wanglab/gogpt-training-data huggingface dataset:
Protein: Guanylate-binding protein 6 (EC 3.6.5.-) (GTP-binding protein 6) (GBP-6) (Guanine nucleotide-binding protein 6) (Q6ZN66)
Organism: Homo sapiens (Human)
Function: Hydrolyzes GTP to GMP in 2 consecutive cleavage reactions (By similarity). Confers protection to several pathogens, including the bacterial pathogens Listeria monocytogenes and Mycobacterium bovis BCG as well as the protozoan pathogen Toxoplasma gondii (By similarity).
Subcellular location: Cytoplasmic vesicle {ECO:0000250|UniProtKB:A0A0G2JDV3}.
Interaction partners:
Sequence:
MESGPKMLAPVCLVENNNEQLLVNQQAIQILEKISQPVVVVAIVGLYRTGKSYLMNHLAGQNHGFPLGSTVQSETKGIWMWCVPHPSKPNHTLVLLDTEGLGDVEKGDPKNDSWIFALAVLLCSTFVYNSMSTINHQALEQLHYVTELTELIKAKSSPRPDGVEDSTEFVSFFPDFLWTVRDFTLELKLNGHPITEDEYLENALKLIQGNNPRVQTSNFPRECIRRFFPKRKCFVFDRPTNDKDLLANIEKVSEKQLDPKFQEQTNIFCSYIFTHARTKTLREGITVTGNRLGTLAVTYVEAINSGAVPCLENAVITLAQRENSAAVQRAADYYSQQMAQRVKLPTDTLQELLDMHAACEREAIAIFMEHSFKDENQEFQKKFMETTMNKKGDFLLQNEESSVQYCQAKLNELSKGLMESISAGSFSVPGGHKLYMETKERIEQDYWQVPRKGVKAKEVFQRFLESQMVIEESILQSDKALTDREKAVAVDRAKKEAAEKEQELLKQKLQEQQQQMEAQDKSRKENIAQLKEKLQMEREHLLREQIMMLEHTQKVQNDWLHEGFKKKYEEMNAEISQFKRMIDTTKNDDTPWIARTLDNLADELTAILSAPAKLIGHGVKGVSSLFKKHKLPF
Protein: UDP glucuronosyltransferase 5 family, polypeptide B1 precursor (UDP glucuronosyltransferase 5 family, polypeptide B2) (F1QNF8)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
- Aldehyde oxidase 6
- Xanthine dehydrogenase/oxidase
- Aromatase
- Cytochrome P450, family 3, subfamily A, polypeptide 65
Sequence:
MIGQIFQPCGQILIALLLVTVPTAQSEKVLVFPVDGSHWVNMNILVEALHAKGHNITVIRMADSWYIKEFSPHYTSINLKSAGGFDEEFFETFAFRLMKIVREGSRWGRLKLEIETWQSTYEMIEIESEMIKNMLEDQPLMQTFRDAKYDLLLTDPLLFGGVILGHFLKLPIVYNVRWTMYNEAHFVSAPSPLSYVPFMMVELSDRMSFFQRVKNVVMFTVAEAQAALLFAPYYNALCEQFIGPGVSFLSLVQGADLWLHRVDFIFEYPRPTMPNIIYMAGFQCKPSKPLPQDLEDFVQSSGDHGVIIMSLGTLVGQLPDDVAEAIAEAFAELPQKIIWRYKGKRPSALGNNTLVMDWMPQNDLLGHPKTRAFVAHGGTNGVQEAIYHGVPIIGFGLIFDQPDNLEKMRVRGAANNVDFATMDKESFLKTVKEVLYDPSYRENMQRLSRLHKDVPVKPLDNAIFWIEFVMRHKGAAHLRTESYKMPWYSYHSVDVILVLISAVSLIILTIYAVIRYFCCRICMRTTKVKLQ
Protein: Protein S100-A12 (Calcium-binding protein in amniotic fluid 1) (CAAF1) (Calgranulin-C) (CAGC) (Cornea-associated antigen) (CO-AG) (Extracellular newly identified RAGE-binding protein) (EN-RAGE) (RAGE-binding protein) (S100 calcium-binding protein A12) (P79105)
Organism: Bos taurus (Bovine)
Function: S100A12 is a calcium-, zinc- and copper-binding protein which plays a prominent role in the regulation of inflammatory processes and immune response. Its pro-inflammatory activity involves recruitment of leukocytes, promotion of cytokine and chemokine production, and regulation of leukocyte adhesion and migration. Acts as an alarmin or a danger associated molecular pattern (DAMP) molecule and stimulates innate immune cells via binding to receptor for advanced glycation endproducts (AGER). Binding to AGER activates the MAP-kinase and NF-kappa-B signaling pathways leading to production of pro-inflammatory cytokines and up-regulation of cell adhesion molecules ICAM1 and VCAM1. Acts as a monocyte and mast cell chemoattractant. Can stimulate mast cell degranulation and activation which generates chemokines, histamine and cytokines inducing further leukocyte recruitment to the sites of inflammation. Can inhibit the activity of matrix metalloproteinases; MMP2, MMP3 and MMP9 by chelating Zn(2+) from their active sites (By similarity).
