wanglab/gogpt-training-data huggingface dataset:
Protein: CD2-associated protein like (Cd2apl protein) (Q5PR31)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
Sequence:
MEGDLNGKRGLFPDNFVKEVRKDEPKSKEESKEPKEAKEVKEESTIQRRASGNVASLVQRISTYGIPAGGIGLQPHSQPRASKKKLKKRQCKVLFEYVPQNEDELELKVGEIIEITEEVEEGWWSGSMNGKSGLFPSNFVKEIDSTEDAENSDVTEEQDTRDGTSSPTSPHPGNGVMAQPKKIKGIGFGDIFREGSVKLRTSLKGPSENMEKTEKPIPPLPSATKPTPLSTPEHPKGEKEAESKAKVKEYCKATFHYEATNQDELDLKEGEVILVLMTM
Protein: Wee1-like protein kinase 1-B (EC 2.7.10.2) (Zygotic wee1-like protein kinase 1B) (Xe-Wee1B) (XeWee1B) (Q8QGV2)
Organism: Xenopus laevis (African clawed frog)
Function: Acts as a zygotic negative regulator of entry into mitosis (G2 to M transition) by protecting the nucleus from cytoplasmically activated cyclin B1-complexed cdk1 before the onset of mitosis by mediating phosphorylation of cdk1 on 'Tyr-15'. Specifically phosphorylates and inactivates cyclin B1-complexed cdk1 reaching a maximum during G2 phase and a minimum as cells enter M phase. Phosphorylation of cyclin B1-cdk1 occurs exclusively on 'Tyr-15' and phosphorylation of monomeric cdk1 does not occur.
Subcellular location: Nucleus {ECO:0000250}.
Interaction partners:
Sequence:
MNVQPRNMNVQPRNMNVQPVRHKLFFSDTDEEEEDGHSTGEDSAFQESDSPVSRQREKQEGKPPGGTWEELEEEEGFGSSPIKSPGDFFMSDSPSYRQLAPASPTRSPQGPTSPIPECPGTPPHKTFRKLRLFDTPHTPKSLLSKARGIGSSALRFRGGTLFREAEKAPKPEFVYSTPQVNINPFTPDSLEIQSSAGLCRGRKRALLNDSCGEDMEGSDCELEDEDIRPAKRIPITESNMKSRYATEFHELEKIGSGEFGSVFKCVKRLDGCIYAIKRSKKPLAGSVDEQNALREVYAHAVLGQHPHVVRYYSAWAEDDHMLIQNEYCNGGSLSDVISENYRTMQYFTEPELKDLLLQVARGLKYIHSMSLVHMDIKPSNIFISRTTLPNTAVEEADDEECGSGKVIYKIGDLGHVTRVSSPQVEEGDSRFLANEVLQENYTHLAKADIFALALTVWSAAGAEPFPTNGDQWHEIRQGKLPRVPQLLSQEFVDLIKLMISPDPEKRPSSVALVKHSVLLSASRKSAEQLRIELDAEKFKNALLQKELKKAQIAKAAAEERAHFPDRIATRSTTQNNRTTRLIGKKMNRSVSLTIY
Protein: RE35738p (Q7YU44)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
Sequence:
MRDAPEDQSVTVSMPASASGSAAGSTGPSSDRRMTQRLLVELLVVVVLVIPICVYEFAVDPVRRGFFCDDESISYPFQDNTITPVMLGLIVGLLPALVMVVVEYVSHLRAGDISATVDLLGWRVSTWYVELGRQSTHFCFGLLLTFDATEVGKYTIGRLRPHFLAVCQPQIADGSMCSDPVNLHRYMENYDCAGEGFTVEDVRQARLSFPSGHSSLAFYAMIYVALYLQRKITWRGSKLSRHFVQFAVVMVAWYTALSRVMDHWHHWSDVLSGSLLGVAGALITAHYIARMFDDGASNILSGGLRRENTAATLQEEVCPTTPPPYSVNNSFSEDQYCSKV
Protein: PAN2-PAN3 deadenylation complex catalytic subunit PAN2 (EC 3.1.13.4) (PAB1P-dependent poly(A)-specific ribonuclease) (Poly(A)-nuclease deadenylation complex subunit 2) (PAN deadenylation complex subunit 2) (G0SAK8)
Organism: Chaetomium thermophilum (strain DSM 1495 / CBS 144.50 / IMI 039719) (Thermochaetoides thermophila)
Function: Catalytic subunit of the poly(A)-nuclease (PAN) deadenylation complex, one of two cytoplasmic mRNA deadenylases involved in mRNA turnover. PAN specifically shortens poly(A) tails of RNA and the activity is stimulated by poly(A)-binding protein PAB1. PAN deadenylation is followed by rapid degradation of the shortened mRNA tails by the CCR4-NOT complex. Deadenylated mRNAs are then degraded by two alternative mechanisms, namely exosome-mediated 3'-5' exonucleolytic degradation, or deadenlyation-dependent mRNA decaping and subsequent 5'-3' exonucleolytic degradation by XRN1. May also be involved in post-transcriptional maturation of mRNA poly(A) tails.
