wanglab/gogpt-training-data huggingface dataset:
Protein: Mitochondrial import inner membrane translocase subunit TIM50 (Q38EV9)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Mitochondrion inner membrane {ECO:0000256|RuleBase:RU365079}; Single-pass membrane protein {ECO:0000256|RuleBase:RU365079}.
Interaction partners:
Sequence:
MVRTTRFSRNSSKPLFQQLQLITSYGLFQEYPPIWSLPLPPQQPRDTGKPTLVLDIDETLIHTVGMRNEGSDSVSFSFFLRPHAKEFLAEVRELYEVVFWTAGTASYCSAVMDALEVQVLQLPRSFYNIDELRVEARGGISTKNVNFYALSRTQTLQGHNYMKYLPMLGRPLNRVIMVDDNVRSFPLHPRNGVKIEPFLPNERVLSEYARIVTDEVKYGQVGQRQYEGEMAKVIECGEEEVARLQADHALMDLIPMLRSAASSTDLTHELDHWRTDEYTKCDDFRETMNSLSVTRQKILGNVLKERRNVPIPPLKQHVMNHGFMEEANAAMKLEQMRHTPSRL
Protein: Rhodanese-like domain-containing protein 9, chloroplastic (Sulfurtransferase 9) (AtStr9) (O48529)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Plastid, chloroplast {ECO:0000305}. Membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}.
Interaction partners:
- Rhodanese-like domain-containing protein 8, chloroplastic
- Rhodanese-like domain-containing protein 7
- Rhodanese-like domain-containing protein 6
- Dual specificity phosphatase Cdc25
- 3-dehydroquinate synthase, chloroplastic
Sequence:
MAGIISPSPTALYFTSNVGGRRLKAVSWAGKSVSGNVIRRRSLRIAAELKFVNAEEAKQLIAEEGYSVVDVRDKTQFERAHIKSCSHIPLFIYNEDNDIGTIIKRTVHNNFSGLFFGLPFTKVNPEFLKSVRNEFSQDSKLLLVCQEGLRSAAAASRLEEAGYENIACVTSGLQSVKPGTFESVGSTELQNAGKAGLITIQGKISAVLGTVLVCAYLFIQFFPDQAEKLFPPTS
Protein: MiRP K channel accessory Subunit (MiRP5) (G5ECI4)
Organism: Caenorhabditis elegans
Interaction partners:
Sequence:
MSTSTQRPPAPTSGSSSTPWTKVVIFIIIGILIVAFIVFAAASIVKYIKSKKQQKQPKKKTKKSTKSRSKSLKSKQSAVTPKKRASPIPPQPAPPSSPKPTEESATPSSSFAPSTEPTPTVPDKVDDGSEDTEHKEQEQQTVLCTYGNGWKSKNQPPHDFSFSIESE
Protein: Zinc finger MYND-type containing 8 (A0A087WYS3)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MDISTRSKDPGSAERTAQKRKFPSPPHSSNGHSPQDTSTSPIKKKKKPGLLNSNNKEQSELRHGPFYYMKQPLTTDPVDVVPQDGRNDFYCWVCHREGQVLCCELCPRVYHAKCLRLTSEPEGDWFCPECEKITVAECIETQSKAMTMLTIEQLSYLLKFAIQKMKQPGTDAFQKPVPLEQHPDYAEYIFHPMDLCTLEKNAKKKMYGCTEAFLADAKWILHNCIIYNGGNHKLTQIAKVVIKICEHEMNEIEVCPECYLAACQKRDNWFCEPCSNPHPLVWAKLKGFPFWPAKALRDKDGQVDARFFGQHDRAWVPINNCYLMSKEIPFSVKKTKSIFNSAMQEMEVYVENIRRKFGVFNYSPFRTPYTPNSQYQMLLDPTNPSAGTAKIDKQEKVKLNFDMTASPKILMSKPVLSGGTGRRISLSDMPRSPMSTNSSVHTGSDVEQDAEKKATSSHFSASEESMDFLDKSTASPASTKTGQAGSLSGSPKPFSPQLSAPITTKTDKTSTTGSILNLNLDRSKAEMDLKELSESVQQQSTPVPLISPKRQIRSRFQLNLDKTIESCKAQLGINEISEDVYTAVEHSDSEDSEKSDSSDSEYISDDEQKSKNEPEDTEDKEGCQMDKEPSAVKKKPKPTNPVEIKEELKSTSPASEKADPGAVKDKASPEPEKDFSEKAKPSPHPIKDKLKGKDETDSPTVHLGLDSDSESELVIDLGEDHSGREGRKNKKEPKEPSPKQDAVQQKEITQSPSTSTITLVTSTQSSPLVTSSGSMSTLVSSVNADLPIATASADVAADIAKYTSKMMDAIKGTMTEIYNDLSKNTTGSTIAEIRRLRIEIEKLQWLHQQELSEMKHNLELTMAEMRQSLEQERDRLIAEVKKQLELEKQQAVDETKKKQWCANCKKEAIFYCCWNTSYCDYPCQQAHWPEHMKSCTQSATAPQQEADAEVNTETLNKSSQGSSSSTQSAPSETASASKEKETSAEKSKESGSTLDLSGSRETPSSILLGSNQGSVSKRCDKQPAYAPTTTDHQPHPNYPAQKYHSRSNKSSWSSSDEKRGSTRSDHNTSTSTKSLLPKESRLDTFWD
Protein: Sodium-dependent noradrenaline transporter (Norepinephrine transporter) (NET) (Solute carrier family 6 member 2) (O55192)
Organism: Mus musculus (Mouse)
Function: Mediates sodium- and chloride-dependent transport of norepinephrine (also known as noradrenaline). Can also mediate sodium- and chloride-dependent transport of dopamine (By similarity).
