wanglab/gogpt-training-data huggingface dataset:
Protein: Transferrin receptor protein 1 (TR) (TfR) (TfR1) (Trfr) (Q90997)
Organism: Gallus gallus (Chicken)
Function: Cellular uptake of iron occurs via receptor-mediated endocytosis of ligand-occupied transferrin receptor into specialized endosomes (By similarity). Endosomal acidification leads to iron release. The apotransferrin-receptor complex is then recycled to the cell surface with a return to neutral pH and the concomitant loss of affinity of apotransferrin for its receptor. Transferrin receptor is necessary for development of erythrocytes and the nervous system (By similarity). Acts as a lipid sensor that regulates mitochondrial fusion by regulating activation of the JNK pathway (By similarity). When dietary levels of stearate (C18:0) are low, promotes activation of the JNK pathway, resulting in HUWE1-mediated ubiquitination and subsequent degradation of the mitofusin MFN2 and inhibition of mitochondrial fusion (By similarity). When dietary levels of stearate (C18:0) are high, TFRC stearoylation inhibits activation of the JNK pathway and thus degradation of the mitofusin MFN2 (By similarity).
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:P02786}; Single-pass type II membrane protein {ECO:0000250|UniProtKB:P02786}. Melanosome {ECO:0000250|UniProtKB:P02786}.
Interaction partners:
- Ovotransferrin
- Hemojuvelin BMP co-receptor.
- Ferritin heavy chain
- Early endosome antigen 1.
- STEAP3 metalloreductase.
- Lysosome-associated membrane glycoprotein 1
- Dynamin 2
- Clathrin heavy chain
- Uncharacterized protein.
- Ferritin
Sequence:
MDHARAALSNLFSVEPMSYTRFSIARQTDGDNSHVEMKLSADDEEGGDIERPEHMHVSMAQPQRNGKRLCFLVIAAVLLLLIGFLIGYLSYRGRIELAARCQDGSGGCEITPTASYLVDGEGTVEEEIQGPPVIFWPELKAMLSKKLSAKNLVDNLRWRVGVDSFEAGEAEDTNMATYIHEEFRNFLDKVWNDEHYIKLQVRGSTKNQVSISINGKEEILETPDAIVAYSESGSVSGKPVYVNYGLKKDFEIIQKVVASLNGTIVIVRAGKITLAEKVANAKEAGAAGVLMYVDSLMYGITDTLIPFGHAHLGTGDPYTPGFPSFNHTQFPPVESSGLPHIAVQTISSSAAARLFSKMDGDTCSEGWKGAIHSCKVTTKQESQIMVKLDVNNSMKDRKILNIFGAIQGFEEPDRYVVIGAQRDSWGPGVAKAGTGTAILLELARVISDIVKNEGYKPRRSIIFASWSAGDYGAVGATEWLEGYSAMLHAKAFTYISLDAPVLGASHVKISASPLLYMLLGSIMKGVKNPAAVSESLYNRLGPDWVKAVVPLGLDNAAFPFLAYSGIPVLSFGFYNKDEEYRFLDTKGDTLENLRKIDNLDALLAAAAEVAGQAALRLTHDHELFLDIGRYSEELLAYQEEFLPYIKEVRELGLTLDWLFFARGDFQRAVTALRRDIANSDGENRVIRRALNDRMMKVEYDFLSPYLSPKDVPFRHIFFGKGPHTLRSLVEHLQLLKTNRSSVDLNLLREQLALATWTIKGAANALGGDIWETDNEF
Protein: Serine/threonine-protein kinase Aurora-3 (AtAur3) (EC 2.7.11.1) (Aurora-like kinase 3) (O64629)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Phosphorylates in vitro histone H3 at 'Ser-10' (H3S10ph) and 'Ser-28' (H3S28ph), but not at 'Thr-3' (H3T3ph) or 'Thr-11' (H3T11ph). Colocalizes with phosphorylated histone H3 during mitosis. Associates with cytoskeletal structures that are necessary for cytokinesis and with the microtubule spindle.
Subcellular location: Cytoplasm, perinuclear region. Nucleus. Chromosome. Chromosome, centromere. Note=Cytoplasmic perinuclear region or in dots around the nucleolus and at the nuclear periphery in interphase cells, associated to centromeric regions of condensed chromosomes at metaphase and dispersed along the entire length of the chromosomes during anaphase (PubMed:16028112). Nucleus (PubMed:15722465). {ECO:0000269|PubMed:15722465, ECO:0000269|PubMed:16028112}.