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03182}.
Interaction partners:
- PAN2-PAN3 deadenylation complex subunit PAN3
- Polyadenylate-binding protein
- CCR4-Not complex 3'-5'-exoribonuclease subunit Ccr4
Sequence:
MDADWDEVTRIAYPAPGTNDFPRPATAVAFDPIAELLWAGFDRGRVCSFYGRDLTRYTAFKIQPASEGPVRQFLFHDKGVIVLGTRSVHMAMRRGPALWNIRHENMKDLRCMSFTSKGTQEIIVAGWQDTMLVIDVLKGDIIKQIPAQHHYSIMKKSRYICAATKTGSVDLIDPLSFKIVRSWQAHASYINDMDAQNDFIVTCGGSLKQQAAQTYMLDPYVNVFDLKNMASMKPMPFPPLAAHVRLHPRMLTTAIVTSQHGQMHVVDIMNPNSSTVRYANISSYVKLFEIAPSGEALVIGDADCNIHLWGSPTKIHFTDMAIPIELPEPEEPAPVLDWSIETPLSSIGLPYYREPLFSAWPADIISDVGAPPLQLEPSFVATLKQAEWGLYGKNTRNVRRNQVEDTRNTNKQSNALQAPKFLSERARESALSSGGDSSSDPQVDQEPEDPNEIESLKPEAPPLYRNLEIKYSKFGVDDFDFGYYNKTRYAGLENHIPNSYANSLLQLMHYTPLLRNMALQHAATACVSDLCLLCELGFVFDMLQKAEGATCQATNMFKALSGTPQAAPLGLLEEETHVPSLATMAQNLSRFLLEKIHNEYRTIPPISTALEQSLFNFPHPPTPDELVAKVLATSAVATIKCMNCRSETTRPGTTHVIDLLYPPPKTAGRGGRASKVTFSQVLKMGVERETTSKGWCSRCQRYQNLQMRKTIHSVPAVLVVNAGVSNQEHRKLWSTPGWLPEEIGIIVDQGQFFCFEGEDLKLHLQRGIHNITVYSLIGMVINIESHSPQKSHLVGIINVAHAEATPPGENKWHLFNDFSVRPVSAAEALTFNAAWKMPAVLLFQIKSANNKSNLDWKTNLDTSILYKDTNPNTEKKTYRTLDQERERPGPDTIVALDTEFVSLKQPEIQMNSDGERETIRPMSHALARVSVVRGQGENEGSAFIDDYIAIREPVVDYLTLYSGITASDLDPRTSKHNLVSLKTAYKKLWVLLNLGCKFLGHGLKQDFRVINIQVPRAQVIDTIEVFYLKSRLRKLSLAFLAWYLLKEDIQLETHDSIEDARTALKLYRKYLEFDDAGILEAMLEDIYKAGRATNFKPPRREDREKELQRQSTPPNSTAPNDCGAKPDGNGNENGGEPATPARKTGGITAPTFGAVNVFGTPSKASSPLPK
Protein: Actin, alpha cardiac muscle 1 (EC 3.6.4.-) (Alpha-cardiac actin) [Cleaved into: Actin, alpha cardiac muscle 1, intermediate form] (P68032)
Organism: Homo sapiens (Human)
Function: Actins are highly conserved proteins that are involved in various types of cell motility and are ubiquitously expressed in all eukaryotic cells.
Subcellular location: Cytoplasm, cytoskeleton.