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:P23975}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Synaptic vesicular amine transporter
- Tyrosine 3-monooxygenase
- Dopamine beta-hydroxylase
- Amine oxidase [flavin-containing] A
- Catechol O-methyltransferase
- Alpha-2A adrenergic receptor
Sequence:
MLLARMNPQVQPELGGADPLPEQPLRPCKTADLLVVKERNGVQCLLASQDSDAQPRETWGKKIDFLLSVVGFAVDLANVWRFPYLCYKNGGGAFLIPYTLFLIIAGMPLFYMELALGQYNREGAATVWKICPFFKGVGYAVILIALYVGFYYNVIIAWSLYYLFASFTLNLPWTNCGHSWNSPNCTDPKLLNASVLGDHTKYSKYKFTPAAEFYERGVLHLHESSGIHDIGLPQWQLLLCLMVVIVVLYFSLWKGVKTSGKVVWITATLPYFVLFVLLVHGVTLPGASNGINAYLHIDFYRLKEATVWIDAATQIFFSLGAGFGVLIAFASYNKFDNNCYRDALLTSTINCVTSFISGFAIFSILGYMAHEHKVNIEDVATEGAGLVFILYPEAISTLSGSTFWAVLFFLMLLALGLDSSMGGMEAVITGLADDFQVLKRHRKLFTCVVTISTFLLALFCITKGGIYVLTLLDTFAAGTSILFAVLMEAIGVSWFYGVDRFSNDIQQMMGFKPGLYWRLCWKFVSPAFLLFVVVVSIINFKPLTYDDYTYPPWANWVGWGIALSSMILVPAYVIYKFLSIRGSLWERVAYGITPENEHHLVAQRDVRQFQLRHWLAI
Protein: 11-beta-hydroxysteroid dehydrogenase 1 (11-DH) (11-beta-HSD1) (EC 1.1.1.146) (7-oxosteroid reductase) (EC 1.1.1.201) (Corticosteroid 11-beta-dehydrogenase isozyme 1) (Q7M3I4)
Organism: Oryctolagus cuniculus (Rabbit)
Function: Controls the reversible conversion of biologically active glucocorticoids such as cortisone to cortisol, and 11-dehydrocorticosterone to corticosterone in the presence of NADP(H). Participates in the corticosteroid receptor-mediated anti-inflammatory response, as well as metabolic and homeostatic processes (By similarity). Plays a role in the secretion of aqueous humor in the eye, maintaining a normotensive, intraocular environment (By similarity). Bidirectional in vitro, predominantly functions as a reductase in vivo, thereby increasing the concentration of active glucocorticoids (By similarity). It has broad substrate specificity, besides glucocorticoids, it accepts other steroid and sterol substrates. It has broad substrate specificity, besides glucocorticoids, it accepts other steroid and sterol substrates. Interconverts 7-oxo- and 7-hydroxy-neurosteroids such as 7-oxopregnenolone and 7beta-hydroxypregnenolone, 7-oxodehydroepiandrosterone (3beta-hydroxy-5-androstene-7,17-dione) and 7beta-hydroxydehydroepiandrosterone (3beta,7beta-dihydroxyandrost-5-en-17-one), among others (By similarity). Catalyzes the stereo-specific conversion of the major dietary oxysterol, 7-ketocholesterol (7-oxocholesterol), into the more polar 7-beta-hydroxycholesterol metabolite (By similarity). 7-oxocholesterol is one of the most important oxysterols, it participates in several events such as induction of apoptosis, accumulation in atherosclerotic lesions, lipid peroxidation, and induction of foam cell formation (By similarity). Mediates the 7-oxo reduction of 7-oxolithocholate mainly to chenodeoxycholate, and to a lesser extent to ursodeoxycholate, both in its free form and when conjugated to glycine or taurine, providing a link between glucocorticoid activation and bile acid metabolism (By similarity). Catalyzes the synthesis of 7-beta-25-dihydroxycholesterol from 7-oxo-25-hydroxycholesterol in vitro, which acts as ligand for the G-protein-coupled receptor (GPCR) Epstein-Barr virus-induced gene 2 (EBI2) and may thereby regulate immune cell migration (By similarity).
