wanglab/gogpt-training-data huggingface dataset:
Protein: RAS guanyl-releasing protein 1 (Calcium and DAG-regulated guanine nucleotide exchange factor II) (CalDAG-GEFII) (Ras guanyl-releasing protein) (O95267)
Organism: Homo sapiens (Human)
Function: Functions as a calcium- and diacylglycerol (DAG)-regulated nucleotide exchange factor specifically activating Ras through the exchange of bound GDP for GTP. Activates the Erk/MAP kinase cascade. Regulates T-cell/B-cell development, homeostasis and differentiation by coupling T-lymphocyte/B-lymphocyte antigen receptors to Ras. Regulates NK cell cytotoxicity and ITAM-dependent cytokine production by activation of Ras-mediated ERK and JNK pathways. Functions in mast cell degranulation and cytokine secretion, regulating FcERI-evoked allergic responses. May also function in differentiation of other cell types.
Subcellular location: Cytoplasm, cytosol. Cell membrane; Peripheral membrane protein. Golgi apparatus membrane; Peripheral membrane protein. Endoplasmic reticulum membrane; Peripheral membrane protein. Note=Found both in the cytosol and associated with membranes. Relocalization to the cell membrane upon activation is F-actin-dependent. Translocates to the Golgi in response to phorbol ester or nerve growth factor. Localizes to somata and dendrites but not to axons of hippocampal pyramidal cells (By similarity). {ECO:0000250}.
Interaction partners:
- Ras-related protein Rap-1b
- Ras-related protein Rap-1A
- 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase gamma-1
- GTPase NRas
- GTPase HRas
- GTPase KRas
- Son of sevenless homolog 1
- Son of sevenless homolog 2
- RAS guanyl-releasing protein 2
- Diacylglycerol kinase alpha
Sequence:
MGTLGKAREAPRKPSHGCRAASKARLEAKPANSPFPSHPSLAHITQFRMMVSLGHLAKGASLDDLIDSCIQSFDADGNLCRSNQLLQVMLTMHRIVISSAELLQKVITLYKDALAKNSPGLCLKICYFVRYWITEFWVMFKMDASLTDTMEEFQELVKAKGEELHCRLIDTTQINARDWSRKLTQRIKSNTSKKRKVSLLFDHLEPEELSEHLTYLEFKSFRRISFSDYQNYLVNSCVKENPTMERSIALCNGISQWVQLMVLSRPTPQLRAEVFIKFIQVAQKLHQLQNFNTLMAVIGGLCHSSISRLKETSSHVPHEINKVLGEMTELLSSSRNYDNYRRAYGECTDFKIPILGVHLKDLISLYEAMPDYLEDGKVNVHKLLALYNHISELVQLQEVAPPLEANKDLVHLLTLSLDLYYTEDEIYELSYAREPRNHRAPPLTPSKPPVVVDWASGVSPKPDPKTISKHVQRMVDSVFKNYDHDQDGYISQEEFEKIAASFPFSFCVMDKDREGLISRDEITAYFMRASSIYSKLGLGFPHNFQETTYLKPTFCDNCAGFLWGVIKQGYRCKDCGMNCHKQCKDLVVFECKKRAKNPVAPTENNTSVGPVSNLCSLGAKDLLHAPEEGPFTFPNGEAVEHGEESKDRTIMLMGVSSQKISLRLKRAVAHKATQTESQPWIGSEGPSGPFVLSSPRKTAQDTLYVLPSPTSPCPSPVLVRKRAFVKWENKDSLIKSKEELRHLRLPTYQELEQEINTLKADNDALKIQLKYAQKKIESLQLEKSNHVLAQMEQGDCS
Protein: Adhesion G protein-coupled receptor A2 (G-protein coupled receptor 124) (E7FBY6)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: Endothelial receptor which functions together with reck to enable brain endothelial cells to selectively respond to Wnt7 signals (wnt7a or wnt7b). Plays a key role in Wnt7-specific responses: Required for normal central nervous system (CNS) vascularization where it functions cell-autonomously in the tip cells of sprouting vessels. Has a role in development of dorsal root ganglia. Acts as a Wnt7-specific coactivator of canonical Wnt signaling: required to deliver reck-bound Wnt7 to frizzled by assembling a higher-order RECK-ADGRA2-Fzd-LRP5-LRP6 complex. Adgra2-tethering function does not rely on its G-protein coupled receptor (GPCR) structure but instead on its combined capacity to interact with RECK extracellularly and recruit the Dishevelled scaffolding protein intracellularly.
Subcellular location: Cell membrane {ECO:0000269|PubMed:26051822, ECO:0000269|PubMed:27979830}; Multi-pass membrane protein {ECO:0000255}. Note=Colocalizes with reck at the plasma membrane. {ECO:0000269|PubMed:26051822}.
