wanglab/gogpt-training-data huggingface dataset:
Protein: T-cell surface glycoprotein CD8 alpha chain (T-lymphocyte differentiation antigen T8/Leu-2) (CD antigen CD8a) (P01732)
Organism: Homo sapiens (Human)
Function: Integral membrane glycoprotein that plays an essential role in the immune response and serves multiple functions in responses against both external and internal offenses. In T-cells, functions primarily as a coreceptor for MHC class I molecule:peptide complex. The antigens presented by class I peptides are derived from cytosolic proteins while class II derived from extracellular proteins. Interacts simultaneously with the T-cell receptor (TCR) and the MHC class I proteins presented by antigen presenting cells (APCs). In turn, recruits the Src kinase LCK to the vicinity of the TCR-CD3 complex. LCK then initiates different intracellular signaling pathways by phosphorylating various substrates ultimately leading to lymphokine production, motility, adhesion and activation of cytotoxic T-lymphocytes (CTLs). This mechanism enables CTLs to recognize and eliminate infected cells and tumor cells. In NK-cells, the presence of CD8A homodimers at the cell surface provides a survival mechanism allowing conjugation and lysis of multiple target cells. CD8A homodimer molecules also promote the survival and differentiation of activated lymphocytes into memory CD8 T-cells.
Subcellular location: [Isoform 1]: Cell membrane {ECO:0000269|PubMed:1460019, ECO:0000269|PubMed:17341584, ECO:0000269|PubMed:17678538}; Single-pass type I membrane protein. Note=CD8A localizes to lipid rafts only when associated with its partner CD8B. {ECO:0000269|PubMed:17341584}.; SUBCELLULAR LOCATION: [Isoform 2]: Secreted {ECO:0000269|PubMed:7923932}.
Interaction partners:
- HLA class I histocompatibility antigen, A alpha chain
- Tyrosine-protein kinase Lck
- HLA class I histocompatibility antigen, alpha chain E
- CD8 subunit beta
- T-cell surface glycoprotein CD4
- HLA class I histocompatibility antigen, alpha chain G
- T-cell surface glycoprotein CD3 zeta chain
- Beta-2-microglobulin
- T-cell surface antigen CD2
- T-cell surface glycoprotein CD3 delta chain
Sequence:
MALPVTALLLPLALLLHAARPSQFRVSPLDRTWNLGETVELKCQVLLSNPTSGCSWLFQPRGAAASPTFLLYLSQNKPKAAEGLDTQRFSGKRLGDTFVLTLSDFRRENEGYYFCSALSNSIMYFSHFVPVFLPAKPTTTPAPRPPTPAPTIASQPLSLRPEACRPAAGGAVHTRGLDFACDIYIWAPLAGTCGVLLLSLVITLYCNHRNRRRVCKCPRPVVKSGDKPSLSARYV
Protein: Keratin, type I cytoskeletal 39 (Cytokeratin-39) (CK-39) (Keratin-39) (K39) (Type I hair keratin Ka35) (Q6IFW3)
Organism: Rattus norvegicus (Rat)
Function: May play a role in late hair differentiation.
Interaction partners:
Sequence:
