wanglab/gogpt-training-data huggingface dataset:
Protein: Protein MCM10 homolog (HsMCM10) (Q7L590)
Organism: Homo sapiens (Human)
Function: Acts as a replication initiation factor that brings together the MCM2-7 helicase and the DNA polymerase alpha/primase complex in order to initiate DNA replication. Additionally, plays a role in preventing DNA damage during replication. Key effector of the RBBP6 and ZBTB38-mediated regulation of DNA-replication and common fragile sites stability; acts as a direct target of transcriptional repression by ZBTB38.
Subcellular location: Nucleus {ECO:0000269|PubMed:11095689, ECO:0000269|PubMed:15136575, ECO:0000269|PubMed:32865517}. Note=Colocalizes with ORC2 in nuclei foci. Associated with chromatin in S phase. From early to mid-S phase located in discrete nuclear foci. In early S phase, several hundred foci appeared throughout the nucleus. In mid-S phase, the foci appeared at the nuclear periphery and nucleolar regions. In the late S and G phases localized to nucleoli.
Interaction partners:
- DNA replication licensing factor MCM7
- DNA replication licensing factor MCM6
- Cell division control protein 45 homolog
- DNA replication licensing factor MCM3
- DNA replication licensing factor MCM4
- WD repeat and HMG-box DNA-binding protein 1
- Cell division control protein 6 homolog
- DNA replication licensing factor MCM2
- DNA replication factor Cdt1
- DNA replication licensing factor MCM5
Sequence:
MDEEEDNLSLLTALLEENESALDCNSEENNFLTRENGEPDAFDELFDADGDGESYTEEADDGETGETRDEKENLATLFGDMEDLTDEEEVPASQSTENRVLPAPAPRREKTNEELQEELRNLQEQMKALQEQLKVTTIKQTASPARLQKSPVEKSPRPPLKERRVQRIQESTCFSAELDVPALPRTKRVARTPKASPPDPKSSSSRMTSAPSQPLQTISRNKPSGITRGQIVGTPGSSGETTQPICVEAFSGLRLRRPRVSSTEMNKKMTGRKLIRLSQIKEKMAREKLEEIDWVTFGVILKKVTPQSVNSGKTFSIWKLNDLRDLTQCVSLFLFGEVHKALWKTEQGTVVGILNANPMKPKDGSEEVCLSIDHPQKVLIMGEALDLGTCKAKKKNGEPCTQTVNLRDCEYCQYHVQAQYKKLSAKRADLQSTFSGGRIPKKFARRGTSLKERLCQDGFYYGGVSSASYAASIAAAVAPKKKIQTTLSNLVVKGTNLIIQETRQKLGIPQKSLSCSEEFKELMDLPTCGARNLKQHLAKATASGIMGSPKPAIKSISASALLKQQKQRMLEMRRRKSEEIQKRFLQSSSEVESPAVPSSSRQPPAQPPRTGSEFPRLEGAPATMTPKLGRGVLEGDDVLFYDESPPPRPKLSALAEAKKLAAITKLRAKGQVLTKTNPNSIKKKQKDPQDILEVKERVEKNTMFSSQAEDELEPARKKRREQLAYLESEEFQKILKAKSKHTGILKEAEAEMQERYFEPLVKKEQMEEKMRNIREVKCRVVTCKTCAYTHFKLLETCVSEQHEYHWHDGVKRFFKCPCGNRSISLDRLPNKHCSNCGLYKWERDGMLKEKTGPKIGGETLLPRGEEHAKFLNSLK
Protein: Separin (EC 3.4.22.49) (Caspase-like protein ESPL1) (Extra spindle poles-like 1 protein) (Separase) (Q14674)
Organism: Homo sapiens (Human)
Function: Caspase-like protease, which plays a central role in the chromosome segregation by cleaving the SCC1/RAD21 subunit of the cohesin complex at the onset of anaphase. During most of the cell cycle, it is inactivated by different mechanisms.
Subcellular location: Cytoplasm. Nucleus.