Subcellular location: Secreted {ECO:0000250}. Cytoplasm {ECO:0000250}. Cytoplasm, cytoskeleton {ECO:0000250}. Cell membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Note=Predominantly localized in the cytoplasm. Upon elevation of the intracellular calcium level, translocated from the cytoplasm to the cytoskeleton and the cell membrane. Upon neutrophil activation is secreted via a microtubule-mediated, alternative pathway (By similarity). {ECO:0000250}.
Interaction partners:
- Protein S100-A8
- Protein S100-A9
- Advanced glycosylation end product-specific receptor
- Natural resistance-associated macrophage protein 1
- High mobility group protein B1
- Interleukin-8
- Toll-like receptor 4
- Protein S100-A7
- Cathelicidin-3
- Protein S100
Sequence:
MTKLEDHLEGIINIFHQYSVRVGHFDTLNKRELKQLITKELPKTLQNTKDQPTIDKIFQDLDADKDGAVSFEEFVVLVSRVLKTAHIDIHKE
Protein: DNA (cytosine-5-)-methyltransferase (EC 2.1.1.37) (A0A0G2JYR2)
Organism: Rattus norvegicus (Rat)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MKGDSRHLNEEEGASGYEDCIIVNGNCSDQSSDTKDAPSPPVLEAICTEPVCTPETRGRRSSSRLSKREVSSLLNYTQDVVGDGDGEADDGDGSDILMMPKLTRETKDARTPSESPAVRTRNSNSISSLERQRTSPRITRGRQGRYHVQEYPVEFPATKSRRRRASSSASTPWSSPASIELMEDVTPKSSSTPSVDLSQDGPQEGMDATQVDAESRDGDSTEYQDDKEFGIGDLVWGKIKGFSWWPAMVVSWKATSKRQAMPGMRWVQWFGDGKFSEIAADKLVALGLFSQHFNLATFNKLVSYRKAMYHTLEKAMVRAGKTFPSRPGDSLEDQLKPMLEWAHGGFKPTGIEGLKPNNKQPEVHKSKVRRSGSRNLEARRRENKSRRRTTIDFAASEYSTPPKRLKTNSYGGKDRGEDEESRERMASDVTNNKGNLEDRCLSCGKKNPVSFHPLFEGGLCQSCRDRFLELFYMYDEDGYQSYCTVCCEGRELLLCSNTSCCRCFCVECLEVLVGTGTAEDAKLQEPWSCYMCLPQRCHGVLRRRKDWNMRLQDFFTTDPDLEEFEPPKLYPAIPAAKRRPIRVLSLFDGIATGYLVLKDLGIKVEKYVASEVCAESIAVGTIKHEGQIKYVNDVRKITKKNIEEWGPFDLVIGGSPCNDLSNVNPARKGLYEGTGRLFFEFYHLLNYTRPKEGDNRPFFWMFENVVAMKVNDKKDISRFLACNPVMIDAIKVSAAHRARYFWGNLPGMNRIFGFPAHYTDVSNMGRGARQKLLGRSWSVPVIRHLFAPLKDYFACE
Protein: tRNA ligase (EC 6.5.1.3) (P43075)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Function: One of the two proteins required for the splicing of precursor tRNA molecules containing introns. The ligation activity requires three enzymatic activities: phosphorylation of the 5' terminus of the 3' half-tRNA in the presence of ATP, opening of the 2'3'-cyclic phosphodiester bond of the 5' half-tRNA leaving a 2'-phosphomonoester and ligation of the two tRNA halves in an ATP-dependent reaction.