MDTKGSTVTISSSTPPQNCSGNTNVRTNSSNKSCYHDVQSTGHALQTPQGQGCRPSPCLYRCPNYLIRTYSFHPCPDDCSRCSDGINSHEKETMQILNERLASYLEKVRMLEGENADLEDKIQEECSKTLPILCPDYLSYYTTIEQLQQKILCTKAENSRLVSQIDNTKLAADDLRAKYEAELSLRQLVEADANGLKQILDALTLSKADLEARVQSLTEELLCLKTNHEEEINSLQCQLGDRINIEVTAAPSVDLNQILQKMRCQYESIVETNRKDVEEWFNTQMEELNQQVVSSSQQQQCCQKDIIELRRTISALEVELQAQHRMRDSQECILAETEARYTALLAQIQSLIHNLEAQVAEIRSALQRQNQEYEVLLDIKSRLECEIATYRSLLESLDGRLPCNPCTTTWEPSCQARAMECLTPVYTSISLPGIHKPCRASGPPSRILVKICTITKEIKDGKVISSHEHVQPCYITRPAKV
Protein: AP2 domain transcription factor AP2Tel (C6KT65)
Organism: Plasmodium falciparum (isolate 3D7)
Interaction partners:
Sequence:
MEKVDIINKNVNSKNNNSHNNDNHDDDNNNNINNDVIFTNFCTNSNSENSLAKKILDSDDMSSVIHNYNNHNNINYHNNINYHKNYHDDNNMNNICVNIQKEYLNNNITYLTNYHQNNHLMEKTKKKKNYPCNNYKDKHTHYQYHISQNKDISKSNEHIDESNFIKKVSFQSNTYDNKNYPCDQTDTINIIFMHKYIYLKNLKKRNYFKKVIMEKSKNHQHRTRNKKFTNNIDTNLNNTKQFIEKYTNDDNYYNVLNKHLQNIYNTIENNKLNNYTNKINNHTYNINKKNIILYKKQKKYNIFYNKYIKSINRDHFKKYFFLLLYRYHISRHTYPNYVFPDIKMVNTNLSLHKMFYFYKNYIVYMDPYYSTYINIHNNINCMKLKNTTQFNTLKNKLSTYNYTNNKEQHKNLNNTIDYNGGHAELNNDDALTQIHNIKDDNITNVKKCTNEYYNYNDNKNHNSSCNHNIINYPSTSCQNTKHVTFCFISDNQSTKKKKKKKIKKKILNGKVELSAEPIFDKNKDQGKSQILFQNRDEQMEYNNIYTINKNNMINELKKKNIKKLMKKKNYEHNYDNNNNNNNDSQTSHSNDISNNLTSHNISISEIYKNSCLRNLNKIREVTDEINMPKYEKNDEHQILHDEILSSSQLDKCVQKGRKKKLGNINDEKTSNIYHIKKNKDNDNISIDKIKENNYFNNFPLDGYHDNNIKSSYNFDGDEDAIKEVQKYIDYIIENEDVDISKINITLNKTYVKINFFLKKYILQYEEFKNSNILFCFGESSEEEVLSERCTSKENVSNKIGNINDACDKTKNDDLINKKKPKQPKNRKINYDAIDTMWQPHFHPHNQEFRVRYRYKGSMRLKTISCKHFGYSNSKKISILFLLRWILCGKQIAEKTKRSRLSICDIDEGRLQELLASKKQKKLSLDIPDDKKEIEKLMLDKKKSLKVKRRKKAMSLDEEKVKKWFSKNMKNDEFYERLYKFNNFVLNNCKDDKVLNKINNIIYNYESEMKKCEKDVGINRVHCDDNKYNDDIKYSDDNKYKDDIKYSDDIKYSDDIKYSDDNKYNDDNKYNDDNKYNDDNKYNDDNKYNDDNKYNDDNKYNDDNKYNDDNKYNDDNKYNDDNHYVYNHYDNIKRTNKRGRKKKRKSNEEEEEEEKKKKNNMDLPCCDKDNYIINKKLKKNHKKNNDTNDTNDSNNNNNNNNISTEQRIPFCIGKQKEMFLKFFKTNMINGNIIQNKYKSSNDKSNNIKVIEDMNNIILDENMYNIAKNICLNNKMDVKNKEYVILSDENNIKRNNIINNNDNDDNNNNYDDDDDDDNIVYGSNKHINNKQRVKKKNNKMVTSCDLLNILSTKNDINDLFIINSENIRNKENLKAANNCLTELKKSIYIKNKNKNMNKIRYSNINDNFIELLNNENIMNNMKISKDKEEKKMEDDNMVNDQTNTLIKTKKKDDIEDSMLYAVYNRLFDLNNKELENDKNINIPNLSTNYDKGSCLLTQSSEELNKNLIDKNSCKKISNVSTCPSLGRNHLLCRDENLRSDNNMCSRSFSHVYKQKNYDIRNNDDMINNNIISVLCNNEKKGMDKDNNISYILKNIKNPNMFNMLFKKKSNNNLLDIKSNYYDYMKEIEIANNKHLEKAYVELLFREYMKINNKDLSKIDSSRGSIKKSSSNSMDSSYNPNMKHRKSKMVDNDNINDICNNNNNNNNKNNKKNNNYNNNNTPVDMCENNYIDTHNSCNNNYSNKINSLVNDVNAYKRILEKYESTHDMNNNKEKMIYQAVKELINSKDVLHKEEKKRKQKTDNKENDLINILNIRKCNDIHGHDNVNNDDYNVITSTSRNVQMNNLYQEKKNLKESEKIHKKYLSHVMYDKKNFDLIKNFIAAIKNNTLQQKEEEQYKNHEEKEKYIHNDTLYEDKIISSLLKNPHILNHKNNMNFKNYNHSDYNNSSDITKEKKKNISVFDENDDEIFTYYMSLKNNLPNIKNINNIKNMF
Protein: ADP-ribosylation factor 1 (EC 3.6.5.2) (P11076)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: GTP-binding protein involved in Golgi vesicle trafficking. May modulate vesicle budding and uncoating within the Golgi apparatus. May recruit the lipid transfer protein VPS13 to Golgi membranes. Recruits polyadenylate-binding protein PAB1 to COPI vesicles, and this is required for correct localization of the asymmetrically distributed ASH1 mRNA.
Subcellular location: Golgi apparatus {ECO:0000269|PubMed:15504911}.