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:7836463}; Single-pass type II membrane protein {ECO:0000269|PubMed:7836463}. Microsome membrane {ECO:0000269|PubMed:7836463}; Single-pass type II membrane protein {ECO:0000269|PubMed:7836463}.
Interaction partners:
- 11-beta-hydroxysteroid dehydrogenase type 2
- 17beta-estradiol 17-dehydrogenase
- Glucocorticoid receptor
- Steroid 17-alpha-hydroxylase/17,20 lyase
- Mineralocorticoid receptor
- Scavenger receptor class B member 1
- GDH/6PGL endoplasmic bifunctional protein
Sequence:
MAFMKKYLLPLLGLFLAYYYYSANEEFRPEMLQGKKVIVTGASKGIGKEIAFHLAKMGAHVVVTARSKETLQEVVAHCLKLGAASAHYIAGTMEDMTFAEQFVAKAGKLMGGLDMLILNHITNASLMFFNNDIHHVRKEMEVNFLSYVVLTVAALPMLKQSNGSIVVVSSLAGKIAHPLIAPYSASKFALDGFFSAIRKEHALTNVNVSITLCVLGLIDTDTAMKEVSGKIDMKAAPKEECALEIIKGGALRQDEVYYGNLQWTPLLLGNPGKRLIEFLHLRKFDISKLVNN
Protein: Probable beta-glucosidase A (EC 3.2.1.21) (Beta-D-glucoside glucohydrolase A) (Cellobiase A) (Gentiobiase A) (Q2UUD6)
Organism: Aspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold)
Function: Beta-glucosidases are one of a number of cellulolytic enzymes involved in the degradation of cellulosic biomass. Catalyzes the last step releasing glucose from the inhibitory cellobiose (By similarity).
Subcellular location: Secreted {ECO:0000250}.
Interaction partners:
- Xylanolytic transcriptional activator xlnR
- Endo-beta-1,4-glucanase celB
- Probable glucan endo-1,3-beta-glucosidase eglC
- Probable 1,4-beta-D-glucan cellobiohydrolase A
- Probable beta-glucosidase I
- Glucanase
- Probable endo-beta-1,4-glucanase B
- cellulase
- Glucanase
- beta-glucosidase
Sequence:
MKLGWIEVAALAAASVVSAKDDLAYSPPFYPSPWADGQGEWAEVYKRAVDIVSQMTLTEKVNLTTGTGWQLERCVGQTGSVPRLNIPSLCLQDSPLGIRFSDYNSAFPAGVNVAATWDKTLAYLRGQAMGEEFSDKGIDVQLGPAAGPLGAHPDGGRNWEGFSPDPALTGVLFAETIKGIQDAGVIATAKHYIMNEQEHFRQQPEAAGYGFNVSDSLSSNVDDKTMHELYLWPFADAVRAGVGAVMCSYNQINNSYGCENSETLNKLLKAELGFQGFVMSDWTAHHSGVGAALAGLDMSMPGDVTFDSGTSFWGANLTVGVLNGTIPQWRVDDMAVRIMAAYYKVGRDTKYTPPNFSSWTRDEYGFAHNHVSEGAYERVNEFVDVQRDHADLIRRIGAQSTVLLKNKGALPLSRKEKLVALLGEDAGSNSWGANGCDDRGCDNGTLAMAWGSGTANFPYLVTPEQAIQNEVLQGRGNVFAVTDSWALDKIAAAARQASVSLVFVNSDSGEGYLSVDGNEGDRNNITLWKNGDNVVKTAANNCNNTVVIIHSVGPVLIDEWYDHPNVTGILWAGLPGQESGNSIADVLYGRVNPGAKSPFTWGKTRESYGSPLVKDANNGNGAPQSDFTQGVFIDYRHFDKFNETPIYEFGYGLSYTTFELSDLHVQPLNASRYTPTSGMTEAAKNFGEIGDASEYVYPEGLERIHEFIYPWINSTDLKASSDDSNYGWEDSKYIPEGATDGSAQPRLPASGGAGGNPGLYEDLFRVSVKVKNTGNVAGDEVPQLYVSLGGPNEPKVVLRKFERIHLAPSQEAVWTTTLTRRDLANWDVSAQDWTVTPYPKTIYVGNSSRKLPLQASLPKAQ
Protein: WD repeat-containing protein LWD1-like (WD-repeat protein GhTTG4) (Q8LJS9)
Organism: Gossypium hirsutum (Upland cotton) (Gossypium mexicanum)
Interaction partners:
