wanglab/gogpt-training-data huggingface dataset:
Protein: Protein efr3 (O59817)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Interaction partners:
- Putative cargo-transport protein ypp1
- Phosphatidylinositol 4-kinase stt4
- Phosphatidylinositol 4-phosphate 5-kinase its3
- Pleckstrin homology domain protein opy1
- Phosphatidylinositol 4-kinase pik1
- Putative uncharacterized transmembrane protein C1235.18
- Protein pdh1
Sequence:
MWLLFRSKHKKLVLRCFPSGKLGETEPNGSPLAYLSYYAASNSSKLRKVAHFLGSRVRHSYYHKRDNEVIIGLKICKTLVQKCRDNINVMASEVVNMLLVASSSKNLEVLSACVDCFATFCDNSGKGSPATFGNEFHSAFNNLVNSFFELSKGIDCVDPQQSKMLGLKAFHALTACKFAGTEGGMRYQPHFAIHCVLINSWSESDQEKKSFIDLVRSTAKSYKPLPPSSTGVSLPEHDEAGDNIDVAIKKLCIRILFNIYTQTDPLFMAESTKSLIHFFAAKSDTPVNLEYISVVLNQILDWTPVELRHSIFFCCLRCLSSSRIVNSETNVMVPYMIYSILNSKNSISGLSVIDVLRDLGSHLINAVNSFDADDQTWYNMCESPSEKLPRRLYLLLVCITCLTKHQYYDEEFADVWREIDTLANSETSSAIQMVALTAFHKLQNEKLNTKKESSAPLSLVTDFLLHSWPKSAERLHTSQSPFVRIKTAEVFYEFLCFLRPSLINFDTILRKSAITSFSVLWDFIYETSWHIERWLKVFSVQSEFYILKLIIQRLYQLYGPVSVTAVLPAMYRGLRPFENDPPRCIAEAVTAYYIIYIGENLKITTLQSSGRKWLDSLSSSLPSSLLNRGSSTHSWEKLTNASTEEVMLPLDMVVNELLEKSPKVFPEDSRLLFAEQSRHPKYTDIIQKLKKPSREKSFTSSSEYSLPFISPASDYQQNPLLHATKSLVSIHQQSQRGEMVSTLKQALSRPHTASTVVRSPSEINLTRQTSNRVPLLDMLNLNRAMSPTPIQSPPYVRT
Protein: rRNA adenine N(6)-methyltransferase (EC 2.1.1.-) (Q585P9)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Periodic tryptophan protein 2, putative
- Bystin, putative
- Bms1-type G domain-containing protein
- Serine/threonine-protein kinase RIO2
- Protein LTV1 homolog
- DNA-directed RNA polymerase
- U3 small nuclear ribonucleoprotein
- CCAAT-binding factor domain-containing protein
- Nrap protein domain-containing protein
- U3 small nucleolar ribonucleoprotein protein IMP3, putative
Sequence:
MPKEQRSVPMGVISAEPLQAAARKLKFTTKVTTLGKPEVRKATKKSAPTGLKTGGSQSGMVFNKGFGQHILKNPLVIAAIVEKAAVKPTDIVLEIGPGTGNLTEKLLQAAKKVIAFEVDPRMVAELNKRFQNSPLAPKLQVIRGNCLDHEFPYFDKCVANVPYAISSALVFKLLKRPNFKCAVLMFQREFALRVCAQPGSEAYCRLSVNSQLLARCSHLMKISKNSFNPPPKVESSVIRLDPKHPAPSVDFEEWDGLVKHIFNRKNKKVSSIFRTKNTVRTLYDKYCSYQRMEGVKDVKTFEEFRQHLESILQEPIFDKRARVLDQESIMELLCCFTKNDIHFV
Protein: Protein-tyrosine-phosphatase (Q8I120)
Organism: Caenorhabditis elegans
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004167}; Single-pass membrane protein {ECO:0000256|ARBA:ARBA00004167}.