Interaction partners:
- Kinetochore protein NDC80 homolog
- Serine/threonine-protein kinase haspin homolog
- Histone H3-like centromeric protein CENH3
- Mitotic spindle checkpoint protein MAD2
- Histone H3.1
- Chromatin structure-remodeling complex protein SYD
- Putative E3 ubiquitin-protein ligase RF4
- Putative E3 ubiquitin-protein ligase RF298
- RING/U-box superfamily protein
- MND1-interacting protein 1
Sequence:
MSKKSTESDAGNTEKQWSLADFEIGRPLGKGKFGRVYLAREAKSKYIVALKVIFKEQIEKYKIHHQLRREMEIQTSLRHPNILRLFGWFHDNERIFLILEYAHGGELYGVLKQNGHLTEQQAATYIASLSQALAYCHGKCVIHRDIKPENLLLDHEGRLKIADFGWSVQSSNKRKTMCGTLDYLAPEMVENRDHDYAVDNWTLGILCYEFLYGNPPFEAESQKDTFKRILKIDLSFPLTPNVSEEAKNLISQLLVKDPSKRLSIEKIMQHPWIVKNADPKGVCASIDI
Protein: Erythrocyte membrane protein 1, PfEMP1 (Q8I2C4)
Organism: Plasmodium falciparum (isolate 3D7)
Interaction partners:
Sequence:
MVTGSGGEDKYKSAKNAKELLDMIGKDVHEIVEKDEAKKYIDELKGNLQKAKGIGELAAFPDTCKRVEQYRSKANGDGKRYPCTELSEKYVERFSNTLGGQCTDSKMRRDGIGACAPYRRLHLCHHNLENIKDVNNIDNDTLLAEVCMAAYYEGESLTRYNPIYQTKYKDSGSTMCTELARSFADIGDIVRGRDLFRGNDEEKKKRDELEKNLKTIFGKIHSRLTKDAQNYYEDNDTDKNYYQLREDWWKVNRDQVWEAITCEAKSDDKYNVIGPDGKITESNKGQCRCFSGDPPTNMDYVPQFLRWFEEWAEDFCRLRKHKLKDAIDKCRTPKGKEKYCDLNRYDCEQTIRGDHDFVEDDVCKGCQYSCSHFVNWIDNQKLEFDKQKRKYKSEIKKYKSEITGGAGGKGKTRKRRSASNENYEGYEKKFYDKFKSRYKEVGEFLGLLNNETTCTKKLNDQGEEEGTINFKNVHSGKHSSGGDGNKTFYRTKYCEACPWCGAQKVEGGWKDKNKDCAKKKERIFDEHNTTTIEILTADKKQLDILKKYSKFCDSVNGTANVEKDKKRVSNGATGKKGNQIVTWQCYFDKEKPSKKNNNCVEGEWKDFEEGKSVKSYNGFFWKWVHDMLIDSMQWRDEHGNCINKDNDNTCRNNKKCNKECGCFQKWVEQKKKEWQNIKKHFDKQTDIVIEGGPLGELSHCGVLEWNLKEEFLKDESTEDKENKVSAEEAKEIKHLKKMLQQAGVDVGDLAAFVGPCTKGPVAGQNTTIDKLLNQEDKDAKDCQSKHNDCPQPPAEEVGVARADTPTQATGGPRPATTKNTEDDDAEEDEEDEEEEEEEEEKENADAGGEDGKEEKSEEKEEDPPAAVEDTAVKRPQQETQPEEAPTATDPSLNVCTTVDKALTDQTNLTKACQQKYEKGREKFPNWKCIPSGDNSTTREGSESGLRRSRRDADSQTPGEKTTPPSGTNQGAICVPPRRRKLYIQKLPDVEFDDKSLRKWFIETAAIETFFLWDRYKKIKAKEKKEKEDAKGQIYESAGEDDEDKDPQEELQRGDIPDGFLRQMFYTLGDYRDILEGKNDILIGKTGTGSAKDEMADKENKIKEAIKKFFQNGDSQLPSGKPGDERKKFWEANEKHIWNAMVCALTYEEKTSSASGGEKNTTITQDDGLKGALIKDGNPKNPQYHYEKVTLENSGPSPKLQTGSPGTSGDNTPLTQFVKIPTFFRWLHEWGSDFCGTRKRMLDKIIFECRGNGKVCSGDGEDCKDQLKHNPSTVRDFLCPTCGRHCSFYKKWIDIKKKEFEEQSNAYTGQKDKCKKDSNNGFYRKLQTYNEAKDFLQTLRPCKTNNENNNGDDKLDFTNPKETFRPAKNCKPCSEFKVKCDYDNCTGANANTCTTRKISPKDIDEKTDPNGNIEMLVSDDSATGFAGDLNDDCKNAHIFKAFREDVWTCGKVCGYNVCKPVKVNGETFDAKKKGENQIIIIRALFKIWLEYFLEDYNKIKKKLNPCRNNGEVSKCINDYDEKHKCVEQWIEKKRAEWEKIKKHYKRQNEKGDTEMISLVRNFLGDVQPQTEVHKAIQPCKDLDKFQDSSYCTVNGSSAKGKDGTQKDIVECLFQKLEEKAKTCSTSTSEETQNTAQCQDTHPDDDLSLEETEEVKAPNICPKDPESKKDEPDDCCEQAKALPKETADVVADNGSGNDEVQEEEESEEKNKGDAAPLPEKPSGDSTSTDQTEPPAPAPQPLPSDNTSDILKTTIPFGIALALTSIAFLFLKKKTHAPLDLFSVIDIPKSDYDIPTKLSPNRYIPYTSGKYRGKRYIYLEGDSGTDSGYTDHYSDITSSSESEYEELDINDIYAPRAPKYKTLIEVVLEPSGKNTTASGNNTTASGNNTTASGNNTTASGKNTTASDTQNDIQNDGIPSSKITDNEWNTLKDEFISQYLQSEQPNDVPNDYKSGNSSTNTNITTMSRHNVDQKPFITSIHDRNLYTGEEYNYNVNMVNSMDDPKYVSNNVYSGIDLINDTLSGNQHIDIYDELLKRKENESFGTNHVKQTSIHSVAKPISDDPLHNQLELFHKWLDRHRDMCEKWNNKEELLDKLKEEWENETHSGNIHTSDSNKTLNTDVSIQIHMDNPKPINEFTNMDTILDDLKTYNEPYYDVQDDIYYDVNDQDVSTVDSNAMDVPSKVQIEMDVNTKLVKEKYPIGDVWDI
Protein: NAD(P)-specific glutamate dehydrogenase (NAD(P)-GDH) (EC 1.4.1.3) (NAD(P)H-dependent glutamate dehydrogenase) (P95544)
Organism: Xylanibacter ruminicola (Prevotella ruminicola)
Function: Catalyzes the reversible oxidative deamination of glutamate to alpha-ketoglutarate and ammonia. P.ruminicola possess both NADP(H)- and NAD(H)-dependent activities on the same enzyme, suggesting that both anabolic and catabolic forms of the enzyme might occur.