Interaction partners:
- Securin-2
- Securin
- G2/mitotic-specific cyclin-B1
- Double-strand-break repair protein rad21 homolog
- Cyclin-dependent kinase 1
- Serine/threonine-protein kinase PLK1
- Structural maintenance of chromosomes protein 3
- Meiotic recombination protein REC8 homolog
- Mitotic checkpoint serine/threonine-protein kinase BUB1
- Cohesin subunit SA-1
Sequence:
MRSFKRVNFGTLLSSQKEAEELLPALKEFLSNPPAGFPSSRSDAERRQACDAILRACNQQLTAKLACPRHLGSLLELAELACDGYLVSTPQRPPLYLERILFVLLRNAAAQGSPEATLRLAQPLHACLVQCSREAAPQDYEAVARGSFSLLWKGAEALLERRAAFAARLKALSFLVLLEDESTPCEVPHFASPTACRAVAAHQLFDASGHGLNEADADFLDDLLSRHVIRALVGERGSSSGLLSPQRALCLLELTLEHCRRFCWSRHHDKAISAVEKAHSYLRNTNLAPSLQLCQLGVKLLQVGEEGPQAVAKLLIKASAVLSKSMEAPSPPLRALYESCQFFLSGLERGTKRRYRLDAILSLFAFLGGYCSLLQQLRDDGVYGGSSKQQQSFLQMYFQGLHLYTVVVYDFAQGCQIVDLADLTQLVDSCKSTVVWMLEALEGLSGQELTDHMGMTASYTSNLAYSFYSHKLYAEACAISEPLCQHLGLVKPGTYPEVPPEKLHRCFRLQVESLKKLGKQAQGCKMVILWLAALQPCSPEHMAEPVTFWVRVKMDAARAGDKELQLKTLRDSLSGWDPETLALLLREELQAYKAVRADTGQERFNIICDLLELSPEETPAGAWARATHLVELAQVLCYHDFTQQTNCSALDAIREALQLLDSVRPEAQARDQLLDDKAQALLWLYICTLEAKMQEGIERDRRAQAPGNLEEFEVNDLNYEDKLQEDRFLYSNIAFNLAADAAQSKCLDQALALWKELLTKGQAPAVRCLQQTAASLQILAALYQLVAKPMQALEVLLLLRIVSERLKDHSKAAGSSCHITQLLLTLGCPSYAQLHLEEAASSLKHLDQTTDTYLLLSLTCDLLRSQLYWTHQKVTKGVSLLLSVLRDPALQKSSKAWYLLRVQVLQLVAAYLSLPSNNLSHSLWEQLCAQGWQTPEIALIDSHKLLRSIILLLMGSDILSTQKAAVETSFLDYGENLVQKWQVLSEVLSCSEKLVCHLGRLGSVSEAKAFCLEALKLTTKLQIPRQCALFLVLKGELELARNDIDLCQSDLQQVLFLLESCTEFGGVTQHLDSVKKVHLQKGKQQAQVPCPPQLPEEELFLRGPALELVATVAKEPGPIAPSTNSSPVLKTKPQPIPNFLSHSPTCDCSLCASPVLTAVCLRWVLVTAGVRLAMGHQAQGLDLLQVVLKGCPEAAERLTQALQASLNHKTPPSLVPSLLDEILAQAYTLLALEGLNQPSNESLQKVLQSGLKFVAARIPHLEPWRASLLLIWALTKLGGLSCCTTQLFASSWGWQPPLIKSVPGSEPSKTQGQKRSGRGRQKLASAPLRLNNTSQKGLEGRGLPCTPKPPDRIRQAGPHVPFTVFEEVCPTESKPEVPQAPRVQQRVQTRLKVNFSDDSDLEDPVSAEAWLAEEPKRRGTASRGRGRARKGLSLKTDAVVAPGSAPGNPGLNGRSRRAKKVASRHCEERRPQRASDQARPGPEIMRTIPEEELTDNWRKMSFEILRGSDGEDSASGGKTPAPGPEAASGEWELLRLDSSKKKLPSPCPDKESDKDLGPRLRLPSAPVATGLSTLDSICDSLSVAFRGISHCPPSGLYAHLCRFLALCLGHRDPYATAFLVTESVSITCRHQLLTHLHRQLSKAQKHRGSLEIADQLQGLSLQEMPGDVPLARIQRLFSFRALESGHFPQPEKESFQERLALIPSGVTVCVLALATLQPGTVGNTLLLTRLEKDSPPVSVQIPTGQNKLHLRSVLNEFDAIQKAQKENSSCTDKREWWTGRLALDHRMEVLIASLEKSVLGCWKGLLLPSSEEPGPAQEASRLQELLQDCGWKYPDRTLLKIMLSGAGALTPQDIQALAYGLCPTQPERAQELLNEAVGRLQGLTVPSNSHLVLVLDKDLQKLPWESMPSLQALPVTRLPSFRFLLSYSIIKEYGASPVLSQGVDPRSTFYVLNPHNNLSSTEEQFRANFSSEAGWRGVVGEVPRPEQVQEALTKHDLYIYAGHGAGARFLDGQAVLRLSCRAVALLFGCSSAALAVRGNLEGAGIVLKYIMAGCPLFLGNLWDVTDRDIDRYTEALLQGWLGAGPGAPLLYYVNQARQAPRLKYLIGAAPIAYGLPVSLR
Protein: Regulatory protein E2 (P17383)
Organism: Human papillomavirus 31
Function: Plays a role in the initiation of viral DNA replication. A dimer of E2 interacts with a dimer of E1 in order to improve specificity of E1 DNA binding activity. Once the complex recognizes and binds DNA at specific sites, the E2 dimer is removed from DNA. E2 also regulates viral transcription through binding to the E2RE response element (5'-ACCNNNNNNGGT-3') present in multiple copies in the regulatory regions of the viral genome. Activates or represses transcription depending on E2RE's position with regards to proximal promoter elements including the TATA-box. Repression occurs by sterically hindering the assembly of the transcription initiation complex.