Interaction partners:
- 2'-phosphotransferase
- 2',3'-cyclic-nucleotide 3'-phosphodiesterase
- non-specific serine/threonine protein kinase
- Ulp1p
Sequence:
MKDSQSDIIELCNKLNEATKLKRNGKSIKLTNFVSNTQIKLDSWKFLEWDYGKPSVQLPIQARGLFTLNNDTIAVRGYDKFFNVEEKPFTKETNLKTSTHGPYEVTLKENGCIIFISGLSTGDIVVCSKHSTGDRIDDNESDKTTTATATATAPTRNHAKQGEFELLQQFDGDQQKVKQLAHYLYENNLTVVAELCDDEFEEHVLPYPKDKSGLYVHGLNYNTITFKTLPMDQVLQFAKEWGFKYVSYLTYDNADELFKFLHKCSETGTYNGREIEGFVIRCHRQSHTNGDTDGDCFFFKYKFEQPYLLYRQFREVTKQLLNGTPINSIKIKKNKPITKKYLQFVEKLFEQEPEIARNFENGFDIIKVRQLFLQSLNETNGMNLLSIDSELSDQLKNLALANGNEGLSTTTKYIFVPIATIGCGKTTVFNTLNNLFPQWTHIQNDNISKKAKLKICDLTLLALEDDDQSVVLFDRNNSASRERRQIFTTIDQKRDEHLDDTVDLKYIAINFIPEDLSEEELWDITYNRVIQRGDNHQSIKSQSDENLVESVMKGFIQRYQPINTSRSPDDQFDHVIHLKLSKDENSSKSSLENVRIIIDDLVQNFPDLIKEKPADELINECFQKALDYKPTFVKNMTANTIKKDPTYYGIAMHYSSILENLEIVSHNEHFQNIKSHIQTEFHVTLGHIASSKQDKAGRVKWKKLVKTLGKGDPNKPKSALKFFADVKLLQIVINTDKLACIKVEILKIYDTNDVLQSEIEPINKQLHITIGCIPPATAVESNITLEELYDNPDEQELKPDGTYKCGDDTLHVFNFDNPDLKLFSQQLFVAYQ
Protein: Zinc finger and BTB domain containing 34 (A0A0C4DFQ2)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MSVEMDSSSFIQFDVPEYSSTVLSQLNELRLQGKLCDIIVHIQGQPFRAHKAVLAASSPYFRDHSALSTMSGLSISVIKNPNVFEQLLSFCYTGRMSLQLKDVVSFLTAASFLQMQCVIDKCTQILESIHSKISVGDVDSVTVGAEENPESRNGVKDSSFFANPVEISPPYCSQGRQPTASSDLRMETTPSKALRSRLQEEGHSDRGSSGSVSEYEIQIEGDHEQGDLLVRESQITEVKVKMEKSDRPSCSDSSSLGDDGYHTEMVDGEQVVAVNVGSYGSVLQHAYSYSQAASQPTNVSEAFGSLSNSSPSRSMLSCFRGGRARQKRALSVHLHSDLQGLVQGSDSEAMMNNPGYESSPRERSARGHWYPYNERLICIYCGKSFNQKGSLDRHMRLHMGITPFVCKFCGKKYTRKDQLEYHIRGHTDDKPFRCEICGKCFPFQGTLNQHLRKNHPGVAEVRSRIESPERTDVYVEQKLENDASASEMGLDSRMEIHTVSDAPD
Protein: Dual specificity protein phosphatase CDC14A (EC 3.1.3.16) (EC 3.1.3.48) (CDC14 cell division cycle 14 homolog A) (Q6GQT0)
Organism: Mus musculus (Mouse)
Function: Dual-specificity phosphatase. Required for centrosome separation and productive cytokinesis during cell division. Dephosphorylates SIRT2 around early anaphase. May dephosphorylate the APC subunit FZR1/CDH1, thereby promoting APC-FZR1 dependent degradation of mitotic cyclins and subsequent exit from mitosis (By similarity). Required for normal hearing.
Subcellular location: Nucleus {ECO:0000250|UniProtKB:Q9UNH5}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250|UniProtKB:Q9UNH5}. Cytoplasm, cytoskeleton, spindle {ECO:0000250|UniProtKB:Q9UNH5}. Cell projection, kinocilium {ECO:0000269|PubMed:27259055, ECO:0000269|PubMed:29293958}. Cytoplasm, cytoskeleton, spindle pole {ECO:0000250|UniProtKB:Q9UNH5}. Cell projection, stereocilium {ECO:0000269|PubMed:29293958}. Note=Centrosomal during interphase, released into the cytoplasm at the onset of mitosis. Subsequently localizes to the mitotic spindle pole and at the central spindle (By similarity). Present along both the transient kinocilia of developing cochlear hair cells and the persistent kinocilia of vestibular hair cells (PubMed:27259055). {ECO:0000250|UniProtKB:Q9UNH5, ECO:0000269|PubMed:27259055}.