Interaction partners:
- ADP-ribosylation factor 2
- ARF guanine-nucleotide exchange factor 2
- ADP-ribosylation factor GTPase-activating protein GCS1
- ADP-ribosylation factor GTPase-activating protein GLO3
- Chitin biosynthesis protein CHS5
- Coatomer subunit gamma
- Protein BCH1
- ARF guanine-nucleotide exchange factor 1
- Coatomer subunit beta
- ADP-ribosylation factor guanine nucleotide-exchange factor SEC7
Sequence:
MGLFASKLFSNLFGNKEMRILMVGLDGAGKTTVLYKLKLGEVITTIPTIGFNVETVQYKNISFTVWDVGGQDRIRSLWRHYYRNTEGVIFVVDSNDRSRIGEAREVMQRMLNEDELRNAAWLVFANKQDLPEAMSAAEITEKLGLHSIRNRPWFIQATCATSGEGLYEGLEWLSNSLKNST
Protein: Variant surface glycoprotein (VSG), putative (Q580P2)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004609}; Lipid-anchor, GPI-anchor {ECO:0000256|ARBA:ARBA00004609}.
Interaction partners:
- Variant surface glycoprotein
Sequence:
MTGRKGSRSSEQLLAVAALLTLVYATKSASTAAITDADTGPAQITNVCKEEFYLSELRKEIAAGITRRRRQRQDLLKLERKYRLAATMATQPNDRCLYSALAAKLEQKAESVQQQADKADDTATTAMGLIDEHVGKLKYAQKLLKTKAAVDATGYSRAGDSSNIYLELTRETIGNGRCTAIDSWGKFSSAHTAIDAAKLTEIKITPDTDLATKIFKDKITITGFNGCTASAVAKTRTFSSVLSTCTVSGSEAVTYARNSADYSYSTSTAAFYKNHDPDQGCEDATAAGEEGATADIKLRYAVCLAVKTIQTDGGKVPPLSGKALKGDKLVTNILRNCLPAYQAVSKPWDSVEAKDLNDFIESAYGADDGKFKEIFDTPLDSRQITVKLNDKSEDKALTALATASERNAATSHSGGQRNKKEIETSKKQPAGAPVASKESEEICKDKAQKECKEEDRCVFKEEKCKVKVTTTTGKDGKTNTTGSNSFVINKAPLLLAFSLALLNF
Protein: Netrin-5 (Netrin-1-like protein) (Q3UQ22)
Organism: Mus musculus (Mouse)
Function: Plays a role in neurogenesis. Prevents motor neuron cell body migration out of the neural tube.
Subcellular location: Secreted {ECO:0000255}.
Interaction partners:
- Netrin receptor DCC
- Neogenin
Sequence:
MTDYRTLFSSPGAGSTVTTPITLSLLLLLSQATSDPCYDPGGRPRFCLPPVTQLVGKAAAPCSQTCALPAASPGPACNSSLTLDLDGSFLLTSVTLRFCTAGPPALVLSAAWATGGPWRPLWRRPAWPGALGGPKKVTFHSPPGPKTRIVASYLRVEFGGKAGLVTTGVRGRCQCHGHAARCATRAQPPRCRCRHHTTGPGCESCRPSHRDWPWRPATPQHPHPCLPCQCHPIGATGGMCNQTSGQCSCKLGVTGLTCNRCGPGYQQSRSPRMPCQRIPEATTTPATTPVASRSDPQCQGYCNVSVSSVHMSLQRYCQQDYVLHAQVSASSSQPSEAVGPEWWRLAVHVLAVFKQRAWPVRRGGQEAWVPRADLICGCLRLRPGADYLLLGRAAQTHDDDNYDPARLILNRHGLALPWRPRWARPLRRLQQKERGGACRGLLPPTRSPGPRN
Protein: Methionine aminopeptidase 1A (MAP 1A) (MetAP 1A) (EC 3.4.11.18) (Peptidase M 1A) (Q9SLN5)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Cotranslationally removes the N-terminal methionine from nascent proteins. The N-terminal methionine is often cleaved when the second residue in the primary sequence is small and uncharged (Met-Ala-, Cys, Gly, Pro, Ser, Thr, or Val).
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03174, ECO:0000269|PubMed:11060042}.
