wanglab/gogpt-training-data huggingface dataset:
Protein: Prothrombin (EC 3.4.21.5) (Coagulation factor II) [Cleaved into: Activation peptide fragment 1; Activation peptide fragment 2; Thrombin light chain; Thrombin heavy chain] (P00734)
Organism: Homo sapiens (Human)
Function: Thrombin, which cleaves bonds after Arg and Lys, converts fibrinogen to fibrin and activates factors V, VII, VIII, XIII, and, in complex with thrombomodulin, protein C. Functions in blood homeostasis, inflammation and wound healing.
Subcellular location: Secreted, extracellular space.
Interaction partners:
- Fibrinogen alpha chain
- Coagulation factor V
- Antithrombin-III
- Fibrinogen beta chain
- Fibrinogen gamma chain
- Heparin cofactor 2
- Coagulation factor X
- Thrombomodulin
- Proteinase-activated receptor 1
- Tissue factor
Sequence:
MAHVRGLQLPGCLALAALCSLVHSQHVFLAPQQARSLLQRVRRANTFLEEVRKGNLERECVEETCSYEEAFEALESSTATDVFWAKYTACETARTPRDKLAACLEGNCAEGLGTNYRGHVNITRSGIECQLWRSRYPHKPEINSTTHPGADLQENFCRNPDSSTTGPWCYTTDPTVRRQECSIPVCGQDQVTVAMTPRSEGSSVNLSPPLEQCVPDRGQQYQGRLAVTTHGLPCLAWASAQAKALSKHQDFNSAVQLVENFCRNPDGDEEGVWCYVAGKPGDFGYCDLNYCEEAVEEETGDGLDEDSDRAIEGRTATSEYQTFFNPRTFGSGEADCGLRPLFEKKSLEDKTERELLESYIDGRIVEGSDAEIGMSPWQVMLFRKSPQELLCGASLISDRWVLTAAHCLLYPPWDKNFTENDLLVRIGKHSRTRYERNIEKISMLEKIYIHPRYNWRENLDRDIALMKLKKPVAFSDYIHPVCLPDRETAASLLQAGYKGRVTGWGNLKETWTANVGKGQPSVLQVVNLPIVERPVCKDSTRIRITDNMFCAGYKPDEGKRGDACEGDSGGPFVMKSPFNNRWYQMGIVSWGEGCDRDGKYGFYTHVFRLKKWIQKVIDQFGE
Protein: Glutathione hydrolase proenzyme 2 (EC 3.4.19.13) (Gamma-glutamyltransferase 2) (Gamma-glutamyltranspeptidase 2) (EC 2.3.2.2) [Cleaved into: Glutathione hydrolase 2 heavy chain; Glutathione hydrolase 2 light chain] (O14194)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Catalyzes the transfer of the gamma-glutamyl moiety of glutathione (GSH) and other gamma-glutamyl compounds to amino acids and peptides. Major GSH-degrading enzyme, catalyzing the hydrolytic release of L-glutamate from GSH. Plays a role in the turnover of the vacuolar GSH, serving as an alternative nitrogen source during nitrogen starvation (By similarity).
Subcellular location: Vacuole membrane {ECO:0000305}; Single-pass type II membrane protein {ECO:0000305}.
Interaction partners:
- Glutathione synthetase large chain
- Putative aminopeptidase C13A11.05
- Glutathione S-transferase 3
- Glutathione reductase
- Glutathione S-transferase 1
- Glutathione S-transferase 2
- Glutamate--cysteine ligase
- Glutathione hydrolase proenzyme 1
- Cys-Gly metallodipeptidase dug1
- Uncharacterized protein C11D3.14c
Sequence:
MSPTDTTPLLYSWDDQSRHQDPDWHKLRNYHGAWYRRISRRRFSQFIFAFGLMTLFVLVYSISSNLHTPTQFTGHKVRGRRGAVASEVPVCSDIGVSMLADGGNAVDAAIASTFCIGVVNFFSSGIGGGGFMLIKHPNETAQSLTFREIAPGNVSKHMFDKNPMLAQVGPLSIAIPGELAGLYEAWKSHGLLDWSKLLEPNVKLAREGFPVTRAMERVLKLPEMAHLLKDPIWQPILMPNGKVLRAGDKMFRPAYAKTLEIIANKGIEPFYRGELTNSMVKFIQDNGGIVTVEDFGNYSTVFADALHTSYRGHDVYTCTLPTSGPALIEGLNILDGYPLNTPSLAFPKRLHLEVEAMKWLSAGRTQFGDPDFLPLDHLDVVSKLLSKEFASQIRNNISLSKTYPWEHYNPSYDLPISHGTTHVSTVDSNNLAVSITSTVNLLFGSQLMDPVTGVVFNDQMDDFSIPGASNAFNLSPSPWNFIEPFKRPQSSSAPTILTDINGDFEMALGASGGSRIVTAVLDSIIKRIDMDYDIESMVASARPHHQLLPDILILESGFSKSVATRMKKYGHKVWRLKQHDTPLSQIQAVTRHHSEYYGMSDPRKYGQAAAY
Protein: Transcription factor SPT20 homolog (p38-interacting protein) (p38IP) (Q7TT00)
Organism: Mus musculus (Mouse)
Function: Required for MAP kinase p38 (MAPK11, MAPK12, MAPK13 and/or MAPK14) activation during gastrulation. Required for down-regulation of E-cadherin during gastrulation by regulating E-cadherin protein level downstream from NCK-interacting kinase (NIK) and independently of the regulation of transcription by FGF signaling and Snail. Required for starvation-induced ATG9A trafficking during autophagy.
