wanglab/gogpt-training-data huggingface dataset:
Protein: Nck-associated protein 1 (NAP 1) (Q640K3)
Organism: Xenopus laevis (African clawed frog)
Function: Part of the WAVE complex that regulates lamellipodia formation. The WAVE complex regulates actin filament reorganization via its interaction with the Arp2/3 complex. Actin remodeling activity is regulated by RAC1 (By similarity). Plays a role in neural tube closure.
Subcellular location: Cell membrane {ECO:0000250}; Single-pass membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Cell projection, lamellipodium membrane {ECO:0000250}; Single-pass membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Note=At the interface between the lamellipodial actin meshwork and the membrane. {ECO:0000250}.
Interaction partners:
Sequence:
MSRSVLQPSQQKLAEKLTILNDRGVGMLTRLYNIKKACGDPKAKPSYLIDKNLESAVKFIVRKFPAVETRNNNQQLAQLQKEKSEILKNLALYYFTFVDVMEFKDHVCELLNTIDVCQVFLDITVNFDLTKNYLDLIVTYTTLMIMLSRIEERKAIIGLYNYSHEMTHGASDREYPRLGQMIVDYENPLKKMMEEFVPHSKSLSDALISLQMVYPRRNLSAEQWRNAQLLSLISAPSTMLNPAQSDTMPCEYLSLDTMEKWIILGFILCHGILNTDATSLNLWKLALQSSSCICLYRDEVLHFHKAAEDLFVNIRGYNKRINDIRECKENAVSHAGATHRERRKFLRSALKELATVLSDQPGLLGPKALFVFMALSFARDEIIWLLRHADNIPKKIADDFMDKHIAELIFYMEELRAHVRKYGPVMQRYYVQYLSGFDAVVLNELVQNLSVCPEDESIIMSSFVNTMTSLSVKQVEDGEVFDFRGMRLDWFRLQAYTSVSKASLSLTDHRELGKMMNTIIFHTKMVDSLVEMLVETSDLSIFCFYSRAFEKMFQQCLELPSQSRYSISFPLLCTHFMSCTHELCPEERHHIGDRSLSLCNMFLDEMAKQARNLITDICTEQCTLSDQLLPKHCAKTISQAVNKKSKKQTGKKGEPEREKPGVESMRKNRLVVTNLDKLHTALSELCFSINYAPNMVVWEHTFTPREYLTSHLEIRFTKSIVGMTMYNQVTQEIAKPSELLTSVRAYMTVLQSIENYVQIDITRVFNNVLLQQTQHLDSHGEPTITSLYTNWYLETLLRQVSNGHIAYFPAMKAFVNLPTENELTFNAEEYSDISEMRALSELLGPYGMKFLSESLMWHISSQVAELKKLVVENVEVLTQMRTSFDKPEQMAAFFKRLTSVDSVLKRMTIIGVILSFRSLAQEALKDVLSYHIPFLVSSVEDFKDHIPRETDMKVAMNVYELSSAAGLPCEIDPALVVALSSQKSETISPEEEYKIACLLMVFVAVSLPTLASNVMSQYSPAIEGHCNNIHCLAKAINQIAAALFTIHKGSIEDRLKEFLALASSSLLKIGQETDKTTTRNRESVYLLLDMIVQESPFLTMDLLESCFPYVLLRNAYHAVYKQSVTSSS
Protein: Forkhead box P3 (D3ZKI1)
Organism: Rattus norvegicus (Rat)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|PROSITE-ProRule:PRU00089}.
Interaction partners:
Sequence:
MPNPRPAKPMAPSLAPGPSPGGLPSWKTAPKGSELLGTRGPGGPFQGRDLRSGAHTSSSSLNPLPPSQLQLSTVDAHGHTPVLQVRPLDNPAMIGLPPPTAATGVFSLKARPGLPPGINVASLEWVSREPALLCTFPRSGTPRKDSNLLAAPQGSYPLLANGVCKWPGCEKAFEEPGEFLKHCQADHLLDEKGKAQCLLQREVVQSLEQQLELEKEKLGAMQAHLAGKMALTKAPPVASVDKSSCCLVATSTQGSVLPAWSSPREASDSLFAVRRHLWGSHGNSTFPEFFHNMDYFKYHNMRPPFTYATLIRWAILEAPERQRTLNEIYHWFTRMFAYFRNHPATWKNAIRHNLSLHKCFVRVESEKGAVWTVDEFEFRKKRSQRPSKCSNPCP
Protein: Aspartate aminotransferase, cytoplasmic (EC 2.6.1.1) (Glutamate oxaloacetate transaminase 1.2) (Transaminase A) (Q22067)
Organism: Caenorhabditis elegans
Function: Biosynthesis of L-glutamate from L-aspartate. Important regulator of levels of glutamate, the major excitatory neurotransmitter of the central nervous system.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:29649217}.