Interaction partners:
- Reversion-inducing cysteine-rich protein with Kazal motifs
- Norrin cystine knot growth factor NDP.
- Protein Wnt
- Low density lipoprotein receptor-related protein 5
- Protein Wnt
- Frizzled-4
- Tetraspanin
- Adhesion G protein-coupled receptor G7, tandem duplicate 1.
Sequence:
MSGPCVRIPFWVRVFLLLLLYRIAAGCPELFSSGCSCTEDRSKAHPTPGTRRKVSCGGKELTETPEVSLLPNRTVSLNLSNNRIRMLKNGSFAGLSSLEKLDLRNNLISTIMPGAFLGLTALRKLDLSSNRIGCLTPEMFQGLTNLTKLNISGNIFSSLDPNVFMELHSLKLVNFHSEFLSCDCGLRWVPSFFRSGSARLGDETLCAYPRRLQNKPLRLLRESDLSCEGPLELHTLSLLPSQRQVVFKGDRLPFHCTASLVDKITALHWRQNGQPVTSDPTKGIHLEESVQHDCTFITSELILSNVHVEASGEWECVVSTGRGNTSCSVEIVVLENSASFCPEQKVNNNRGEFRWPRTLAGITSYQHCLQLRYPSLTLGGGVEQKKASRNCDRSGRWEEADYSQCLYTNDITRILHTFILMPVNASNAVTLAHQVRSYTLEAAGFTDTVDVLYVAQMMHKFMDYVTELRELSEVLVEMGSNLMQVDDQILARAQREERACSSIVYTLETLAWPQLHSHAQDLSRYSRNIVMEAHLIRPAHFTGISCTVYQRREGAAGSQVHDGADLSLEQQLRFRCTTGTHNTSLNAFHLKNAVALATVSLPATLFPPNAPPDCKLQFVAFRNGRFFPFTSNFTGHSDLARRRGISTPVIYAGLDGCSMWNQSDPIIVSLRHTSPGHDPVAAHWNSQALGHHGSWSLDGCQLIHSDVSISTLRCSVLSNYAVLQEIPDFPGSPSIPVEVLHPVIYTCTAVLLLCLFTIIITYILHHSSIRITRKSWHTLLNTSFHVAMTSAVFAGGITLTGYPIVCQAVGIVLHYSSLSTLLWIGVSARVIYKEALLRTPQQLEGESAVQPTQRPMLRFYLIAGGVPLIICGITAAVNINNYGDNIPYCWLVWQPSFGAFYIPAGLIILVTWIYFLCTVFCLRQRNFQESKDLQCSASDPSNLPESQPALSGSTSLLSTDSGVSPVHAGTTVEDQYSLKVQCLALMATQFVFVGLWCCGAMAVWHVDRERKLFSCLYGGTATGLGIFLVLHHCFKRLDVQAAWLGCCPGYHRSQPMPAYSHPCTVTVGVQSASERGSQLFVACHPPTDPNHYSSSARSSSTQSGTASITVVPSKLTNLLQVSQDNANNASRAPAGTNTNTSTSTENNKPTNNLLPSLLPVQQPQRRKACSRTKGGNTQYHHRGDARSHYRLKALRAGGGGSMGALGPSGTEHSNIYHVHKHASSENGSLRNSHSEGQNGLLTNGRHRGEGLATSPSEGSDGGSSGSRKPFPLLPSVARRAAMQQNAQCRSASKDNLKLAAAAERESKRSSFPLNMSSNVTATASLSTVSAPNGTLKGSVVELDTSGTDQSQGSVGMKSRVWKSETTV
Protein: Ethylene-responsive transcription factor ERN1 (ERF transcription factor ERN1) (NF box-binding protein 1) (Protein ERF REQUIRED FOR NODULATION 1) (A2Q5W1)
Organism: Medicago truncatula (Barrel medic) (Medicago tribuloides)
Function: Transcription factor involved in symbiotic nodule signaling in response to rhizobial Nod factors (NFs). Binds to the GCC-box (NF-responsive box) of ENOD11 promoter. Acts as transcriptional activator of NF-responsive box-containing target gene promoters in root hairs. Functions as a transcriptional regulator required for root infection by symbiotic rhizobia, infection thread (IT) formation and maintenance, and nodule development. Necessary for NF-induced gene expression and spontaneous nodulation activated by CCAMK. Functions downstream of CCAMK to activate nodulation gene expression. Involved in early stages of root nodule development. Functions redundantly with ERN2. Is essential with ERN2 for the initiation of root hair infection, and nodule organogenesis and development. Required for accurate expression of the NF signaling genes ENOD11 and ENOD12.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00366, ECO:0000269|PubMed:17827349, ECO:0000269|PubMed:23077241}.
