFTLYRSLSKANTENMNIFFSPLGIATSLAMLSLGAKGDTHSQLYSTLGYGAFTPEQVNNAYEHLYHMLGHTGEAMQLDMGNALALRDGFKPLAKFLEDAKHFYASEGFTVDFKNPAEATAEINKFIAKKTQDKITDMVKDLDPDTAMMLINYVFFRGKWDKPFDATLTHKADFKVDENTKVQVDMMKRTGRYELYQDQDNFTTVVILPYKGNSSMMVVLPNDGKMEHVEAFINKDYLKHVHEHLFRTNVDIFMPKFSTSTSYSLGDHLKDMGVVSAFGDSADFSAISEDTKLKVSKVTHKAVLSVDEKGTEAAAVTTIEIMPMSLPDTIMLNRPFLLFILEDSTKSIVFMGKVTNPSSK
Protein: Uncharacterized protein (Q386G2)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MDTLTYVCRECEASALRIEVPLISVKATAFNDDVPALISSHRRLLCMNMKQSNRLRVLTHRGSYAEVEVGATVLRNLVSSEGLLEHCYFFAAGGNVVARLAPIRQANGDVKIEKREVRLPEEVYGVTVGYGDIVYVLGRSCAFEVHMESSKTSPIGLAPRTFVKHSVIGYHQQAKLLLAPAKANCLDLVSATAGTSVLPKVWEPHANSMPTAAFFFQRRSFSNENSDNLFIVTASHGNRELRLWSYSQRTKTFTLKQDISITMEDDGVVDGDENAFLISCTPTEEYITLCSKQRPLAVVLELNRSSFKVDRVTSWRLNGPVLGSVAAVSKMTESASSTSVEYQVILTVRTATGFYGEVLDVEKPAEASNTPSLRTNSASSWFPKNEAAHIGGTEIALPTALTSVSSSVLGDKTTNAVPQGVASNIVRQQASQFCETLRSIDERVVNLQKHASEAMRLLQEAWEREKAQTIGREFAIRNKGRLEQQQQVAGQSTDNLTPRQQELLEEIRSIVEKSEQLAVDTATEVVKAQLSRRLKDAVAKGAKEADQVELSSGTPIVRSTDSMRLFSNGVDAAVRTLVRAVKGYHKTMKTVVDSSSAATASCVAKAREFTASLNREKQLLASELMATMEVVRHGGAPTQPVDPDALVARAIALAEANDWVTSFTTVLGASDITVLLHFLESEVCVNNVTAMVNPQSITLPIFLSLCLQLSFELNNLQGLIPSRVKALHAFFVEWDDTLKDMKSRAADGNSKHKPMFELTKRELRNVLEQLEIVDDKAVDRCSRNNLRLLKKLIHFLVT
Protein: Elongation factor G, mitochondrial (EF-Gmt) (EC 3.6.5.-) (Elongation factor G 1, mitochondrial) (mEF-G 1) (Elongation factor G1) (hEFG1) (Q96RP9)
Organism: Homo sapiens (Human)
Function: Mitochondrial GTPase that catalyzes the GTP-dependent ribosomal translocation step during translation elongation. During this step, the ribosome changes from the pre-translocational (PRE) to the post-translocational (POST) state as the newly formed A-site-bound peptidyl-tRNA and P-site-bound deacylated tRNA move to the P and E sites, respectively. Catalyzes the coordinated movement of the two tRNA molecules, the mRNA and conformational changes in the ribosome. Does not mediate the disassembly of ribosomes from messenger RNA at the termination of mitochondrial protein biosynthesis.
Subcellular location: Mitochondrion {ECO:0000255|HAMAP-Rule:MF_03061}.