Interaction partners:
Sequence:
MEEDEEALLLKEFESSSEVEETTTVEPTSDPFGDSISTISCKYGIINNLEALLNKVASGWKYHVSNTDNVKDAWFRLDNATSRICGHIGALVGPPTNVRVEATSNSTAVVQWDFESQKADSFVVKYMHEPGNRMDTEKWKQLPVVSIDKENPKRFAVVSDLNAHKPYAFCVLAVKNNRQGPCSDPPTVLESVTPTYMVQNLRVLWKTSNSVQLTWEYNGPRNVGFYVNHTGRKDYVNHELQEKTMSTPGFGQDVDEKHREYLWTNLRPHMMYTIHVGVRTLPPGARKYWPQEVVTITDPTGPPFVDVPKLVDSSGTQPGQQMIRLTPATEEYGPISHYWIILVPANYSTEDVVNLDPIELEKATAEKRAQLARSLSVSPSKKLKRKASEVGDDSQSASYHPKEKRARRATVPGAYVTARLSADRVKQQYRNNQPFIVGDSQLYDGFTNYPLEHNLHYRLMMRAFAKNDVRTKDSFEQRAPMSEKLSRMYSDSVLTEPFTIKSALRGASQKSSPWVGACIAFLVLFSIVGMLICWWLRCNKKSAGRHPRHGSITKVALTGNIMNGGGGIPGETSKLLSTSNEYGRQIMNPYEQMNGNHHMESSMDLYPLPTSHSRSNGYAPVPVAIPSLPNNGNNMTTVSHPAVPIAELANHIERLRMNNNAGFQSEFESIETGQHFTWEHSSADMNKHKNRYANVAAYDHSRVVLSNVEGYPGMDYINANYVDGYDKPRSYIATQGPLPETFSDFWRMVWEEQSVTIVMLTNLEERSRVKCDQYWPSRGTATYGDIEVTLLESVHLAHYTMRTMRLKMVGEPEVREIKHLQYTAWPDHGVPDHPTPFLIFLKRVKTLNPNDAGPIISHCSAGIGRTGAFIVIDCMLERLRYDNTVDIYGCVTALRAQRSYMVQTEEQYIFIHDAVLDAVNSGSTEVPASRLHQHLHILSQPSADQLSGIDMEFRHLTTLKWTSNRCTVANLPVNRPKNRMLSAVPYDSNRVIMRLLPGADGSDYINASWIDGYKERGAYIATQAPTNETAADFWRAIWEHNSPIIAMLVRTNERGQEQCSDYWPLETGVQVGMLVVEPMAEYDMKHYHLREFRISDINTREVRTVRQFHFMEWPDVGKPHTADHFLDFVTQVHNTYAQFGCTGPITVHCCSGAGRTAVFIALSIILDRMRAEHVVDVFTTVKLLRTERQNMIQEPEQYHFLYLAAYEYLAAYDNFS
Protein: MAR-binding filament-like protein 1 (Matrix attachment region-binding filament-like protein 1) (P93203)
Organism: Solanum lycopersicum (Tomato) (Lycopersicon esculentum)
Function: Binds DNA. Interacts with chromatin via matrix attachment regions (MARs). Likely to participate in nuclear architecture by connecting chromatin with the nuclear matrix and potentially with the nuclear envelope.
Subcellular location: Plastid, chloroplast {ECO:0000255, ECO:0000269|PubMed:16331467}. Plastid, chloroplast thylakoid membrane {ECO:0000269|PubMed:16331467}; Single-pass membrane protein {ECO:0000255}; Stromal side {ECO:0000250|UniProtKB:Q9M7J4}. Plastid, chloroplast stroma, chloroplast nucleoid {ECO:0000250|UniProtKB:Q9M7J4}. Nucleus {ECO:0000269|PubMed:16331467, ECO:0000269|PubMed:8953774}. Nucleus matrix {ECO:0000269|PubMed:16331467, ECO:0000269|PubMed:8953774}. Note=Is in the membrane-bound (insoluble) protein fraction of the leaves. Forms punctate structures within the chloroplasts of epidermal mature leaf cells and isolated mesophyll protoplasts. Distributed throughout chloroplasts locating to small patches (By similarity). Associates with thylakoid membranes in mature leaf chloroplasts. Has a direct physical interaction with nucleoids in mature leaf chloroplasts (By similarity). {ECO:0000250|UniProtKB:Q9LW85, ECO:0000250|UniProtKB:Q9M7J4}.
Interaction partners:
- WPP domain-containing protein
- MFP1 attachment factor 1
- Nucleoside phosphorylase domain-containing protein
Sequence:
MATSCFPPFSASSSSLCSSQFTPLLSCPRNTQICRKKRPVMASMHSENQKESNVCNRRSILFVGFSVLPLLNLRARALEGLSTDSQAQPQKEETEQTIQGSAGNPFVSLLNGLGVVGSGVLGSLYALARNEKAVSDATIESMKNKLKDKEDAFVSMKKQFESELLSEREDRNKLIRREGEERQALVNQLKSAKTTVISLGQELQNEKKLAEDLKFEIKGLQNDLMNTKEDKKKLQEELKEKLDLIQVLEEKITLLTTEIKDKEVSLRSNTSKLAEKESEVNSLSDMYQQSQDQLMNLTSEIKELKDEIQKRERELELKCVSEDNLNVQLNSLLLERDESKKELHAIQKEYSEFKSNSDEKVASDATLGEQEKRLHQLEEQLGTALSEASKNEVLIADLTREKENLRRMVDAELDNVNKLKQEIEVTQESLENSRSEVSDITVQLEQLRDLSSKLEREVSKLQMELEETRASLQRNIDETKHSSELLAAELTTTKELLKKTNEEMHTMSDELVAVSENRDSLQTELVNVYKKREHTRNELKQEKTIVRTLEEELKFLESQITREKELRKSLEDELEKATESLDEINRNVLALAEELELATSRNSSLEDEREVHRQSVSEQKQISQEAQENLEDAHSLVMKLGKERESLEKRAKKLEDEMAAAKGEILRLRSQINSVKAPVEDEEKVVAGEKEKVNVQQ
Protein: Glycine dehydrogenase (decarboxylating), mitochondrial (EC 1.4.4.2) (Glycine cleavage system P protein) (Glycine decarboxylase) (Glycine dehydrogenase (aminomethyl-transferring)) (P26969)
Organism: Pisum sativum (Garden pea) (Lathyrus oleraceus)
Function: The glycine cleavage system catalyzes the degradation of glycine. The P protein binds the alpha-amino group of glycine through its pyridoxal phosphate cofactor; CO(2) is released and the remaining methylamine moiety is then transferred to the lipoamide cofactor of the H protein.