Interaction partners:
- Calcium and calcium/calmodulin-dependent serine/threonine-protein kinase DMI-3
Sequence:
MEIQFQQPNMQNQKAGISVTNKGGKFKGRNRNSNNTNKFVGVRQRPSGRWVAEIKDTTQKIRMWLGTFETAEEAARAYDEAACLLRGSNTRTNFITHVSLDSPLASRIRNLLNNRKGDKKQEDGAVASAPSNSKTTISNTSTITSNDDNKESTLSTCATRNTELFEDAYKPDLSNCKEVFESGSQSNISCGFGPFFDHFSFTQLLDMAKNDDITDASSLELSEFERMKVERQISASLYAINGVHEYMETVQESNEALWDLPPLCSLFC
Protein: N-acyl-phosphatidylethanolamine-hydrolyzing phospholipase D 2 (NAPE-2) (EC 3.1.4.54) (Q965X9)
Organism: Caenorhabditis elegans
Function: D-type phospholipase that hydrolyzes N-acyl-phosphatidylethanolamines (NAPEs) to produce bioactive N-acylethanolamines/fatty acid ethanolamides (NAEs/FAEs) and phosphatidic acid. NAEs are bioactive lipids that are involved in diverse physiological processes such as growth and lifespan.
Interaction partners:
Sequence:
MSAPTTSSSTDEDFAKPVKNGKTFANPKSFTNWGGIPGISDGFKFAFTETNHENVPCDKKILDVEIPVHNITADDFHSESDLFATWLGHATVLVDLEGVKFVTDPVWADRASFTSFAGPKRYRPPPMKLEDLPDLDFAVVSHDHYDHLDADAVKKITDRNPQIKWFVPLGMKKWMEGQGIGVDGSSTAVTELNWGESSEFVKNGKTYTIWCLPAQHWGQRGLFDRNHRLWSGWAVIGENRRFYYSGDTGHCDGEFKKFGEKLGPFDLAAIPIGAYEPRWFMKSQHINPEEAIEVHKLIRAKNSIGIHWGTYHMGSTEYYLEPRDKLKELMDAREDLKNTSFVTIEMGRIWEASDQ
Protein: Cytosolic Fe-S cluster assembly factor NUBP2 homolog (Q4Q9E8)
Organism: Leishmania major
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496, ECO:0000256|HAMAP-Rule:MF_03039}.
Interaction partners:
Sequence:
MQSPSVAEGAAPPSGAGGSDAAATVASAGLFQVKNIILVLSGKGGVGKSTVACQLALALAHVHHKQVGLLDVDVCGPSVPKICGLEGCDVYRGEKGWIPVSSQAKAATAGSPGSAPGAAAPSGDLKVMSIAYLLPSDKDAVVWRGPKKDAMIKQFVTDVHWGPLDYLIIDTPPGTSDEHLTLCEVLRSFRPSGAVIVTTPQDVSTDDVKKELSFCHKLQLRCLGIVENMSGFVCPHCAHCTDIFSKGGGRKLAEMYEVAFLGAIPIDPNLSLAEDMGRVFVKESPSQTVDAVTAVIDAIVQQVERAKA
Protein: Nucleoprotein (Nucleocapsid protein) (NC) (Protein N) (Q6UPD4)
Organism: SARS coronavirus HB
Subcellular location: Host cell {ECO:0000256|ARBA:ARBA00004340}. Virion {ECO:0000256|HAMAP-Rule:MF_04096, ECO:0000256|PIRNR:PIRNR003888}. Host endoplasmic reticulum-Golgi intermediate compartment {ECO:0000256|HAMAP-Rule:MF_04096}. Host Golgi apparatus {ECO:0000256|HAMAP-Rule:MF_04096}. Note=Located inside the virion, complexed with the viral RNA. Probably associates with ER-derived membranes where it participates in viral RNA synthesis and virus budding. {ECO:0000256|HAMAP-Rule:MF_04096, ECO:0000256|PIRNR:PIRNR003888}.
Interaction partners:
Sequence:
MSDNGPQSNQRSAPRITFGGPTDSTDNNQNGGRNGARPKQRRPQGLPNNTASWFTALTQHGKEELRFPRGQGVPINTNSGPDDQIGYYRRATRRARGGDGKMKELSPRWYFYYLGTGPEASLPYGANKEGIVWVATEGALNTPKDHIGTRNPNNNAATVLQLPQGTTLPKGFYAEGSRGGSQASSRSSSRSRGNSRNSTPGSSRGNSPARMASGGGETALALLLLDRLNRLESKVSGKGQQQQGQTVTKKSAAEASKKPRQKRTATKQYNVTQAFGRRGPEQTQGNFGDQDLIRQGTDYKHWPQIAQFAPSASAFFGMSRIGMEVTPSGTWLTYHGAIKLDDKDPQFKDNVILLNKHIDAYKTFPPTEPKKDKKKKTDEAQPLPQRQKKQPTVTLLPAADMDDFSRQLQNSMSGASADSTQA
Protein: Max-binding protein MNT (Class D basic helix-loop-helix protein 3) (bHLHd3) (Myc antagonist MNT) (Protein ROX) (Q99583)
Organism: Homo sapiens (Human)
Function: Binds DNA as a heterodimer with MAX and represses transcription. Binds to the canonical E box sequence 5'-CACGTG-3' and, with higher affinity, to 5'-CACGCG-3'.