Interaction partners:
- Malate dehydrogenase, cytoplasmic
- Malate dehydrogenase, mitochondrial
- alanine transaminase
- Glutamate dehydrogenase
- L-lactate dehydrogenase
- 4-hydroxyphenylpyruvate dioxygenase
- Aspartate aminotransferase
- Tyrosine aminotransferase
- Putative protein C31H2.4
- Aspartate aminotransferase
Sequence:
MSFFDGIPVAPPIEVFHKNKMYLDETAPVKVNLTIGAYRTEEGQPWVLPVVHETEVEIANDTSLNHEYLPVLGHEGFRKAATELVLGAESPAIKEERSFGVQCLSGTGALRAGAEFLASVCNMKTVYVSNPTWGNHKLVFKKAGFTTVADYTFWDYDNKRVHIEKFLSDLESAPEKSVIILHGCAHNPTGMDPTQEQWKLVAEVIKRKNLFTFFDIAYQGFASGDPAADAWAIRYFVDQGMEMVVSQSFAKNFGLYNERVGNLTVVVNNPAVIAGFQSQMSLVIRANWSNPPAHGARIVHKVLTTPARREQWNQSIQAMSSRIKQMRAALLRHLMDLGTPGTWDHIIQQIGMFSYTGLTSAQVDHLIANHKVFLLRDGRINICGLNTKNVEYVAKAIDETVRAVKSNI
Protein: Anaerobic nitrite reductase AHB2 (EC 1.7.2.-) (ARAth GLB2) (Hb2) (Non-symbiotic hemoglobin 2) (O24521)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: May not function as an oxygen storage or transport protein, but might act as an oxygen sensor or play a role in electron transfer, possibly to a bound oxygen molecule. Has a low affinity for O(2).
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:A2XE98}. Nucleus {ECO:0000250|UniProtKB:A2XE98}.
Interaction partners:
- Nitrate reductase 2
- Nitrate reductase 1
- Two-on-two hemoglobin-3
Sequence:
MGEIGFTEKQEALVKESWEILKQDIPKYSLHFFSQILEIAPAAKGLFSFLRDSDEVPHNNPKLKAHAVKVFKMTCETAIQLREEGKVVVADTTLQYLGSIHLKSGVIDPHFEVVKEALLRTLKEGLGEKYNEEVEGAWSQAYDHLALAIKTEMKQEES
Protein: Protein VACUOLELESS1 (Vacuolar protein sorting-associated protein 16 homolog) (Q93VQ0)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Required for vacuole biogenesis and vacuole enlargment in dividing and expanding cells. Involved in the docking or fusion of prevacuolar vesicles. Important for the function of both male and female gametophytes, but is not essential for the germination and development of pollen.
Subcellular location: Vacuole membrane {ECO:0000269|PubMed:12589039}; Peripheral membrane protein {ECO:0000269|PubMed:12589039}. Prevacuolar compartment membrane {ECO:0000269|PubMed:12589039}; Peripheral membrane protein {ECO:0000269|PubMed:12589039}.
Interaction partners:
- Vacuolar sorting protein 3
- Vacuolar protein sorting-associated protein 41 homolog
- Vacuolar protein-sorting-associated protein 33 homolog
- Vacuolar protein-sorting-associated protein 11 homolog
- Vacuolar sorting protein 18
- Vacuolar sorting protein 39
- Transducin family protein / WD-40 repeat family protein
- Vacuolar fusion protein CCZ1 homolog A
- Vesicle-associated membrane protein 727
- Vesicle-associated membrane protein 713
Sequence:
MANVSVAAEWQLLYDRYYRKPEIYQMKWKHVDLSRNKVACASFGGPIAVIRDDSKIVQLYAESALRKLRIFNSAGILLSETVWKHPGGRLIGMSWSDDQTLICIVQDGTIYRYNIHAELIEPNMSMGQECFEQNVVECVFWGNGVVCLTEGGQLICIFDFKTMKPSKLPDVPGLAEDDLLQPICLTVREPKYTMSGIAEVLVAVGDDIFVVEEDMVQTIRFDEPSVDDSEMQNDDSGNLIGVVQKMIVSPNGKFLTLFTHDGRIVVVDMETKQIAIDYSCESALPPQQMAWCGMDSVLLYWDEDLMMVGPVGDPVHYFYDEPIILIPECDGVRILSNTNLEFLQRVPDSTESIFKIGSTSPAALLYDALDHFDRRSAKADENLRLIRSSLSEAVESCIDAAGHEFDVTRQRALLRAASYGQAFCSNFQRERVQETCRTLRVLNAVRDPAIGIPLSIQQYKLLTPVVLISRLINANCHLLALRISEYLDMNKEVVIMHWACAKITASPSTPDSHLLEILLDKLQLCKGISYAAVATHADNCGRRKLAAMLVEHEPRSTKQVPLLLSIGEEDTALVKATESGDTDLVYLVIFHIWQKRPPLEFFAMIQGRVLARDLFVAYARCHKHEFLKDFFLSTGQIHEVAFLLWKESWDMGKNPMASKGSPLHGPRIKLIEKARNLFSQTKEHTFESKAAEEHAKLLKIQHELEASTKQAIFVDSSINDTIRTCIVLGNNRAAIKVKTEFKVSDKRWYWLKAFALATIKDWAALEKFSKEKRPPMGFRPFVEACIDADEKAEALKYIPKLSDLVERGEAYARIGMAKEAADCAAQANDGGELLERFRKTFVQNAIFDTLLMPFQGAS
Protein: At1g45200 (Triacylglycerol lipase-like 1) (Q8L7S1)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
Sequence:
MSKTNMKFCNSYFLVDPTKASFLDLLLLLFSSNLTSARFIDSPPDTLKGFRRSFASRWILALAIFLQKVLMLLSKPFAFIGQKLTYWLNLLTANGGFFNLILNLMSGKLVKPDKSSATYTSFIGCSDRRIELDEKINVGSIEYKSMLSIMASKISYESKPYITSVVKNTWKMDLVGNYDFYNAFQESKLTQAFVFKTSSTNPDLIVVSFRGTEPFEAADWCTDLDLSWYEMKNVGKVHAGFSRALGLQKDGWPKENISLLHQYAYYTIRQMLRDKLGRNKNLKYILTGHSLGGALAALFPAILAIHGEDELLDKLEGIYTFGQPRVGDEDFGEFMKGVVKKHGIEYERFVYNNDVVPRVPFDDKYLFSYKHYGPCNSFNSLYKGKVREDAPNANYFNLLWLIPQLLTGLWEFIRSFILQFWKGDEYKENWLMRFVRVVGIVFPGGSNHFPFDYVNSTRLGGLVRPPPTTTPEDKLALIA
Protein: 3-ketodihydrosphingosine reductase (KDS reductase) (EC 1.1.1.102) (3-dehydrosphinganine reductase) (Q556J2)
Organism: Dictyostelium discoideum (Social amoeba)
Function: Catalyzes the reduction of 3-ketodihydrosphingosine (KDS) to dihydrosphingosine (DHS).
Subcellular location: Endoplasmic reticulum {ECO:0000305}.
Interaction partners:
- Serine palmitoyltransferase 1
- Serine palmitoyltransferase 2
- sphingolipid 4-desaturase
- Neutral ceramidase A
- Sphingosine kinase A
- Sphingosine kinase B
- Probable sphingosine-1-phosphate phosphatase
- Putative alkaline ceramidase dcd3B
- Putative alkaline ceramidase dcd3A
- Neutral ceramidase B
Sequence:
MIIYILFSLLAAVIVHLVYKKQTGFKLKGKHIVVVGGSSGIGKELVYELLKENIASISVISRSLDKLRSVVDDCPSEVCTKSTPLNVGSLKSKIEIYSCDITNKIKVKETIAQIVSKNQGGKIDCLINCAGFAIPGYFIEQDEEIFEKTMQLDYFGSLYATKEVVPLMIENGGQGGHIVFVSSTCGLVGVPGYSTYCPSKFALRGLAETLRSELKPYKITFSVVYPPDTDTPGYQQENLTKPEETVAISGGGKAVSPLEVAKSIVSGIKNGDYHIAYDVPTKLCAVLSPGLTPFYFSFFDILLAPICRLVGIIAMNQNDAEVLKSWKKRNQLKK
Protein: COP9 signalosome complex subunit 1 (CSN complex subunit 1) (SGN1) (O94308)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Component of the COP9 signalosome (CSN) complex that acts as an regulator of the ubiquitin (Ubl) conjugation pathway by mediating the deneddylation of the cullin subunit of SCF-type E3 ubiquitin-protein ligase complexes (By similarity). Required, indirectly, for activation of ribonucleotide reductase through the degradation of the protein spd1, thereby supplying deoxyribonucleotides for DNA replication and repair.
Subcellular location: Cytoplasm. Nucleus.