Interaction partners:
- Small ribosomal subunit protein bS16m
- Ribosome-recycling factor, mitochondrial
- Elongation factor Ts, mitochondrial
- Large ribosomal subunit protein bL12m
- Small ribosomal subunit protein uS7m
- Large ribosomal subunit protein bL21m
- Large ribosomal subunit protein bL9m
- Small ribosomal subunit protein uS9m
- Large ribosomal subunit protein bL17m
- Small ribosomal subunit protein bS6m
Sequence:
MRLLGAAAVAALGRGRAPASLGWQRKQVNWKACRWSSSGVIPNEKIRNIGISAHIDSGKTTLTERVLYYTGRIAKMHEVKGKDGVGAVMDSMELERQRGITIQSAATYTMWKDVNINIIDTPGHVDFTIEVERALRVLDGAVLVLCAVGGVQCQTMTVNRQMKRYNVPFLTFINKLDRMGSNPARALQQMRSKLNHNAAFMQIPMGLEGNFKGIVDLIEERAIYFDGDFGQIVRYGEIPAELRAAATDHRQELIECVANSDEQLGEMFLEEKIPSISDLKLAIRRATLKRSFTPVFLGSALKNKGVQPLLDAVLEYLPNPSEVQNYAILNKEDDSKEKTKILMNSSRDNSHPFVGLAFKLEVGRFGQLTYVRSYQGELKKGDTIYNTRTRKKVRLQRLARMHADMMEDVEEVYAGDICALFGIDCASGDTFTDKANSGLSMESIHVPDPVISIAMKPSNKNDLEKFSKGIGRFTREDPTFKVYFDTENKETVISGMGELHLEIYAQRLEREYGCPCITGKPKVAFRETITAPVPFDFTHKKQSGGAGQYGKVIGVLEPLDPEDYTKLEFSDETFGSNIPKQFVPAVEKGFLDACEKGPLSGHKLSGLRFVLQDGAHHMVDSNEISFIRAGEGALKQALANATLCILEPIMAVEVVAPNEFQGQVIAGINRRHGVITGQDGVEDYFTLYADVPLNDMFGYSTELRSCTEGKGEYTMEYSRYQPCLPSTQEDVINKYLEATGQLPVKKGKAKN
Protein: Beaten path Ia, isoform B (X2J8L2)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- GH26014p
- Fasciclin-2
- GH14967p
- Sidestep, isoform C
Sequence:
MRFPQNAYQTALTTILLALTLEMTAALRDVRVRVPHAVRRSEKAILKCFYDIEDDSLYSVKWYKGRREFYRYTPKETPPMKVFHFPGVKVRRVSSNESQVVLDAVTMATSGKYSCEVSADAPSFHTLIAAAELEVIETPHNAPFITGIRPRYRVGDILRGNCTSRHSRPAANLTWTVNNEEVNPALVRHHKILRDARNDMETAVVGIHFVVTDQHFDNGKLKLRCSAQLHDVYWKTTEKIILETDLFPKHGNGANGNHVNPDDFYDQYALHEDHLHNKKNSYLTQLQEFFFYHFVPSGEEDDGTEGGLGDGGAAWRGAGSSSSRLSPSSSQSCWMVGGSLMAVLSWTLARQLVSPLQAMMTKTGGATCNMSGRCASRRTRAHGMRVSATKQKQKQRQMQQEHRKSCLRVSKSSWKGRGYVCGCGFGRINSRCIRQLT
Protein: Protein Wnt-7a (P24383)
Organism: Mus musculus (Mouse)
Function: Ligand for members of the frizzled family of seven transmembrane receptors that functions in the canonical Wnt/beta-catenin signaling pathway. Plays an important role in embryonic development, including dorsal versus ventral patterning during limb development, skeleton development and urogenital tract development. Required for central nervous system (CNS) angiogenesis and blood-brain barrier regulation. Required for normal, sexually dimorphic development of the Mullerian ducts, and for normal fertility in both sexes. Required for normal neural stem cell proliferation in the hippocampus dentate gyrus. Required for normal progress through the cell cycle in neural progenitor cells, for self-renewal of neural stem cells, and for normal neuronal differentiation and maturation. Promotes formation of synapses via its interaction with FZD5.
Subcellular location: Secreted, extracellular space, extracellular matrix {ECO:0000305}. Secreted {ECO:0000305|PubMed:20530549}.