Interaction partners:
- Autophagy-related protein 9A
- Transcriptional adapter 1
- SPT3, SAGA and STAGA complex component
- SAGA-associated factor 29
- Transformation/transcription domain-associated protein
- Transcription initiation factor TFIID subunit 12
- Transcription initiation factor TFIID subunit 10
- Transcriptional adapter 3
- Transcriptional adapter 2-alpha
- STAGA complex 65 subunit gamma
Sequence:
MQQAVEQALDCAEYIVESAQQRPPKRKYLSSGRKSIFQKLYDLYVEECEKEPEVKKLRRNVNLLEKLVMQETLSCLVVNLYPGNEGYSLMLRGKNGSDSETIRLPYEEGELLEYLDAEELPPILVDLLEKSQVNIFHCGCVIAEIRDYRQSSNMKSPGYQSRHILLRPTMQTLVCDVHSITSDNHKWTQEDKLLLESQLILATAEPLCLDPSVAVACTANRLLYNRQKMNTRPMKRCWKRYSRSSLNRQQDLSHGPPPPQLRLLDFLQKRKERKAGQHYDLKISKAGNCVDMWKRSPCNLAVPSEVDVEKYAKVEESIKSDDSQPTMWPAHDVKDDYVFECEGGNQYQKTKLTILQSLGDPLYYGKIQPWKADEENDSQMSPSHSSADDHSNWFVIGSKTDAERVVNQYQELVQNEAKCPVKMSHSSSGSAALSPGEEAEQAETSSIQSSVLGKGVKHRPPPIKLPSGSGNSSSGNYFTAQQASSFLKSPTPPPSCKPSLSRKSSVDLSQVSMLSPAALSPASSSQRHES
Protein: DnaJ homolog subfamily C member 4 (DnaJ-like protein HSPF2) (Multiple endocrine neoplasia type 1 candidate protein number 18) (Q9NNZ3)
Organism: Homo sapiens (Human)
Subcellular location: Membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}.
Interaction partners:
- Vascular endothelial growth factor B
Sequence:
MPPLLPLRLCRLWPRNPPSRLLGAAAGQRSRPSTYYELLGVHPGASTEEVKRAFFSKSKELHPDRDPGNPSLHSRFVELSEAYRVLSREQSRRSYDDQLRSGSPPKSPRTTVHDKSAHQTHSSWTPPNAQYWSQFHSVRPQGPQLRQQQHKQNKQVLGYCLLLMLAGMGLHYIAFRKVKQMHLNFMDEKDRIITAFYNEARARARANRGILQQERQRLGQRQPPPSEPTQGPEIVPRGAGP
Protein: Mycobactin import ATP-binding/permease protein IrtB (EC 7.2.2.-) (Iron-regulated transporter B) (P9WQJ7)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: Part of the ABC transporter complex IrtAB involved in the import of iron-bound mycobactin (Fe-MBT) and carboxymycobactin (Fe-cMBT) (By similarity). Transmembrane domains (TMD) form a pore in the membrane and the ATP-binding domain (NBD) is responsible for energy generation (By similarity). Required for replication in human macrophages and in mouse lungs.
Subcellular location: Cell inner membrane {ECO:0000269|PubMed:18461140}; Multi-pass membrane protein {ECO:0000255|PROSITE-ProRule:PRU00441, ECO:0000269|PubMed:18461140}.