Interaction partners:
- Peptide deformylase 1B, chloroplastic/mitochondrial
- Methionine aminopeptidase 2A
- Peptide deformylase 1A, chloroplastic/mitochondrial
- Large ribosomal subunit protein uL18y
- Large ribosomal subunit protein uL18z
- Adenylate kinase 4
- Large ribosomal subunit protein uL23z
- Large ribosomal subunit protein uL23y
- 60S ribosomal export protein NMD3
- Large ribosomal subunit protein eL38z/eL38y
Sequence:
MASESDASSIATLSCARCEKPAHLQCPKCIDLKLPREQASFCTQECFKAAWSSHKSVHVKAQLSSIGDQNSDLISQGWLYCVKKGQARTPKLPHFDWTGPLKQYPISTKRVVPAEIEKPDWAIDGTPKVEPNSDLQHVVEIKTPEQIQRMRETCKIAREVLDAAARVIHPGVTTDEIDRVVHEATIAAGGYPSPLNYYFFPKSCCTSVNEVICHGIPDARKLEDGDIVNVDVTVCYKGCHGDLNETYFVGNVDEASRQLVKCTYECLEKAIAIVKPGVRFREIGEIVNRHATMSGLSVVRSYCGHGIGDLFHCAPNIPHYARNKAVGVMKAGQTFTIEPMINAGGWRDRTWPDGWTAVTADGKRSAQFEHTLLVTETGVEVLTARLPSSPDVYPWLTK
Protein: Furrowed, isoform B (A8JUT1)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MGKKFTLGEKIQYTCPKGHSLLGQTERECRLDGTWSGSSPTCKYVDCGSLPELKFGSIHMSEERTSFGVVATYSCHENYTLIGNENRTCAMDGWSGKQPECLVDWCPDPQPIAGGDVRFNDKRAGSTATYVCEPGYVLVGEAIISCGLGGEWSSKTPSCRFVDCGAPARPNRGIAILLNGTTTVNSVVKYECDEDHWLDGQSELYCTREGKWSGEAPVCELVTCETPSVPSGSFVIGYDYNVHSKIQYNCDPGHIMHGTPVLECLDSGEWSADAPYCEYIDCGTILPIPYGSHKYVTNTTYVGSEVVFSCSQSHKLSGVLKRTCLESAVWSDASPKCEEIRCPEPKLAAHSLLSVTGNDRMYGRTLIRTSESSQNTAQTYKIGALAKYRCERGYKMVGEALATCTDSGQWSGTIPECVYVECGAPEGINNGKVVLATNATYYGAAVLYECNVNFKLNGVSRRLCTEHGNWSHEAPECVEVVCDTPNINENLIVEAGPRAVGSVATFKCAKGRIMMGNDTRVCQKNGKWTGKSPTCRPVDCGRPLAIENGRVIVVNDSTLYGGSAEYHCIPNYNRIGQYLRKCTEDGAWSGKQPRCELATAEGQETSELGTGVGIGATVIVALLVIFGLIFLYRNKARPVKNTENVQAAETKDERNAAVMSYSTLEANNRMHMDNNPSATFNTFHGGAGGRSNGGGNPDANSNGERLNNNRSENIYDQIPNEQFYDAPYEMRTNDEVYEPEPVASNVITINGISVR
Protein: RuvB-like helicase (EC 3.6.4.12) (G0RYC2)
Organism: Chaetomium thermophilum (strain DSM 1495 / CBS 144.50 / IMI 039719) (Thermochaetoides thermophila)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|RuleBase:RU363048}.
Interaction partners:
- RuvB-like helicase
- Uncharacterized protein
- Vps72/YL1 C-terminal domain-containing protein
- DNA helicase
- Actin-like protein
- SWR1-complex protein 4
- Actin-related protein 4
- Histone H2A
- Vps72/YL1 C-terminal domain-containing protein
- INO80 complex subunit B-like conserved region domain-containing protein
Sequence:
MAAPLVTSVTETKELRGLNLIAAHSHIRGLGVDADTLEPRPSSQGLVGQEKARKAAAVVLEMIKQGKIAGRAVLIAGPPSTGKTAIAMGMAQSLGQDVPFTTLAASEIFSLEMSKTEALTQAFRKSIGVRIKEESEIMEGEVVEIQIDRSVTGGAKQGKLTIKTTDMEAIYDMGSKMIDAMTKERVMAGDIISIDKSSGKITKLGRSYARSRDYDAMGVDTKFLQCPEGELQKRKEVVHTVSLHEIDVINSRTQGFLALFSGDTGEIRSEIRDQINTKVAEWKEEGKAEIVPGVLFIDEVHMLDIECFSYINRALESDLAPIVIMASNRGVSRIRGTDYKSPHGLPLDFLDRVVIINTHPYTPDELRQILSIRAQEEEVDLTPDALALLTKIGQEAGLRYASNLITTSQLIAAKRRAKQVGVEDVQRSFKLFYDPARSVRFVQESEKRLIGNDGVVDFSYQGAAEAAAPTLPAAAPVDPVGGEKMDMS
Protein: Lens fiber major intrinsic protein (Aquaporin-0) (MIP26) (MP26) (P09011)
Organism: Rattus norvegicus (Rat)
Function: Water channel. Channel activity is down-regulated by CALM when cytoplasmic Ca(2+) levels are increased. May be responsible for regulating the osmolarity of the lens. Interactions between homotetramers from adjoining membranes may stabilize cell junctions in the eye lens core. Plays a role in cell-to-cell adhesion and facilitates gap junction coupling (By similarity).
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:P30301}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q6J8I9}. Cell junction {ECO:0000250|UniProtKB:Q6J8I9}. Note=Localizes to thin cell-cell junctions in lens fiber cells. {ECO:0000250|UniProtKB:Q6J8I9}.