Subcellular location: Mitochondrion.
Interaction partners:
Sequence:
MERARRLANRATLKRLLSEAKQNRKTESTSTTTTTPLPFSLSGSSSRYVSSVSNSILRGRGSKPDNNVSRRVGGFLGVGYPSQSRSISVEALKPSDTFPRRHNSATPDEQTKMAESVGFDTLDSLVDATVPKSIRLKEMKFNKFDGGLTEGQMIEHMKDLASKNKVFKSFIGMGYYNTHVPPVILRNIMENPAWYTQYTPYQAEISQGRLESLLNFQTMITDLTGLPMSNASLLDEGTAAAEAMSMCNNIQKGKKKTFIIASNCHPQTIDICQTRADGFELKVVVKDLKDIDYKSGDVCGVLVQYPGTEGEVLDYGEFIKKAHANEVKVVMASDLLALTVLKPPGEFGADIVVGSAQRFGVPMGYGGPHAAFLATSQEYKRMMPGRIIGVSVDSSGKQALRMAMQTREQHIRRDKATSNICTAQALLANMAAMYAVYHGPEGLKAIAQRVHGLAGVFALGLKKLGLEVQDLGFFDTVKVKTSNAKAIADAAIKSEINLRVVDGNTITAAFDETTTLEDVDKLFKVFAGGKPVSFTAASLAPEFQNAIPSGLVRESPYLTHPIFNTYQTEHELLRYIHRLQSKDLSLCHSMIPLGSCTMKLNATTEMMPVTWPSFTDLHPFAPTEQAQGYQEMFNNLGDLLCTITGFDSFSLQPNAGAAGEYAGLMVIRAYHLSRGDHHRNVCIIPASAHGTNPASAAMVGMKIVTIGTDAKGNINIEELKKAAEKHKDNLSAFMVTYPSTHGVYEEGIDDICKIIHDNGGQVYMDGANMNAQVGLTSPGWIGADVCHLNLHKTFCIPHGGGGPGMGPIGVKKHLAPFLPSHPVVPTGGIPAPENPQPLGSISAAPWGSALILPISYTYIAMMGSQGLTDASKIAILNANYMAKRLESYYPVLFRGVNGTVAHEFIIDLRGFKNTAGIEPEDVAKRLMDYGFHGPTMSWPVAGTLMIEPTESESKAELDRFCDALISIRKEIAEVEKGNADVHNNVLKGAPHPPSLLMADAWTKPYSREYAAFPAAWLRGAKFWPTTGRVDNVYGDRNLVCTLLPASQAVEEQAAATA
Protein: 5-hydroxytryptamine receptor 7 (5-HT-7) (5-HT7) (5-HT-X) (GPRFO) (Serotonin receptor 7) (P32305)
Organism: Rattus norvegicus (Rat)
Function: This is one of the several different receptors for 5-hydroxytryptamine (serotonin), a biogenic hormone that functions as a neurotransmitter, a hormone, and a mitogen. The activity of this receptor is mediated by G proteins that stimulate adenylate cyclase. This receptor is implicated in the regulation of mammalian circadian rhythms.
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:P34969}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P34969}.