Interaction partners:
- NAD-dependent protein deacetylase sirtuin-1
- Fizzy-related protein homolog
- Dual specificity protein phosphatase CDC14B
- Separin
- Cell division cycle protein 23 homolog
- Cell division cycle protein 16 homolog
- Cell division cycle protein 27 homolog
- Serine/threonine-protein kinase PLK1
- Mitogen-activated protein kinase 6
- Cyclin-dependent kinase 1
Sequence:
MAAESGELIGACEFMKDRLYFATLRNRPKSTINIHYFSIDEELVYENFYADFGPLNLAMVYRYCCKLNKKLKSYSLSRKKIVHYTSFDQRKRANAAFLIGAYAVIYLKKTPEEAYRALLSGSNPPYLPFRDASFGNCTYNLTVLDCLQGIRKGLQHGFFDFETFDAEEYEHYERVENGDFNWIVPGKFLAFSGPHPKSKIENGYPLHAPEAYFPYFKKNNVTTIVRLNKKIYEAKRFTDAGFEHYDLFFIDGSTPSDNIVRRFLNICENTEGAIAVHCKAGLGRTGTLIACYVMKHYRFTHAEIIAWIRICRPGSIIGPQQHFLKEKQASLWVQGDIFRSKLKNRPSSEGSITKIISTLDDMSIGANLSKLQSTERIGENNFEDEDMEIKNNVTQGDKLRALKSQRHPRSSPSCAFRSDDMKGHQRAMAQTFRLSSSPQPTMSTMKTSKVCLSPSVTAKKISRGSLSSGANIRSFSINSRLASSLGNLNAGTEEPETKKTTSLTKAAFIASPFTSFLNGSTQTPGRNYPELNNNQYTRSSNSNSSSSSSGLGGNLNSSPVPQSAKPEEHTTILRPSFPGSLSSSSVRFLSRSIPSLQSEYVHY
Protein: Glucuronan lyase A (Q5BHH6)
Organism: Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Interaction partners:
Sequence:
MFSRLLSTTVLVALALTSQAAQTFSNTGTIAGWDSTNQEHRGTVQEVSNVAFEGSQALKVTQVYDSSYSGRYHSELVHNAGYRRGETVFYGFAFRLQQDWDFTSQSYNLAQFIADFNDSGCDDWMPSTMIWLQGNQLYSRVKTGTVCAQQTQTFANLASVSAGEWHKIVLQVKWESDSTGFFKVWFDGEKVKEVYDIKTTIAHDRQFHFRVGLYANAWHDQGRLEGSQGTRQVWYDEIGIGSAFADADPSQW
Protein: Protein orai-2 (Transmembrane protein 142B) (Q8BH10)
Organism: Mus musculus (Mouse)
Function: Ca(2+) release-activated Ca(2+)-like (CRAC-like) channel subunit which mediates Ca(2+) influx and increase in Ca(2+)-selective current by synergy with the Ca(2+) sensor, STIM1.
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:Q96SN7}; Multi-pass membrane protein {ECO:0000255}. Note=Colocalizes with STIM1 upon store depletion. {ECO:0000250|UniProtKB:Q96SN7}.
Interaction partners:
- Stromal interaction molecule 1
- Stromal interaction molecule 2
- Protein orai-3
- Calcium release-activated calcium channel protein 1
- Short transient receptor potential channel 6
- Short transient receptor potential channel 1
- Pyridine nucleotide-disulfide oxidoreductase domain-containing protein 1
- Short transient receptor potential channel 3
- Short transient receptor potential channel 4
Sequence:
MSAELNVPMDPSAPACPEPGHKGMDYRDWVRRSYLELVTSNHHSVQALSWRKLYLSRAKLKASSRTSALLSGFAMVAMVEVQLETKYQYPQPLLIAFSACTTVLVAVHLFALLISTCILPNVEAVSNIHNLNSISESPHERMHPYIELAWGFSTVLGILLFLAEVVLLCWIKFLPVDAKDQPGSHSHTGWQAALVSTIIMVPVGLIFVVFTIHFYRSLVRHKTERHNREIEELHKLKVQLDGHERSLQVV
Protein: RTX toxin-activating lysine-acyltransferase (EC 2.3.1.-) (A3N293)
Organism: Actinobacillus pleuropneumoniae serotype 5b (strain L20)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496, ECO:0000256|RuleBase:RU368102}.
Interaction partners:
- APX-IA
- Membrane fusion protein
- Toxin RTX-I translocation ATP-binding protein
- RTX-II toxin determinant A
- Transferrin-binding protein 1 Tbp1
- Predicted TonB dependent/Ligand-Gated channel
- Transferrin-binding protein A
- Leukotoxin translocation ATP-binding protein LktB
- Surface lipoprotein assembly modifier C-terminal beta-barrel domain-containing protein
Sequence:
MSKKINGFEVLGEVAWLWASSPLHRKWPLSLLAINVLPAIESNQYVLLKRDGFPIAFCSWANLNLENEIKYLDDVASLVADDWTSGDRRWFIDWIAPFGDSAALYKHMRDNFPNELFRAIRVDPDSRVGKISEFHGGKIDKKLASKIFQQYHFELMSELKNKQNFKFSLVNS
Protein: T-box transcription factor 5b (T-box transcription factor TBX5b) (Tbx5b transcription factor) (E3W6T6)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}. Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|PROSITE-ProRule:PRU00201}.