Subcellular location: Host nucleus {ECO:0000255|HAMAP-Rule:MF_04001}.
Interaction partners:
Sequence:
METLSQRLNVCQDKILEHYENDSKRLCDHIDYWKHIRLECVLMYKAREMGIHSINHQVVPALSVSKAKALQAIELQMMLETLNNTEYKNEDWTMQQTSLELYLTAPTGCLKKHGYTVEVQFDGDVHNTMHYTNWKFIYLCIDGQCTVVEGQVNCKGIYYVHEGHITYFVNFTEEAKKYGTGKKWEVHAGGQVIVFPESVFSSDEISFAGIVTKLPTANNTTTSNSKTCALGTSEGVRRATTSTKRPRTEPEHRNTHHPNKLLRGDSVDSVNCGVISAAACTNQTRAVSCPATTPIIHLKGDANILKCLRYRLSKYKQLYEQVSSTWHWTCTDGKHKNAIVTLTYISTSQRDDFLNTVKIPNTVSVSTGYMTI
Protein: Membrane fusion protein p14 (Q80FJ1)
Organism: Reptilian orthoreovirus
Interaction partners:
Sequence:
MGSGPSNFVNHAPGEAIVTGLEKGADKVAGTISHTIWEVIAGLVALLTFLAFGFWLFKYLQKRRERRRQLTEFQKRYLRNSYRLSEIQRPISQHEYEDPYEPPSRRKPPPPPYSTYVNIDNVSAI
Protein: Receptor-type tyrosine-protein phosphatase alpha (EC 3.1.3.48) (F1QE38)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004251}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004251}.
Interaction partners:
- Growth factor receptor-bound protein 2
- U-box domain-containing 5.
- Leucine zipper putative tumor suppressor 3
- Threonine synthase-like 2
- Zinc finger protein 366.
- Growth factor receptor-bound protein 2a
- Zinc finger protein 367
- Receptor-type tyrosine-protein phosphatase delta-like
- DDRGK domain-containing protein 1
- Four and a half LIM domains 2b
Sequence:
MQVSFLQGSMGVCPLLLHVAFVALSTAQTLPHLSGAVQTTKPTPHPPTTPLIIVTNGSPTAAPTSTPSPQLIATKAFNDSEGTAAPEATTAPPVVPPPAVPIPTVVLPVPPTPTAASPSLTTNKTGDHQTTVLAPAGTPTPDPTSTQSSSEPETETPYTPADATTADVNKPEGEEQDDTAIMAVMVALSSLLVIVFIIIILYMLRFKKYKQAGSHSNSFRLTNGRADDTELQSVPLLARSPSTNRKYPPLPVDKLEEEMNRRMADDNKLFREEFNALPVCPIQASCDAASKEENKEKNRYVNILPYDHSRVHLTSLEGVPDSDYINASYINGYQEKNKFIAAQGPKEETVNDYWRMIWEQNTATIVMVTNLKERKECKCAQYWPDQGCWTYGNIRVSVEDTMILVDYTIRKFCIQQVGDVSGKKPQRLVTQFHFTSWPDFGVPFTPIGMLKFLKKVKNCNPQYAGPIMVHCSAGVGRTGTFIVIDAMLDMMGAERKVDVFGFVTRIRAQRCQMVQTDMQYVFIFQALLEHYLYGDTELEVTSLETHMNKLYAPLPGAGCGGLEAEFKKLTSIKIQNDKMRTGNLPANMKKNRVLQIIPYEFNRVIIPVKRGEENTDYINASFIDGYRQKDSYMACQGPLQHTIEDYWRMIWEWRSCSIVMLTELEERGQEKCAQYWPTDGVMVCGDMSIELKREEESESYTVRDLLVTNNRENKSRAVRQFHFHGWPEVGIPSDGKGMINIIAAVQKQQQQSGNHPITVHCSAGAGRTGTFCALSTVLERVKAEGILDVFQTVKSLRLQRPHMVQTLEQYEFCYKVVQEYIDAFSDYANFK
Protein: Zinc finger CCCH domain-containing protein 58 (AtC3H58) (Zinc finger CCCH domain-containing protein ZFN-like 3) (Q6NPN3)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Nucleus {ECO:0000250}.