Interaction partners:
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein subunit gamma
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein G
- Neuroendocrine secretory protein 55
- Guanine nucleotide-binding protein subunit gamma
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein subunit gamma
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein subunit gamma
Sequence:
MMDVNSSGRPDLYGHLRSLILPEVGRGLQDLSPDGGAHPVVSSWMPHLLSGFLEVTASPAPTWDAPPDNVSGCGEQINYGRVEKVVIGSILTLITLLTIAGNCLVVISVCFVKKLRQPSNYLIVSLALADLSVAVAVMPFVSVTDLIGGKWIFGHFFCNVFIAMDVMCCTASIMTLCVISIDRYLGITRPLTYPVRQNGKCMAKMILSVWLLSASITLPPLFGWAQNVNDDKVCLISQDFGYTIYSTAVAFYIPMSVMLFMYYQIYKAARKSAAKHKFPGFPRVQPESVISLNGVVKLQKEVEECANLSRLLKHERKNISIFKREQKAATTLGIIVGAFTVCWLPFFLLSTARPFICGTSCSCIPLWVERTCLWLGYANSLINPFIYAFFNRDLRTTYRSLLQCQYRNINRKLSAAGMHEALKLAERPERSEFVLQNSDHCGKKGHDT
Protein: Glutathione-regulated potassium-efflux system protein KefB (K(+)/H(+) antiporter) (NEM-activable K(+)/H(+) antiporter) (P45522)
Organism: Escherichia coli (strain K12)
Function: Pore-forming subunit of a potassium efflux system that confers protection against electrophiles. Catalyzes K(+)/H(+) antiport.
Subcellular location: Cell inner membrane {ECO:0000255|HAMAP-Rule:MF_01412, ECO:0000269|PubMed:15919996}; Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_01412, ECO:0000269|PubMed:15919996}.
Interaction partners:
- Glutathione-regulated potassium-efflux system ancillary protein KefG
- Glutathione-regulated potassium-efflux system ancillary protein KefF
- Uncharacterized protein YheV
- Na
- Glutathione-regulated potassium-efflux system protein KefC
- Potassium-transporting ATPase potassium-binding subunit
- Low affinity potassium transport system protein Kup
Sequence:
MEGSDFLLAGVLFLFAAVAAVPLASRLGIGAVLGYLLAGIAIGPWGLGFISDVDEILHFSELGVVFLMFIIGLELNPSKLWQLRRSIFGVGAAQVLLSAALLAGLLMLTDFAWQAAVVGGIGLAMSSTAMALQLMREKGMNRSESGQLGFSVLLFQDLAVIPALALVPLLAGSADEHFDWMKVGMKVLAFVGMLIGGRYLLRPVFRFIAASGVREVFTAATLLLVLGSALFMDALGLSMALGTFIAGVLLAESEYRHELETAIDPFKGLLLGLFFISVGMSLNLGVLYTHLLWVVISVVVLVAVKILVLYLLARLYGVRSSERMQFAGVLSQGGEFAFVLFSTASSQRLFQGDQMALLLVTVTLSMMTTPLLMKLVDKWLSRQFNGPEEEDEKPWVNDDKPQVIVVGFGRFGQVIGRLLMANKMRITVLERDISAVNLMRKYGYKVYYGDATQVDLLRSAGAEAAESIVITCNEPEDTMKLVEICQQHFPHLHILARARGRVEAHELLQAGVTQFSRETFSSALELGRKTLVTLGMHPHQAQRAQLHFRRLDMRMLRELIPMHADTVQISRAREARRELEEIFQREMQQERRQLDGWDEFE
Protein: Altered inheritance of mitochondria protein 21 (P40563)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Involved in mitochondrial migration along actin filaments.
Subcellular location: Cytoplasm, cytoskeleton, actin patch {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:19053807}. Note=Cortical actin patches. Localizes at the shmoo tip.
Interaction partners:
- Topoisomerase I damage affected protein 2
- Myosin tail region-interacting protein MTI1
- F-actin-capping protein subunit beta
- Actin-binding protein
- F-actin-capping protein subunit alpha
- Transgelin
- Myosin-5
- Actin cytoskeleton-regulatory complex protein SLA1
- Protein YSC84
- Reduced viability upon starvation protein 167
Sequence:
MPSEVTPKVPERPSRRKTSELFPLSGSESGDIKANSEPPTPAGTPNVPTRRPILKAKTMTSFESGMDQESLPKVPLQRPVRRSTTEELNNVMNNTSKELEEIESLISKHNIHNVSRKKSPTSVEEGKVAAIHQNGQRSASDNKTSTNPSPLEKNEHEGAEGNESAISPSNLVNKSNNEVTEHSDSEDLTEKQKVHAALDNEAGDRSHFEEKLIPGDMKVQVDVSKDVEEGSLNALPPSGITESDDKAEKFTKHPESSLEELQKHQEQQEEKIFQNPTDEESTTSLNEKQEGKDNMEVNSQPQGPSDTETVIAATSSNVPSQIASEEENDVPVIPRSRPKKDFEAHVQKEELPNTQEKRVSEECDSTLISTEEESKIPKIPSERPKRRAPPPVPKKPSSRIAAFQEMLQKQQQQDLHNNGNSSATTASADIAKKHTDSSITSDTTKADFTSKLNGLFALPGMVNPGQLPPSLEKKLSSPDTESKLGPQDQSQAKTGPLGGTRRGRGPRGRKLPSKVASVEKIEEDDNTNKIEIFNNWNVSSSFSKEKVLIDTTPGEQAERALDEKSKSIPEEQREQSPNKMEAALCPFELDEKEKLPANAESDPLSQLPQTNAVGNRKAISEESLSPSEAIANRDQNDTTEIQEQQMEDQMEVDMERELSGGYEDVDSALHSEEASFHSL