Subcellular location: Nucleus.
Interaction partners:
- Max-like protein X
- Protein max
- Max dimerization protein 4
- Myc proto-oncogene protein
- Paired amphipathic helix protein Sin3a
- Max dimerization protein 3
- Carbohydrate-responsive element-binding protein
- Max dimerization protein 1
- N-myc proto-oncogene protein
Sequence:
MSIETLLEAARFLEWQAQQQQRAREEQERLRLEQEREQEQKKANSLARLAHTLPVEEPRMEAPPLPLSPPAPPPAPPPPLATPAPLTVIPIPVVTNSPQPLPPPPPLPAAAQPLPLAPRQPALVGAPGLSIKEPAPLPSRPQVPTPAPLLPDSKATIPPNGSPKPLQPLPTPVLTIAPHPGVQPQLAPQQPPPPTLGTLKLAPAEEVKSSEQKKRPGGIGTREVHNKLEKNRRAHLKECFETLKRNIPNVDDKKTSNLSVLRTALRYIQSLKRKEKEYEHEMERLAREKIATQQRLAELKHELSQWMDVLEIDRVLRQTGQPEDDQASTSTASEGEDNIDEDMEEDRAGLGPPKLSHRPQPELLKSTLPPPSTTPAPLPPHPHPHPHSVALPPAHLPVQQQQPQQKTPLPAPPPPPAAPAQTLVPAPAHLVATAGGGSTVIAHTATTHASVIQTVNHVLQGPGGKHIAHIAPSAPSPAVQLAPATPPIGHITVHPATLNHVAHLGSQLPLYPQPVAVSHIAHTLSHQQVNGTAGLGPPATVMAKPAVGAQVVHHPQLVGQTVLNPVTMVTMPSFPVSTLKLA
Protein: F-box associated ubiquitination effector family protein (F4IDS9)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
Sequence:
MESLPHEVVERILEKTCCGFSAEIHGCIETMEIIDRISILPTKTIDTASAIRSREDYFNPDLKHLTTLVLGSSSSVTIPTPWEKDKEKEKEKEKEDEEFFLVSFDSCDGLVCLYKYWKSGYVVNPTTRWYRPLPLSQLQQLLISLGRSVFELGYTVCDIGFGKDKITGTYKPVWLYNSLEIGLENATTCEVFDFNTNAWRYVSPTAPYREETKILSFDLHTETFRVVSKAPFTNVKAFDIVMCNLGNRLCVSEKNWPNQVIWSFNSGNKTWHKMFSINLDVTSHWFGNHIAAVMPLALFYEKKKKKKLLFYCRVRSRTLMVYDPETESYDVAFNDYSIGYPLCYFQSLISIS
Protein: M-zodatoxin-Lt8a (M-ZDTX-Lt8a) (Cytoinsectotoxin-1a) (CIT-1a) (P85253)
Organism: Lachesana tarabaevi (Spider)
Function: Insecticidal, cytolytic and antimicrobial peptide. Has insecticidal activity against the flesh fly S.carnaria, and against the cockroach N.cinerea. Has insecticidal activity against D.melanogaster. Has hemolytic activity against human erythrocytes (EC(50)=6 uM). Has cytolytic activity against insect Sf9 cells (EC(50)=1 uM) and human leukocytes (EC(50)=3 uM). Has antibacterial activity against the Gram-positive bacteria A.globiformis VKM Ac-1112 (MIC=0.5 uM), and B.subtilis VKM B-501 (MIC=0.6-0.9 uM), and against the Gram-negative bacteria E.coli C600 (MIC=0.5 uM), E.coli DH5alpha (MIC=0.9 uM), E.coli MH1 (MIC=0.5 uM), P.aeruginosa PAO1 (MIC=1.9 uM), and P.fluorescens VKM B-894 (MIC=3.8 uM). Lacks antimicrobial activity against the Gram-positive bacteria M.luteus and S.aureus, and against the Gram-negative bacterium S.marcescens. Forms voltage-dependent, ion-permeable channels in membranes. At high concentration causes cell membrane lysis.
Subcellular location: Secreted {ECO:0000269|PubMed:18215128, ECO:0000269|PubMed:27287558}.