Interaction partners:
Sequence:
MERYGGAGEDESRSDPSHEWSAQGTETGIEASMWRLGLRGGGGGGETFPERPDEPDCIYYLRTGVCGYGSRCRFNHPRNRAPVLGGLRTEAGEFPERMGQPVCQHFMRTGTCKFGASCKYHHPRQGGGGDSVTPVSLNYMGFPLRPGEKECSYFMRTGQCKFGSTCRYHHPVPPGVQAPSQQQQQQLSAGPTMYPSLQSQTVPSSQQYGVVLARPQLLPGSYVQSPYGYGQMVLPPGMVPYSGWNPYQASVSAMPSPGTQPSMGTSSVYGITPLSPSAPAYQSGPSSTGVSNKEQTFPQRPEQPECQYFMRTGDCKFGTSCRFHHPMEAASPEASTLSHIGLPLRPGAVPCTHFAQHGICKFGPACKFDHSLGSSSLSYSPSPSSLTDMPVAPYPSSLGTLAPSSSSDQCTELISSSSIEPITTTTGGSETVAAGVSSMTSDVSHPEPAETNKGDSASNEAKTSS
Protein: At3g03280 (T17B22.3 protein) (Q9M9P6)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- HTH-type transcriptional regulator
- D-ribose-binding periplasmic protein
- 6,7-dimethyl-8-ribityllumazine synthase
- Emb|CAB85509.1
- At3g10120
- 6,7-dimethyl-8-ribityllumazine synthase
- Uncharacterized protein At5g66580
- Uncharacterized protein At3g50800
- HTH-type transcriptional regulator
- At1g21010
Sequence:
MGNYVSCALNKTSSSPLAKVILPDGGVRDIHVPTKAAELMMEMPSYFLVDTKSVKVGRKFIPLAADDDLDLGGCHVYVAFPMTRATSAANASDMARLYLTGKKRTKNCGHRRVSPENEDNDDVRLIGPKLNLEDIEEFSAAEFIHRISVSKSKKPQLETIAEDHVP
Protein: Pleckstrin-2 (Q9WV52)
Organism: Mus musculus (Mouse)
Function: May help orchestrate cytoskeletal arrangement. Contribute to lamellipodia formation. Overexpression of pleckstrin 2 causes large lamellipodia and peripheral ruffle formation.
Subcellular location: Cell projection, lamellipodium membrane; Peripheral membrane protein. Cytoplasm, cytoskeleton.
Interaction partners:
- Mcf.2-transforming sequence.
- RAC-alpha serine/threonine-protein kinase
- Tyrosine-protein kinase BTK
- 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase delta-1
- Oxysterol-binding protein 1
- Guanine nucleotide exchange factor MSS4
- Cell division control protein 42 homolog
- Proto-oncogene tyrosine-protein kinase Src
Sequence:
MEDGVLKEGFLVKRGHIVHNWKARWFILRQNTLLYYKLEGGRRVTPPKGRIVLDGCTITCPCLEYENRPLLIKLKTRTSTEYFLEACSREERDSWAFEITGAIHAGQPGKIQQLHILKNSFKLPPHISLHRIVDKMHDTSTGIRPSPNMEQGSTYKKTFLGSSLVDWLISSNFAASRLEAVTLASMLMEENFLRPVGVRSMGAIRSGDLAEQFLDDSTALYTFAESYKKKVSSKEEISLSTMELSGTVVKQGYLSKQGHKRKNWKVRRFVLRKDPAFLHYYDPSKEENRPVGGFSLRGSLVSALEDNGVPTGVKGNVQGNLFKVITKDDTHYYIQASSKAERAEWIEAIKKLT
Protein: Serpentine Receptor, class AB (Class A-like) (O17010)
Organism: Caenorhabditis elegans
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
- Serpentine Receptor, class T
- Serpentine Receptor, class J
- Seven TM Receptor
- Serpentine Receptor, class T
- Serpentine Receptor, class J
- Serpentine receptor class r-10
- Serpentine Receptor, class D
- Serpentine receptor class r-10
- Serpentine Receptor, class T
- Serpentine Receptor, class D
Sequence:
MSCDEEILEKIVNSVTLRVVEILMLILSTISIPVLFHMFHRCKNTQLFHFNIRLISAFHCLCLMIHCIARVFQHGADLFLYFSDIPICEKVPSVKRCLATRIPYIFGLFCASYSTVFMVLERTIATKNYKKYENRHKTLGYCFIFGQIFMGTTTTIAIFYKFDFNQGQEFCSGSQSSDPAYMIIPESVAILSNFIAFFQFGKLMRINTKIRVGSSENNLSQKYQIEENLNVVRILRAFTKCDFVFILIYFTMGIPFHLVGKHLDHADYYALFEVIYFVPIYSLIMPAYIYQFSKKQRVERINRVEQKIQVSEDAYFQFIHKQWT
Protein: Mitogen-activated protein kinase kinase kinase 1 (ARAKIN) (AtMEKK1) (MAP kinase kinase kinase 1) (EC 2.7.11.25) (Q39008)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: The MEKK1, MKK1/MKK2 and MPK4 function in a signaling pathway that modulates the expression of genes responding to biotic and abiotic stresses and also plays an important role in pathogen defense by negatively regulating innate immunity. Involved in the innate immune MAP kinase signaling cascade (MEKK1, MKK4/MKK5 and MPK3/MPK6) downstream of bacterial flagellin receptor FLS2. May be involved in the cold and salinity stress-mediated MAP kinase signaling cascade (MEKK1, MKK1/MKK2 and MPK4/MPK6). Activates by phosphorylation the downstream MKK2, MKK4 and MKK5 in a calcium-dependent manner.