Interaction partners:
- Tropomyosin alpha-1 chain
- Myosin-7
- Troponin T, cardiac muscle
- Tropomyosin alpha-3 chain
- Myosin-binding protein C, cardiac-type
- Troponin I, cardiac muscle
- Myosin light chain 3
- Myosin regulatory light chain 2, ventricular/cardiac muscle isoform
- Myosin-6
- Vitamin D-binding protein
Sequence:
MCDDEETTALVCDNGSGLVKAGFAGDDAPRAVFPSIVGRPRHQGVMVGMGQKDSYVGDEAQSKRGILTLKYPIEHGIITNWDDMEKIWHHTFYNELRVAPEEHPTLLTEAPLNPKANREKMTQIMFETFNVPAMYVAIQAVLSLYASGRTTGIVLDSGDGVTHNVPIYEGYALPHAIMRLDLAGRDLTDYLMKILTERGYSFVTTAEREIVRDIKEKLCYVALDFENEMATAASSSSLEKSYELPDGQVITIGNERFRCPETLFQPSFIGMESAGIHETTYNSIMKCDIDIRKDLYANNVLSGGTTMYPGIADRMQKEITALAPSTMKIKIIAPPERKYSVWIGGSILASLSTFQQMWISKQEYDEAGPSIVHRKCF
Protein: Protein phosphatase 1 regulatory inhibitor subunit 16B (CAAX box protein TIMAP) (TGF-beta-inhibited membrane-associated protein) (Q8VHQ3)
Organism: Mus musculus (Mouse)
Function: Regulator of protein phosphatase 1 (PP1) that acts as a positive regulator of pulmonary endothelial cell (EC) barrier function. Protects the endothelial barrier from lipopolysaccharide (LPS)-induced vascular leakage. Involved in the regulation of the PI3K/AKT signaling pathway (By similarity). Involved in the regulation of angiogenesis and endothelial cell proliferation through the control of ECE1 dephosphorylation, trafficking and activity (By similarity). Involved in the regulation of endothelial cell filopodia extension (By similarity). May be a downstream target for TGF-beta1 signaling cascade in endothelial cells (By similarity). Involved in PKA-mediated moesin dephosphorylation which is important in EC barrier protection against thrombin stimulation. Promotes the interaction of PPP1CA with RPSA/LAMR1 and in turn facilitates the dephosphorylation of RPSA/LAMR1 (By similarity). Involved in the dephosphorylation of EEF1A1 (By similarity).
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:Q96T49}. Cell membrane {ECO:0000305}; Lipid-anchor {ECO:0000305}. Nucleus {ECO:0000250|UniProtKB:Q96T49}. Cell projection {ECO:0000250|UniProtKB:Q96T49}. Note=Colocalizes with RPSA/LAMR1 in the cell membrane (By similarity). Localizes to the perinuclear region (By similarity). Colocalizes with PTEN at the tip of EC projections (By similarity). {ECO:0000250|UniProtKB:Q95N27, ECO:0000250|UniProtKB:Q96T49}.
Interaction partners:
- Serine/threonine-protein phosphatase PP1-beta catalytic subunit
Sequence:
MASHVDLLTELQLLEKVPTLERLRAAQKRRAQQLKKWAQYEQDLLHRKRKHERKRSTGGRRKKVSFEASVALLEASLRNDAEEVRYFLKNKVSPDLCNEDGLTALHQCCIDNFEEIVKLLLSHGANVNAKDNELWTPLHAAATCGHINLVKILVQYGADLLAVNSDGNMPYDLCEDEPTLDVIETCMAYQGITQEKINEMRAAPEQKMISDIHCMIAAGQDLDWIDGQGATLLHIAGANGYLRAAELLLDHGVRVDVKDWDGWEPLHAAAFWGQMPMAELLVSHGASLSARTSMDEMPIDLCEEEEFKVLLLELKHKHDVIMKSQLRHKSSLSRRTSSAGSRGKVVRRASLSDRTNLYRKEYEGEAILWQQRSAAEDQRTSTYNGDIRETRTDQENKDPNPRLEKPVLLSEFSTKISRGELDGPVENGLRAPVSTYQYALANGDIWKMHEMPDYSMAYGNPGVADVPPPWSGFKEQSPQTLLELKRQRAAAKLLSHPFLSTHLGSSVARSGESSSEGKAPLIGGRTSPYSSNGTSVYYTVTSGDPPLLKFKAPMEEMEEKVHGCCRIS
Protein: VIN3-like protein 2 (Vernalization5/VIN3-like protein 1) (Q9SUM4)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Maybe involved in both the vernalization and photoperiod pathways by regulating gene expression. Binds preferentially to dimethylated histone H3 'Lys-9' (H3K9me2). Promotes flowering in non-inductive photoperiods (e.g. short days) through the maintenance of the epigenetically repressed state of MAF5 via H3K9me2 and plant homeodomain / polycomb repressive complex 2 (PHD-PRC2)-dependent H3K27me3.
Subcellular location: Nucleus {ECO:0000250}. Note=Probably DNA-associated. {ECO:0000250}.