Interaction partners:
Sequence:
MANPMFESLRACSGGNSPAMDFERDKDSGHHGRNKTGSPPLQTQLSQQSMEGIKVYLHEKDLWAKFHDVTTEMIITKAGRRMFPSYKVKVTGLNPKAKYILLMDIISADEHRYKFADNKWSISGKAEPAIPGRLYVHPDSPASGAHWMRQLVSFQKLKLTNNHLDPFGHIILNSMHKYQPRLHIVKADERNSFGSSNTSFCTHSFAETTFIAVTSYQNHTITQLKIENNPFAKGFRGNDDIELHRMSRTPSKEYPLVPRSTARQRAAPPSPDCLSRSEYTVTQKPSPGFTCSDTSGDQSLTETPSIHDPTYPLFSYQLSPDVAPSSMDTTQHQPCMYGGSQVGMEELRWASYSDSTTYQSFSSAKEMSGTFVPPADLSQELYPQYTCEVGVQSHCMMTDFSLYACNRSFSQNQQPNNWCGGS
Protein: Dihydrolipoamide acetyltransferase component of pyruvate dehydrogenase complex (EC 2.3.1.-) (Q57Z16)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- 3-methyl-2-oxobutanoate dehydrogenase
- 2-oxoisovalerate dehydrogenase subunit alpha
- Dihydrolipoamide dehydrogenase, putative
- Dihydrolipoyl dehydrogenase
- Dihydrolipoamide dehydrogenase, point mutation
- Dihydrolipoamide dehydrogenase, putative
- Isovaleryl-coA dehydrogenase, putative
- Pyruvate dehydrogenase E1 component subunit beta
- oxoglutarate dehydrogenase
- 2-oxoglutarate dehydrogenase subunit, putative
Sequence:
MRSFMYMCRQVQGARFIQITRSRCGRTIPYKLADIGEGIKEVEVVTLYVKPGDRIGEFEKICEVQSDKATVEITSRYAGVITTVHIEAGEKAHVGEPIVDIEVNDTDETQKPSCGTVDCNVSDQFNNGGVPVAEEGDSCAADCTTEISKDFTKVLATPAVREFARSRGVNITDVKGTGKDGRVLREDVLSYAGKSCYNDDVVVRLDTGLRKAMVSSMTKAGSVPSFTACDEVEVSQLLNFQHILRDALNSSSEGVRDGSKVSLMPLFIKAASQSLLQYPELNAHVSSECDKLFVKKAHHIGFAMDTPKGLVVPVVRDVQQKSVAELVHEVNELVTLGRKSQIPPDRMKDGTFTLSNIGPIGAIYATPMLNPPQVAIGAIGRIQQLPRFDASGNVVRANILAMSWTADHRVIDGATLVRFSNAFKRCLESPGLLIAGEVA
Protein: Adenosine deaminase RNA specific (F1MUM9)
Organism: Bos taurus (Bovine)
Interaction partners:
- Adenosine deaminase
- NFX1-type zinc finger-containing protein 1
- Tetratricopeptide repeat and ankyrin repeat containing 1
- ATP-dependent RNA helicase A
- Interferon-induced GTP-binding protein Mx1
Sequence:
MDPRQGYSLNRYQARPAQGYEHSRHRHQQPERGPCRDSFQLQQIEFLKGQLPEVPLFGKQPPSLPPFLPGLWPRFPGPPARGGPLQIRGVPRGVPLRSQVLPRRFQRPFPRGHIRPWRGVDRLSSHFQGLTISQDQEQRTLELLDELGDGKATTARDLARKLQAPKKDINRVLYSLAEKGKLHQEAGSPPLWRATVPVQAQNQPSQETRAESQTPGAPSPDSSVETEGRSTPCGLEEPPEPLDMAEIKEKICDHLFNVSSSSALNLAKNIGLTKARDVNAVLIDLERQGDVYRQGTTPPIWYLTDKKRERIQIKRNKDSVPETTQAAAVLETGKTTEGPTCNSPASDASNSTVTPGKVENGQEPVVKLKLKQEATAEPVKLKPPVYDNGPSKTGYVDFENGQWATDDIPDDLNSIHAAPGEFRAIMEMPSFYSHGLPRCSPYKKLTECQLKNPISGLLEYAQFASQTCEFNMIEQSGPPHEPRFKFQVVINGREFPPAEAGSKKVAKQDAAMKAMTILLEEAKAKDSGRSEESYHYSSEKESEKTAESQTATPSATSFLSGKNPVTTLLECVHKLGSSCEFRLLSREGPAHDPKFQYCVAMGTHTFPTASAPSKKAAKQMAAEEAMKALQGEATSSTSSEDQPGSTNTEAFDNLESVMPNKVRRISELVRYLNTNPVGGLLEYARSHGFAAEFKLVDQSGPPHEPKFVYQAKVGGRWFPAVCAHSKKQGKQEAADAALRVLIGEDEKAERMGFTEVTPVTGASLRRTMLLLSRSPEAKRKTLPLTGSTFHDQIAMLSHRCFNALTNSFQPSLLGRKILAAIIMKKDSDDLGVVVSLGTGNRCVKGDSLSLKGETVNDCHAEIISRRGFIRFLYSELMKYNPQTAKDSIFEPAKGGEKLQIKKSVSFHLYISTAPCGDGALFDKSCSDRAVESTDSRHYPVFENPKQGKLRTKVENGEGTIPVESSDIVPTWDGIRLGERLRTMSCSDKILRWNVLGLQGALLTHFLQPVYLKSVTLGYLFSQGHLTRAICCRVTRDGSAFEDGLRHPFIVNHPKVGRVSVYDSKRQSGKTKETSVNWCLADGYDLEILDGTRGTVDGPRNELSRVSKKNIFLLFKKLCSFRYRRDLLRLSYGEAKKAARDYEIAKNYFKKSLKDMGYGNWISKPQEEKNFYLCPV