Subcellular location: Cell membrane {ECO:0000269|PubMed:20724845}. Endosome {ECO:0000269|PubMed:20724845}.
Interaction partners:
- Mitogen-activated protein kinase kinase 1
- Mitogen-activated protein kinase kinase 4
- Mitogen-activated protein kinase kinase 2
- Mitogen-activated protein kinase kinase 5
- Mitogen-activated protein kinase kinase 6
- LRR receptor-like serine/threonine-protein kinase EFR
- LRR receptor-like serine/threonine-protein kinase FLS2
- BRASSINOSTEROID INSENSITIVE 1-associated receptor kinase 1
- Disease resistance protein SUMM2
- High mobility group B protein 6
Sequence:
MDRILARMKKSTGRRGGDKNITPVRRLERRDAARNINYDAASCSSSSAEDLSVSTSSLMTRSLEFPEPTSFRIGGGVGEMDRIYRSLGVSGPDDLAISFDAWEACKKRSSSDVVNRFKSFDLDKVRDQDLSEEGPSGVVVGSDSMNHKVQGQDLSEAGPSGGIVTELSEIGNLITPVDRLVADGVVENRRVMERTPTIVKSKGYLVPNNVVAVGVGVGGGIKGLRPPVLKPPPAMKRPPIDHRGSSWDFLTHFAPSETVKRPSSSSSSSEDGCDEEEGKEEEAEAEEMGARFIQLGDTADETCSFTTNEGDSSSTVSNTSPIYPDGGAIITSWQKGQLLGRGSFGSVYEGISGDGDFFAVKEVSLLDQGSQAQECIQQLEGEIKLLSQLQHQNIVRYRGTAKDGSNLYIFLELVTQGSLLKLYQRYQLRDSVVSLYTRQILDGLKYLHDKGFIHRDIKCANILVDANGAVKLADFGLAKVSKFNDIKSCKGTPFWMAPEVINRKDSDGYGSPADIWSLGCTVLEMCTGQIPYSDLEPVQALFRIGRGTLPEVPDTLSLDARLFILKCLKVNPEERPTAAELLNHPFVRRPLPSVGSGGSGSASPLLRR
Protein: Chaperone DnaJ-domain superfamily protein (Expressed protein) (Q8RYC5)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Heat shock 70 kDa protein 17
Sequence:
MWCSDWGDSHGFDFFDFEDYKDHYKVLELNCDASDDEIRSSFIRLALKWHPDKFKEEDSATSRFQEINEAYQVLSDPIARQEYDKKRMRRIYEHNTELLNEYKELILTCNGLGVKHYLW
Protein: Tumor necrosis factor ligand superfamily member 15 (TNF ligand-related molecule 1) (Vascular endothelial cell growth inhibitor) [Cleaved into: Tumor necrosis factor ligand superfamily member 15, membrane form; Tumor necrosis factor ligand superfamily member 15, secreted form] (O95150)
Organism: Homo sapiens (Human)
Function: Receptor for TNFRSF25 and TNFRSF6B. Mediates activation of NF-kappa-B. Inhibits vascular endothelial growth and angiogenesis (in vitro). Promotes activation of caspases and apoptosis.
Subcellular location: Membrane {ECO:0000305|PubMed:11911831, ECO:0000305|PubMed:11923219}; Single-pass type II membrane protein {ECO:0000305|PubMed:11911831, ECO:0000305|PubMed:11923219}.; SUBCELLULAR LOCATION: [Tumor necrosis factor ligand superfamily member 15, secreted form]: Secreted.
Interaction partners:
- Tumor necrosis factor receptor superfamily member 6B
- Tumor necrosis factor receptor superfamily member 25
- Tumor necrosis factor ligand superfamily member 8
- Coiled-coil domain-containing protein 122
- Nucleotide-binding oligomerization domain-containing protein 2
- Tumor necrosis factor receptor superfamily member 21
- Tumor necrosis factor receptor superfamily member 14
- Tumor necrosis factor receptor superfamily member 1A
- Purine nucleoside phosphorylase LACC1
- Tumor necrosis factor ligand superfamily member 18
Sequence:
MAEDLGLSFGETASVEMLPEHGSCRPKARSSSARWALTCCLVLLPFLAGLTTYLLVSQLRAQGEACVQFQALKGQEFAPSHQQVYAPLRADGDKPRAHLTVVRQTPTQHFKNQFPALHWEHELGLAFTKNRMNYTNKFLLIPESGDYFIYSQVTFRGMTSECSEIRQAGRPNKPDSITVVITKVTDSYPEPTQLLMGTKSVCEVGSNWFQPIYLGAMFSLQEGDKLMVNVSDISLVDYTKEDKTFFGAFLL
Protein: Neamine transaminase BtrB (EC 2.6.1.93) (Butirosin biosynthesis protein B) (Q4H4F5)
Organism: Niallia circulans (Bacillus circulans)
Function: 6'-oxoglucosaminyl:L-glutamate aminotransferase that catalyzes pyridoxal-5'-phosphate-mediated transamination for the conversion of paromamine to neamine in the biosynthetic pathway of butirosin.