Interaction partners:
- Mycobactin import ATP-binding/permease protein IrtA
- Phenyloxazoline synthase MbtB
- Salicyl-AMP ligase / salicyl-S-ArCP synthetase
- Peptide synthetase MbtE
- Salicylate synthase
- L-lysine N6-monooxygenase MbtG
- Protein Rv3402c
- Chaperone protein DnaK
- Conserved ATPase
- Lysine N-acyltransferase MbtK
Sequence:
MIRTWIALVPNDHRARLIGFALLAFCSVVARAVGTVLLVPLMAALFGEAPQRAWLWLGWLSAATVAGWVLDAVTARIGIELGFAVLNHTQHDVADRLPVVRLDWFTAENTATARQAIAATGPELVGLVVNLVTPLTSAILLPAVIALALLPISWQLGVAALAGVPLLLGALWASAAFARRADTAADKANTALTERIIEFARTQQALRAARRVEPARSLVGNALASQHTATMRLLGMQIPGQLLFSIASQLALIVLAGTTAALTITGTLTVPEAIALIVVMVRYLEPFTAVSELAPALESTRATLGRIGSVLTAPVMVAGSGTWRDGAVVPRIEFDDVAFGYDGGSGPVLDGVSFCLQPGTTTAIVGPSGCGKSTILALIAGLHQPTRGRVLIDGTDVATLDARAQQAVCSVVFQHPYLFHGTIRDNVFAADPGASDDQFAQAVRLARVDELIARLPDGANTIVGEAGSALSGGERQRVSIARALLKAAPVLLVDEATSALDAENEAAVVDALAADPRSRTRVIVAHRLASIRHADRVLFVDDGRVVEDGSISELLTAGGRFSQFWRQQHEAAEWQILAE
Protein: Brakeless-A (RE69316p) (Scribbler, isoform C) (Scribbler, isoform E) (Q9NBW0)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MEKKLAKVALNSSNVATESNIKNNKLLANLSAAGAATATTATTGTATTTTATTANQALNFNNKTKATANATAASANNRHNNNNNSSAIKKHTNTKQLAGKSPACNSSSSSLSSSSSSNSSESKDTNFEYEDEWNIGGIPELLDDLDADIEKSAHSSGGGNQATALNAKQANSSSTSSSSSSKGGASSSSSSAAATGSSSSHKSHKTTLHSNLSATSPTTIKFTRQPVAIGGANSSSSSSAAAAPSGGSANVVAKGSSSSSSSTSSSSSGKHHHHHHHHSNSSSSGSSSKGYKSALVAQLNSPSPLNSNSKSLSGSGSGSGNTNGAAGAGAGSTLSSSTFAGFSKGGSLVSSSAGAAAALAAGSGQQGSKFSAGGMSSQTGSGSGGNNTSNSNNSSSGSGGSGSGSSTGNTASGSGNNNSTSAGGPPSSQGGNNGNGSGSSSSSSSGKSSAKMSIDHQATLDKGLKMKIKRTKPGTKSSEAKHEIVKATDQQQNGALGAGSNNSANEDGSSGSSSTNASSLGSTNSSSSASSGSSSSSGSSSSSSKKHLNNASSGSGSSSSGGGSQNNASGHASGGGSSGSSQSTPQGTKRGSSGHRREKTKDKNAHSNRMSVDKSAAAASAAGEKDTPEKCSGTGAGGSPCSCNGDVGAPCSHHACIRRAAHMSNSAGNANSSAGTGQSGGSSSMSAVPPGVFTPSAGSPSTGSPSTVVPAAASLLAATGAASSSASQMASSSAGGVGGSGGGANAPGPPGKESAGSIKISSHIAAQLAAAAASNSYSGSGANTNQGQNSNAGGNGGSESKAAAAAQAKLMAPGMISATMHHTISVPAGTGTGDDDTKSPPAKRVKHEAGASGAGGGKEMVDICIGTSVGTITEPDCLGPCEPGTSVTLEGIVWHETEGGVLVVNVTWRGKTYVGTLLDCTRHDWAPPR
Protein: Elongation factor 2 (EF-2) (EC 3.6.5.-) (P05197)
Organism: Rattus norvegicus (Rat)
Function: 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.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:P13639}. Nucleus {ECO:0000250|UniProtKB:P13639}. Note=Phosphorylation by CSK promotes cleavage and SUMOylation-dependent nuclear translocation of the C-terminal cleavage product. {ECO:0000250|UniProtKB:P13639}.