Protein: BCNT-C domain-containing protein (Q57YH0)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MSSSSSSTSTDVANSSGSDNGDDSVSTQSNRSSSSDSVSLISSTCSITDRIRETGGGCGDAVATERLEREQRLRRLLSQRKVGNTVPLHDGKIAEPFSMRKGTLDPDDGVILSTFSNALLFQRLLSVLSSSDALARSQSFDEVLAVANPIFFRKLKAPLGEGSTEASQPQHFRPVVHSECAQLDRSGIVVHRRKRERHGHWVAAGEKKSAMGDSSGVRTMSTSSGLIQKSHAQWERYLTKELQEEGVSLQSFRQQRQDDSYLEKQRFLERSQWAEYQHELQVDARRRELKASRAIRRGESEMN
Protein: Universal stress protein A-like protein (Q8LGG8)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Tetratricopeptide repeat protein SKI3
- Cold-regulated 413 inner membrane protein 2, chloroplastic
Sequence:
MGSEPTKVMVAVNASTIKDYPNPSISCKRAFEWTLEKIVRSNTSDFKILLLHVQVVDEDGFDDVDSIYASPEDFRDMRQSNKAKGLHLLEFFVNKCHEIGVGCEAWIKTGDPKDVICQEVKRVRPDFLVVGSRGLGRFQKVFVGTVSAFCVKHAECPVMTIKRNADETPSDPADD
Protein: AP-3 complex subunit beta (O45718)
Organism: Caenorhabditis elegans
Subcellular location: Cytoplasmic vesicle, clathrin-coated vesicle membrane {ECO:0000256|ARBA:ARBA00004145}; Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004145}; Cytoplasmic side {ECO:0000256|ARBA:ARBA00004145}. Golgi apparatus {ECO:0000256|ARBA:ARBA00004555}.
Interaction partners:
- AP-3 complex subunit delta
- AP-3 complex subunit mu
- AP complex mu/sigma subunit domain-containing protein
- AP-1 complex subunit gamma
- Transcription initiation factor TFIID subunit 5
- AP-2 complex subunit alpha
- AP-1 complex subunit mu-1-I
- Ras-related protein Rab
- Glycosyltransferase family 92 protein
- ABC-type antigen peptide transporter
Sequence:
MTSFVEGLTSPEMEIAEGGVILDNRTRFADLKAMLDSNKDNLKVDAMKRIINLIAKGKDVSELFAAVVKNVAAKNVELKKLVFVYLVRYAEEQQDLALLSISTFQRALKDPNQLIRGSALRVLTSIRVPMVAPIMLLAIKDAVRDMSPYVRKVAAHAIPKLYSLEPELEPQLVDCIDFLLADRRSLVLGSAVYAFDEICPHRLDLLHKHFRALCRGLADVDEWGQIVMINMLTRYARHELADPDRGPPDTDVVLLLNSARPLLQSRNCSVVMAVVQLFYHVAPKAQLSQIARALVRLLRGPRETQYVVLTNIATICERNPVEEGTYAISKTMFDPFLKSFFVRSCDSSLVKKLKLHVLTSLVSEANVHIILRELQTYVHMSDLASPAVEAIGRCAVRVGAVSDQCMTGLVQLISSSDEKVVCSAVVVIKRLLHASAPLNLLSRLMRLMPNMIAAQARACVIWLVATHVEQVLHMAPDFLRLIAKKFSTENELVKLEALKLAVKLWLVKRDDSEKIVQYVFQLARFDLSYDVRDRCRFLRNLMFNTEILSQHMEEIFMSKKPAPELISSFKERDKFQLGSLSHVLNQRCTKYIDLPEFPATSSDSLLRKEAHAPNELKLDDSDEEEDDDDEDEEEDEDEEEEDEDEEDEEEEENESEEEEEDDEDEESEEESDEEDEEEEEEDDSEPEEKPNPKPSTKKQALILNKSKPMNGKPKTERNDLDLLIDVDFSAAGSRQIMDATHIEEKEIELLNVIEGNGLILSISYPRINDGQYTAIRFGITNKTDGDLLGVELKTEEGLDVKGNSIIGDIPSGARVSVDLLVDFGDSATSREWILTRDDGHEKHFRFEVPYGEQVQPIRLSPEDISKERSRLGGLNRHVIQLENPINPSSIALFVNAFSSDLTIFTCQTRSRKDVCILTVSEKSIECCCDNSVIGRMLAFSVSKNC
Protein: 1-deoxy-D-xylulose 5-phosphate reductoisomerase (DXP reductoisomerase) (EC 1.1.1.267) (1-deoxyxylulose-5-phosphate reductoisomerase) (2-C-methyl-D-erythritol 4-phosphate synthase) (P9WNS1)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: Catalyzes the NADPH-dependent rearrangement and reduction of 1-deoxy-D-xylulose-5-phosphate (DXP) to 2-C-methyl-D-erythritol 4-phosphate (MEP).