Interaction partners:
- Aquaporin
- Aquaporin-11
- Calmodulin-like protein 4
- Calmodulin-like protein 3
- Filensin
- Gap junction alpha-8 protein
- Gamma-crystallin S
- Aquaporin-3
- Lens fiber membrane intrinsic protein
- Aquaporin-9
Sequence:
MWELRSASFWRAIFAEFFATLFYVFFGLGSSLRWAPGPLHVLQVALAFGLALATLVQTVGHISGAHVNPAVTFAFLVGSQMSLLRAFCYIAAQLLGAVAGAAVLYSVTPPAVRGNLALNTLHAGVSVGQATTVEIFLTLQFVLCIFATYDERRNGRMGSVALAVGFSLTLGHLFGMYYTGAGMNPARSFAPAILTRNFSNHWVYWVGPIIGGGLGSLLYDFLLFPRLKSVSERLSILKGARPSDSNGQPEGTGEPVELKTQAL
Protein: thr operon leader peptide (thr operon attenuator) (P0AD86)
Organism: Escherichia coli (strain K12)
Function: This protein is involved in control of the biosynthesis of threonine.
Interaction partners:
- leu operon leader peptide
- trp operon leader peptide
- Bifunctional aspartokinase/homoserine dehydrogenase 1
- ilv operon leader peptide
Sequence:
MKRISTTITTTITITTGNGAG
Protein: EH domain-binding protein 1 (Q8NDI1)
Organism: Homo sapiens (Human)
Function: May play a role in actin reorganization. Links clathrin-mediated endocytosis to the actin cytoskeleton. May act as Rab effector protein and play a role in vesicle trafficking. Required for perinuclear sorting and insulin-regulated recycling of SLC2A4/GLUT4 in adipocytes (By similarity).
Subcellular location: Cytoplasm {ECO:0000269|PubMed:14676205}. Membrane {ECO:0000269|PubMed:14676205}. Endosome {ECO:0000305|PubMed:27552051}. Note=Mostly found in cytosol and plasma membrane.
Interaction partners:
- EH domain-containing protein 2
- Ras-related protein Rab-8A
- EH domain-containing protein 3
- Ras-related protein Rab-10
- Diphosphoinositol polyphosphate phosphohydrolase 3-beta
- EH domain-containing protein 1
- Rabenosyn-5
- PDZ and LIM domain 5
Sequence:
MASVWKRLQRVGKHASKFQFVASYQELMVECTKKWQPDKLVVVWTRRSRRKSSKAHSWQPGIKNPYRGVVVWPVPENIEITVTLFKDPHAEEFEDKEWTFVIENESPSGRRKALATSSINMKQYASPMPTQTDVKLKFKPLSKKVVSAALQFSLSCIFLREGKATDEDMQSLASLMSMKQADIGNLDDFEEDNEDDDENRVNQEEKAAKITEIVNQLNALSSLDEDQDDCIKQANMRSAKSASSSEELINKLNFLDEAEKDLATVNSNPFDDPDAAELNPFGDPDSEEPITETASPRKTEDSFYNNSYNPFKEVQTPQYLNPFDEPEAFVTIKDSPPQSTKRKNIRPVDMSKYLYADSSKTEEEELDESNPFYEPKSTPPPNNLVNPVQELETERRVKRKAPAPPVLSPKTGVLNENTVSAGKDLSTSPKPSPIPSPVLGRKPNASQSLLVWCKEVTKNYRGVKITNFTTSWRNGLSFCAILHHFRPDLIDYKSLNPQDIKENNKKAYDGFASIGISRLLEPSDMVLLAIPDKLTVMTYLYQIRAHFSGQELNVVQIEENSSKSTYKVGNYETDTNSSVDQEKFYAELSDLKREPELQQPISGAVDFLSQDDSVFVNDSGVGESESEHQTPDDHLSPSTASPYCRRTKSDTEPQKSQQSSGRTSGSDDPGICSNTDSTQAQVLLGKKRLLKAETLELSDLYVSDKKKDMSPPFICEETDEQKLQTLDIGSNLEKEKLENSRSLECRSDPESPIKKTSLSPTSKLGYSYSRDLDLAKKKHASLRQTESDPDADRTTLNHADHSSKIVQHRLLSRQEELKERARVLLEQARRDAALKAGNKHNTNTATPFCNRQLSDQQDEERRRQLRERARQLIAEARSGVKMSELPSYGEMAAEKLKERSKASGDENDNIEIDTNEEIPEGFVVGGGDELTNLENDLDTPEQNSKLVDLKLKKLLEVQPQVANSPSSAAQKAVTESSEQDMKSGTEDLRTERLQKTTERFRNPVVFSKDSTVRKTQLQSFSQYIENRPEMKRQRSIQEDTKKGNEEKAAITETQRKPSEDEVLNKGFKDTSQYVVGELAALENEQKQIDTRAALVEKRLRYLMDTGRNTEEEEAMMQEWFMLVNKKNALIRRMNQLSLLEKEHDLERRYELLNRELRAMLAIEDWQKTEAQKRREQLLLDELVALVNKRDALVRDLDAQEKQAEEEDEHLERTLEQNKGKMAKKEEKCVLQ
Protein: Actin-related protein 2/3 complex subunit 5-B (Actin-related protein 2/3 complex subunit 5-like) (Q6DE18)
Organism: Xenopus laevis (African clawed frog)
Function: Component of the Arp2/3 complex, a multiprotein complex that mediates actin polymerization upon stimulation by nucleation-promoting factor (NPF) (By similarity). The Arp2/3 complex mediates the formation of branched actin networks in the cytoplasm, providing the force for cell motility (By similarity). In addition to its role in the cytoplasmic cytoskeleton, the Arp2/3 complex also promotes actin polymerization in the nucleus, thereby regulating gene transcription and repair of damaged DNA (Probable). The Arp2/3 complex promotes homologous recombination (HR) repair in response to DNA damage by promoting nuclear actin polymerization, leading to drive motility of double-strand breaks (DSBs) (By similarity).