Interaction partners:
- Large ribosomal subunit protein eL18
- Large ribosomal subunit protein uL4
- Small ribosomal subunit protein uS2
- Large ribosomal subunit protein uL3
- Elongation factor 1-gamma
- Small ribosomal subunit protein uS7
- Eukaryotic elongation factor 2 kinase
- Large ribosomal subunit protein uL14
- Small ribosomal subunit protein eS1
- Large ribosomal subunit protein uL5
Sequence:
MVNFTVDQIRAIMDKKANIRNMSVIAHVDHGKSTLTDSLVCKAGIIASARAGETRFTDTRKDEQERCITIKSTAISLFYELSENDLNFIKQSKDGSGFLINLIDSPGHVDFSSEVTAALRVTDGALVVVDCVSGVCVQTETVLRQAIAERIKPVLMMNKMDRALLELQLEPEELYQTFQRIVENVNVIISTYGEGESGPMGNIMIDPVLGTVGFGSGLHGWAFTLKQFAEMYVAKFAAKGEGQLGAAERAKKVEDMMKKLWGDRYFDPANGKFSKSANSPDGKKLPRTFCQLILDPIFKVFDAIMNFRKEETAKLIEKLDIKLDSEDKDKEGKPLLKAVMRRWLPAGDALLQMITIHLPSPVTAQKYRCELLYEGPPDDEAAMGIKSCDPKGPLMMYISKMVPTSDKGRFYAFGRVFSGVVSTGLKVRIMGPNYTPGKKEDLYLKPIQRTILMMGRYVEPIEDVPCGNIVGLVGVDQFLVKTGTITTFEHAHNMRVMKFSVSPVVRVAVEAKNPADLPKLVEGLKRLAKSDPMVQCIIEESGEHIIAGAGELHLEICLKDLEEDHACIPIKKSDPVVSYRETVSEESNVLCLSKSPNKHNRLYMKARPFPDGLAEDIDKGEVSARQELKARARYLAEKYEWDVAEARKIWCFGPDGTGPNILTDITKGVQYLNEIKDSVVAGFQWATKEGALCEENMRGVRFDVHDVTLHADAIHRGGGQIIPTARRCLYASVLTAQPRLMEPIYLVEIQCPEQVVGGIYGVLNRKRGHVFEESQVAGTPMFVVKAYLPVNESFGFTADLRSNTGGQAFPQCVFDHWQILPGDPFDNSSRPSQVVAETRKRKGLKEGIPALDNFLDKL
Protein: LD29830p (Splicing regulatory protein 54) (Q9VL71)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- RNA-binding protein 1
- LD32469p
- LD40489p
- Serine/threonine-protein kinase Doa
- Uncharacterized protein, isoform B
- Polyadenylate-binding protein 2
- Pre-mRNA-processing factor 17
- Pre-mRNA-splicing factor Slu7
- Splicing factor U2af 38 kDa subunit
- Frost
Sequence:
MAGGNTPRVIQVTNIAPQATKDQMQTLFGNIGKIEEIRLYPTIRDVSCPVQSRICYVKYTDTTSVPVAQHLTNTVFIDRALIVIPVLAIPEEYRALEMLKNGTIVPGLQKPDSKLPPEVINRIEGQLPQQVIKTYDPKLVEFNLPEYPALPSFYDARKIEEIRRTIIVCDVKNEWRLDDLMECFQRAGEVKYARWAEKDNKTYCMIEFCEQTSIIHALRMQGQEFKGGHLSVYHSTYSITKPEAKSNEAAQAEIEEAMTIVKEAQSMISAAIDPVIGMLAKDKRRRSRSRSRSRDRRTSRSRSHRSTSRRRSRRSGSRERRSVSRSRRSRSRGKHSSRSRSKRSRSRHRRSSSRSRRSRSRGGKHSRSSRSRGKRSRSRHRRSTSRSRSSRSHGTGGGGSGNGKRSRSRERSKKSHRSEKHSSRSPRSRSKRSSPSPPPATGSKSRSSRSKDPVIVSAKSSRRRDRSRTPETRKLKSISEDTEVKSSRSSADSKSRKSVSVEKSDNMDISNSP
Protein: RNA-binding protein, putative (Q387F5)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MQEGQLFQSMMSVNFLTDRPVSPISSASTAEVTAGHDISTINRTLDASFMYDDGALMDFDSKHWIRVTRLDPSTSSKTLRQMFYPYGGDEAFVIWDNAVVGYVGFDNHFMAELAVEKMNTFIPCRQAQALCVRPASMDEVVLARSAVSSGQESIVPLLYSDCPIKCIVQVIEGHRQPSYCAMELVEEVKRAPRSLFARVSETLSQLKANSFLVEEFREALVRNLLLHIFEEDHTDTKANCGVLLGELFCSGFLTGDPFQIASGILQRGVKSIGQIDNVCAVAHACASLPFAMSKASFWALVGQLSLQTEEPLRSALRGHIRRFHQSTEFISPKPTANAPLPTADRAASSFPGLKMRTVYVSHLPASMPQRTFMDLLTSCGGVNKVRVCRGKGYTTLFAFVEMATADGVAAALRLGRANVLGCNIRLQMARNPIQDSQSDDAVINANGTVACECLFGRHGGTLGDVASDKGY
Protein: Ring finger protein 38 (A0A0G2K8H9)
Organism: Rattus norvegicus (Rat)