Interaction partners:
Sequence:
MKATEVIEKLKAKFPGQPEYIQAVSQVLGTIEEEYNKHPEFEKANLIERLCVPDRILQFRVSWVDDNGNVQTNLGYRVQHNNAIGPYKGGLRFHKSVNASILKFLAFEQTFKNSLTTLPMGGAKGGSDFDPHGKSDMEVMRFCQAFMNELYRLIGPDEDVPAGDIGVGGREVGYMFGQYKKLTHQFQGILTGKGLEFGGSLIRPEATGYGNVYFLEDMLKTRGESLEGKTVLVSGSGNVAQYTIEKLLQLGAKPVTCSDSNGYIYDPDGIDAEKLAFIMELKNVKRGRIKEYAEKYGVKYVENARPWGEKADIATPCATQDEINEAEAKTLIANGVFAVSEGANMPTEPAAIKVFQDAKILYCPGKASNAGGVATSGLEMSQNSERLSWTREEVDTKLHNIMDEIHANCVKYGTEPDGYINYVKGANVAGFMKVAKAMMAQGIY
Protein: Metalloendopeptidase (EC 3.4.24.-) (Q2HQL9)
Organism: Caenorhabditis elegans
Interaction partners:
Sequence:
MHSVGFWHEHSRADRDDHIKINWDNILPGMKSQFDKISAVLQDLQGENYDYKSIMHYDSTAFSRNGRNTIETVENGFTQVIGTAMDLSPLDIVKINKLYSCKTKKKEKVKPATTEEPHQLIPQVVDKNSVDSGEKCVDHFADCPHFAQYCTRASFFFVMKSYCPFTCKHCPGDRKLKKSG
Protein: Protein maelstrom homolog (Q8BVN9)
Organism: Mus musculus (Mouse)
Function: Plays a central role during spermatogenesis by repressing transposable elements and preventing their mobilization, which is essential for the germline integrity. Acts via the piRNA metabolic process, which mediates the repression of transposable elements during meiosis by forming complexes composed of piRNAs and Piwi proteins and governs the methylation and subsequent repression of transposons. Its association with piP-bodies suggests a participation in the secondary piRNAs metabolic process. Required for the localization of germ-cell factors to the meiotic nuage.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:18694567, ECO:0000269|PubMed:20011505}. Nucleus {ECO:0000269|PubMed:16787967, ECO:0000269|PubMed:18694567}. Note=Component of the meiotic nuage, also named P granule, a germ-cell-specific organelle required to repress transposon activity during meiosis. Recruited to perinuclear nuage during spermatogenesis. Specifically localizes to piP-bodies, a subset of the nuage which contains secondary piRNAs. PIWIL2 is required for its localization to piP-bodies. PubMed:16787967, reported an association with the nuclear XY body, however, PubMed:18694567 showed that it is not the case because the antibody used by PubMed:16787967 still stains the nuclear XY body in spermatocytes lacking Mael. Moreover other antibodies raized against the same epitope used in PubMed:16787967 do not recognize any epitopes on XY chromosomes but show a clear localization to the meiotic nuage. {ECO:0000269|PubMed:16787967, ECO:0000269|PubMed:18694567, ECO:0000269|PubMed:20011505}.
Interaction partners:
- ATP-dependent RNA helicase TDRD9
- Tudor and KH domain-containing protein
- Piwi-like protein 4
- Piwi-like protein 2
- Tudor domain-containing protein 1
- ATP-dependent RNA helicase DDX4
- Piwi-like protein 1
- Inactive peptidyl-prolyl cis-trans isomerase FKBP6
- Small RNA 2'-O-methyltransferase
- ADP/ATP translocase 4
Sequence:
MPNRRASRNAYYFFVQEKIPELRRRGLPVARVADAIPYCSADWALLREDEKEKYSEMAREWRAAQGKDSGPSEKQKLVSTPLRRPGMLVPKPSISPPDMSNLSIKSDQALLGGIFYFLNIFSHGELPPHCEQRFLPCEIGCVKYSLQEGIMADFHSFIHPGEIPRGFRFHCQAASDSSHKIPISNFEFGHDQATVLQNLYKFIHPNPGNWPPIYCKSDDRARVNWCLKRMERASEIRQDLELLTVEDLVVGIYQQKFLKEPSKTWVRSLLDVAMWDYSSNTRCKWHEENDILFCALAVCKKIAYCISNSLATLFGIQLTGAHVPLQDYEASNSVTPKMVVLDAGRYQKLRVESPGFCHFNSYNQEQRSNTSTGYYPSGVKISGPHSSVRGRGITRLLESISNSSNNIHRFSSCETSLSPYTPQKDGYKPFSSFS
Protein: Fibroblast growth factor 3 (FGF-3) (Heparin-binding growth factor 3) (HBGF-3) (Proto-oncogene Int-2) (P11487)
Organism: Homo sapiens (Human)
Function: Plays an important role in the regulation of embryonic development, cell proliferation, and cell differentiation. Required for normal ear development.
Subcellular location: Secreted {ECO:0000305}.