Interaction partners:
- COP9 signalosome complex subunit 5
- COP9 signalosome complex subunit 4
- COP9 signalosome complex subunit 3
- COP9 signalosome complex subunit 7
- COP9 signalosome complex subunit 2
- DNA damage-binding protein 1
- Cullin-4
- Ubiquitin-like protein 1
- Cullin-3
- Cullin-1
Sequence:
MSLNLLVNQEELKRYLDEYGVWSKIFRALFVARNSKPLRSFCVHYAIKELKEKTYNLELYQSLFEEFQDCFENEQLDVEWVESVTFHRKQNLEQLRRELKAYKNNLIRESIRAAQLDLASFFADVGQFDSALRSYAKVREYCTNAGQIAHLSLELMRISIWIGNYSHVLAFGSRAKSTVSAAMELTSPIYAYCGLANFCLGDYEEALAHFLKVETDTSDGIITKTDISVYISLCALACWDHKRLIQELERNEEFNALSDLDPSLRRCLQAKCNRKYSLLLDTLQQNAQDYSLDMYLAPQLTNLFSLIRERSLLDYLIPYSALPFSKIAVDFHIDENFIEKNLLEIIEAKKLNGKVDSLQKRVYIEPSSEPENFEDIKNIAQTSLLYSKALYLQTLAAMNTENTDDEAPVIAQTNITAEDSQN
Protein: Leucine-rich repeat and fibronectin type-III domain-containing protein 5 (Q8BXA0)
Organism: Mus musculus (Mouse)
Function: Cell adhesion molecule that mediates homophilic cell-cell adhesion in a Ca(2+)-independent manner. Promotes neurite outgrowth in hippocampal neurons (By similarity).
Subcellular location: Membrane {ECO:0000269|PubMed:16828986}; Single-pass type I membrane protein {ECO:0000269|PubMed:16828986}.
Interaction partners:
- Receptor-type tyrosine-protein phosphatase delta
- Receptor-type tyrosine-protein phosphatase S
- Interleukin-1 receptor accessory protein-like 1
Sequence:
MEKFLFYLFLIGIAVRAQICPKRCVCQILSPNLATLCAKKGLLFVPPNIDRRTVELRLADNFVTNIKRKDFANMTSLVDLTLSRNTISFITPHAFADLRNLRALHLNSNRLTKITNDMFSGLSNLHHLILNNNQLTLISSTAFDDVFALEELDLSYNNLETIPWDAVEKMVSLHTLSLDHNMIDNIPKGTFSHLHKMTRLDVTSNKLQKLPPDPLFQRAQVLATSGIISPSTFALSFGGNPLHCNCELLWLRRLSREDDLETCASPALLTGRYFWSIPEEEFLCEPPLITRHTHEMRVLEGQRATLRCKARGDPEPAIHWISPEGKLISNATRSLVYDNGTLDILITTVKDTGAFTCIASNPAGEATQTVDLHIIKLPHLLNSTNHIHEPDPGSSDISTSTKSGSNASSSNGDTKMSQDKIVVAEATSSTALLKFNFQRNIPGIRMFQIQYNGTYDDTLVYRMIPPTSKTFLVNNLASGTMYDLCVLAIYDDGITSLTATRVVGCIQFTTEQDYVRCHFMQSQFLGGTMIIIIGGIIVASVLVFIIILMIRYKVCNNNGQHKVTKVSNVYSQTNGAQMQGCSVTLPQSMSKQAMGHEENAQCCKVASDNAIQSSETCSSQDSSTTTSALPPTWTSSAPVSQKQKRKTGTKPSAEPQSEAVTNVESQNTNRNNSTALQLASCPPDSVTEGPTSQRAHTKPNALLTNVDQNVQETQRLESI
Protein: Protein arginine N-methyltransferase 5 (EC 2.1.1.320) (D4A0E8)
Organism: Rattus norvegicus (Rat)
Subcellular location: Cytoplasm {ECO:0000256|PIRNR:PIRNR015894}. Nucleus {ECO:0000256|PIRNR:PIRNR015894}.