Interaction partners:
- 2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase
- 1-deoxy-D-xylulose-5-phosphate synthase
- 4-hydroxy-3-methylbut-2-en-1-yl diphosphate synthase
- 1-deoxy-D-xylulose-5-phosphate synthase
- 2-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase
- 4-diphosphocytidyl-2-C-methyl-D-erythritol kinase
- 4-hydroxy-3-methylbut-2-enyl diphosphate reductase 1
- Zinc metalloprotease Rip1
- Decaprenyl diphosphate synthase
- 4-hydroxy-3-methylbut-2-enyl diphosphate reductase 2
Sequence:
MTNSTDGRADGRLRVVVLGSTGSIGTQALQVIADNPDRFEVVGLAAGGAHLDTLLRQRAQTGVTNIAVADEHAAQRVGDIPYHGSDAATRLVEQTEADVVLNALVGALGLRPTLAALKTGARLALANKESLVAGGSLVLRAARPGQIVPVDSEHSALAQCLRGGTPDEVAKLVLTASGGPFRGWSAADLEHVTPEQAGAHPTWSMGPMNTLNSASLVNKGLEVIETHLLFGIPYDRIDVVVHPQSIIHSMVTFIDGSTIAQASPPDMKLPISLALGWPRRVSGAAAACDFHTASSWEFEPLDTDVFPAVELARQAGVAGGCMTAVYNAANEEAAAAFLAGRIGFPAIVGIIADVLHAADQWAVEPATVDDVLDAQRWARERAQRAVSGMASVAIASTAKPGAAGRHASTLERS
Protein: Hyaluronan and proteoglycan link protein 1a (Q1LXE1)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
Sequence:
MIALFSVALMVFASSLHVEAQDSESRVKVYANRGDNITLPCRLDGQSTLFGNRIKWTKIEDDSTETDVLISMGFHKKAYGSYQDRAYLLEVDDSDATLVITDLDVNDYGTYRCEFIDGMNDMTLEVDLEVQGKDSLSFTGVVFPYSPRLGRYNLNFQNAVAACQEQDAVVASFEQLYGEWKSGLDWCNAGWLSDGTVQYPITKPREPCGGARATAGLRNYGQRDKSNSRYDVFCFTAGLKGRFYYMIQPKKLNFDEAVDACKGDGAEIAKVGHMFAAWKLQGYDRCDAGWLADGSVRYPISRPRKNCSPTEAAVRFVGFPDKKQKLYGVYCYKAQQ
Protein: Kinesin-like protein KIN-13B (AtKINESIN-13B) (AtKIN13B) (Q940Y8)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Acts redundantly with KIN13A to modulate cell wall synthesis and cell expansion via the THE1 pathway.
Interaction partners:
- Mitotic spindle checkpoint protein MAD2
- Protein SHI RELATED SEQUENCE 3
- Kinesin-like protein KIN-10A
- C-terminal binding protein AN
- Cyclin-T1-5
- Cyclin-dependent kinases regulatory subunit 2
- Kinesin-like protein KIN-5A
Sequence:
MSGRQRSVAAAVHHQRQLSDNPLDMSSSNGRWLQSTGLQHFQSSANDYGYYAGGQGGGGQAARGYQNAQRGNEFFGEPTTPQYGARPTNQRKNNDESEFSPGLLDLHSFDTELLPEIPVSNQLDGPSLFNPSQGQSFDDFEAYNKQPNRSRVLAENLAAEKERMNAVAKIKVVVRKRPLNKKESTKNEEDIVDTHANCLTVHETKLKVDLTAYVEKHEFVFDAVLDEEVSNDEVYRETVEPVVPLIFQRIKATCFAYGQTGSGKTYTMKPLPLKASRDILRLMHHTYRNQGFQLFVSFFEIYGGKLYDLLSERKKLCMREDGKQQVCIVGLQEYRVSDTDAIMELIERGSATRSTGTTGANEESSRSHAILQLAIKKSVEGNQSKPPRLVGKLSFIDLAGSERGADTTDNDKQTRLEGAEINKSLLALKECIRALDNDQGHIPFRGSKLTEVLRDSFMGNSRTVMISCISPSSGSCEHTLNTLRYADRVKSLSKGNASKKDVSSSTMNLRESTKIPLSSALPTPSNFDDDVNEMWTEENDEFDASDYEQDKQMWKKNGKLEPSYNGMAQERIPKPTIQMKSRDMPRPDMKKSNSDDNLNALLQEEEDLVNAHRKQVEDTMNIVKEEMNLLVEADQPGNQLDGYISRLNTILSQKAAGILQLQNRLAHFQKRLREHNVLVSTTGY
Protein: Rifin (Q8IBD9)
Organism: Plasmodium falciparum (isolate 3D7)
Interaction partners:
Sequence:
MKIHYINILLFELPLNILIYNQRNHNSTTHHTLKIPITRLLCECELYAPSNYDNDPEMKEVMEIFDRQTSERFHEYDERMKTTRQKCREQCDKEIEKIILKDKLEKELMDKFATLHTDMQSDAIPTCVCEKSVADKTEKVCLNCGKTMGAVAPAWGLISGLWYATWSQYVSAKILEVGISEGIKEGLTQIMKFTISLYPKANLPNITVTQMLSSGKFTNNVTLFDMVQHINNTMYTTLEAEEYSKFCGVVSSMAKYKNITFNRTYGKYSTAVTEAVTQGKTNAINTLTPATNTLTTAIIASMVAIVVIVLVMIIIYLILRYRRKKKMKKKLQYIKLLEE
Protein: Lysosome-associated membrane glycoprotein 3 (LAMP-3) (Lysosomal-associated membrane protein 3) (DC-lysosome-associated membrane glycoprotein) (DC LAMP) (CD antigen CD208) (Q7TST5)
Organism: Mus musculus (Mouse)
Function: Lysosomal membrane glycoprotein which plays a role in the unfolded protein response (UPR) that contributes to protein degradation and cell survival during proteasomal dysfunction. Plays a role in the process of fusion of the lysosome with the autophagosome, thereby modulating the autophagic process. Promotes hepatocellular lipogenesis through activation of the PI3K/Akt pathway. May also play a role in dendritic cell function and in adaptive immunity.