- DNA damage-binding protein 1
- DNA damage-binding protein 1a-like
- DNA excision repair protein ERCC-8-like
- DNA excision repair protein ERCC-8-like
- WD-40 repeat-containing protein MSI1
- WD-40 repeat-containing protein MSI1-like
- Denticleless protein homolog
- Denticleless protein homolog
- Denticleless protein homolog A-like isoform X1
- Denticleless protein homolog isoform X1
Sequence:
MTATSDPNPEVSDEQQKRSEIYTYEAPWYIYAMNWSVRRDKKYRLAIASLLEQYPNRLQIVQLDDSNGEIRSDPNLSFDHPYPATKTIFIPDKDCQKPDLLATSSDFLRIWRISDDGSRVDLKSLLNGNKNSEFCGPLTSFDWNEAEPKRIGTSSIDTTCTIWDIEKETVDTQLIAHDKEVYDIAWGGVGVFASVSADGSVRVFDLRDKEHSTIIYESSEPDAPLVRLGWNKQDPRYMATIIMDSAKVVVLDIRFPTLPVVELRRHQASVNAVAWAPHSSCHICTAGDDSQALIWDLSSMGQPVKGGLDPILAYTAGAEIEQLQWSSSQPDWVAIAFSTKLQILRV
Protein: cDNA FLJ59090, highly similar to Vacuolar ATP synthase subunit d (B7Z788)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MVVEFRHMRNHAYEPLASFLDFITYSYMIDNVILLITGTLHQRSIAELVPKCHPLGSFEQMEAVNIAQTPAELYNAILVDTPLAAFFQDCISEQDLDEMNIEIIRNTLYKAYLESFYKFCTLLGGTTADAMCPILEFEADRRAFIITINSFGTELSKEDRAKLFPHCGRLHPEGLAQLARADDYEQVKNVADYYPEYKLLFEGAGSNPGDKTLEDRFFEHEVKLNKLAFLNQFHFGVFYAFVKLKEQECRNIVWIAECIAQRHRAKIDNYIPIF
Protein: Methionine-R-sulfoxide reductase B2, mitochondrial (MsrB2) (EC 1.8.4.12) (EC 1.8.4.14) (Q9Y3D2)
Organism: Homo sapiens (Human)
Function: Methionine-sulfoxide reductase that specifically reduces methionine (R)-sulfoxide back to methionine. While in many cases, methionine oxidation is the result of random oxidation following oxidative stress, methionine oxidation is also a post-translational modification that takes place on specific residue. Upon oxidative stress, may play a role in the preservation of mitochondrial integrity by decreasing the intracellular reactive oxygen species build-up through its scavenging role, hence contributing to cell survival and protein maintenance.
Subcellular location: Mitochondrion {ECO:0000269|PubMed:18424444, ECO:0000269|PubMed:25078755}.
Interaction partners:
- Mitochondrial peptide methionine sulfoxide reductase
- Thioredoxin
- Cystathionine beta-synthase-like protein
- Cystathionine beta-synthase
Sequence:
MARLLWLLRGLTLGTAPRRAVRGQAGGGGPGTGPGLGEAGSLATCELPLAKSEWQKKLTPEQFYVTREKGTEPPFSGIYLNNKEAGMYHCVCCDSPLFSSEKKYCSGTGWPSFSEAHGTSGSDESHTGILRRLDTSLGSARTEVVCKQCEAHLGHVFPDGPGPNGQRFCINSVALKFKPRKH
Protein: Vitamin B12 import system permease protein BtuC (P06609)
Organism: Escherichia coli (strain K12)
Function: Part of the ABC transporter complex BtuCDF involved in vitamin B12 import. Involved in the translocation of the substrate across the membrane.
Subcellular location: Cell inner membrane; Multi-pass membrane protein.