Protein: DRE-binding protein 3a (Q076D8)
Organism: Gossypium hirsutum (Upland cotton) (Gossypium mexicanum)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MAESDPSSTNVPPKDQPPPPTVPIPDAPPQEQSPKPSSTPLVSSKEGVSGNPTSRKLSAVYRGVRSRSGKWVSEIREPRKTTRIWLGTYPTPEMAATAYDVAALALKGPDAELNFPDMVHSYPKVGSTSATDIRAAAASAAASRLLPKSVTNTGSLSKNEDTTSTTAMEITCSGQEFIDEEELLNFPNLVVDMAGGMLVSPPNWINSPPSDDSPDNSDVDTLWTYT
Protein: CD2-associated protein (F1LRS8)
Organism: Rattus norvegicus (Rat)
Function: Seems to act as an adapter protein between membrane proteins and the actin cytoskeleton (By similarity). In collaboration with CBLC, modulates the rate of RET turnover and may act as regulatory checkpoint that limits the potency of GDNF on neuronal survival. Controls CBLC function, converting it from an inhibitor to a promoter of RET degradation. May play a role in receptor clustering and cytoskeletal polarity in the junction between T-cell and antigen-presenting cell (By similarity). May anchor the podocyte slit diaphragm to the actin cytoskeleton in renal glomerolus. Also required for cytokinesis. Plays a role in epithelial cell junctions formation (By similarity).
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:Q9Y5K6}. Cell projection, ruffle {ECO:0000250|UniProtKB:Q9Y5K6}. Cell junction {ECO:0000250|UniProtKB:Q9Y5K6}. Note=Colocalizes with F-actin and BCAR1/p130Cas in membrane ruffles (By similarity). Located at podocyte slit diaphragm between podocyte foot processes (By similarity). During late anaphase and telophase, concentrates in the vicinity of the midzone microtubules and in the midbody in late telophase (By similarity). {ECO:0000250|UniProtKB:Q9JLQ0, ECO:0000250|UniProtKB:Q9Y5K6}.
Interaction partners:
- Podocin
- Nephrin
- Kin of IRRE-like protein 1
- Synaptopodin
- Tight junction protein ZO-1
- E3 ubiquitin-protein ligase CBL
- Ras and Rab interactor 3
- Alpha-actinin-4
- Capping protein regulator and myosin 1 linker 1
- T-cell surface antigen CD2
Sequence:
MVDYIVEYDYDAVHDDELTIRVGEIIRNVKKLQEEGWLEGELNGRRGMFPDNFVKEIKRETEPKDDNLPIKRERPGNVASLVQRISTYGLPAGGIQPHPQTKAMKKKTKKRQCKVLFEYSPQNEDELELTVGDVIDVIEEVEEGWWSGTLNNKLGLFPSNFVKELESTDDGEMHDAQEESEVSLTGPTSPMPSPGNGSEPAPGSVTQPKKIRGVGFGDIFKEGSVKLRTRTSSSETEEKKSEKPLILQSLGSRTQNVEVTKPDIDGKIKAKEYCKTVFPYTGTNEDELTFREGEIIHLISKETGEAGWWKGELNGKEGVFPDNFAVQISELDKDFPKPKKPPPPAKGPAPKPDPLAGEKKTFPLKAEDRDEKSLLEQKPSKPAAPQVPPKKPTPPTKANNLLRSPGTMYPKRPEKPVPPPPPTAKINGEVSTISSKIDTEPLSKPKLDPEQLPVRPKSVDLDALVARNSKETDNVNFDDIASSENLLHLTANRPKMPGRRLPGRFNGGHSPTQSPEKTLKLPKDDDSGNIKPSEFKKDAGYSSKPSLSAPSSASKVNTAAFLSPLELKAKVEADDGKKSSLDELRAQIIELLCIVDALKKDHGKELEKLRRELEEEKAMRSNLEVEIAKLKKAVLLS
Protein: SEC24 homolog B, COPII coat complex component (D3ZW15)
Organism: Rattus norvegicus (Rat)
Subcellular location: Cytoplasm, cytosol {ECO:0000256|ARBA:ARBA00004514}. Cytoplasmic vesicle, COPII-coated vesicle membrane {ECO:0000256|ARBA:ARBA00004299}; Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004299}; Cytoplasmic side {ECO:0000256|ARBA:ARBA00004299}. Endoplasmic reticulum membrane {ECO:0000256|ARBA:ARBA00004397}; Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004397}; Cytoplasmic side {ECO:0000256|ARBA:ARBA00004397}.