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:Q68FI4}. Cell projection {ECO:0000250|UniProtKB:Q68FI4}. Nucleus {ECO:0000269|PubMed:29925947}.
Interaction partners:
- Actin-related protein 2/3 complex subunit 4
- Actin-related protein 3-A
- Actin-related protein 2/3 complex subunit 3-A
- Actin-related protein 2/3 complex subunit 2-B
- Actin-related protein 3-B
- Actin-related protein 2/3 complex subunit 1A-A
- Actin-related protein 2/3 complex subunit 2-A
- Actin-related protein 2/3 complex subunit 3-B
- Actin-related protein 2/3 complex subunit 1A-B
- Actin-related protein 2/3 complex subunit 1B-A
Sequence:
MAKNTLSSRFRKVDIDEYDENKFVDDQLQEEPAEPQGPDEAEVDSLIRQGELLRAFQSALRNSPVNSKNQVAKERTQAIVLKVLTSFKSNEIEKAVNTLDPNGIDLLMKYIYKGFEKPTENSSAILLQWHEKAFVIGGLGSIVRVLTSRKTV
Protein: Transaminase A (Q964F0)
Organism: Trypanosoma brucei
Interaction partners:
Sequence:
MGKPDPILGLGQDFRMDPAKRKVNLSIGVYRDDADQPFVLECVKQATLGTNMDYAPVTGIASFVEEAQKLCFGPTCAALRDGRIASCQTLGGTGALRIGGDLLNRFVANCNRIYGPDVGYPNHESIFAKAGMELTPYSYYDPATKGLNLAGMLECLDKAPEGSVILVHACAHNPTGVDPTHDDWRQVCDVIKRRNHIPFVDMAYQGFATGQLDYDAFVPRHLVDMVPNLIVAQSFSKNFGLYGHRCGALHLSTASAEEAKRLVSQLALLIRPMYSNPPLYGAWVVSSILKDPQLTALWKKELKQMSSRIAEVRKRLVSELKACGSVHDWSHIERQVGMMAYTGLTREQVELLRSEYHIYMTLNGRAAVSGLNSTNVEYVSQAIHNVTK
Protein: Cilia- and flagella-associated protein 44 (A8J1V4)
Organism: Chlamydomonas reinhardtii (Chlamydomonas smithii)
Function: Flagellar protein involved in sperm flagellum axoneme organization and function.
Subcellular location: Cell projection, cilium, flagellum {ECO:0000269|PubMed:15998802}. Cytoplasm, cytoskeleton, flagellum axoneme {ECO:0000250|UniProtKB:Q57WH1}.