Interaction partners:
Sequence:
MSGSAAAAVAVAAATSAAAAAAAHFQPRPSSPRPGPAEIGPPRRPRPPPPPPPPRPEPITAGRLSPPGHGSLRSGAQGVGACGRAPGAGSVGASFQCQSIHHDHICHDDSDKISPGANSAPLPGHPNKVICERVRLPSLFPLLPSDQDTTIQEDAHFKAFFQSEDSPSPKRQRLSHSVFDYTSASPAPSPPMRPWEMTSNRQPPSVRPNQHHFSGERCNTPARNRRSPPVRRQRGRRERLSRHNSISQDENYHHLPYAQQQAIEEPRAFHPPNVSPRLLHPAAHPPQQNAVMVDIHDQLHQGTVPVSYTVTTVAPHGIPLCTGQHIPACSTQQVPGCSVVFSGQHLPVCSVPPPMLQACSVQHLPVPYAAFPPLISSDPFLLHPPHLSPHHPPHLPPPGQFVPFQTQQSRSPLQRIENEVELLGEHLQVGSFTYPPSAHPPTLPPSAPLQFLTHDPLHQEVSFGVPYPPFMPRRLTGRSRYRSQQPVPPPTYHPSLLPYVLSMLPVPPTVGPTFSFELDVEDGEVENYEALLNLAERLGEAKPRGLTKADIEQLPSYRFNPSNHQSEQTLCVVCMCDFESRQLLRVLPCNHEFHAKCVDKWLKGNRTCPICRADASEVHRDSE
Protein: DNA repair and telomere maintenance protein nbs1 (O43070)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Required for DNA damage repair and S-phase DNA damage checkpoint. Involved in telomere length maintenance and maintenance of chromatin structure.
Subcellular location: Nucleus {ECO:0000269|PubMed:12944481}. Chromosome {ECO:0000269|PubMed:19804755}. Chromosome, telomere {ECO:0000269|PubMed:12944481, ECO:0000269|PubMed:12944482}. Note=Localizes to DNA double-strand breaks (DSBs); recruited to DNA damage sites. {ECO:0000269|PubMed:19804755}.
Interaction partners:
- Double-strand break repair protein rad32
- Serine/threonine-protein kinase tel1
- DNA repair protein rad50
- DNA endonuclease ctp1
- Exodeoxyribonuclease 1
- Protein kinase rad3
- ATP-dependent DNA helicase II subunit 1
- BRCT-containing protein 1
- Flap endonuclease 1
- DNA repair protein rhp51
Sequence:
MWIIEAEGDILKGKSRILFPGTYIVGRNVSDDSSHIQVISKSISKRHARFTILTPSEKDYFTGGPCEFEVKDLDTKFGTKVNEKVVGQNGDSYKEKDLKIQLGKCPFTINAYWRSMCIQFDNPEMLSQWASNLNLLGIPTGLRDSDATTHFVMNRQAGSSITVGTMYAFLKKTVIIDDSYLQYLSTVKESVIEDASLMPDALECFKNIIKNNDQFPSSPEDCINSLEGFSCAMLNTSSESHHLLELLGLRISTFMSLGDIDKELISKTDFVVLNNAVYDSEKISFPEGIFCLTIEQLWKIIIERNSRELISKEIERLKYATASNSTPQKIIQPQRHIQKNIVDDLFSVKKPLPCSPKSKRVKTLENLSIMDFVQPKQMFGKEPEGYLSNQSNNGSAQNKKSGDNSEKTKNSLKSSSKKSANTGSGQGKTKVEYVSYNSVDKGNSSPFKPLELNVVGEKKANAEVDSLPSENVQESEDDKAFEENRRLRNLGSVEYIRIMSSEKSNANSRHTSKYYSGRKNFKKFQKKASQKAPLQAFLSLSEHKKTEVFDQDDTDLEPVPRLMSKVESIPAGASSDKSGKSSISKKSSNSFKELSPKTNNDEDDEFNDLKFHF
Protein: (-)-alpha pinene synthase 1, chloroplastic (EC 4.2.3.119) ((-)-beta pinene synthase 1, chloroplastic) (EC 4.2.3.120) (Terpene synthase (-)alphapin1) (PbTPS-(-)alphapin1) (R9QMY9)
Organism: Pinus banksiana (Jack pine) (Pinus divaricata)
Function: Monoterpene synthase (TPS) involved in the biosynthesis of monoterpene natural products included in conifer oleoresin secretions and volatile emissions; these compounds contribute to biotic and abiotic stress defense against herbivores and pathogens. Catalyzes the conversion of (2E)-geranyl diphosphate (GPP) to (-)-alpha-pinene and, to a lower extent, to (-)-beta-pinene.