Interaction partners:
- Protein SEC13 homolog
- Protein transport protein sec16
- Protein transport protein Sec31B
- Protein transport protein SEC23
- Protein transport protein Sec31A
- Small COPII coat GTPase SAR1B
- WD_REPEATS_REGION domain-containing protein
- SEC24 homolog D, COPII coat complex component
- Protein transport protein SEC23
- SEC24 homolog C, COPII coat complex component
Sequence:
MSAPAGSPHPAAGARMPPKLGGAVSGLAPPQQNGPAQSQMQVPSGYGLPHQNYMAPSGHYSQGPGKMTSLPLDNQCENYYSRPYTAPTQNVGTPSSANQPGAQLMYGRGPSAPHMGASMPGPFQGAPASASHSYPSASQPYSSLGNRYSSPATYSATASVASQGYPSTCSHYPISTVSNVVYPNVSYPSLPASEPYGQMFTSQSAPPPARPLKESYSGPSTAVAYPSRPPPPPSQHQQQQQQQQQQQQQSHSGYSSLPWSGPGLPPAQDSLIRNQMGSLAIPNSHPAINVADSLSCPITENVQPPKPSSVVATVLPGPSSTRMPPAPSHPVGPVPSAPPPPEQMQTKGMQYGDYVNNQASSTPTPLSSASDDEEEEDEDEEAGVDSSSTTSSASPLPNSYDALEGGSYPDMHSSSASSPVPDRAPEPNSTLVPTPTAAQPAKVAKPFGYGYPTLQPAYQNAAAPPTTAHPSGPAYSGYPQQYPGVHQLSSGLGGLSLQSSPQPESLRPVNLTQEKNILPATPIWAPVPNLSAELSKLNCSPDSFRCTLTSIPQTQALLNKAKLPLGLLLHPFRDLTQLPVITSNTIVRCRSCRTYINPFVSFIDQRRWKCNLCYRVNDVPEEFLYNPLTRSYGEPHKRPEVQNSTVEFIASSDYMLRPPQPAVYLFVLDVSHNAVEAGYLTVLCQSLLENLDKLPGDSRTRIGFMTFDSTIHFYNLQEGLSQPQMLIVSDIDDVFLPTPDSLLVNLYESKELIKDLLNALPNMFINTRETHSALGPALQAAFKLMSPTGGRVSVFQTQLPSLGAGLLQSREDPNQRSSTKVVHHLGPATDFYKKLALDCSGQQTAVDLFLLSSQYSDLASLACMSKYSAGCIFYYPSFHSTHNPSQAEKLQKDLKRYLTRKIGFEAVMRIRCTKGLSMHTFHGNFFVRSTDLLSLANINPDAGFAVQLSIEESLADTSLVCFQTALLYTSSKGERRIRVHTLCLPVVSSLADVYAGVDVQAAICLLANMAVDRSVSSSLSDARDALVNAVVDPLSAYSSAVSSVPRSTLTAPSSLKLLPLYVLALLKQKAFRTGTSTRLDDRVYAMCQMKSQPLVHLMKMIHPNLYRIDRLTDEGAIHVNDRVVPQPPLQKLSAEKLTREGAFLMDCGSVFYIWIGKGCDSNFIENVLGYPDFGSIPQKMTHLPELDTLPSERTRSFVTWLRDSRPLSPVLHVVKDESPARTDFFQHLVEDRTEAALSYYEFLIHVQQQVCK
Protein: Cell division protein FtsZ (P9WN95)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: Essential cell division protein that forms a contractile ring structure (Z ring) at the future cell division site. The regulation of the ring assembly controls the timing and the location of cell division. One of the functions of the FtsZ ring is to recruit other cell division proteins to the septum to produce a new cell wall between the dividing cells. Binds GTP and shows GTPase activity.
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00909}. Note=Assembles at midcell at the inner surface of the cytoplasmic membrane. {ECO:0000255|HAMAP-Rule:MF_00909}.