Interaction partners:
Sequence:
MPLMVLLLSQRTGGVAQLLSVHGLDTHRRNNLVLLDEDTAASCIAGQLVLLSLSTGARRYLPGRDGGGVGAVAVHPSRTLLAVGEKARPGPASAGPAVYIYSYPGLEVVKVLRGGTERAYSALAFDGERGDTLASVGHFPDFLLTLWDWRQEAIVLRAKAFSQDVYGVAFSPYFEGQLTTSGQGHIRFWRMASTFTGLKLQGAIGKFGNVELSDVAAFVELPDGKVLSSTETGELLLWDGGLIKVVLTRPGSRPCHDGPIEALLLDRPAGRVLSAGADGRVRMWDFGAVNDAEPREDSHSLELSPLDEVVVAEGAALSALLADSGGRRWVVADKAGNVYTVALPPAGPVGKGAVVTRVASHPAGAVAGLQLSARTHTALVASADGCLRALDYVSGAVLAEAATPQRITAFTPLPAASPACPGGAMTAATGYRDGVVRLHARCAEGLALVGVAKAHKGAVAALAVSADGGRLVSAGEDGSVFFFDLTAQPQPGTGVPGMPACGLLAPRAFIKLPSGSGTVTCGVWEAAEGGGVLLGTNRGTILSVPLPPPDLNTHHSYEWAAGTSAVSSYQLVVPKPKRPKKKKGKNDGEEGDKEGGEQDEGQGGEDKGGEQADGEGGSKEGGEEGRAAEEEEEEEADDEADGGAGGPSSTTGELISLTLAPNEPGALLVTAGGVGHAARKAWRVRMGEPLAAPLLEGFASAPVTCLAHAGPEGRLALLGSGDGLVRLQALEEPFGSAAPGALPLWEAPLHDMQSGRVSGLGLSHDGAYLVTAAADGALHLLALALPPELAPPPTTQPGDEPLPGPAALPLRPPDVLAAAAYTLEEEKQQAERDQQVREAEEKKLSVRQRLGLIRAEFEALLAENEAAPEALRLPRADLEVDPGLRALMEAEALRREEVARLELAWESERQRLGLAKLRRYFLDGLESERVVLHSLRGSSTVTTFRVAKLSDETRAELAAMRQAARAAAAASAAAGGEGGAGGRDTDARGKGSDTGGGPGGDAAARARLAEATAALEEGTASGKLNKADLRRLARKRREAEWAAFNGTRPDDTYDSPADLAAIEEARRTIGDFKLKSDPNYVVPEEERLTPQRKRLAMLELEEALHDIAAAFNAKFFALRDVKRKVLADVRVKLAALAELAAAAGAATGGADPDATAAAYLAPFSGLPSGLLPEEEPAEAREAVTDADLAAFAARKAEDERKAAAAAAGGLGGFAGAAAGPKKPAAGGAAPAGGALAGGAAGSGSVAHGAGGPSAGGQQGLTAAEEALAKMMAAVPQSELEKGLAAYNRRRVEHMRSKLSEEITAMLDAFDDAHSALKAEKLGLEADVKAGQMRLLVGLQELQLLREFDKRESVLLAKRQAKLDDKQEIVDKIAECTDKLETKRLELEGLVARRAAVVAELDAVVPESDPFREALVRVFHRRIKRSKKKAGGGGGEDDYDSEEDEEDEDMGDDEVDDDDDGGEEVCPPGCDQSVYERVCDLREKRLDEEDMIAEFTKTIEVLRKEKEALAKKQRLVEQGLAAVNADMAEFQKEKQGRLNQVEVIVALRMHQIEYLLDGCLPDDLSACLVFSASQLRRLQARVDELEEEKAGLRAAHKELRRQHAALLRDKADKEARVAELEARAHDVQMLKFGQVIDLELLDRVSSSRGTEELREDLKKQELAYARELAEWDAKINARMDELVVLTRENTACLNAVSELTAAQRRLESGLTATRKGLFADPVQQRRAEVEERDALVALVNAQAAELDRLKGQLLALRRKDTSMYA
Protein: Glutathione S-transferase P 2 (Gst P2) (EC 2.5.1.18) (GST YF-YF) (GST class-pi) (GST-piA) (P46425)
Organism: Mus musculus (Mouse)
Function: Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles. Cannot metabolize 1-chloro-2,4-dinitrobenzene.
Interaction partners:
- Glutathione S-transferase P 1
- Glutathione S-transferase
- Glutathione S-transferase omega-1
- Peroxiredoxin-6
- Glutathione S-transferase theta-2
- Peroxiredoxin-6
- Glutathione S-transferase omega-2
- TNF receptor-associated factor 2
- Glutathione S-transferase theta-1
- Microsomal glutathione S-transferase 1
Sequence:
MPPYTIVYFPSPGRCEAMRMLLADQGQSWKEEVVTIDTWMQGLLKPTCLYGQLPKFEDGDLTLYQSNAILRHLGRSLGLYGKNQREAAQVDMVNDGVEDLRGKYGTMIYRNYENGKNDYVKALPGHLKPFETLLSQNQGGKAFIVGDQISFADYNLLDLLLIHQVLAPGCLDNFPLLSAYVARLSARPKIKAFLSSPEHVNRPINGNGKQ
Protein: Ichor (Q9VHJ6)
Organism: Drosophila melanogaster (Fruit fly)
Function: Transcriptional activator. In tracheal terminal cells, regulates the transcription of factors involved in the formation of a mature apical extracellular matrix (aECM) which is essential for the integrity and shape of seamless tubes.
Subcellular location: Nucleus {ECO:0000269|PubMed:29309404}.