Interaction partners:
Sequence:
MKYFVVALALVAAFACIAESKPAESEHELAEVEEENELADLEDAVWLEHLADLSDLEEARGFFGNTWKKIKGKADKIMLKKAVKIMVKKEGISKEEAQAKVDAMSKKQIRLYLLKYYGKKALQKASEKL
Protein: Nucleoporin NUP116/NSP116 (Nuclear pore protein NUP116/NSP116) (Q02630)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Functions as a component of the nuclear pore complex (NPC). NPC components, collectively referred to as nucleoporins (NUPs), can play the role of both NPC structural components and of docking or interaction partners for transiently associated nuclear transport factors. Active directional transport is assured by both, a Phe-Gly (FG) repeat affinity gradient for these transport factors across the NPC and a transport cofactor concentration gradient across the nuclear envelope (GSP1 and GSP2 GTPases associated predominantly with GTP in the nucleus, with GDP in the cytoplasm). Plays an important role in several nuclear export and import pathways including poly(A)+ RNA, tRNA, pre-ribosome, and protein transport. By binding ATPase AFG2, promotes AFG2-mediated release of shuttling protein RLP24 from pre-60S ribosomal particles.
Subcellular location: Nucleus, nuclear pore complex {ECO:0000269|PubMed:10891509}. Nucleus membrane; Peripheral membrane protein; Cytoplasmic side. Nucleus membrane; Peripheral membrane protein; Nucleoplasmic side. Note=Biased towards cytoplasmic side.
Interaction partners:
- mRNA export factor GLE2
- Importin subunit beta-1
- Nucleoporin NUP159
- Nucleoporin NSP1
- Nucleoporin NUP42
- Nucleoporin NUP82
- Protein transport protein SEC13
- Nucleoporin SEH1
- Nucleoporin NUP57
- Nucleoporin NUP2
Sequence:
MFGVSRGAFPSATTQPFGSTGSTFGGQQQQQQPVANTSAFGLSQQTNTTQAPAFGNFGNQTSNSPFGMSGSTTANGTPFGQSQLTNNNASGSIFGGMGNNTALSAGSASVVPNSTAGTSIKPFTTFEEKDPTTGVINVFQSITCMPEYRNFSFEELRFQDYQAGRKFGTSQNGTGTTFNNPQGTTNTGFGIMGNNNSTTSATTGGLFGQKPATGMFGTGTGSGGGFGSGATNSTGLFGSSTNLSGNSAFGANKPATSGGLFGNTTNNPTNGTNNTGLFGQQNSNTNGGLFGQQQNSFGANNVSNGGAFGQVNRGAFPQQQTQQGSGGIFGQSNANANGGAFGQQQGTGALFGAKPASGGLFGQSAGSKAFGMNTNPTGTTGGLFGQTNQQQSGGGLFGQQQNSNAGGLFGQNNQSQNQSGLFGQQNSSNAFGQPQQQGGLFGSKPAGGLFGQQQGASTFASGNAQNNSIFGQNNQQQQSTGGLFGQQNNQSQSQPGGLFGQTNQNNNQPFGQNGLQQPQQNNSLFGAKPTGFGNTSLFSNSTTNQSNGISGNNLQQQSGGLFQNKQQPASGGLFGSKPSNTVGGGLFGNNQVANQNNPASTSGGLFGSKPATGSLFGGTNSTAPNASSGGIFGSNNASNTAATTNSTGLFGNKPVGAGASTSAGGLFGNNNNSSLNNSNGSTGLFGSNNTSQSTNAGGLFQNNTSTNTSGGGLFSQPSQSMAQSQNALQQQQQQQRLQIQNNNPYGTNELFSKATVTNTVSYPIQPSATKIKADERKKASLTNAYKMIPKTLFTAKLKTNNSVMDKAQIKVDPKLSISIDKKNNQIAISNQQEENLDESILKASELLFNPDKRSFKNLINNRKMLIASEEKNNGSQNNDMNFKSKSEEQETILGKPKMDEKETANGGERMVLSSKNDGEDSATKHHSRNMDEENKENVADLQKQEYSEDDKKAVFADVAEKDASFINENYYISPSLDTLSSYSLLQLRKVPHLVVGHKSYGKIEFLEPVDLAGIPLTSLGGVIITFEPKTCIIYANLPNRPKRGEGINVRARITCFNCYPVDKSTRKPIKDPNHQLVKRHIERLKKNPNSKFESYDADSGTYVFIVNHAAEQT
Protein: Hippocalcin-like protein 1 (Calcium-binding protein BDR-1) (HLP2) (Visinin-like protein 3) (VILIP-3) (P37235)
Organism: Homo sapiens (Human)
Function: May be involved in the calcium-dependent regulation of rhodopsin phosphorylation.