Interaction partners:
- Fibroblast growth factor receptor 1
- Fibroblast growth factor receptor 2
- Fibroblast growth factor receptor 4
- Klotho
- Pro-epidermal growth factor
- Fibroblast growth factor receptor 3
- Fibroblast growth factor-binding protein 1
- Basement membrane-specific heparan sulfate proteoglycan core protein
- Decorin
- Epidermal growth factor receptor
Sequence:
MGLIWLLLLSLLEPGWPAAGPGARLRRDAGGRGGVYEHLGGAPRRRKLYCATKYHLQLHPSGRVNGSLENSAYSILEITAVEVGIVAIRGLFSGRYLAMNKRGRLYASEHYSAECEFVERIHELGYNTYASRLYRTVSSTPGARRQPSAERLWYVSVNGKGRPRRGFKTRRTQKSSLFLPRVLDHRDHEMVRQLQSGLPRPPGKGVQPRRRRQKQSPDNLEPSHVQASRLGSQLEASAH
Protein: Caveolae-associated protein 4 (Muscle-related coiled-coil protein) (Muscle-restricted coiled-coil protein) (A2AMM0)
Organism: Mus musculus (Mouse)
Function: Modulates the morphology of formed caveolae in cardiomyocytes, but is not required for caveolar formation. Facilitates the recruitment of MAPK1/3 to caveolae within cardiomyocytes and regulates alpha-1 adrenergic receptor-induced hypertrophic responses in cardiomyocytes through MAPK1/3 activation. Contributes to proper membrane localization and stabilization of caveolin-3 (CAV3) in cardiomyocytes. Induces RHOA activation and activates NPPA transcription and myofibrillar organization through the Rho/ROCK signaling pathway.
Subcellular location: Cytoplasm, myofibril, sarcomere {ECO:0000269|PubMed:18332105}. Cytoplasm {ECO:0000269|PubMed:18332105}. Cytoplasm, cytosol {ECO:0000269|PubMed:19546242}. Membrane, caveola {ECO:0000269|PubMed:19546242, ECO:0000269|PubMed:24567387}. Cell membrane, sarcolemma {ECO:0000269|PubMed:19546242}. Cell membrane {ECO:0000269|PubMed:26497963}. Note=In cardiomyocytes, accumulates in the Z-line of the sarcomere. In vascular smooth muscle cells, detected diffusely throughout the cytoplasm (PubMed:18332105). Localizes in the caveolae in a caveolin-dependent manner (PubMed:19546242). {ECO:0000269|PubMed:18332105, ECO:0000269|PubMed:19546242}.
Interaction partners:
- Caveolin-3
- Caveolae-associated protein 2
Sequence:
MEHNGSASNAGKIHQNRLSSVTEDEDQDAALTIVTVLDRVASVVDSVQASQKRIEERHREMGNAIKSVQIDLLKLSQSHSNTGYVVNKLFEKTRKVSAHIKDVKARVEKQQVRVTKVETKQEEIMKKNKFRVVIFQEDIPCPASLSVVKDRSLPENQEEAEEVFDPPIELSSDEEYYVEESRSARLRKSGKEHIDHIKKAFSRENMQKTRQTLDKKVSGIRTRIVTPERRERLRQSGERLRQSGERLRQSGERFKKSISSAAPSKEAFKIRSLRKAKDPKAEGQEVDRGMGVDIISGSLALGPIHEFHSDEFSETEKEVTKGGYSPQEGGDPPTPEPLKVTFKPQVRVEDDESLLLELKQSS
Protein: GTP-binding protein Rheb (EC 3.6.5.-) (Ras homolog enriched in brain) (Q15382)
Organism: Homo sapiens (Human)
Function: Activates the protein kinase activity of mTORC1, and thereby plays a role in the regulation of apoptosis. Stimulates the phosphorylation of S6K1 and EIF4EBP1 through activation of mTORC1 signaling. Has low intrinsic GTPase activity.
Subcellular location: Endomembrane system {ECO:0000269|PubMed:22002721}; Lipid-anchor {ECO:0000269|PubMed:22002721}; Cytoplasmic side {ECO:0000269|PubMed:15489334}. Lysosome membrane {ECO:0000269|PubMed:24529379, ECO:0000269|PubMed:33157014}; Lipid-anchor {ECO:0000269|PubMed:22002721}; Cytoplasmic side {ECO:0000269|PubMed:15489334}. Golgi apparatus membrane {ECO:0000269|PubMed:22002721}; Lipid-anchor {ECO:0000305|PubMed:22002721}; Cytoplasmic side {ECO:0000305|PubMed:22002721}. Endoplasmic reticulum membrane {ECO:0000269|PubMed:22002721}; Lipid-anchor {ECO:0000269|PubMed:22002721}; Cytoplasmic side {ECO:0000269|PubMed:22002721}. Cytoplasm, cytosol {ECO:0000269|PubMed:22002721}. Note=Farnesylation is required for recruitment to lysosomal membranes, where it activates the mTORC1 complex. {ECO:0000269|PubMed:24529379}.