Subcellular location: Plastid, chloroplast {ECO:0000255}.
Interaction partners:
Sequence:
MSPVSVISLPSDLCLPTSFIDRSGRELIPLHITIPNVAMRRQGKLMTRASMSMNLRTAVSDDAVIRRRGDFHSNLWDDDFIQSLSAPYGEPSYRERAERLIGEVKNSFNSMSNEDSESITPLDDLIQRLWMVDSVERLGIDRHFKKEIKSALDHVYSYWSEKGIGCGRESVVTDLNSTALGLRTLRLHGYDVSAEVLNHFKNQSGQFACTLKQTEDQIRTVLNLYRASLIAFPGEKVMDEAETFSAKYLKDALQKVPVSSLSREIGDVLEYGWHTYLPRLEARNYIDVFGQDTGNSQSYMKTEKLLELAKLEFNIFHALQKRELEYLVRWWKGSGSPQMTFCRHRHVEYYTLASCIAFEPQHSGFRLGFAKACHIITVLDDMYDTFGTLDELELFTSAIKRWDPSATECLPEYMKGVYMIVYNTVNEMSQEADKAQGRDTLNYCRQAWEEYIDAYMQEAKWIASGEVPTFEEYYENGKVSSGHRVSALQPILTTDIPFPEHVLKEVDIPSKLNDLASAILRLRGDTRCYQADRARGEEASCISCYMKDNPGTTEEDALNHINAMISDVIKGLNWELLKPNSSVPISAKKHAFDISRAFHYGYKYRDGYSVASIETKSLVKRTVIDPVTL
Protein: Kinesin family member 21A (H0YI78)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
QREELTKRREKLSKRREKIVKENGEGDKNVANINEEMESLTANIDYINDSISDCQANIMQMEEAKEEGETLDVTAVINACTLTEARYLLDHFLSMGINKGLQAAQKEAQIKVLEGRLKQTEITSATQNQLLFHMLKEKAELNPELDALLGHALQENVEDSTDEDAPLNSPGSEGSTLSSDLMKLCGEVKPKNKARRRTTTQMELLYADSSELASDTSTGDASLPGPLTPVAEGQEIGMNTETSGTSAREKELSPPPGLPSKIGSISRQSSLSEKKIPEPSPVTRRKAYEKAEKSKAKEQKQGIINPFPASKGIRAFPLQCIHIAEGHTKAVLCVDSTDDLLFTGSKDRTCKVWNLVTGQEIMSLGGHPNNVVSVKYCNYTSLVFTVSTSYIKVWDIRDSAKCIRTLTSSGQVTLGDACSASTSRTVAIPSGENQINQIALNPTGTFLYAASGNAVRMWDLKRFQSTGKLTGHLGPVMCLTVDQISSGQDLIITGSKDHYIKMFDVTEGALGTVSPTHNFEPPHYDGIEALTIQGDNLFSGSRDNGIKKWDLTQKDLLQQVPNAHKDWVCALGVVPDHPVLLSGCRGGILKVWNMDTFMPVGEMKGHDSPINAICVNSTHIFTAADDRTVRIWKARNLQDGQISDTGDLGEDIASN
Protein: 2-dehydro-3-deoxygluconokinase (EC 2.7.1.45) (2-keto-3-deoxygluconokinase) (3-deoxy-2-oxo-D-gluconate kinase) (KDG kinase) (E0J5J4)
Organism: Escherichia coli (strain ATCC 9637 / CCM 2024 / DSM 1116 / LMG 11080 / NBRC 13500 / NCIMB 8666 / NRRL B-766 / W)
Function: Catalyzes the phosphorylation of 2-keto-3-deoxygluconate (KDG) to produce 2-keto-3-deoxy-6-phosphogluconate (KDPG).
Interaction partners:
Sequence:
MSKKIAVIGECMIELSEKGADVKRGFGGDTLNTSVYIARQVDPAALTVHYVTALGTDSFSQQMLDAWHGENVDTSLTQRMENRLPGLYYIETDSTGERTFYYWRNEAAAKFWLESEQSAAICEELANFDYLYLSGISLAILSPTSREKLLSLLRECRANGGKVIFDNNYRPRLWASKEETQQVYQQMLECTDIAFLTLDDEDALWGQQPVEDVIARTHNAGVKEVVVKRGADSCLVSIAGEGLVDVPAVKLPKEKVIDTTAAGDSFSAGYLAVRLTGGSAENAAKRGHLTASTVIQYRGAIIPREAMPA
Protein: Phospholipase A2 (EC 3.1.1.4) (Phosphatidylcholine 2-acylhydrolase) (I7GQA7)
Organism: Xylocopa appendiculata circumvolans (Japanese carpenter bee)
Function: PLA2 catalyzes the calcium-dependent hydrolysis of the 2-acyl groups in 3-sn-phosphoglycerides.