Subcellular location: Membrane {ECO:0000305}; Lipid-anchor {ECO:0000305}.
Interaction partners:
Sequence:
MGKQNSKLRPEVLQDLRENTEFTDHELQEWYKGFLKDCPTGHLTVDEFKKIYANFFPYGDASKFAEHVFRTFDTNGDGTIDFREFIIALSVTSRGKLEQKLKWAFSMYDLDGNGYISRSEMLEIVQAIYKMVSSVMKMPEDESTPEKRTDKIFRQMDTNNDGKLSLEEFIRGAKSDPSIVRLLQCDPSSASQF
Protein: Protein SSX2 (Cancer/testis antigen 5.2) (CT5.2) (Synovial sarcoma, X breakpoint 2) (Tumor antigen HOM-MEL-40) (Q16385)
Organism: Homo sapiens (Human)
Function: Could act as a modulator of transcription.
Subcellular location: Nucleus.
Interaction partners:
Sequence:
MNGDDAFARRPTVGAQIPEKIQKAFDDIAKYFSKEEWEKMKASEKIFYVYMKRKYEAMTKLGFKATLPPFMCNKRAEDFQGNDLDNDPNRGNQVERPQMTFGRLQGISPKIMPKKPAEEGNDSEEVPEASGPQNDGKELCPPGKPTTSEKIHERSGPKRGEHAWTHRLRERKQLVIYEEISDPEEDDE
Protein: SIR4-interacting protein SIF2 (P38262)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Antagonizes telomeric silencing in yeast. May recruit SIR4 to non-telomeric sites or repression.
Subcellular location: Nucleus.
Interaction partners:
- Probable histone deacetylase HOS2
- SET domain-containing protein 3
- Protein HOS4
- Probable DNA-binding protein SNT1
- Peptidyl-prolyl cis-trans isomerase
- NAD-dependent protein deacetylase HST1
- Suppressor of mar1-1 protein
- Histone deacetylase RPD3
- Transcriptional regulatory protein PHO23
- Meiosis-specific transcription factor NDT80
Sequence:
MSITSEELNYLIWRYCQEMGHEVSALALQDETRVLEFDEKYKEHIPLGTLVNLVQRGILYTESELMVDSKGDISALNEHHLSEDFNLVQALQIDKEKFPEISSEGRFTLETNSESNKAGEDGASTVERETQEDDTNSIDSSDDLDGFVKILKEIVKLDNIVSSTWNPLDESILAYGEKNSVARLARIVETDQEGKKYWKLTIIAELRHPFALSASSGKTTNQVTCLAWSHDGNSIVTGVENGELRLWNKTGALLNVLNFHRAPIVSVKWNKDGTHIISMDVENVTILWNVISGTVMQHFELKETGGSSINAENHSGDGSLGVDVEWVDDDKFVIPGPKGAIFVYQITEKTPTGKLIGHHGPISVLEFNDTNKLLLSASDDGTLRIWHGGNGNSQNCFYGHSQSIVSASWVGDDKVISCSMDGSVRLWSLKQNTLLALSIVDGVPIFAGRISQDGQKYAVAFMDGQVNVYDLKKLNSKSRSLYGNRDGILNPLPIPLYASYQSSQDNDYIFDLSWNCAGNKISVAYSLQEGSVVAI
Protein: Endoplasmic reticulum transmembrane protein 1 (P35723)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: May play a role in anterograde transport of membrane proteins from the endoplasmic reticulum to the Golgi.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:14562095, ECO:0000269|Ref.8}; Multi-pass membrane protein {ECO:0000269|PubMed:14562095, ECO:0000269|Ref.8}.
Interaction partners:
- Vesicle-associated membrane protein-associated protein SCS2
- Endoplasmic reticulum transmembrane protein 3
- Transcriptional repressor OPI1
Sequence:
MSLYFTTLFLLLTVEMVMLFIFVLPLPFRIRRGIFSTYNQLTAKQQIKTIIFITGCLVGLLFIDSWKRSQIRVSLYHNDNSGSIGSSAVTPIQALASRAYNQRNMYISGFILYFSICIPTVMSIVKRLVKYQGLINEQEKQKLNKPSSNSKKDSNEADSTKLQEELRKKQISLEGLQKQVKNLEKYFDEKNQPGNVAAAEASKKGN
Protein: Protein GIS3 (Q12418)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Subcellular location: Cytoplasm {ECO:0000269|PubMed:14562095}. Nucleus {ECO:0000269|PubMed:14562095}.