Interaction partners:
Sequence:
MKQETVKSSEQLLSVLGTYIDSPVDPFRKERVMFSRGSGAYLFDYDGGNYIDLMNGKGSIILGHNDPSVNAALRNFLEQDREVVTGPSKPIIDLAERIKKDSALPDAKVSFYTTGTAACRAAVYAARDYSGKKIVLSSGYHGWDPMWRQQGPLLEPNEDGVIEFYFIPELLERALTAHKDQVALVIFSPDYTYLSASTMERILGICRAHGVLVCCDDVKQGYRHRQGSSLELVTTEKADMYVFSKGLSNGHRISCVVSSDEIMAETKEHTYTAYYQMLPILSSLETLKKMESGKGYDLIRSYGQTLTGNLKELFVQSSLPIEVNGSSIFQLVFGDEELEEAFYREAFIQGLILFEGDNQSLSLCMDKDVQVDLIRRFANVTDVLSEQFKHLRGKEVTTEQTFRTAWNMIDGASDLLPYEKQLKLLDNLIGGG
Protein: Amyloid beta precursor like protein 2 (Amyloid beta (A4) precursor-like protein 2) (Amyloid protein homolog) (Amyloid-like protein 2) (APLP-2) (CDEI box-binding protein) (CDEBP) (Sperm membrane protein YWK-II) (P15943)
Organism: Rattus norvegicus (Rat)
Function: May play a role in the regulation of hemostasis. The soluble form may have inhibitory properties towards coagulation factors. May interact with cellular G-protein signaling pathways. May bind to the DNA 5'-GTCACATG-3'(CDEI box). Inhibits trypsin, chymotrypsin, plasmin, factor XIA and plasma and glandular kallikrein. Modulates the Cu/Zn nitric oxide-catalyzed autodegradation of GPC1 heparan sulfate side chains in fibroblasts (By similarity).
Subcellular location: Membrane; Single-pass type I membrane protein.
Interaction partners:
- Amyloid beta precursor protein binding family B member 1
- Nicastrin
- Amyloid-beta precursor protein
- Major prion protein
- Beta-secretase 1
- Tumor necrosis factor receptor superfamily member 21
- Presenilin-1
- Presenilin-2
Sequence:
MAATGTAAAAATGKLLVLLLLGLTAPAAALAGYIEALAANAGTGFAVAEPQIAMFCGKLNMHVNIQTGKWEPDPTGTKSCLGTKEEVLQYCQEIYPELQITNVMEANQPVNIDSWCRRDKKQCRSHIVIPFKCLVGEFVSDVLLVPENCQFFHQERMEVCEKHQRWHTVVKEACLTEGMTLYSYGMLLPCGVDQFHGTEYVCCPQTKVVDSDSTMSKEEEEEEEEDEEEDYALDKSEFPTEADLEDFTEAAADEDEDEEEEEEEEGEEVVEDRDYYYDSFKGDDYNEENPTEPSSDGTISDKEIAHDVKAVCSQEAMTGPCRAVMPRWYFDLSKGKCVRFIYGGCGGNRNNFESEDYCMAVCKTMIPPTPLPTNDVDVYFETSADDNEHARFQKAKEQLEIRHRSRMDRVKKEWEEAELQAKNLPKAERQTLIQHFQAMVKALEKEAASEKQQLVETHLARVEAMLNDRRRIALENYLAALQSDPPRPHRILQALRRYVRAENKDRLHTIRHYQHVLAVDPEKAAQMKSQVMTHLHVIEERRNQSLSLLYKVPYVAQEIQEEIDELLQEQRADMDQFTSSISENPVDVRVSSEESEEIPPFHPFHPFPSLSENEDTQPELYHPMKKGSGMAEQDGGLIGAEEKVINSKNKMDENMVIDETLDVKEMIFNAERVGGLEEEPDSVGPLREDFSLSSSALIGLLVIAVAIATVIVISLVMLRKRQYGTISHGIVEVHPMLTPEERHLNKMQNHGYENPTYKYLEQMQI
Protein: TAR-binding protein (O97468)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MDFVQVSEEEGDEPIQLPAEEDGTLLLSTLQAQFPGSCGLKYRNLDTKAVRGVRSNEGRLFPPSVESGWGEYAYFCVFPKENKRKSDDNLENSTAKTKRIETRLRCTDLIVLGLPWKTTEESLREYFETYGEVLMAQIKKDTKSGQSKGFGFVRFGSYDAQMRVLTNRHLIDGRWCEVKVPNSKGMGHQVPCKVFVGRCTEDINSDDLREYFSKFGEVTDVFIPRPFRAFSFVTFLDPDVAQSLCGEDHIIKGVSVHVSNAAPKAEQNRNQQVQSYNYNSANSFGMHSYHPQGNHMNPGRNGHHRGNNQHNAHGGENAIVPNNHNIGTAGYGMGGNNYGGNSGGGYHNNGGNHSSGGNTNRQDGGSQYNSRQSNFHGMNQPHNGNVGGSNGWMNRGHLDMPNLQALGINSQGSSSSNQGQNMSNQSMLNLNSLPINPALVAAALNQWSLVGNQLQNQNQDQQGGNFLSWMAQNGGHNNANNFGGRKGPNNPNNNPAANGIKTDNSEPQNGNTGWSNQSSGSQNAAEKSNFL
Protein: Serine rich endogenous peptide 7 (AtSCOOP7) (Phytocytokine SCOOP7) (Precursor of serine rich endogenous peptide phytocytokine 7) (A8MS31)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Brassicaceae-specific phytocytokine (plant endogenous peptide released into the apoplast) perceived by MIK2 in a BAK1/SERK3 and SERK4 coreceptors-dependent manner, that modulates various physiological and antimicrobial processes including growth prevention and reactive oxygen species (ROS) response regulation.