Interaction partners:
- Methylosome protein WDR77
- Methylosome subunit pICln
- Protein arginine N-methyltransferase 1
- Coordinator of PRMT5 and differentiation stimulator
- Protein arginine N-methyltransferase 7
- Small nuclear ribonucleoprotein Sm D3
- Serine/threonine-protein kinase RIO1
- Protein arginine N-methyltransferase 3
- SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily A member 4
- Small nuclear ribonucleoprotein Sm D1
Sequence:
MAAMAVGGAGGSRVSSGRDLNCVPEIADTLGAVAKQGFDFLCMPVFHPRFKREFIQEPAKNRPGPQTRSDLLLSGRDWNTLIVGKLSPWIHPDSKVEKIRRNSEAAMLQELNFGAYLGLPAFLLPLNQEDNTNLARVLTNHIHTGHHSSMFWMRVPLVAPEDLRDDVIENAPTAHTEEYSGEEKTWLWWHNFRTLCDYSKRIAVALEIGADLPSSHVIDRWLGEPIKAAILPTSIFLTNKKGFPVLSKMQQRLIFRLLKLEVQFIITGTNHHSEKEFCSYLQYLEYLSQNRPPPNAYELFAKGYEDYLQSPLQPLMDNLESQTYEVFEKDPIKYSQYQQAIYKCLLDRVPEEEKETNVQVLMVLGAGRGPLVNASLRAAKQAERRIRLYAVEKNPNAVVTLENWQFEEWGSQVTVVSSDMREWVAPEKADIIVSELLGSFADNELSPECLDGAQHFLKDDGVSIPGEYTSFLAPISSSKLYNEVRACREKDRDPEAQFEMPYVVRLHNFHQLSAPQPCFTFSHPNRDPMIDNNRYCTLEFPVEVNTVLHGFAGYFETVLYRDITLSIRPETHSPGMFSWFPIFFPIKQPITVHEGQNICVRFWRCSNSKKVWYEWAVTAPVCSSIHNPTGRSYTIGL
Protein: DNA processing protein DprA (Protein Smf) (P39813)
Organism: Bacillus subtilis (strain 168)
Function: Protein that helps load RecA onto ssDNA during transformation. Binds cooperatively to circular ssDNA, is able to bridge different segments of DNA. Favors the loading of RecA onto SsbA- or SsbB-coated ssDNA and formation of RecA-DNA filaments. RecA-ATP cannot catalyze homologous DNA strand exchange; SsbA and DprA activate strand exchange by RecA-ATP.
Subcellular location: Cytoplasm. Note=Localizes mostly to the cell poles during the development of competence (PubMed:17630974). During competence a number of proteins (at least CoiA, ComFA, ComGA, DprA, RecA and SsbB) are thought to colocalize at the cell pole, in a disruption of ssbB DprA no longer accumulates (PubMed:17630974). {ECO:0000269|PubMed:17630974}.
Interaction partners:
- Protein RecA
- Single-stranded DNA-binding protein B
- ComE operon protein 3
- Competence protein ComFA
- Competence protein CoiA
- Single-stranded DNA-binding protein A
- ComE operon protein 1
- Competence protein ComGA
- Competence protein ComFC
- Prepilin leader peptidase/N-methyltransferase
Sequence:
MDQAAVCLTICRINQLLSPSLLLKWWKADPSMSLTSPVLQTVTRDQIKAAALKNEIEQFYPKLPRVLAAYREQGINTIPISSKQYPFWLKSIYDPPAVLFAKGDMTLLSKGRKIGIVGTRNPTAYGKQVVNHLTKEICRKGWVIVSGLASGIDGMSHAASIKAKGRTIGVIAGGFQHIYPRENLQLADHMAKHHILLSEHPPETKPQKWHFPMRNRIISGLSEGVIVVQGKEKSGSLITAYQALEQGREVFAVPGSLFDPYAGGPIKLIQQGAKAIWSAEDIFEELPERNVQYTEPF
Protein: Hydrogen-dependent growth transcriptional repressor (Q747A3)
Organism: Geobacter sulfurreducens (strain ATCC 51573 / DSM 12127 / PCA)
Interaction partners:
- ATP synthase gamma chain
- citrate synthase
Sequence:
MGRMRENPRYNVISMRISDEERDRLQAIMEATHKSVSDIMREAMELFSVQLEQSQPGDQKAA
Protein: Discoidin-1 subunit A (Discoidin-1 subunit alpha) (Discoidin I chain A) (P02886)
Organism: Dictyostelium discoideum (Social amoeba)
Function: Galactose- and N-acetylgalactosamine-binding lectin. May play a role in cell-substratum adhesion rather than in cell-cell adhesion. May be necessary for the maintenance of normal elongate morphology during aggregation.
Subcellular location: Cytoplasm.