Interaction partners:
- Regulatory-associated protein of mTOR
- Serine/threonine-protein kinase mTOR
- Tuberin
- Target of rapamycin complex subunit LST8
- Hamartin
- BCL2/adenovirus E1B 19 kDa protein-interacting protein 3
- Proline-rich AKT1 substrate 1
- DEP domain-containing mTOR-interacting protein
- Retinal rod rhodopsin-sensitive cGMP 3',5'-cyclic phosphodiesterase subunit delta
- TBC1 domain family member 7
Sequence:
MPQSKSRKIAILGYRSVGKSSLTIQFVEGQFVDSYDPTIENTFTKLITVNGQEYHLQLVDTAGQDEYSIFPQTYSIDINGYILVYSVTSIKSFEVIKVIHGKLLDMVGKVQIPIMLVGNKKDLHMERVISYEEGKALAESWNAAFLESSAKENQTAVDVFRRIILEAEKMDGAASQGKSSCSVM
Protein: Integrin subunit alpha 9 (D3ZN51)
Organism: Rattus norvegicus (Rat)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004479, ECO:0000256|RuleBase:RU003762}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004479, ECO:0000256|RuleBase:RU003762}.
Interaction partners:
- Integrin beta-1
- Vascular cell adhesion protein 1
- Integrin beta-3
- Osteopontin
- Tenascin
- Integrin subunit alpha 5
- Paxillin
- Integrin beta
- Tenascin-R
- Integrin alpha-7
Sequence:
MGGPAAKGTGAGGLRALLLALVAAGVPAGAYNIDAQRPVRFQGPPGSFFGYAVLEHFHDNTRWVLVGAPKADSKYSTSVKSPGAVFKCRVHTNPDRRCTELDMARERNRGESCGKTCRGDRDDEWMGVSLARQPKADGRVLACAHRWKNIYYETDHILPHGFCYLIPSNLQAKGRMLIPCYEEYKKKYGEEHGSCQAGIAGFFTEELVIMGAPGSFYWAGTLKVLNLTDNTYFKLNDDAIMNRRYTYLGYAVTAGHFSHPSVTDVVGGAPQDEGIGKVYIFRADRRSGTLIKIFQASGKKMGSYFGSSLCAVDLNMDGLSDLLVGAPMFSEIRDEGQVTVYLNQGHGVLEEQLTLTGDAAYNAHFGESIASLGDLDDDGFPDVAVGAPMEDDFAGTVYIYHGDAQGIVPQYSMKLSGRKINPILQMFGQSISGGIDMDGNGYPDVTVGAFLSDSVVLLRARPVITVDVSIFLPGSINITAPQCHDGQQPVNCLNVTVCFRFHGKNVPGEIGLNYNLTADVAQKEKGQLPRVYFVLLGETAGQVSERLQLTHMDEVCHHYVAHVKRRVQDVISPIVFEAAYSLGEHVIGEEDRELPDLTPVLRWKKGQRIAQKNQTVFERNCRSEDCAADLQLRGKLLLSSVDEKTTHLALGAVKNISLNISISNLGDDAYDANVSFNVSRELFFINMWQKEEMGISCELLESDFLKCSVGFPFMRSKSKYEFSVIFDTSHLSGEEEILSFIVTAQSGNMERSEALHDNTLTLTIPLVHEVDTSITGIVSPTSFVYGESVDASNFIQLDDQECHFQPVNITLQVYNMGPSTLPGSSVSISFPSRLSPGGAEMFQVQDMVVSQEKGNCSLQRNPTPCIIPQEQENIFHTIFAFFSKSGRKVLDCEKTGSFCLTLHCNLSALPKEESRAIDLYMLLNTEILKKDSSSVIQFMARAKVKVEPALRVVEIANGNPEETLVVFEALHNLEPRGYVVGWIIAISLLVGILIFLLLAVLLWKMGFFRRRYKEIIEAEKNRKENEEAWDWVQKNQ
Protein: Bowman-Birk type proteinase inhibitor B5 (HOSPI-B5) (C0HLT1)
Organism: Hyacinthus orientalis (Common hyacinth)
Function: Serine protease inhibitor. Inhibits trypsin (Ki = 41 nM) and weakly inhibits chymotrypsin (Ki = 410 nM). Does not inhibit bacterial subtilisin.