Interaction partners:
- Protein GIS4
Sequence:
MLLDVNTNHTLMHDAHVHEHCLIKSIRDDGALHSWSDSSKVFYPKSFYATATNKKNNKLASASMNKTATSNRTVSDEIYFHSTKPQFDGQGSAERTRTLTKRNSFKRTRILKARDDSELLNENRSSLMTPSLSSVMSQVRKTNSAKTLSGECPIHEGHLTQSIKRKFSEEAQSDCSSLSSSKLHPLTDDIADAVDLQTPAIGDEVLAEPVVPKMKIININDLDLFDDWEVKDLVDIFPPVYERRPRSSSALSLVSASSDAKLRPTSVDFQIIDKKGGKTSRRKSRSKSTTENMIYENDLVELEQWPSASPSPETDGSIASSELLPNKRIRQKSLNTNFLKLYSIETSCKRKSILPEVEVDDHLLKQLTYSEIRSLEIKKEPNVSTNDIKLALITRKKLWSDMVHETRNDLFGDSTPWNLHFVATTSNTEPSQGRESASEHATADLKSSLVRVHSDVKPWFNNGGTMLKPCGKLNLGKVTNKTSAPTREIQYVVKGWCDSRFL
Protein: Esophagus cancer-related gene-2 interaction susceptibility protein (Q8IZW4)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
RRARCWHKAPERQRQGLKPGFSWAGADAQSGVGSCHLGNCWDLQSQRCHLHSMVLILPASWPEGHPDHKSGGLSVCLHLPQRCLLSFPTHSSLFGVRGGTGQLAQDLLIIAAQVFE
Protein: Serine/threonine-protein phosphatase PP-Z (EC 3.1.3.16) (P78968)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Cytoplasm {ECO:0000269|PubMed:10759889}. Note=Nucleus; nuclear rim.
Interaction partners:
- Probable thymidylate synthase
- Serine/threonine-protein phosphatase PP1-1
- RNA polymerase II subunit A C-terminal domain phosphatase ssu72
- Serine/threonine-protein phosphatase PP1-2
- Set1 complex component swd2
- Uncharacterized RING finger protein P8B7.15c
- Polyadenylation factor subunit 2
- Endoribonuclease ysh1
- Protein cft1
- Cleavage factor two protein 2
Sequence:
MGQGSSKHADSKLDSYPSFSRSDTQGSIKSLKSLKTVLGKGKDSNHDRRTSTDTTHSRHRYPETPPSLPPPPSPGILATSPAVLQKHQQEDSGNSSQSPTSPHPSNQPAMLSPSTAASQHHHHHSSSSSYAVSPTSPTSPTSSGPIGSNFDSASEHNGPVYPQDQQGPVIIPNSAISSTDPDDPETVVSLNVDEMIQRLIHVGYSRKSSKSVCLKNAEITSICMAVREIFLSQPTLLELTPPVKIVGDVHGQYSDLIRLFEMCGFPPSSNYLFLGDYVDRGKQSLETILLLFLYKIRYPENFFLLRGNHECANITRVYGFYDECKRRCNIKIWKTFINTFNCLPIASVVAGKIFCVHGGLSPSLSHMDDIREIPRPTDVPDYGLLNDLLWSDPADTENDWEDNERGVSFVFNKNVIRQFLAKHDFDLICRAHMVVEDGYEFFNDRTLCTVFSAPNYCGEFDNWGAVMSVNSELLCSFELIKPLDQAAIRRELKKSKRSGMAIYQSPPAEQVTQSV
Protein: Granzyme M (EC 3.4.21.-) (Met-1 serine protease) (Hu-Met-1) (Met-ase) (Natural killer cell granular protease) (P51124)
Organism: Homo sapiens (Human)
Function: Cleaves peptide substrates after methionine, leucine, and norleucine. Physiological substrates include EZR, alpha-tubulins and the apoptosis inhibitor BIRC5/Survivin. Promotes caspase activation and subsequent apoptosis of target cells.
Subcellular location: Secreted. Cytoplasmic granule. Note=Granules of large granular lymphocytes.
Interaction partners:
- Beta-secretase 1
- Ubiquitin thioesterase otulin
- Granzyme H
Sequence:
MEACVSSLLVLALGALSVGSSFGTQIIGGREVIPHSRPYMASLQRNGSHLCGGVLVHPKWVLTAAHCLAQRMAQLRLVLGLHTLDSPGLTFHIKAAIQHPRYKPVPALENDLALLQLDGKVKPSRTIRPLALPSKRQVVAAGTRCSMAGWGLTHQGGRLSRVLRELDLQVLDTRMCNNSRFWNGSLSPSMVCLAADSKDQAPCKGDSGGPLVCGKGRVLARVLSFSSRVCTDIFKPPVATAVAPYVSWIRKVTGRSA
Protein: Asparagine--tRNA ligase, cytoplasmic (EC 6.1.1.22) (Asparaginyl-tRNA synthetase) (AsnRS) (Asparaginyl-tRNA synthetase 1) (O43776)
Organism: Homo sapiens (Human)
Function: Catalyzes the attachment of asparagine to tRNA(Asn) in a two-step reaction: asparagine is first activated by ATP to form Asn-AMP and then transferred to the acceptor end of tRNA(Asn). In addition to its essential role in protein synthesis, acts as a signaling molecule that induced migration of CCR3-expressing cells. Has an essential role in the development of the cerebral cortex, being required for proper proliferation of radial glial cells.