Interaction partners:
- SAC domain-containing protein
- Aldo-keto reductase
- Secreted protein A
Sequence:
MSTQGLVQLLANAQCHLRTSTNYNGVHTQFNSALNYKNNGTNTIDGSEAWCSSIVDTNQYIVAGCEVPRTFMCVALQGRGDADQWVTSYKIRYSLDNVSWFEYRNGAAVTGVTDRNTVVNHFFDTPIRARSIAIHPLTWNGHISLRCEFYTQPVQSSVTQVGADIYTGDNCALNTGSGKREVVVPVKFQFEFATLPKVALNFDQIDCTDATNQTRIGVQPRNITTKGFDCVFYTWNENKVYSLRADYIATALE
Protein: Serine-threonine kinase receptor-associated protein (Q9SSS7)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- At1g52720
- Serine-threonine kinase receptor-associated protein
- Serine-threonine kinase receptor-associated protein
- La-related protein 6C
- La-related protein 6A
- Thioredoxin-like 3-2, chloroplastic
- F-box/kelch-repeat protein At5g49000
- Small ribosomal subunit protein uS11y
- Probable protein S-acyltransferase 15
- Alpha carbonic anhydrase 3
Sequence:
MEKKKVTIPQVCHGHSRPVVDLFYSPITPDGFFLISASKDSHPMLRNGETGDWIGTFEGHKGAVWSSCLDNNALRAASASADFSAKLWDALTGDVLHSFEHKHIVRACAFSEDTKSLLTGGFEKILRVFDMNRLDAPPTEVDKSPGSIRTLTWLHSDQTILSSCTDIGGVRLWDVRSGKIVQTLETKSPVTSAEVSQDGRYITTADGSTVKFWDANHFGLVKSYDMPCNIESASLEPKSGEKFVAGGEDMWVRVFDFYTGEEIGCNKGHHGPVHCVRFTPTGLSYASGSEDGTIRIWQTTPANPEENETSSRRVKHSVDEVSKKIEGFHINKEGKTAEKPSDT
Protein: Dorsal interacting protein 1, isoform A (IP01991p) (Q9W381)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MDIFESFCRTCGNECLESLSIYNECAQVLDQMVPIADMLASCLPASLPPLDPEDDYPKQICRICVKKLSMAYEFSHQWLGAHGEFNVALKFEQRRRRSQASKSQSHTQTQTHPVEPKNEQLPTVLAEAVSTKRAATPTNEFSSDSGPAFKCGFCGECFYTEKACKFHLKFSHKDL
Protein: Sugar transporter SWEET (O44620)
Organism: Caenorhabditis elegans
Subcellular location: Endomembrane system {ECO:0000256|ARBA:ARBA00004127}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004127}.
Interaction partners:
- Sugar transporter SWEET1
- Sugar transporter SWEET
Sequence:
MFLEIFTVWLGIFSIGFTFLPMFMVLDWHKRGTADGFSSVNFVLPMLVQSFWLRHGYMTNDQTNIIINSINLVFFAFYVSAFAYYQPKRKYLIGQIVAAALAVKVAFAYVDTHDSASINDAMGSMAAGAQIFSLVGGIYEIKRAISMGTTEYIPAGFQFAIFTLILQWLLFGILHGNQFIAISNAAGLLVNIATLALYFFYPPLTWTVPIFNIPPQNKDAKKVE
Protein: Moesin (Membrane-organizing extension spike protein) (O35763)
Organism: Rattus norvegicus (Rat)
Function: Ezrin-radixin-moesin (ERM) family protein that connects the actin cytoskeleton to the plasma membrane and thereby regulates the structure and function of specific domains of the cell cortex. Tethers actin filaments by oscillating between a resting and an activated state providing transient interactions between moesin and the actin cytoskeleton. Once phosphorylated on its C-terminal threonine, moesin is activated leading to interaction with F-actin and cytoskeletal rearrangement. These rearrangements regulate many cellular processes, including cell shape determination, membrane transport, and signal transduction. The role of moesin is particularly important in immunity acting on both T and B-cells homeostasis and self-tolerance, regulating lymphocyte egress from lymphoid organs (By similarity). Modulates phagolysosomal biogenesis in macrophages (By similarity). Participates also in immunologic synapse formation (By similarity).
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:P26038}; Peripheral membrane protein {ECO:0000250|UniProtKB:P26041}; Cytoplasmic side {ECO:0000250|UniProtKB:P26041}. Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:P26041}. Apical cell membrane {ECO:0000250|UniProtKB:P26041}; Peripheral membrane protein {ECO:0000250|UniProtKB:P26041}; Cytoplasmic side {ECO:0000250|UniProtKB:P26041}. Cell projection, microvillus membrane {ECO:0000250|UniProtKB:P26041}; Peripheral membrane protein {ECO:0000250|UniProtKB:P26041}; Cytoplasmic side {ECO:0000250|UniProtKB:P26041}. Cell projection, microvillus {ECO:0000250|UniProtKB:P26041}. Note=Phosphorylated form is enriched in microvilli-like structures at apical membrane. Increased cell membrane localization of both phosphorylated and non-phosphorylated forms seen after thrombin treatment (By similarity). Localizes at the uropods of T lymphoblasts (By similarity). {ECO:0000250|UniProtKB:P26038, ECO:0000250|UniProtKB:P26041}.