Interaction partners:
- Vitamin B12 import ATP-binding protein BtuD
- Vitamin B12-binding protein
- Iron
- Maltose/maltodextrin transport system permease protein MalG
- Iron
- Thioredoxin/glutathione peroxidase BtuE
- Fe
- Maltose/maltodextrin import ATP-binding protein MalK
- Ribose import permease protein RbsC
- Vitamin B12 transporter BtuB
Sequence:
MLTLARQQQRQNIRWLLCLSVLMLLALLLSLCAGEQWISPGDWFTPRGELFVWQIRLPRTLAVLLVGAALAISGAVMQALFENPLAEPGLLGVSNGAGVGLIAAVLLGQGQLPNWALGLCAIAGALIITLILLRFARRHLSTSRLLLAGVALGIICSALMTWAIYFSTSVDLRQLMYWMMGGFGGVDWRQSWLMLALIPVLLWICCQSRPMNMLALGEISARQLGLPLWFWRNVLVAATGWMVGVSVALAGAIGFIGLVIPHILRLCGLTDHRVLLPGCALAGASALLLADIVARLALAAAELPIGVVTATLGAPVFIWLLLKAGR
Protein: AP complex subunit sigma (Q19123)
Organism: Caenorhabditis elegans
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004236}. Membrane, coated pit {ECO:0000256|ARBA:ARBA00004277}; Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004277}; Cytoplasmic side {ECO:0000256|ARBA:ARBA00004277}.
Interaction partners:
- AP-2 complex subunit alpha
- AP-2 complex subunit mu
- AP complex subunit beta
- FCH domain only protein 2
- Intersectin-1
- Probable clathrin heavy chain 1
- AP-1 complex subunit gamma
- EHS-1
- AP-3 complex subunit delta
- NECAP PHear domain-containing protein
Sequence:
MIRFILIQNRAGKTRLAKWYMHFDDDEKQKLIEEVHACVTVRDAKHTNFVEFRNFKIVYRRYAGLYFCICVDITDNNLYYLEAIHNFVEVLNEYFHNVCELDLVFNFYKVYTVVDEMFLAGEIRETSQTKVLKQLLMLTSLE
Protein: Kinesin-like protein (Q9XU12)
Organism: Caenorhabditis elegans
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000256|ARBA:ARBA00004245}.
Interaction partners:
- Cytosolic carboxypeptidase 6
- Aurora kinase
- Calponin-homology
- Aurora/IPL1-related protein kinase 2
- Kinesin-like protein
- Kinesin motor domain-containing protein
- Patronin
- Meiotic spindle formation protein mei-1
- Protein regulator of cytokinesis 1
- Protein CLASP-2
Sequence:
MKSCRSCKENPEVQRKRAEKPWRRAPKAKSEVEKHGIGPPDSDSGEEISFPWYNVTGKMLVVGMHVEIKRSDGRIHGAVIAEVKSNGRFMVEWYEKGETKGKESSLEELLTLNPSLQAPKPTPPPQPPQKTLQASTAVNRQNGIHAQSMILDDEDTFLLDHINMIPAKGASANKRPTGAFTQHVPVRMAPPSEKPLPTRRAPSPKEDAAPAPKSTRTTAAFKPDLDSTAITVPKHTARRTVVVAPAPAPVPAPPIANMTSQRAPSPVARVPSPKNVPRSYPQQDVQPSNGNFAFAEMIRNYRAQIDYRPLSMFDGVNENRISVCVRKRPLNKKELTKAEVDVITIPSRDITILHQPQTRVDLTKYLDNQKFRFDYSFDEYANNELVYRFTAAPLVKTVFDNGTATCFAYGQTGSGKTHTMGGDFSGKKQNASMGIYALTARDVFRMLEQPQYRRKDLSVHCAFFEIYGTKTYDLLNDKAELRVLEDKMQKVQVVGLKEEQAHNEQDVLELINKGTLVRTAGTTSANANSSRSHAIFQIILRQGKKVWGKFSLIDLAGNERGQDTRECDRDTRKEGANINTSLLALKECIRGMARNSSHVPFRQSKLTMVLRDSFIGEKSRTVMISMISPGISSSDHTLNTLRYADRVKEMGTDGSGEATPIRDEELFLPPSADKSDEEYDEMVEKQEHRRVAVDHVRNLKDMSEKIIRETTIVLSNEPSAAQKAECLAKLDQLAQIVSNTRVAVENV
Protein: Figainin 2 (Br22) (A0A2L2DDD0)
Organism: Boana raniceps (Chaco tree frog) (Hyla roeschmanni)
Function: Antimicrobial peptide that displays antibacterial, antiprotozoal, and antiviral activity. Exhibits antibacterial activity against the Gram-positive bacteria S.epidermidis ATCC 12228 (MIC=4 uM), E.casseliflavus ATCC 700327 (MIC=4 uM), S.aureus ATCC 25923 (MIC=8 uM) and E.faecalis ATCC 29212 (MIC=8 uM), and the Gram-negative bacteria E.coli ATCC 25922 (MIC=8 uM), K.pneumoniae ATCC 13883 (MIC=8 uM), the multi-resistant clinical isolate strain K.pneumoniae carbapanemase (KPC) MR (MIC=16 uM), and P.aeruginosa ATCC 27853 (MIC=32 uM). Displays antiprotozoal activity against the epimastigote form of T.cruzi (IC(50)=6.32 uM). Does not show antimicrobial against the fungi C.albicans ATCC 90028 and C.parapsilosis ATCC 22019. Displays antiviral activity against the human viruses chikungunya (EC(50)=17.9 uM), Dengue serotype 4 (EC(50)=20.8 uM) and Yellow Fever (EC(50)=21.8 uM). Shows moderate cytolytic activity against human erythrocytes (HC(50)=48.9 uM), and activates the oxidative burst in human neutrophils. Also displays anti-proliferative effects against MCF-7 breast cancer cells (IC(50)=15.3 uM) and B16F10 murine melanoma cells (IC(50)=12.8 uM).