Subcellular location: Cell surface {ECO:0000250|UniProtKB:Q9UQV4}. Lysosome membrane {ECO:0000250|UniProtKB:Q9UQV4}; Single-pass type I membrane protein {ECO:0000255}. Cytoplasmic vesicle membrane {ECO:0000250|UniProtKB:Q9UQV4}; Single-pass type I membrane protein {ECO:0000255}. Early endosome membrane {ECO:0000250|UniProtKB:Q9UQV4}; Single-pass type I membrane protein {ECO:0000255}. Note=During dendritic cell maturation, detected on cytoplasmic vesicles (the MHC II compartment) that contain MHC II proteins, LAMP1, LAMP2 and LAMP3. Detected on lysosomes in mature dendritic cells. {ECO:0000250|UniProtKB:Q9UQV4}.
Interaction partners:
- Macrosialin
- Lysosome-associated membrane glycoprotein 1
Sequence:
MPGQISAVAVLFLSLTVILHGYQIREKEFPKARGYLQYTATSAEQITTKPLLQLINQRSHITLASRFKDDYIQMAAETSAIENTAHITMKTVTPVTTKSLPPISSASYTFVRSNNAHMTASSTDDTIGSGSIAHLPVPTTRASLAIVNYITGRATQLGGQTTLPKTFFTASHKSTTNQRPTLSTNVLGTSTPTHKDRSTTSPVPLVPRPTLVTWSSPAKIGTYEVLNGSRLCIKAEMGLALIVQEKDLDSATQRYFNIDPSLTHASGKCDSQKSNLFLNFQGGSVNITFTKEENLYYISEVGAYLTISNTEKTYQGKKNTLMMFETVVGHSFKCVSEQSIQLSAQLQMKTMNIHLQAFDFEGDSFGNVNECLSDYTVVLPMVAIIVVVICVVGLSVYKIRQRHQSSAYQRI
Protein: Glycerol-3-phosphate phosphatase (G3PP) (EC 3.1.3.21) (Aspartate-based ubiquitous Mg(2+)-dependent phosphatase) (AUM) (EC 3.1.3.48) (Phosphoglycolate phosphatase) (PGP) (Q8CHP8)
Organism: Mus musculus (Mouse)
Function: Glycerol-3-phosphate phosphatase hydrolyzing glycerol-3-phosphate into glycerol. Thereby, regulates the cellular levels of glycerol-3-phosphate a metabolic intermediate of glucose, lipid and energy metabolism. Was also shown to have a 2-phosphoglycolate phosphatase activity and a tyrosine-protein phosphatase activity. However, their physiological relevance is unclear. In vitro, has also a phosphatase activity toward ADP, ATP, GDP and GTP.
Interaction partners:
- Glyoxylate reductase/hydroxypyruvate reductase
- 2-Hydroxyacid oxidase 1
- 2-Hydroxyacid oxidase 2
Sequence:
MAEAEAGGDEARCVRLSAERAKLLLAEVDTLLFDCDGVLWRGETAVPGAPETLRALRARGKRLGFITNNSSKTRTAYAEKLRRLGFGGPVGPEAGLEVFGTAYCSALYLRQRLAGVPDPKAYVLGSPALAAELEAVGVTSVGVGPDVLHGDGPSDWLAVPLEPDVRAVVVGFDPHFSYMKLTKAVRYLQQPDCLLVGTNMDNRLPLENGRFIAGTGCLVRAVEMAAQRQADIIGKPSRFIFDCVSQEYGINPERTVMVGDRLDTDILLGSTCSLKTILTLTGVSSLEDVKSNQESDCMFKKKMVPDFYVDSIADLLPALQG