Subcellular location: Cytoplasm {ECO:0000305|PubMed:9421509}.
Interaction partners:
- Bifunctional glutamate/proline--tRNA ligase
- Glutamyl-tRNA
- Glutamyl-tRNA
- Tyrosine--tRNA ligase, cytoplasmic
- Isoleucine--tRNA ligase, cytoplasmic
- Glutamyl-tRNA
- Leucine--tRNA ligase, cytoplasmic
- Alanine--tRNA ligase, cytoplasmic
- Asparagine synthetase
- Glycine--tRNA ligase
Sequence:
MVLAELYVSDREGSDATGDGTKEKPFKTGLKALMTVGKEPFPTIYVDSQKENERWNVISKSQLKNIKKMWHREQMKSESREKKEAEDSLRREKNLEEAKKITIKNDPSLPEPKCVKIGALEGYRGQRVKVFGWVHRLRRQGKNLMFLVLRDGTGYLQCVLADELCQCYNGVLLSTESSVAVYGMLNLTPKGKQAPGGHELSCDFWELIGLAPAGGADNLINEESDVDVQLNNRHMMIRGENMSKILKARSMVTRCFRDHFFDRGYYEVTPPTLVQTQVEGGATLFKLDYFGEEAFLTQSSQLYLETCLPALGDVFCIAQSYRAEQSRTRRHLAEYTHVEAECPFLTFDDLLNRLEDLVCDVVDRILKSPAGSIVHELNPNFQPPKRPFKRMNYSDAIVWLKEHDVKKEDGTFYEFGEDIPEAPERLMTDTINEPILLCRFPVEIKSFYMQRCPEDSRLTESVDVLMPNVGEIVGGSMRIFDSEEILAGYKREGIDPTPYYWYTDQRKYGTCPHGGYGLGLERFLTWILNRYHIRDVCLYPRFVQRCTP
Protein: Flagellar secretion chaperone FliS (P26608)
Organism: Escherichia coli (strain K12)
Subcellular location: Cytoplasm, cytosol {ECO:0000305}.
Interaction partners:
- Flagellar protein FliT
- Flagellar hook-associated protein 3
- Flagellin
- Flagellar hook-associated protein 2
- Flagellar hook-associated protein 1
- Flagellum-specific ATP synthase
- Flagellar biosynthesis protein FlhA
- Flagellar motor switch protein FliG
- Flagellar assembly protein FliH
- Negative regulator of flagellin synthesis
Sequence:
MYAAKGTQAYAQIGVESAVMSASQQQLVTMLFDGVLSALVRASLFMQDNNQQGKGVSLSKAINIIENGLRVSLDEESKDELTQNLIALYSYMVRRLLQANLRNDVSAVEEVEALMRNIADAWKESLLSPSLIQDPV
Protein: Ponticulin-like protein C4 (Q54LC1)
Organism: Dictyostelium discoideum (Social amoeba)
Subcellular location: Cell membrane {ECO:0000305}; Lipid-anchor, GPI-anchor {ECO:0000305}.
Interaction partners:
- CMP/dCMP-type deaminase domain-containing protein
- PhoPQ-activated pathogenicity-related protein
- Probable phosphoglycerate mutase
- Secreted protein A
Sequence:
MKFTKSLLLLIVAVFASSNAAETFSNFQVTNSEASSPCVTTPVELKVNTCQSACGSILNVLPVTGSTSKFTFNQFGAQDTKCAATPTSSNEFTCVDGKSKVAIGSTTYSVVCVPDKTNSSESDSSDSTRIGASFALAAAALLSMIAL
Protein: Proline-rich 7 (synaptic) (Proline-rich protein 7 isoform X1) (E7EXZ8)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
- DNA-directed RNA polymerase III subunit RPC5 isoform X1
Sequence:
MVMSQGTYTFLACFAGFWLIWALIVMLCCFCSFAQRKLKRRREERLREQCLRALEMEPLECTSGGYPPREPPQFCPPLQMLSPQLPVTHTLPQANWTVPEADTDVFGKPPCYEEAVLMEDPPPPYSEVLADPRGGTYTKPASSSSREHQESETSKMAPVTVFPECGYSSLIRLPSARRWDSLGHLLSNMDLNHNNLPVEPQASAIATMPREGRTHTDIGLRGLQSLDQHYGLPTAFPLLGRSTAV