Subcellular location: Secreted {ECO:0000269|PubMed:32443921}.
Interaction partners:
Sequence:
MAFLKKSLFLVLFLGIVSLSVCEEEKREGEEKEEKREEEEGKEENEDGNEEHKEKRFLGAILKIGHALAKTVLPMVTNAFKPKQ
Protein: Mimecan (Osteoglycin) (B4DI63)
Organism: Homo sapiens (Human)
Subcellular location: Secreted, extracellular space, extracellular matrix {ECO:0000256|ARBA:ARBA00004498}.
Interaction partners:
Sequence:
MLAKISTTWKLFLKLLGPEILLSSLKSRHSFSHSPSHLGLMHRHEHLLRKTTKNFKTATTTLQSTLLLLLLVPLIKPAPPTQQDSRIIYDYGTDNFEESIFSQDYEDKYLDGKNIKEKETVIIPNEKSLQLQKDEAITPLPPKKENDEMPTCLLCVCLSGSVYCEEVDIDAVPPLPKESAYLYARFNKIKKLTAKDFADIPNLRRLDFTGNLIEDIEDGTFSKLSLLEELSLAENQLLKLPVLPPKLTLFNAKYNKIKSRGIKANAFKKLNNLTFLYLDHNALESVPLNLPESLRVIHLQFNNIASITDDTFCKANDTSYIRDRIEEIRLEGNPIVLGKHPNSFICLKRLPIGSYF
Protein: Synaptotagmin-3 (Synaptotagmin III) (SytIII) (O35681)
Organism: Mus musculus (Mouse)
Function: Ca(2+) sensor involved in Ca(2+)-dependent exocytosis of secretory vesicles through Ca(2+) and phospholipid binding to the C2 domain. Ca(2+) induces binding of the C2-domains to phospholipid membranes and to assembled SNARE-complexes; both actions contribute to triggering exocytosis. Plays a role in dendrite formation by melanocytes.
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:P40748}; Single-pass membrane protein {ECO:0000255}. Cytoplasmic vesicle, secretory vesicle membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000255}.
Interaction partners:
Sequence:
MSGDYEDDLCRRALILVSDLCARVRDADTNDRCQEFNELRIRGYPRGPDADISVSLLSVIVTFCGIVLLGVSLFVSWKLCWVPWRDKGGSAVGGGPLRKDLAPGVGLAGLVGGGGHHLGASLGGHPLLGGPHHHGHTAHHPPFAELLEPGGLGGSEPPEPSYLDMDSYPEAAVASVVAAGVKPSQTSPELPSEGGTGSGLLLLPPSGGGLPSAQSHQQVTSLAPTTRYPALPRPLTQQTLTTQADPSTEERPPALPLPLPGGEEKAKLIGQIKPELYQGTGPGGRRGGGSGEAGAPCGRISFALRYLYGSDHLVVRILQALDLPAKDSNGFSDPYVKIYLLPDRKKKFQTKVHRKTLNPIFNETFQFSVPLAELAQRKLHFSVYDFDRFSRHDLIGQVVLDNLLELAEQPPDRPLWRDILEGGSEKADLGELNFSLCYLPTAGRLTVTIIKASNLKAMDLTGFSDPYVKASLISEGRRLKKRKTSIKKNTLNPTYNEALVFDVAPESVENVGLSIAVVDYDCIGHNEVIGVCRVGPEAADPHGREHWAEMLANPRKPVEHWHQLVEEKTLSSFTKGGKGLSEKENSE
Protein: Centrin-B (DdCen) (Q54X77)
Organism: Dictyostelium discoideum (Social amoeba)
Function: Plays a fundamental role in microtubule-organizing center structure and function.
Subcellular location: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250}.