Interaction partners:
- LD41978p
- Serine protease filzig
Sequence:
MKFCSMNGPSESEVESLLMSPCWGPPQTSAQDQYLLDGHKLLLEHDLDSLPSDADQKNSLDVLDNLLLNGSSLNALSDLKPLPPFTGYTGHLSINGISGHHYHAIAQRLPDESNNNYMQSAYHPQNQSNPTSTTQSNGGSNSNSNNSNEHNIVSSSTCLPESVLSGSGGGGGGNDACLADVKLFADSQLDSKLYSVADSCVMNGSGSGSAANGNGSGPSIATLTPIDQVADSLHNSGVRIYKDLTEYVDMNSIDDIAAIIGSAIADTTVPNQLDKDDNNDTRDSWMDLDAWIDGNCIQQESAKVLVSQQDSLGDFILPHSPLPMHASSSTLQSLLSHGYMPLLQNRLQNGPPNGNSSGGGGGANQGAGIKGDPQAPTSTSYCNELAAATSSSCSPPGSVVSTTDNPNGLMINPRYLSNPTNNQATGNLHQQGGYSMQASGLSLKDNGLCSPDLLGNYPHTTTASTTGSEMRTGAPKAKRSRSQKKSNQQQQQQQQQQQQQGDGGGQPTTPQMSAISPSGFSASDLSGLLGKEKPVHRCSICNRGFLNKSNIKVHLRTHTGEKPFRCDVCAKAFRQKAHLLKHQQIHKRIGRD
Protein: Azurocidin (Cationic antimicrobial protein CAP37) (Heparin-binding protein) (HBP) (hHBP) (P20160)
Organism: Homo sapiens (Human)
Function: This is a neutrophil granule-derived antibacterial and monocyte- and fibroblast-specific chemotactic glycoprotein. Binds heparin. The cytotoxic action is limited to many species of Gram-negative bacteria; this specificity may be explained by a strong affinity of the very basic N-terminal half for the negatively charged lipopolysaccharides that are unique to the Gram-negative bacterial outer envelope. It may play a role in mediating recruitment of monocytes in the second wave of inflammation. Has antibacterial activity against the Gram-negative bacterium P.aeruginosa, this activity is inhibited by LPS from P.aeruginosa. Acting alone, it does not have antimicrobial activity against the Gram-negative bacteria A.actinomycetemcomitans ATCC 29532, A.actinomycetemcomitans NCTC 9709, A.actinomycetemcomitans FDC-Y4, H.aphrophilus ATCC 13252, E.corrodens ATCC 23834, C.sputigena ATCC 33123, Capnocytophaga sp ATCC 33124, Capnocytophaga sp ATCC 27872 or E.coli ML-35. Has antibacterial activity against C.sputigena ATCC 33123 when acting synergistically with either elastase or cathepsin G.
Subcellular location: Cytoplasmic granule membrane {ECO:0000269|PubMed:2312733, ECO:0000269|PubMed:2501794}; Peripheral membrane protein {ECO:0000269|PubMed:2312733}; Cytoplasmic side {ECO:0000269|PubMed:2312733}. Note=Localizes to azurophil granules of neutrophil granulocytes. Also called primary granules, these specialized lysosomes of the neutrophil formed early during promyelocyte development store antibacterial proteins and peptides. {ECO:0000269|PubMed:2312733, ECO:0000269|PubMed:2501794}.
Interaction partners:
- Myeloblastin
- Neutrophil elastase
- Myeloperoxidase
- Cathepsin G
- Bactericidal permeability-increasing protein
- Eosinophil cationic protein
- Defensin alpha 4
- Cell adhesion molecule CEACAM8
- Lactotransferrin
- Pleiotrophin
Sequence:
MTRLTVLALLAGLLASSRAGSSPLLDIVGGRKARPRQFPFLASIQNQGRHFCGGALIHARFVMTAASCFQSQNPGVSTVVLGAYDLRRRERQSRQTFSISSMSENGYDPQQNLNDLMLLQLDREANLTSSVTILPLPLQNATVEAGTRCQVAGWGSQRSGGRLSRFPRFVNVTVTPEDQCRPNNVCTGVLTRRGGICNGDGGTPLVCEGLAHGVASFSLGPCGRGPDFFTRVALFRDWIDGVLNNPGPGPA
Protein: E3 ubiquitin-protein ligase ATL59 (EC 2.3.2.27) (RING-H2 finger protein ATL59) (RING-type E3 ubiquitin transferase ATL59) (Q9SN27)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: E3 ubiquitin-protein ligase able to catalyze polyubiquitination with ubiquitin-conjugating enzyme E2 UBC8, UBC10, UBC11, and UBC34 in vitro.
Subcellular location: Membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}.
Interaction partners:
- GLABROUS1 enhancer-binding protein-like 1
- F-box/kelch-repeat protein At1g67480
Sequence:
MSFIDPRTYIPSNSTESQILKFTFIVCVPICVILIVLLVLYIMRRNSNTNVDWSSLGGFVPTNNNLSTAELGLSKDIREMLPIVIYKESFTVNDTQCSVCLGDYQAEEKLQQMPSCGHTFHMECIDLWLTSHTTCPLCRLSLIPKPSVDLSHQSIEIVSSIENTNGGEASTQPDSQSATEAIIHIDDVEEGNRDSIEVVKESEENDRNSVGTSDGCCSCRLGEKA