Interaction partners:
- Cell division protein SepF
- Probable peptidoglycan glycosyltransferase FtsW
- Cell division protein FtsQ
- Penicillin-binding protein PbpB
- UDP-N-acetylglucosamine--N-acetylmuramyl-
- Cell wall synthesis protein Wag31
- Peptidoglycan glycosyltransferase RodA
- UDP-N-acetylmuramate--L-alanine ligase
- UDP-N-acetylmuramoylalanine--D-glutamate ligase
- Protein RecA
Sequence:
MTPPHNYLAVIKVVGIGGGGVNAVNRMIEQGLKGVEFIAINTDAQALLMSDADVKLDVGRDSTRGLGAGADPEVGRKAAEDAKDEIEELLRGADMVFVTAGEGGGTGTGGAPVVASIARKLGALTVGVVTRPFSFEGKRRSNQAENGIAALRESCDTLIVIPNDRLLQMGDAAVSLMDAFRSADEVLLNGVQGITDLITTPGLINVDFADVKGIMSGAGTALMGIGSARGEGRSLKAAEIAINSPLLEASMEGAQGVLMSIAGGSDLGLFEINEAASLVQDAAHPDANIIFGTVIDDSLGDEVRVTVIAAGFDVSGPGRKPVMGETGGAHRIESAKAGKLTSTLFEPVDAVSVPLHTNGATLSIGGDDDDVDVPPFMRR
Protein: T. brucei spp.-specific protein (Q384L6)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MEEGTYAGQLGTQNLDSVVETDETNFLHERLSSKISNGFASSAYWGATGELPPREPDDVAGKKPHCFEMELNRKLVPFPEDKTSLPRILDYSHVGLHRLRDGAEDPPKLNEAQLRALEAGGSASGDNTLKRRGLPLLERTTTQGRTIGKGILGPEALNALREGNANISAAEANREQLKSKPFTSADPNAYRPTSWDYCDMTGIDPSSYWVTALDQESVGMPAVYKSRYNLVEKEGPVRRERTTLMLERGKTVDKKQLRDTLDGINAEAVPQGYKTWSAGHWMSTTHDAHAPYDIGGATEINKRNATVPLPRTYHTLTPVHEETVLSQTQRHLNRHNGKWATEYSVSYKDSFDEAEVNKAYSKRSIFDIRDGAYTMHPYAHHPRDDTATGENYTPAQIVPGQYTSIARQPLHARNAIK
Protein: UPF0291 protein SP_1473 (Q97PW7)
Organism: Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4)
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01103}.
Interaction partners:
Sequence:
MDPKKIARINELAKKKKTEGLTPEEKVEQAKLREEYIEGYRRAVRHHIEGIKIVDEEGNDVTPEKLRQVQREKGLHGRSLDDPNS
Protein: Acid beta-fructofuranosidase 4, vacuolar (At beta fruct4) (AtBETAFRUCT4) (EC 3.2.1.26) (Acid invertase 4) (AI 4) (Acid sucrose hydrolase 4) (Vacuolar invertase 4) (Inv-V4) (VAC-INV 4) (VI 4) (Q39041)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Possible role in the continued mobilization of sucrose to sink organs. Regulates root elongation.
Subcellular location: Vacuole {ECO:0000269|PubMed:12773619}. Endoplasmic reticulum membrane {ECO:0000269|PubMed:21899678, ECO:0000269|PubMed:23737500}; Single-pass type II membrane protein. Golgi apparatus membrane {ECO:0000269|PubMed:21899678, ECO:0000269|PubMed:23737500}; Single-pass type II membrane protein. Golgi apparatus, trans-Golgi network membrane {ECO:0000269|PubMed:21899678}; Single-pass type II membrane protein. Prevacuolar compartment membrane {ECO:0000269|PubMed:21899678}; Single-pass type II membrane protein. Vacuole membrane {ECO:0000269|PubMed:21899678}; Single-pass type II membrane protein. Vacuole lumen {ECO:0000269|PubMed:21899678, ECO:0000269|PubMed:23737500}. Note=Located in the lytic vacuole but not in the protein storage vacuole. Remains inserted into membranes on its way to the lytic vacuole, following the classical sorting pathway from the endoplasmic reticulum. Released into the lumen of the vacuole from the tonoplast through a proteolytic processing. {ECO:0000269|PubMed:21899678, ECO:0000269|PubMed:23737500}.