Interaction partners:
- DNA repair protein Rad4 family protein
- SAC3/GANP/THP3 conserved domain-containing protein
- Transcription and mRNA export factor ENY2
- PCI domain-containing protein 2 homolog
- UV excision repair protein RAD23 homolog
- Probable serine/threonine-protein kinase roco6
- Probable serine/threonine-protein kinase roco11
- Probable serine/threonine-protein kinase roco5
- Probable serine/threonine-protein kinase roco8
- Probable serine/threonine-protein kinase qkgA
Sequence:
MVKTNTNKLTDDQISEIKESFDMFKSDNGKLDNDQIKYAFKALGCEITEETLELIKKKGQKSISFNSFFELVSPYIPKRDSMSTLEQAFKLFVKDGSGITFKDLKKVAINIGEECSDSDLYDMIEFADTDGDGVINKSEFISLMTTKKVL
Protein: Neuropilin (Q6T868)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004479}.
Interaction partners:
Sequence:
MDFWISHQRIAFIFCFVLKVSAKESETCGGHLDASGAGYITSPGYPLEYPPHQSCQWVISAPEPSQRIVLNFNPHFELERLDCRYDFIEIRDGNSESADLLGKHCSNIAPPAIISSGPFIHIKFVSDYAHQGAGFSLRYEIFKTGAEHCFRNFSSPTGVIESPGFPDKYPHNLECSFIIIAPPQTEVTLTFQTFDLENDPLLMGEGECKYDWLDVWDGLPQVGPLIGRYCGSKIPPKIQSSTGLLSLSFHTDMAVAKDGFSARYNMTHNEVSDTFHCSNAFGLESGKISDDQISASTSFYDGRWQPRQARLNNEDNAWTPGEDSNKEYIQVDLQFLKVLTGIATQGAISKETQKSYYVTTFKLEVSTNGEDWMFYRHGKNHKIFHANTDPSEVVLNRIPQPVLARFVRIRPQTWNNGIALRFELYGCQITDAPCSELQGMLSGLLPDSQISASSMRDLHWSPGAARLVASRSGWFPSPAQPIAGEEWLQVDLGTPRTVRGVITQGARSGDGGTSSENRAFVRKYRLAHSLNGKDWNFVIDSKTSMPKLFEGNTNYDTPELRRFEELPAQFIRIYPERWSPAGIGMRMEVLGCNLPETSTPALETSKPTQPTSVETSTTQKPSPVTSAALPSHKGLCDFEQGWCGWTLDLDSDFSWVMHSSSKSSALGQSHNLSMGSNSLGNYLYIEASPETQGQKARLFSPGVDPDTGPLCLMFSYQLEDQGTLRVLLQNKQQEKTLLWSLSGDQQPIWREGRTIIPRSPDELKVVIEGFFEGTKGHIWIDNIHMSGNTPLEECTQPFSAFPPDMIVKKPEVGNGRLFTGKDHINAGFQFPEWGTAETPSEPPVTHVIDKDNSWLYSLDPILLTIIVMSSLGVLLGAVCAGLLLYCTCSYGGLTSRSSTTLENYNFELYDGIKHKVKLNQQRCCSEA
Protein: Casein kinase I isoform epsilon (CKI-epsilon) (CKIe) (EC 2.7.11.1) (Q9JMK2)
Organism: Mus musculus (Mouse)
Function: Casein kinases are operationally defined by their preferential utilization of acidic proteins such as caseins as substrates (By similarity). Participates in Wnt signaling (By similarity). Phosphorylates DVL1 (By similarity). Phosphorylates DVL2 (By similarity). Phosphorylates NEDD9/HEF1. Central component of the circadian clock. In balance with PP1, determines the circadian period length, through the regulation of the speed and rhythmicity of PER1 and PER2 phosphorylation. Controls PER1 and PER2 nuclear transport and degradation. Inhibits cytokine-induced granuloytic differentiation (By similarity).
Subcellular location: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000269|PubMed:19414593}.