Interaction partners:
- Polycomb group protein VERNALIZATION 2
- Histone-binding protein MSI1
- VIN3-like protein 1
- Histone-lysine N-methyltransferase EZA1
- Polycomb group protein FERTILIZATION-INDEPENDENT ENDOSPERM
- Protein VERNALIZATION INSENSITIVE 3
- WD-40 repeat-containing protein MSI4
- PWWP domain-containing protein 1
- WD-40 repeat-containing protein MSI5
- PWWP domain-containing protein 2
Sequence:
MDSSLDGAAGDSSKCSEMSVDEKRQLVYELSKQSHLAAEVLQAWSRQEILQILCAEMGKERKYTGLTKVKIIETLLKIVSEKNSGECEGKKRDSDCLPIQRNTKRQRKVDNPSRYVIPATNIVTSNNASGSCSSVNTKGESTTIYCKNLACRAVLRQEDSFCRRCSCCICRKYDDNKDPSLWLTCSSDPPFEGESCGFSCHLECAFNTEKSGLGKDKQSEGCCFYCVSCGKANSLLECWKKQLTIAKETRRVEVLCYRLFLVQKLLKSSTKYRNLCEVVDEAVKTLEADVGPLTGLPMKMGRGIVNRLHSGPDVQKLCSSALESLETIATTPPDVAALPSPRSSKMQQDCSYVLSNEISADTATTGSTKIRFEDVNATSLTVVLASNEIPSPPNIVHYSIWHRKVPEKDYPEKSTCTLFIPNTRFVVSGLAPASEYCFKVVSYSGTREMGVDEINVLTRSAEEGANCSSAVERSVSPLTNCSTLSSNPSSVEAESNNDYIVPKKPSSKNEDNNSPSVDESAAKRMKRTTDSDIVQIEKDVEQIVLLDDEEQEAVLDKTESETPVVVTTKSLVGNRNSSDASLPITPFRSDEIKNRQARIEISMKDNCNNGDHSANGGTESGLEHCVKIIRQLECSGHIDKNFRQKFLTWYSLRATSQEIRVVKIFIDTFIDDPMALAEQLIDTFDDRVSIKRSAVGGSGASAVVPSGFCMKLWH
Protein: Cytochrome oxidase assembly protein SHY1 (SURF1 homolog of Yeast) (SURF1-like protein) (P53266)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Required for efficient assembly of cytochrome c oxidase in the mitochondrial inner membrane. Involved in a step that couples MSS51-COX14-dependent regulation of COX1 translation to early steps of cytochrome c oxidase assembly.
Subcellular location: Mitochondrion inner membrane {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:14576278, ECO:0000269|PubMed:9162072}; Multi-pass membrane protein {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:14576278, ECO:0000269|PubMed:9162072}.
Interaction partners:
- Heme A synthase COX15
- Protoheme IX farnesyltransferase, mitochondrial
- Cytochrome c oxidase assembly protein COX11
- Protein MSS51, mitochondrial
- Cytochrome c oxidase assembly factor 2
- Cytochrome c oxidase assembly factor 3, mitochondrial
- Cytochrome c oxidase subunit 6, mitochondrial
- Cytochrome c oxidase subunit 1
- Cytochrome c oxidase assembly protein COX14
- Cytochrome c oxidase assembly factor 1
Sequence:
MSLLGARSTYRWFSIAASIPTKNAIGKSTYLLASRNQQYRGIITSTVDWKPIKTGKSPNDDSRRERSFGKKIVLGLMFAMPIISFYLGTWQVRRLKWKTKLIAACETKLTYEPIPLPKSFTPDMCEDWEYRKVILTGHFLHNEEMFVGPRKKNGEKGYFLFTPFIRDDTGEKVLIERGWISEEKVAPDSRNLHHLSLPQEEHLKVVCLVRPPKKRGSLQWAKKDPNSRLWQVPDIYDMARSSGCTPIQFQALYDMKDHPIIEEHTRNEASQNNSTSSLWKFWKREPTTAVNGTQAVDNNTSKPRSRQEMPTDQTIEFDERQFIKAGVPIGRKPTIDLKNNHLQYLVTWYGLSFLSTIFLIVALRKAKRGGVVSQDQLMKEKLKHSRKYM
Protein: Protein phosphatase PhpP (EC 3.1.3.16) (PP2C-type phosphatase) (Ser/Thr phosphoprotein phosphatase) (STPP) (Q8KY51)
Organism: Streptococcus pneumoniae
Function: Protein phosphatase able to dephosphorylate StkP-P and a phosphothreonine residue in a phosphopeptide synthetic substrate. PhpP and its cognate protein kinase StkP appear to constitute a functional signaling couple in vivo, PhpP's primary role probably being to control phosphorylation levels of StkP and of its targets (which include LocZ, DivIVA and KhpB (also called EloR/Jag)). PhpP thus performs an essential control of StkP activity. Overexpression confers an stkP deletion-like phenotype.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:19502404, ECO:0000269|PubMed:22431591}. Note=Mainly localizes to the midcell division sites. PhpP and StkP interact within a membrane-associated protein complex facing the cytoplasm.