Interaction partners:
- Low-density lipoprotein receptor-related protein 5
- Frizzled-7
- Frizzled-2
- Frizzled-5
- Frizzled-4
- Low-density lipoprotein receptor-related protein 6
- Frizzled-10
- Frizzled-9
- Protein-serine O-palmitoleoyltransferase porcupine
- Wnt inhibitory factor 1
Sequence:
MTRKARRCLGHLFLSLGIVYLRIGGFSSVVALGASIICNKIPGLAPRQRAICQSRPDAIIVIGEGSQMGLDECQFQFRNGRWNCSALGERTVFGKELKVGSREAAFTYAIIAAGVAHAITAACTQGNLSDCGCDKEKQGQYHRDEGWKWGGCSADIRYGIGFAKVFVDAREIKQNARTLMNLHNNEAGRKILEENMKLECKCHGVSGSCTTKTCWTTLPQFRELGYVLKDKYNEAVHVEPVRASRNKRPTFLKIKKPLSYRKPMDTDLVYIEKSPNYCEEDPVTGSVGTQGRACNKTAPQASGCDLMCCGRGYNTHQYARVWQCNCKFHWCCYVKCNTCSERTEMYTCK
Protein: Candida glabrata strain CBS138 chromosome L complete sequence (Q6FKF2)
Organism: Candida glabrata (strain ATCC 2001 / BCRC 20586 / JCM 3761 / NBRC 0622 / NRRL Y-65 / CBS 138) (Yeast) (Nakaseomyces glabratus)
Interaction partners:
- Transcription factor
- Cell division control protein 42
- Serine/threonine-protein kinase STE20
- non-specific serine/threonine protein kinase
- Candida glabrata strain CBS138 chromosome L complete sequence
- M-phase inducer phosphatase
- Candida glabrata strain CBS138 chromosome M complete sequence
- Candida glabrata strain CBS138 chromosome M complete sequence
- Candida glabrata strain CBS138 chromosome B complete sequence
Sequence:
MSPSREDSVYLAKLAEQAERYEEMVESMKEVASSGQELSVEERNLLSVAYKNVIGARRASWRIISSIEQKEESKEKAEHQVELIRTYRGKIETELTKISDDILSVLDSHLIPSATSGESKVFYYKMKGDYHRYLAEFSSGDVRDKATEASLEAYKTASEIATTELPPTHPIRLGLALNFSVFYYEIQNSPDKACHLAKQAFDDAIAELDTLSEESYKDSTLIMQLLRDNLTLWTSDMSEAQDEQNDEPPK
Protein: Potassium transporter 3 (AtKT3) (AtKUP4) (AtPOT3) (Tiny root hair 1 protein) (Q9FE38)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: High-affinity potassium transporter required for tip growth of root hairs.
Subcellular location: Cell membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
- K
- Potassium channel KAT3
- K
- Probable magnesium transporter NIPA4
- Cytochrome b561 and DOMON domain-containing protein At2g04850
- Potassium channel GORK channel)
- Potassium channel AKT2/3
- Aluminum-activated malate transporter 5
- Potassium inward rectifier
- K
Sequence:
MADRRNRCNQILLLAYQSFGLVFGDLSISPLYVYKCTFYGGLRHHQTEDTIFGAFSLIFWTITLLSLIKYMVFVLSADDNGEGGIFALYALLCRHARFSLLPNQQAADEEISTYYGPGDASRNLPSSAFKSLIERNKRSKTALLVLVLVGTSMVITIGVLTPAISVSSSIDGLVAKTSLKHSTVVMIACALLVGLFVLQHRGTNKVAFLFAPIMILWLLIIATAGVYNIVTWNPSVYKALSPYYIYVFFRDTGIDGWLSLGGILLCITGTEAIFAELGQFTATSIRFAFCCVVYPCLVLQYMGQAAFLSKNFSALPSSFYSSIPDPFFWPVLMMAMLAAMVASQAVIFATFSIVKQCYALGCFPRVKIVHKPRWVLGQIYIPEINWVVMILTLAVTICFRDTRHIAFAFGLACMTLAFVTTWLMPLIINFVWNRNIVFSVLFILFFGTIELIFVASALVKIPKGGWITLLLSLFFTFITYVWHYGSRKKYLCDQHNKVPMKSILSLGPSLGIIKVPGMGLIYTELASGVPATFKHFLTNLPAFYQVVVFVCCKTVPIPYVPQKERYLIGRIGPKTYRMYRCIIRAGYKDVNKDGDDFEDELVMSIAEFIQLESEGYGGSNTDRSIDGRLAVVKASNKFGTRLSRSISEANIAGSSRSQTTVTNSKSPALLKLRAEYEQELPRLSMRRMFQFRPMDTKFRQPQVKEELFDLVNAKDAEVAYIVGHGHVKAKRNSVFVKQLVVNVAYSFLRKNCRSPGVMLNIPHICLIKVGMNYYL
Protein: Transposase (P96233)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Interaction partners:
- Uncharacterized protein
- Aminotransferase class I/II-fold pyridoxal phosphate-dependent enzyme
Sequence:
MDRVRRVVTDRDSGAGALARHPLAGRRTDPQLAAFYHRLMTTQRHCHTQATIAVARKLAERTRVTITTGRPYQLRDTNGDPVTARGAKELIDAHYHVDTRTHPHNRAHTDTMQNSKPAR
Protein: Signal peptidase complex subunit 2 (Microsomal signal peptidase subunit 2) (Q9UTQ9)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Component of the signal peptidase complex (SPC) which catalyzes the cleavage of N-terminal signal sequences from nascent proteins as they are translocated into the lumen of the endoplasmic reticulum. Enhances the enzymatic activity of SPC and facilitates the interactions between different components of the translocation site.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:16823372}; Multi-pass membrane protein {ECO:0000269|PubMed:16823372}.