Subcellular location: Secreted {ECO:0000255, ECO:0000269|PubMed:28546807}.
Interaction partners:
Sequence:
MHALRSSVLALWLCLHVSVRAWMTYRSANGLDEYEPEDRIIFVGTKWCGNGNVAEGPEDLGSLKETDACCREHDMCPDLIEAGQSKHGLTNTASYTRLNCACDEKFYNCLKNSSETGSGAVRFTYFTLLGTMCYRNEHPLICVKKGWFSCSKYELDQSQPKRYQWFDVSSNFAFPRMLT
Protein: Endonuclease III (EC 4.2.99.18) (DNA-(apurinic or apyrimidinic site) lyase) (P9WQ11)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: DNA repair enzyme that has both DNA N-glycosylase activity and AP-lyase activity. The DNA N-glycosylase activity releases various damaged pyrimidines from DNA by cleaving the N-glycosidic bond, leaving an AP (apurinic/apyrimidinic) site. The AP-lyase activity cleaves the phosphodiester bond 3' to the AP site by a beta-elimination, leaving a 3'-terminal unsaturated sugar and a product with a terminal 5'-phosphate. Has a preference for oxidized pyrimidines, such as thymine glycol (prefers 5S isomers) 5,6-dihydrouracil:G, 5-hydroxyuracil:G, 5-hydroxycytosine:G and urea:A. Cleaves ssDNA containing an AP site.
Interaction partners:
- Adenine DNA glycosylase
- Endonuclease 8 2 lyase Nei 2)
- Formamidopyrimidine-DNA glycosylase 1
- Possible membrane-anchored thioredoxin-like protein
- Endonuclease 8 1 lyase Nei 1)
- Possible membrane protein
- Probable exodeoxyribonuclease III protein XthA
- Serine protease Rv3671c
- Probable endonuclease 4
- DNA ligase B
Sequence:
MPGRWSAETRLALVRRARRMNRALAQAFPHVYCELDFTTPLELAVATILSAQSTDKRVNLTTPALFARYRTARDYAQADRTELESLIRPTGFYRNKAASLIGLGQALVERFGGEVPATMDKLVTLPGVGRKTANVILGNAFGIPGITVDTHFGRLVRRWRWTTAEDPVKVEQAVGELIERKEWTLLSHRVIFHGRRVCHARRPACGVCVLAKDCPSFGLGPTEPLLAAPLVQGPETDHLLALAGL
Protein: Thr6-bradykinin (Bradykinin-related peptide) (C0HLT7)
Organism: Polybia occidentalis (Paper wasp)
Function: When injected into the rat central nervous system, exhibits antinociceptive effects such as increasing hot plate and tail flick withdrawal latencies in a dose- and time-dependent fashion. Likely to act on the bradykinin receptor B2 (BDKRB2). The greatest antinociceptive effects occurs 30 minutes after injection in hot plate (ED(50)=6.82 nM) and tail flick tests (ED(50)=2.94 nM).
Subcellular location: Secreted {ECO:0000269|PubMed:17533426, ECO:0000269|Ref.2}.
Interaction partners:
Sequence:
RPPGFTPFR
Protein: Spore germination protein 2 (SPG2) (P15520)
Organism: Dictyostelium discoideum (Social amoeba)
Subcellular location: Secreted {ECO:0000305}.
Interaction partners:
- Stalk-specific protein A
- Spore germination protein 270-11
Sequence:
MNIRNSLILIISTILFFSIINGSLSLDPTCVGAPDGQVYLFSSWDFKGDRYVYNVSQGYLSLSDGFRGNVQSFISGADVCFVKWYPIEQYQITAGESHRNYAALTNFGQRMDAIIPGNCSNIVCSPK
Protein: BCL2/adenovirus E1B 19 kDa protein-interacting protein 3 (O55003)
Organism: Mus musculus (Mouse)
Function: Apoptosis-inducing protein that can overcome BCL2 suppression. May play a role in repartitioning calcium between the two major intracellular calcium stores in association with BCL2 (By similarity). Involved in mitochondrial quality control via its interaction with SPATA18/MIEAP: in response to mitochondrial damage, participates in mitochondrial protein catabolic process (also named MALM) leading to the degradation of damaged proteins inside mitochondria. The physical interaction of SPATA18/MIEAP, BNIP3 and BNIP3L/NIX at the mitochondrial outer membrane may play a critical role in the translocation of lysosomal proteins from the cytoplasm to the mitochondrial matrix (By similarity). The physical interaction of SPATA18/MIEAP, BNIP3 and BNIP3L/NIX at the mitochondrial outer membrane regulates the opening of a pore in the mitochondrial double membrane in order to mediate the translocation of lysosomal proteins from the cytoplasm to the mitochondrial matrix (By similarity). Plays an important role in the calprotectin (S100A8/A9)-induced cell death pathway (By similarity).