Interaction partners:
Sequence:
MEISLLTDVGQKRTNNQDYVNHYVNRAGRTMIILADGMGGHRAGNIASEMAVTDLGVAWVDTQIDTVNEVREWFAHYLEIENQKIHQLGQDEAYRGMGTTLEVLAIIDNQAIYAHIGDSRIGLIRGEEYHQLTSDHSLVNELLKAGQLTPEEAEAHPQKNIITQSIGQKDEIQPDFGTVILESGDYLLLDSDGLTNMISGSEIRDIVTSDIPLADKTETLVRFANNAGGLDNITVALVSMNEEDAE
Protein: Uncharacterized protein (Q57W86)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- NEDD8-activating enzyme E1 regulatory subunit
- Uncharacterized protein
Sequence:
MSVSAPTISAASREELVAYVKQLQQHLKEGEVKLMQIDKLEEEVETLKQKLEEKNGAVAALTEQSKMLSEMLVADEETKRILLLQMEESCVGGKTRECDSSITVSRASSALRAENNAQITPTGLKRAEANADKERTGMGEASLNPTALRSRNDEIAELEQKVRELTEVNSFYTAIVEHHDEEERVRADEGCCSTAIKAKVEGSVNLERLHERIGNLESERDNLRRLLRHNEREKENLNKELRDLREELSRLEIDVVAVEKWKVEECFAQCPAPVSLAIPGCGGSPVQGGDAVTSRTFAKVVTPIRYKGDGGKRIPKHLKRGPSVNAANEQYPLLTSPRQSRSLLQFDSLPEIHLLNPTRQEQMLLERVELYRRHVEEMSAHEVDRQRSFDEIEQARAELFTEMNFKLDEQRREIQRLNKEIALVTEGYSESRIQAKRSYHAEGTPKSAEVESLCSSETIFVPKGRAAELEVVPVGNEKNARSDSKNSIENKGVPSTGQSETAKIKHSGTLENKLFAPFEEGCPLSGSEWTWYHMDMVEKYERVDIAYKEQETFAGILMWNQIAVLSIASELMTRARGAQSEVSSLQTRLAEVQALVSSLEHQKESLVEELGRLREAHVNEPEDGGEGSTSFDVLKTNQQVFTQAVPLTEAWGPLLCVCDAYSEIVEGQIAVLRTLSEGEDATRIKGSEIKMNTASAAPPYRDVHLQGPETDANKPSGLVDTDGDEEFQMRLRGGNWLAFPPDSDVFPSDNTTKLHEATDDGTTGLGRGNAEALPKAPLATGPSQETYLSDNAHPPYRAKREIGCGVCAEAHGAPEGHVTQAPVTHQHLQSGPLSWGSFSNAITSEGCGDDGTGSRNTGQLKNALENLFCDANASQPATYQETREDNSCTFAAEFDPFA
Protein: Vacuole localized DSC protein 1 (P40570)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Component of the vacuole-localized DSC E3 ubiquitin ligase complex involved in the targeting of the complex to the vacuole membrane via the AP3 pathway to ubiquinate vacuolar membrane proteins. Competes with GLD1 to determine the subcellular localizations of the DSC complex.