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:B3H7I1}. Secreted, extracellular space, apoplast {ECO:0000250|UniProtKB:B3H7I1}. Note=The precursor of SCOOP7, PROSCOOP7, accumulates at the plasma membrane and is proteolytically cleaved to release the SCOOP7 in the apoplasm. {ECO:0000250|UniProtKB:B3H7I1}.
Interaction partners:
- Cysteine-rich receptor-like protein kinase 38
- RPW8-like protein 4
- Aspartyl protease AED1
Sequence:
MGKKCSSKFRQMLVLVLLLIVFTCLSVTAPLSVTAKPTSFKVKARGIEDEGQERTHSLNSKKSSRSVEKTHHSEGRRLSNVFPNAGIRAGPSKSGQGGGRIPVAAS
Protein: Short/branched chain specific acyl-CoA dehydrogenase, mitochondrial (H2KZG6)
Organism: Caenorhabditis elegans
Interaction partners:
- Probable enoyl-CoA hydratase, mitochondrial
- Probable enoyl-CoA hydratase, mitochondrial
- Acetyl-CoA acetyltransferase homolog, mitochondrial
- Probable 3-ketoacyl-CoA thiolase
- 3-ketoacyl-CoA thiolase
- Hydroxyacid-oxoacid transhydrogenase, mitochondrial
- Acetyl-CoA C-acetyltransferase
- Trifunctional enzyme subunit alpha, mitochondrial
- Trifunctional enzyme subunit alpha, mitochondrial
- Lipoamide acyltransferase component of branched-chain alpha-keto acid dehydrogenase complex, mitochondrial
Sequence:
MSTSTTKILKQAMNIISTIRSSYSTATAVSISRHCEDFTGTPPPVNLLTENELFFADTVRKFSKDVVKPLVREMDKYSKMSPIVTQGVFENGLMGVHVPEEYGGSGSSFFNAMIVIEELAKTDPSVSAMVGIHNTLPVSMIIDYGTEEQKLKYLPRLCSDSLASFCISESGAGSDAFALKTIAKRDGDHFLISGTKMWITNSGEAQVFVVFANADPSQKYKGITCFIVERSADGLTVDKEEDKLGIRASSTCQVHFDNVRVHKSAILGEYGKGYKYAIECLNAGRIAIGAQMIGLAQGCFDQTIPYLQQREQFGQRLIDFQGLQHQIAQARTEIEAARLLVYNAARMKEYGIPYVREAAMAKLFASQVATSTSAQCVKWLGGVGFTKEFPAEKFYRDAMIGEIYEGTSNIQLNTIAKLIDNEYKWKN
Protein: Golgi-associated kinase 1A (Protein FAM198A) (Q9UFP1)
Organism: Homo sapiens (Human)
Subcellular location: Secreted {ECO:0000305}. Endoplasmic reticulum {ECO:0000250|UniProtKB:Q3UY90}. Golgi apparatus {ECO:0000250|UniProtKB:Q3UY90}. Membrane, caveola {ECO:0000269|PubMed:30188967}. Note=Requires caveolae biogenesis to be secreted from the endoplasmic reticulum going through the Golgi apparatus where is post-translationally processed to the mature form. {ECO:0000250|UniProtKB:Q3UY90}.