Interaction partners:
- alpha-D-xyloside xylohydrolase
- Probable galactinol--sucrose galactosyltransferase 4
- Probable fructokinase-1
- Probable fructokinase-2
- Probable fructokinase-3
- Probable fructokinase-5
- Probable fructokinase-4
- Probable fructokinase-6, chloroplastic
- Probable fructokinase-7
- Hexokinase-1
Sequence:
MASSDALLPISAREEEPLCPYTRLPMADPNQETHGPRRRRPFKGLLAVSFGLLFIAFYVALIATHDGSRSNDEGIDETETITSRARLAGVSEKRNDGLWKLSGDRNTPAFEWNNSMLSWQRTAFHFQPEQNWMNDPNGPLFYKGWYHFFYQYNPNAAVWGDIVWGHAVSRDLIHWVHLPIAMVADQWYDSNGVWTGSATFLPDGSIVMLYTGSTDKAVQVQNLAYPEDPNDPLLLKWVKFPGNPVLVPPPGILPKDFRDPTTAWKTSEGKWRITIGSKLNKTGISLVYDTIDFKTYEKLDTLLHRVPNTGMWECVDFYPVSKTAGNGLDTSVNGPDVKHIVKASMDDTRFDHYAVGTYFDSNGTWIPDDPTIDVGMTASLRYDYGKFYASKSFYDQNKGRRVLWSWIGESDSEASDVQKGWSSLQGIPRTVVLDTKTGKNLVQWPVEEIKSLRLSSKQFDLEVGPGSVVPVDVGSAAQLDIEAEFEINKESLDKIIGNASVVAEAEEFSCEKSGGSTVRGALGPFGFSVLATESLSEQTPVYFYVAKGKDSELKTFFCTDTSRSSVANDVVKPIYGSVVPVLKGEKLTMRILVDHSIVEAFGQGGRTCITSRVYPTTAIYGAAKLFLFNNALDATVTASFTVWQMNSAFIHPYSDEAVRALSRT
Protein: Protein phosphatase 1 regulatory subunit 1A (Protein phosphatase inhibitor 1) (I-1) (IPP-1) (P19103)
Organism: Rattus norvegicus (Rat)
Function: Inhibitor of protein-phosphatase 1. This protein may be important in hormonal control of glycogen metabolism. Hormones that elevate intracellular cAMP increase I-1 activity in many tissues. I-1 activation may impose cAMP control over proteins that are not directly phosphorylated by PKA. Following a rise in intracellular calcium, I-1 is inactivated by calcineurin (or PP2B). Does not inhibit type-2 phosphatases.
Interaction partners:
- Serine/threonine-protein phosphatase PP1-gamma catalytic subunit
- Serine/threonine-protein phosphatase PP1-alpha catalytic subunit
- Serine/threonine-protein phosphatase PP1-beta catalytic subunit
- cAMP-dependent protein kinase catalytic subunit alpha
- cAMP-dependent protein kinase catalytic subunit beta
- Serine/threonine-protein phosphatase 2A 56 kDa regulatory subunit beta isoform
- Calcineurin subunit B type 1
- Protein phosphatase 3 catalytic subunit alpha
- Serine/threonine-protein phosphatase
- Serine/threonine-protein phosphatase 2B catalytic subunit beta isoform
Sequence:
MEPDNSPRKIQFTVPLLEPHLDPEAAEQIRRRRPTPATLVLTSDQSSPEVDEDRIPNPLLKSTLSMSPRQRKKMTRTTPTMKELQTMVEHHLGQQKQGEEPEGATESTGNQESCPPGIPDTGSASRPDTSGTAQKPAESKPKTQEQRGVEPSTEDLSAHMLPLDSQGASLV
Protein: Protein PLANT CADMIUM RESISTANCE 11 (AtPCR11) (Q9SX24)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: May be involved in heavy metals transport.
Subcellular location: Membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}.
Interaction partners:
- Probable ADP-ribosylation factor GTPase-activating protein AGD13
- Anther-specific protein BCP1
- F-box protein At3g62230
- Shaggy-related protein kinase beta
- At4g35700
- Transcription factor DUO1
- Tubby-like F-box protein 6
- Tubby-like F-box protein 7
- Cytochrome C oxidase assembly factor
- Myosin-16
Sequence:
MNLSSNDQPSQGRIKAKDWSTDLCECWMDINSCCLTCWCPCVAFGRIAEVVDRGSTSCGVSGAMYMIIFMLTGYGGSSLYSCFYRTKLRAQYNLKERPCCDCCVHFCCEPCALCQEYRQLQHNRDLDLVIGWHGNMERHARLAASTPSAPPLQAPMSRLV
Protein: COA8 family protein CG14806, mitochondrial (COA8) (APOPT1 family protein CG14806, mitochondrial) (Cytochrome c oxidase assembly factor 8) (Q9W549)
Organism: Drosophila melanogaster (Fruit fly)
Function: May be required for cytochrome c complex (COX) assembly and function, COX being the terminal component of the mitochondrial respiratory chain.
Subcellular location: Mitochondrion inner membrane {ECO:0000250|UniProtKB:Q9CQW7}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q96IL0}; Matrix side {ECO:0000250|UniProtKB:Q96IL0}.
Interaction partners:
- FI08815p
- Protein MIX23
- Uridine-cytidine kinase
Sequence:
MNKCFRCQPRISLFQFSLPRCYAAVQPGCPPPQEKPVVGLPHKPDPKTVKCDYIGPPDAQSNLRPYVRHYGDEETRLARSLRLKRIEVEAWNTDFWTKHNKRFYEEKEDFIRLHKESGTSEVSADQMSHFYKAFLDKNWRIHIMYNISWYLKNFDILTLAAAVQLQRLLALAKRRS