Interaction partners:
- Signal peptidase complex subunit 1
- Signal peptidase complex subunit 3
- Signal peptidase complex catalytic subunit sec11
- Mitochondrial inner membrane protease subunit 1
- Mitochondrial inner membrane protease subunit 2
Sequence:
MPKYNVSDFKSKFDKELTNHFNKNGYKQSFVFEDIRLLIAIACIIPAGLAFGIEYVYGFGVLKSYLKYLLPLYFLASCLLTFWSSVVKGSTVYVATKKERHIKISADTFLPLKNKPLITTKFTVLKNRNAVQLEWSVPVAHIFEEDGQISSATFEAEISKYLSQIEN
Protein: Protein Wfdc21 (Wdnm1-like protein) (Q8BTE6)
Organism: Mus musculus (Mouse)
Function: May promote activation of the metalloproteinase MMP2.
Subcellular location: Secreted {ECO:0000269|PubMed:18492766}.
Interaction partners:
Sequence:
MKLGAFLLLVSLITLSLEVQELQAAVRPLQLLGTCAELCRGDWDCGPEEQCVSIGCSHICTTN
Protein: Mevalonate kinase (Q65XX9)
Organism: Caenorhabditis elegans
Interaction partners:
- Diphosphomevalonate decarboxylase
- 3-hydroxy-3-methylglutaryl coenzyme A reductase
- Phosphomevalonate kinase
- Farnesyl pyrophosphate synthase
- PAN-3 domain-containing protein
- Histone-lysine N-methyltransferase, H3 lysine-79 specific
- Hydroxymethylglutaryl-CoA synthase
- hydroxymethylglutaryl-CoA lyase
- Acetyl-CoA acetyltransferase homolog, mitochondrial
- Acetyl-CoA C-acetyltransferase
Sequence:
MPVAAPEEHEKVVTVCGELVRSLDANGKEMVIRREVSVTETRESRDTSLKVEIPSEQEIELPVIVHDKPKLIKQEVSVVEPLELQESVESTELSVTSKESTEQLPSKDSLDSPSGSTSRAGSSVSATASPMHRNTTSQHGGLFVSAPGKIILFGEHAVVYGRTAIAGSIDLRTYVSLYTSADGRIYLSLPDLGVEKTWMLKDLLKAADRLAAEYPIEEDQPPSLEILVPIARKLSGSCEDQCGVQHLAILAFWYLLLGVAHRKRDLLAVKATVRFKLPSCVGLGSSGAYCVCIATSLLQTAGLIPPPSIVADEQGNLTWEEDHLDIIRKWATAAESLIHGRASGLDAAVCTFGGVASFKPGHRIEHLKNLPDLRVILVNSKVERNTARMVQTVKERLKKFPEVVDAMFGSIDAISLDAAKILHRPLLEENGGGDTGSTVQENGLGPFGGNMVEQDHHSLQPTRTASVRSSSLSSYVGGGKRNSSASVISATSEKGENVDTFSKLNDLCRINNQLLIALGVGHPKVDLICTTLARYGIHPKMTGAGGGGSVFAFLKPNTPQTLLDMIDGELRSHGFEVWQPPLGGPGVVEHQTRPELFQTPVSSTQCSTPASKHK