Interaction partners:
- Glycosaminoglycan xylosylkinase
- Extracellular serine/threonine protein kinase FAM20C
Sequence:
MASWLRRKLRGKRRPVIAFCLLMILSAMAVTRFPPQRPSAGPDPGPMEPQGVTGAPATHIRQALSSSRRQRARNMGFWRSRALPRNSILVCAEEQGHRARVDRSRESPGGDLRHPGRVRRDITLSGHPRLSTQHVVLLREDEVGDPGTKDLGHPQHGSPIQETQSEVVTLVSPLPGSDMAALPAWRATSGLTLWPHTAEGRDLLGAENRALTGGQQAEDPTLASGAHQWPGSVEKLQGSVWCDAETLLSSSRTGGQAPPWLTDHDVQMLRLLAQGEVVDKARVPAHGQVLQVGFSTEAALQDLSSPRLSQLCSQGLCGLIKRPGDLPEVLSFHVDRVLGLRRSLPAVARRFHSPLLPYRYTDGGARPVIWWAPDVQHLSDPDEDQNSLALGWLQYQALLAHSCNWPGQAPCPGIHHTEWARLALFDFLLQVHDRLDRYCCGFEPEPSDPCVEERLREKCQNPAELRLVHILVRSSDPSHLVYIDNAGNLQHPEDKLNFRLLEGIDGFPESAVKVLASGCLQNMLLKSLQMDPVFWESQGGAQGLKQVLQTLEQRGQVLLGHIQKHNLTLFRDEDP
Protein: Fimbrial protein (A0A384KL23)
Organism: Yersinia pestis
Interaction partners:
Sequence:
MLTTVFIAQSQPAQAASSCAGTADCHIQVSFGGEYVEDTCEVSINGASSAESVSLPTLSTSKLNIDGAEAGNQAFQIALKLCPANRSVDLRFTAADSSRNPDVITGNLQNELADDYSRNVQVRLSKATGQQMFVGRENSVQEYVIPATGEDITHYFLAGYYAKGTNAVTPGQVKATAGIELVYK
Protein: Interferon C (C1IRY3)
Organism: Salmo salar (Atlantic salmon)
Subcellular location: Secreted {ECO:0000256|ARBA:ARBA00004613}.
Interaction partners:
Sequence:
MPCQLQGQLVRITHNLLRDMGGNFPLECLQENVFVAFPATAFASSGAPQLSSSGAKAIYETLKNIDILFEADDLPTQWDQQKLENFQNIVYRQIEESKCMMGSVDTSDYLIRTEGLNTYLGNIAAVLKEKNFSYC
Protein: Metallo-beta-lactamase IMP-1 (EC 3.1.26.-) (EC 3.5.2.6) (B2 metallo-beta-lactamase) (BLA-IMP) (IMP-1) (Beta-lactamase type II) (Metallo-beta-lactamase type II) (P52699)
Organism: Serratia marcescens
Function: Confers resistance to the different beta-lactams antibiotics (penicillin, cephalosporin and carbapenem) via the hydrolysis of the beta-lactam ring.
Subcellular location: Periplasm {ECO:0000305}.
Interaction partners:
Sequence:
MSKLSVFFIFLFCSIATAAESLPDLKIEKLDEGVYVHTSFEEVNGWGVVPKHGLVVLVNAEAYLIDTPFTAKDTEKLVTWFVERGYKIKGSISSHFHSDSTGGIEWLNSRSIPTYASELTNELLKKDGKVQATNSFSGVNYWLVKNKIEVFYPGPGHTPDNVVVWLPERKILFGGCFIKPYGLGNLGDANIEAWPKSAKLLKSKYGKAKLVVPSHSEVGDASLLKLTLEQAVKGLNESKKPSKPSN
Protein: Uncharacterized protein, isoform E (A8DYI9)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004236}. Late endosome {ECO:0000256|ARBA:ARBA00004603}.
Interaction partners:
Sequence:
MRSVEEIKAEYPLHWHIWHNELEQLQAAIDQNDKEKIDPRGRTPLMLAVRLANLPCVKCLLAAKCNATYEYEGWSIVQEAVCTGDVDILTAIIEVRDLQRHVQRVTHVPKLLQHLLDAPDFYIEMKWEFTSWVPLMSRLCPSDTYKVYKRGANVRIDTTLLGFDNNTWQRGNRSYIFKGAKETATMIEIDHDTNEVMVEEMSSDIGDIVAIPPALGTVRARLNAPVITNNIEMDKISFERNKCGIWGWRSEKSEMINGYNCKVYGASNVEFVTKTRMDHLSEEQIKNKTARTPLHSLLGIADEDYVSPADAAAALKDRTPSPRLEEASNAGVENGGRNSPAPGNQSNGSSAGASGTSTPKSSVTPEEYFTQEFDLHGRDVGGPKNLSTKVQRFRANLWLAEEHPIRLQEQVLPILDLMSTMASPHVSKLRDFITMQLPAGFPVKVEIPLFHVLNACITFGNVFALTTPVDHVATLQEQDRVTCLVDDRCFDIPAHYTNRGSDVRRQIPLDEDDMLQYAIEQSLVETSGACGVDARDDDKVDIWEVLRGQNVVGSDLLPEDDEQLQRGHRLSSHLLSPHRQQYGRYSPSPKHQPQSFPHSQLQLEPQTRGRSASAGAQFKNDLGYMKKIFK