Interaction partners:
- Na
- Radixin
- Ezrin
- CD44 antigen
- Intercellular adhesion molecule 1
- Sodium/hydrogen exchanger 1
- Vascular cell adhesion protein 1
- Actin, cytoplasmic 1
- Membrane cofactor protein
- Actin, cytoplasmic 2
Sequence:
MPKTISVRVTTMDAELEFAIQPNTTGKQLFDQVVKTIGLREVWFFGLQYQDTKAFSTWLKLNKKVTAQDVRKESPLLFKFRAKFYPEDVSEELIQDITQRLFFLQVKEGILNDDIYCPPETAVLLASYAVQSKYGDFNKEVHKSGYLAGDKLLPQRVLEQHKLNKDQWEERIQVWHEEHRGMLREDAVLEYLKIAQDLEMYGVNYFSIKNKKGSELWLGVDALGLNIYEQNDRLTPKIGFPWSEIRNISFNDKKFVIKPIDKKAPDFVFYAPRLRINKRILALCMGNHELYMRRRKPDTIEVQQMKAQAREEKHQKQMERALLENEKKKRELAEKEKEKIEREKEELMEKLKQIEEQTKKAQQELEEQTRRALELEQERKRAQSEAEKLAKERQEAEEAKEALLQASRDQKKTQEQLASEMAELTARVSQLEMARKKKESEAEECHQKAQMVQEDLEKTRAELKTAMSTPHVAEPAENEHDEQDENGAEASAELRADAMAKDRSEEERTTEAEKNERVQKHLKALTSELANARDESKKTTNDMIHAENMRLGRDKYKTLRQIRQGNTKQRIDEFESM
Protein: Dual specificity protein phosphatase 21 (EC 3.1.3.16) (EC 3.1.3.48) (Low molecular weight dual specificity phosphatase 21) (LMW-DSP21) (Q9H596)
Organism: Homo sapiens (Human)
Function: Can dephosphorylate single and diphosphorylated synthetic MAPK peptides, with preference for the phosphotyrosine and diphosphorylated forms over phosphothreonine.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:12408986}. Nucleus {ECO:0000269|PubMed:12408986}. Mitochondrion inner membrane {ECO:0000250|UniProtKB:Q9D9D8}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q9D9D8}; Matrix side {ECO:0000250|UniProtKB:Q9D9D8}. Cytoplasm, cytoskeleton, flagellum axoneme {ECO:0000250|UniProtKB:Q9D9D8}.
Interaction partners:
Sequence:
MTASASSFSSSQGVQQPSIYSFSQITRSLFLSNGVAANDKLLLSSNRITAIVNASVEVVNVFFEGIQYIKVPVTDARDSRLYDFFDPIADLIHTIDMRQGRTLLHCMAGVSRSASLCLAYLMKYHSMSLLDAHTWTKSRRPIIRPNNGFWEQLINYEFKLFNNNTVRMINSPVGNIPDIYEKDLRMMISM
Protein: ATPase H+ transporting V0 subunit D1 (F7FFW7)
Organism: Rattus norvegicus (Rat)
Interaction partners:
Sequence:
MSFFPELYFNVDNGYLEGLVRGLKAGVLSQADYLNLVQCETLEGAFIEHGTCHFIYTGTGWIESTGVHCSLPISPAGFTGSVLSQLPWSMTSLYEETLVAKDQKADLKLHLQSTDYGNFLANEASPLTVSVIDDKLKEKMVVEFRHMRNHAYEPLASFLDFITYSYMIDNVILLITGTLHQRSIAELVPKCHPLGSFEQMEAVNIAQTPAELYNAILVDTPLAAFFQDCISEQDLDEMNIEIIRNTLYKAYLESFYKFCTLLGGTTADAMCPILEFEADRRAFIITINSFGTELSKEDRAKLFPHCGRLYPEGLAQLARADDYEQVKNVADYYPEYKLLFEGAGSNPGDKTLEDRFFEHEVKLNKLAFLNQFHFGVFYAFVKLKEQECRNIVWIAECIAQRHRAKIDNYIPIF
Protein: Peroxisomal membrane protein PEX28 (Peroxin-28) (P38848)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Involved in the regulation of peroxisome number, size and distribution.
Subcellular location: Peroxisome membrane {ECO:0000269|PubMed:12707309}; Multi-pass membrane protein {ECO:0000269|PubMed:12707309}.