Subcellular location: Vacuole membrane {ECO:0000269|PubMed:29355480}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Transmembrane E3 ubiquitin-protein ligase 1
- Golgi/endosome-localized DSC protein 1
- UBX domain-containing protein 3
- DSC E3 ubiquitin ligase complex subunit 3
- DSC E3 ubiquitin ligase complex subunit 2
Sequence:
MLHLEDDNGRQRSVIANLQKFVYCCLYLRFIKDGSLFLILLGWIISSLCDFIQELTLRYLKKNYLEVGRDNDQEDDESLAIRGLETPIVRMIINKAIRYYQGLILLETAYCIVYHIRLDVSRDICSKPYGFVIMLLIREFTCPVPTAFPSKLLLVLLDILLLFCQIVIINGSLSSSLQNVKLIVKELNAEEEGALNILKLNTWHMDATGPELIVLKNHDKSIPQQADGDDATEITPLLNIAE
Protein: eIF-4F 25 kDa subunit (Q9VSG1)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Eukaryotic translation initiation factor 4E-binding protein
- Polyadenylate-binding protein
- Eukaryotic translation initiation factor 4G1, isoform B
- Eukaryotic initiation factor 4A
- Eukaryotic initiation factor 4B
- ATP-dependent RNA helicase
- Cytoplasmic FMR1-interacting protein
- ATP-dependent RNA helicase me31b
- Eukaryotic translation initiation factor 5
- Eukaryotic translation initiation factor 4G2, isoform A
Sequence:
MVYTGYVSNGLQNAEETAWVPYGDPNDWSHGLAVYDGLELMSGNEEELQPSLNRVMKNIDYDLAMKHPLEHTWTLWHLENDRTKRWAEMLVDVTSFNTVEDFFSVYYFVKPPSDLKIFNDYMVFKKNIRPMWEDDTNKNGGRWILLLDKASRTYIDKMWHDLLLCMIGECFQHSDEICGVVINVRNKANKLSLWTKDSRNVEAILSIGRQIKELLHLGIMEIQYQVHKDAMVNHGPNVNAIYTL
Protein: Sodium/potassium-transporting ATPase subunit beta-2 (Adhesion molecule in glia) (AMOG) (Sodium/potassium-dependent ATPase subunit beta-2) (P14415)
Organism: Homo sapiens (Human)
Function: This is the non-catalytic component of the active enzyme, which catalyzes the hydrolysis of ATP coupled with the exchange of Na(+) and K(+) ions across the plasma membrane. The exact function of the beta-2 subunit is not known.
Subcellular location: Cell membrane; Single-pass type II membrane protein.
Interaction partners:
- Sodium/potassium-transporting ATPase subunit alpha-2
- Sodium/potassium-transporting ATPase subunit alpha-3
- Sodium/potassium-transporting ATPase subunit alpha-1
- Sodium/potassium-transporting ATPase subunit alpha-4
- Sodium/potassium-transporting ATPase subunit beta-1
- Sodium/potassium-transporting ATPase subunit gamma
- Sodium/potassium-transporting ATPase subunit beta-3
- Phospholemman
- cGMP-dependent protein kinase 1
- Protein ATP1B4
Sequence:
MVIQKEKKSCGQVVEEWKEFVWNPRTHQFMGRTGTSWAFILLFYLVFYGFLTAMFTLTMWVMLQTVSDHTPKYQDRLATPGLMIRPKTENLDVIVNVSDTESWDQHVQKLNKFLEPYNDSIQAQKNDVCRPGRYYEQPDNGVLNYPKRACQFNRTQLGNCSGIGDSTHYGYSTGQPCVFIKMNRVINFYAGANQSMNVTCAGKRDEDAENLGNFVMFPANGNIDLMYFPYYGKKFHVNYTQPLVAVKFLNVTPNVEVNVECRINAANIATDDERDKFAGRVAFKLRINKT
Protein: KxDL motif-containing protein 1 (Q9BQD3)
Organism: Homo sapiens (Human)
Function: As part of the BORC complex may play a role in lysosomes movement and localization at the cell periphery. Associated with the cytosolic face of lysosomes, the BORC complex may recruit ARL8B and couple lysosomes to microtubule plus-end-directed kinesin motor. May be involved in the biogenesis of lysosome-related organelles such as melanosomes (By similarity).
Subcellular location: Lysosome membrane {ECO:0000305|PubMed:25898167}.
Interaction partners:
- BLOC-1-related complex subunit 6
- BLOC-1-related complex subunit 5
- Biogenesis of lysosome-related organelles complex 1 subunit 2
- Biogenesis of lysosome-related organelles complex 1 subunit 1
- BLOC-1-related complex subunit 8
- BLOC-1-related complex subunit 7
- SNARE-associated protein Snapin
- Ubiquitin-ribosomal protein eS31 fusion protein
- Ubiquitin-ribosomal protein eL40 fusion protein
- Tropomyosin alpha-1 chain
Sequence:
MDLPDSASRVFCGRILSMVNTDDVNAIILAQKNMLDRFEKTNEMLLNFNNLSSARLQQMSERFLHHTRTLVEMKRDLDSIFRRIRTLKGKLARQHPEAFSHIPEASFLEEEDEDPIPPSTTTTIATSEQSTGSCDTSPDTVSPSLSPGFEDLSHVQPGSPAINGRSQTDDEEMTGE
Protein: AMSH-like protease sst2 (EC 3.4.19.-) (Suppressor of ste12 deletion protein 2) (Q9P371)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Zinc metalloprotease that specifically cleaves 'Lys-63'-linked polyubiquitin chains. Does not cleave 'Lys-48'-linked polyubiquitin chains (By similarity). Plays a role in the multivesicular body (MVB) sorting pathway. Required for ubiquitin-dependent sorting of proteins into the endosome and subsequent trafficking to the vacuole. May regulate MVB sorting through deubiquitination of ubiquitinated ESCRT proteins.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16823372}. Endosome {ECO:0000269|PubMed:16823372}.