Interaction partners:
- Cryptochrome-1
- Period circadian protein homolog 2
- Period circadian protein homolog 1
- Basic helix-loop-helix ARNT-like protein 1
- Circadian locomoter output cycles protein kaput
- Glycogen synthase kinase-3 beta
- Period circadian protein homolog 3
- Axin-1
- Neuronal PAS domain-containing protein 2
- Cryptochrome-2
Sequence:
MELRVGNKYRLGRKIGSGSFGDIYLGANIASGEEVAIKLECVKTKHPQLHIESKFYKMMQGGVGIPSIKWCGAEGDYNVMVMELLGPSLEDLFNFCSRKFSLKTVLLLADQMISRIEYIHSKNFIHRDVKPDNFLMGLGKKGNLVYIIDFGLAKKYRDARTHQHIPYRENKNLTGTARYASINTHLGIEQSRRDDLESLGYVLMYFNLGSLPWQGLKAATKRQKYERISEKKMSTPIEVLCKGYPSEFSTYLNFCRSLRFDDKPDYSYLRQLFRNLFHRQGFSYDYVFDWNMLKFGAARNPEDVDRERREHEREERMGQLRGSATRALPPGPPTGATANRLRSAAEPVASTPASRIQQTGNTSPRAISRADRERKVSMRLHRGAPANVSSSDLTGRQEVSRLAASQTSVPFDHLGK
Protein: Biogenesis of lysosomal organelles complex-1, subunit 2 (Biogenesis of lysosome-related organelles complex 1 subunit 2 isoform 2) (E9QEJ0)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
Sequence:
MAATGDEAAAMDSISKAPAPPTELNLTAEPENSREATTSDTTENQKPKRPNDGGVETAEEATEPAEPDINELCRDMFDKMSVFLQGELTATCEDYKLLENMNKLTSLKYMEMKDISINISRNLQDLNQKYASLQPYLDQINQIEEQVTALEQAAYKLDTYSKKLEAKFKKLEKR
Protein: Tripartite motif-containing protein 44 (Protein DIPB) (Q96DX7)
Organism: Homo sapiens (Human)
Function: May play a role in the process of differentiation and maturation of neuronal cells (By similarity). May regulate the activity of TRIM17. Is a negative regulator of PAX6 expression.
Interaction partners:
- Ubiquitin carboxyl-terminal hydrolase 39
- Four-jointed box protein 1
- E3 ubiquitin-protein ligase TRIM17
- Gamma-butyrobetaine dioxygenase
- Paired box protein Pax-6
Sequence:
MASGVGAAFEELPHDGTCDECEPDEAPGAEEVCRECGFCYCRRHAEAHRQKFLSHHLAEYVHGSQAWTPPADGEGAGKEEAEVKVEQEREIESEAGEESESEEESESEEESETEEESEDESDEESEEDSEEEMEDEQESEAEEDNQEEGESEAEGETEAESEFDPEIEMEAERVAKRKCPDHGLDLSTYCQEDRQLICVLCPVIGAHQGHQLSTLDEAFEELRSKDSGGLKAAMIELVERLKFKSSDPKVTRDQMKMFIQQEFKKVQKVIADEEQKALHLVDIQEAMATAHVTEILADIQSHMDRLMTQMAQAKEQLDTSNESAEPKAEGDEEGPSGASEEEDT
Protein: UDP-glucose 6-dehydrogenase (UDP-Glc dehydrogenase) (UDP-GlcDH) (UDPGDH) (EC 1.1.1.22) (O60701)
Organism: Homo sapiens (Human)
Function: Catalyzes the formation of UDP-alpha-D-glucuronate, a constituent of complex glycosaminoglycans. Required for the biosynthesis of chondroitin sulfate and heparan sulfate. Required for embryonic development via its role in the biosynthesis of glycosaminoglycans (By similarity). Required for proper brain and neuronal development.
Interaction partners:
- UDP-glucuronic acid decarboxylase 1
- UTP--glucose-1-phosphate uridylyltransferase
- UDP-glucose 4-epimerase
- UDP-glucuronosyltransferase 1A1
- dTDP-D-glucose 4,6-dehydratase
- UDP-glucuronosyltransferase 1A6
- UDP-glucuronosyltransferase 1A8
- UDP-glucuronosyltransferase 1A7
- UDP-glucuronosyltransferase 1A10
- UDP-glucuronosyltransferase 1A4
Sequence:
MFEIKKICCIGAGYVGGPTCSVIAHMCPEIRVTVVDVNESRINAWNSPTLPIYEPGLKEVVESCRGKNLFFSTNIDDAIKEADLVFISVNTPTKTYGMGKGRAADLKYIEACARRIVQNSNGYKIVTEKSTVPVRAAESIRRIFDANTKPNLNLQVLSNPEFLAEGTAIKDLKNPDRVLIGGDETPEGQRAVQALCAVYEHWVPREKILTTNTWSSELSKLAANAFLAQRISSINSISALCEATGADVEEVATAIGMDQRIGNKFLKASVGFGGSCFQKDVLNLVYLCEALNLPEVARYWQQVIDMNDYQRRRFASRIIDSLFNTVTDKKIAILGFAFKKDTGDTRESSSIYISKYLMDEGAHLHIYDPKVPREQIVVDLSHPGVSEDDQVSRLVTISKDPYEACDGAHAVVICTEWDMFKELDYERIHKKMLKPAFIFDGRRVLDGLHNELQTIGFQIETIGKKVSSKRIPYAPSGEIPKFSLQDPPNKKPKV