Interaction partners:
- Peroxisomal membrane protein PEX30
- Peroxisomal membrane protein PEX32
- Peroxisomal membrane protein PEX31
- L-2-aminoadipate reductase
- Peroxisomal membrane protein PMP27
Sequence:
MSETSSSRRSASKDAVKSYFAGKYNKVLDSILEAEAAISKSPTVAEDLSGSSSSGNSEMSHPSLTASSATSQGISKKELLQQIAGSLFSTSIERLKTAHSSEVSSTPEYSVNDSYGEQECRECDGVFKCSAHFEGAPEYYDDETESGPALEPMTSNSEKDPFIDVFLDKLISRLVPEKLPEREHFSSKTTIEHDLDTGRVPVFSATTLGSNFKKLSKKMGSIFELQDSIVRLLTWRNPTGTVTSLILFTLICFNPMYLVILPIFRFVYGIVVPGYVRKHPLQRSIYPLKRNHGSSLLYDVCYEGKNEYSYGQQFFSKSFMDTLESRNQEIDEISELDKRTENTGELKQGMKVLINLRDMQNMTSGTLHVIEAINSFLRKSSSFQNEECSTKRFFTGFLLIVFLKILSPFVNWSYVCSIFAWCLLIYMHPRAHPKIISFFKTGTMGKEYKNLKKREHQALNMIFDEQPETKFIEIFEIYKKALLPNDWKFFRYSNRIFDPQDPYRRAQQFPPGVDSLADVIPPTGWSFDPNFEWKIDNDVDRWVVERGLNLPITGEFLFDPMFKRRRLIHRVIKNATPVA
Protein: Intron-encoded RNA maturase bI4 (RNA maturase SCbI4) [Cleaved into: Truncated, nonfunctional cytochrome b; RNA maturase bI4 (EC 3.1.-.-)] (P03879)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Mitochondrial mRNA maturase required for splicing of intron 4 of the cytochrome b (COB) gene, containing its own coding sequence, and intron 4 in COX1, coding for the related homing endonuclease aI4. In vivo splicing requires in addition the imported mitochondrial leucyl-tRNA synthetase NAM2. Both proteins seem to stimulate the intrinsic ribozyme activity of intron bI4 through binding to and stabilizing specific secondary and tertiary structure elements in the RNA.
Subcellular location: Mitochondrion.
Interaction partners:
- Cytochrome b-c1 complex subunit Rieske, mitochondrial
- Cytochrome c1, heme protein, mitochondrial
- Cytochrome c oxidase subunit 2
- Intron-encoded DNA endonuclease aI5 beta
- Intron-encoded DNA endonuclease aI5 alpha
- Cytochrome c oxidase subunit 3
- Cytochrome b mRNA maturase bI2
- Cytochrome c oxidase subunit 1
- Putative COX1/OXI3 intron 2 protein
- Intron-encoded DNA endonuclease aI4
Sequence:
MAFRKSNVYLSLVNSYIIDSPQPSSINYWWNMGSLLGLCLVIQIVTGIFMAMHYSSNIELAFSSVEHIMRDVHNGYILRYLHANGASFFFMVMFMHMAKGLYYGSYRSPRVTLWNVGVIIFILTIATAFLGYCCVYGQMSHWGATVITNLFSAIPFVGNDIVSWLWGGFSVSNPTIQRFFALHYLVPFIIAAMVIMHLMALHIHGSSNPLGITGNLDRIPMHSYFIFKDLVTVFLFMLILALFVFYSPNTLGQNMALLLITYVINILCAVCWKSLFIKYQWKIYNKTTYYFIIQNILNTKQLNNFVLKFNWTKQYNKMNIVSDLFNPNRVKYYYKEDNQQVTNMNSSNTHLTSNKKNLLVDTSETTRTTKNKFNYLLNIFNMKKMNQIITKRHYSIYKDSNIRFNQWLAGLIDGDGYFCITKNKYASCEITVELKDEKMLRQIQDKFGGSVKLRSGVKAIRYRLQNKEGMIKLINAVNGNIRNSKRLVQFNKVCILLNIDFKEPIKLTKDNAWFMGFFDADGTINYYYSGKLKIRPQLTISVTNKYLHDVEYYREVFGGNIYFDKAKNGYFKWSINNKELHNIFYTYNKSCPSKSNKGKRLFLIDKFYYLYDLLAFKAPHNTALYKAWLKFNEKWNNN
Protein: CDC-like kinase 1 (A0A8I6A7Y4)
Organism: Rattus norvegicus (Rat)
Interaction partners:
Sequence:
MRHSKRTYCPDWDERDWDYGTWRSSSSHKRRKRSHSSARDYKRCKYNHSKTTDSYYLESRSIHEKAYHSRRYVDEYRNDYMTYEPGYPYGEPGSRYQNHSSKSSGRSGRSSYKSKHRSHHHTSHRRSHGMKLLIL