Interaction partners:
- Polyubiquitin
- Ubiquitin-ribosomal protein eL40A fusion protein
- Ubiquitin-ribosomal protein eL40B fusion protein
- Ubiquitin-ribosomal protein eS31A fusion protein
- Ubiquitin-ribosomal protein eS31B fusion protein
- Class E vacuolar protein-sorting machinery protein hse1
- Probable ubiquitin carboxyl-terminal hydrolase 4
- Vacuolar protein sorting-associated protein 24
- 26S proteasome regulatory subunit rpn7
- Probable 26S proteasome regulatory subunit rpn9
Sequence:
MNILQGSEAPLSYEEIASRAGAFDFNKNIPLKNWLRTSTTISKQAHVYVSEHDYSNGVFLLFRYCELFMKCQKHPDAAAYKKELFDYYQGVRNALEEIELIKPIVKEQYEQYQCQKNDLDDLKKLSMKDSQPSLEKPVSYVDEPILEQWALSDLQILPPSSTDLLSPDSQKLSKSSSDLPQFDYPSLNSSPTFNSNLPISSSRFEKTSLSDSKLVSPEPLDDNKDIQFIKKPIYTRTSEPRPKPAGTFKIHAYTEGGKPLRTIYLPKLLKKVFLDVVKPNTKKNLETCGILCGKLRQNAFFITHLVIPLQEATSDTCGTTDEASLFEFQDKHNLLTLGWIHTHPTQTCFMSSVDLHTHCSYQLMLPEAIAIVMAPSKNTSGIFRLLDPEGLQTIVKCRKPGLFHPHEGKVYTMVAQPGHVREINSKLQVVDLRVK
Protein: Vacuolar protein sorting-associated protein 35 (G3V8A5)
Organism: Rattus norvegicus (Rat)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004170}; Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004170}.
Interaction partners:
- Vacuolar protein sorting-associated protein 26A
- VPS26 retromer complex component B
- Vacuolar protein sorting-associated protein 29
- Sorting nexin-2
- Sorting nexin-1
- Sorting nexin-3
- Sorting nexin-5
- TBC1 domain family member 5
- Sorting nexin
- WASH complex subunit 2
Sequence:
MPTTQQSPQDEQEKLLDEAIQAVKVQSFQMKRCLDKNKLMDALKHASNMLGELRTSMLSPKSYYELYMAISDELHYLEVYLTDEFAKGRKVADLYELVQYAGNIIPRLYLLITVGVVYVKSFPQSRKDILKDLVEMCRGVQHPLRGLFLRNYLLQCTRNILPDEGEPTDEETTGDISDSMDFVLLNFAEMNKLWVRMQHQGHSRDREKRERERQELRILVGTNLVRLSQLEGVNVERYKQIVLTGILEQVVNCRDALAQEYLMECIIQVFPDEFHLQTLNPFLRACAELHQNVNVKNIIIALIDRLALFAHREDGPGIPAEIKLFDIFSQQVATVIQSRQDMPSEDVVSLQVSLINLAMKCYPDRVDYVDKVLETTVEIFNKLNLEHIATSSAVSKELTRLLKIPVDTYNNILTVLKLKHFHPLFEYFDYESRKSMSCYVLSNVLDYNTEIVSQDQVDSIMNLVSTLIQDQPDQPVEDPDPEDFADEQSLVGRFIHLLRSEDPDQQYLILNTARKHFGAGGNQRIRFTLPPLVFAAYQLAFRYKENSQMDDKWEKKCQKIFSFAHQTISALIKAELAELPLRLFLQGALAAGEIGFENHETVAYEFMSQAFSLYEDELSDSKAQLAAITLIIGTFERMKCFSEENHEPLRTQCALAASKLLKKPDQGRAVSTCAHLFWSGRNTDKNGEELHGGKRVMECLKKALKIANQCMDPSLQVQLFIEILNRYIYFYEKENDAVTIQVLNQLIQKIREDLPNLESSEETEQINKHFHNTLEHLRSRRESPESEGPIYEGLIL
Protein: Isoprimeverose transporter (Isoprimeverose cation symporter) (P96792)
Organism: Lactiplantibacillus pentosus (Lactobacillus pentosus)
Function: Involved in the metabolism of isoprimeverose. Transports isoprimeverose into the cell. Transport is driven by the proton motive force generated by malolactic fermentation. Cannot transport D-xylose.