Subcellular location: Mitochondrion. Mitochondrion outer membrane {ECO:0000250}; Single-pass membrane protein {ECO:0000250}. Note=Coexpression with the EIB 19-kDa protein results in a shift in NIP3 localization pattern to the nuclear envelope. Colocalizes with ACAA2 in the mitochondria. Colocalizes with SPATA18 at the mitochondrion outer membrane (By similarity). {ECO:0000250}.
Interaction partners:
- Apoptosis regulator Bcl-2
- Gamma-aminobutyric acid receptor-associated protein
- GTP-binding protein Rheb
- Bcl-2-like protein 1
- Gamma-aminobutyric acid receptor-associated protein-like 2
- Gamma-aminobutyric acid receptor-associated protein-like 1
- Beclin-1
- FUN14 domain-containing protein 1
- Microtubule-associated protein 1 light chain 3 beta
- Microtubule-associated protein 1A
Sequence:
MSQSGEENLQGSWVELHFSNGNGSSVPASVSIYNGDMEKILLDAQHESGRSSSKSSHCDSPPRSQTPQDTNRAEIDSHSFGEKNSTLSEEDYIERRREVESILKKNSDWIWDWSSRPENIPPKEFLFKHPKRTATLSMRNTSVMKKGGIFSADFLKVFLPSLLLSHLLAIGLGIYIGRRLTTSTSTF
Protein: GH14566p (Smg6) (Q9VBZ6)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- LD36341p
- Regulator of nonsense transcripts 1 homolog
- FI21285p1
- RE04053p
- Serine/threonine-protein kinase Smg1
- 5'-3' exoribonuclease 1
- Eukaryotic translation release factor 3, isoform A
- Eukaryotic translation initiation factor 4G1, isoform B
- Nuclear cap-binding protein subunit 1
- Eukaryotic initiation factor 4A-III
Sequence:
MSRKGTREQNDISLIIGTLPKRLQNKIAASCSHAAAAATTTKALETENAENAEPVATTANASRPVEILSNASTGGGKPDAQSKQPVLDTSGKMAWEGGIPGILRVTTSVAGDVNRNGQGQGKNKSGNSARRRGRKDKEHATQSPVTRTRLTTEHPDWFEPLLGLPHAKNIVHLYDQLMVLNQRNLILINWKNFCYIHDQLQDAFKQLLLEQLKFVCEHKVDVFFWKLLFYNVRNYLKRQQTDQAHTHTLLLIEQAIKFYRMLYDKLMAKCVASSRCDSALKVVAQRLLICLGDLTRYRVNHVKATDYMEAARYYQRAQELVPGNGAPFNQLAVISIYHHKRFDAVYYYVRSLLTSNSIQSAKESLLDLFDEIRRKYEETEMKQSPMHYAAGSKNQKSKQMRKEVWIYPDGIRRLHRTDDKGNKAKGNKATMAEVNRYEEMPPEEILPRIVSLYLYLLGKLYTGTDVDSLYPLLRKLQIQIGVALRHENLLSRSKLLKIVALNLFVVEHNKPKTSRREMRYHSFNFANSFFGLMMKKTNQLLAGFVEDSTNVQCLPEEDFATVNTYLQFVNVYVRWLSISLDVWEPVRSEEHSFIDCWAELTILFEYIECLMGKHKLEKNEILLDEDVALRGFTPLGRETLSMDYLKRGSERLQFFERVRRIGQFQEYYVQHQEALQQPLESSFTVEHLNAAMKNALENYDAESCGLAANVSKIQCKAVEELLCRSTDSDVSELCKLKKELEAKARVKQICTSKLEDILKFVDTKIYIEVRPRYLLPDTNCFIDCLEDFEKLSTEFKRYTLIIPLTVVKELDGLSKGVKLDSYRSSKQTQRIHHFDEVSSRAKKSLEFIKSAKGNVKCATTKGSFVNASVFALVEEEYLSNDDKILATAMAVSKTAKTEQCTDGKCFIQTELVLITTDRNLRVKALSRNLAVSALDEFLQWAKDCREST