Subcellular location: Cell membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Alpha-xylosidase XylQ
- Xylose repressor
Sequence:
MSVSMQHHSSEASPATQPASVIHKNMVPWSERFSYSLSDFACNLSFSLVSTYLMFFYTDVFGISAAIVGTLFLVARIVDAFDGPFWGIMIDHTHTRWGKSRPYWLWFAIPFAVFSVLCFTVPNMSTGMKVVWAYVTYIGVDVLYSAVNIPITSILPSLTSNPQERVTLSTIRQFMGTLGATIISTIALPLVAYFGGGSTSSAHGWFMVALIMAVIAMVIFFIVFANTKERVQTVQSKKSIPIKTSLKALKRNWPWVIVIFINFIYWLGMQTRSQVTVYFFKYNMHDATLASFILGLQLVALLAVVITPWTAKRIGKRNTMLMGMLLAIVGQLILWGGSKALNVPTITVGTIVGYLGTGFVSGLIAVMLADSVDYGEWKNGVRAEGIVTSFSSFSAKFGMGIGGAVTGLILSAGGYVANHAQSAQALNAIEMNYVWVPIVGFGLSAIALLFYKVDKIEPKMLADLEQKHAQENALADDQK
Protein: Ribulose bisphosphate carboxylase small subunit (RuBisCO small subunit) (P54206)
Organism: Synechocystis sp. (strain ATCC 27184 / PCC 6803 / Kazusa)
Function: RuBisCO catalyzes two reactions: the carboxylation of D-ribulose 1,5-bisphosphate, the primary event in carbon dioxide fixation, as well as the oxidative fragmentation of the pentose substrate in the photorespiration process. Both reactions occur simultaneously and in competition at the same active site. Although the small subunit is not catalytic it is essential for maximal activity.
Subcellular location: Carboxysome {ECO:0000255|HAMAP-Rule:MF_00859, ECO:0000269|PubMed:17993516}. Note=This cyanobacterium makes beta-type carboxysomes. RuBisCO associates with both the internal and shell portion of carboxysomes (PubMed:17993516). In the carboxysome RuBisCO is organized into a paracrystalline array (By similarity). {ECO:0000250|UniProtKB:Q31NB2, ECO:0000269|PubMed:17993516}.
Interaction partners:
- Ribulose bisphosphate carboxylase large chain
- Carboxysome assembly protein CcmM
- Phosphoribulokinase
- RuBisCO chaperone RbcX
- Phosphoglycerate kinase
- Phosphoglycolate phosphatase
- Slr0458 protein
- Slr1762 protein
- Carboxysome assembly protein CcmN
- Slr0697 protein
Sequence:
MKTLPKERRYETLSYLPPLTDQQIAKQVEFLLDQGFIPGVEFEEDPQPETHFWTMWKLPFFGGATANEVLAEVRECRSENPNCYIRVIGFDNIKQCQTVSFIVHKPNQNQGRY
Protein: Probable sugar phosphate/phosphate translocator At3g17430 (Q9LRP2)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
- KH domain-containing protein At4g26480
- Pentatricopeptide repeat-containing protein At4g19440
- Probable RNA methyltransferase At5g51130
- Cationic amino acid transporter 1
- K
Sequence:
MAKMINKTLVLTYIYLLIYIILSSGVILYNKWVLSPKYFNFPLPITLTMIHMGFAGFVAFLLIRVFKVVAPVKMTFEIYATCVVPISAFFASSLWFGNTAYLHISVAFIQMLKALMPVATFIMAVVCGTDKPRCDVFSNMLLVSVGVVISSYGEIHFNIVGTVYQVTGIFAEALRLVLTQVLLQKKGLTLNPITSLYYIAPCSFVFLALPWYVLEKPTMEVSQIQFNFWIFFSNALCALALNFSIFLVIGRTGAVTIRVAGVLKDWILIALSTVIFPESTITGLNITGYAIALCGVVMYNYIKVRDVKASQPTADSLPDRINKEYKMEKKSSDKFNPNDSVEIPRVGGEVNDEEAPLITSRLSHIGRTQLGNHAA