Interaction partners:
Sequence:
GRRPCCNECGICDRSLDPMCICEDLVPQCHEGCQACEEVDTGTPMYQCRSFEYYHCGTPCL
Protein: Noggin (P97466)
Organism: Mus musculus (Mouse)
Function: Essential for cartilage morphogenesis and joint formation. Inhibitor of bone morphogenetic proteins (BMP) signaling which is required for growth and patterning of the neural tube and somite. Inhibits chondrocyte differentiation through its interaction with GDF5 and, probably, GDF6 (By similarity).
Subcellular location: Secreted.
Interaction partners:
- Bone morphogenetic protein 7
- Bone morphogenetic protein 4
- Bone morphogenetic protein 2
- Growth/differentiation factor 5
- Bone morphogenetic protein 5
- Bone morphogenetic protein 6
- Growth/differentiation factor 6
- Growth/differentiation factor 7
- Bone morphogenetic protein 8A
- R-spondin-1
Sequence:
MERCPSLGVTLYALVVVLGLRAAPAGGQHYLHIRPAPSDNLPLVDLIEHPDPIFDPKEKDLNETLLRSLLGGHYDPGFMATSPPEDRPGGGGGPAGGAEDLAELDQLLRQRPSGAMPSEIKGLEFSEGLAQGKKQRLSKKLRRKLQMWLWSQTFCPVLYAWNDLGSRFWPRYVKVGSCFSKRSCSVPEGMVCKPSKSVHLTVLRWRCQRRGGQRCGWIPIQYPIISECKCSC
Protein: Cytochrome P450 3A (EC 1.14.14.-) (Q90WD3)
Organism: Oncorhynchus mykiss (Rainbow trout) (Salmo gairdneri)
Subcellular location: Endoplasmic reticulum membrane {ECO:0000256|RuleBase:RU368049}. Microsome membrane {ECO:0000256|RuleBase:RU368049}.
Interaction partners:
Sequence:
MMSFLPYFSAETWTLLALLITLIVVYGYWPYGVFTKMGIPGPKPLPYFGTMLEYKKGITNFDTECFQKYGKIWGIYDGRQPVLCIMDKSIIKTVLIKECYNIFTNRRDFHLNGEMFDALSVVEDDAWRRIRSVLSPSFTSGRLKEMFGIMKQHSANLLNGMKKQADKDQTIEVKEFFGPYSMDVVTSTAFSVDIDSLNNPSDPFVSNVKKMVKFDLLNPLFLLVALFPFTGPILEKMKFSFFPTAVLDFFYASLIKIKSGRDTGNSTNRVDFLQLMIDSQKGSDTKTGEEQTKGLTDHEILSQAMIFIFAGYETSSSTMSFLAYNLATNHHVMTKLQEEIDTVFPNKAPIQYEALMQMDYLDCVLNGSLRLYPVAPRLERVAKKTVEINGIVIPKDCVVLVPTWALHRDPEIWSDPEEFKPERFSKENKEPIDPYTYMPFGAGPRNCIGMRFAMIMMKLAMVEILQSFTFSVCDETEIPLEIDNQGLLMPKRPIKLRLEPRNNTLSNTTATSLKSPTT
Protein: BLOC-2 complex member HPS5 (Alpha-integrin-binding protein 63) (Hermansky-Pudlak syndrome 5 protein) (Ruby-eye protein 2 homolog) (Ru2) (Q9UPZ3)
Organism: Homo sapiens (Human)
Function: May regulate the synthesis and function of lysosomes and of highly specialized organelles, such as melanosomes and platelet dense granules. Regulates intracellular vesicular trafficking in fibroblasts. May be involved in the regulation of general functions of integrins.
Subcellular location: Cytoplasm, cytosol {ECO:0000269|PubMed:15030569}.
Interaction partners:
- BLOC-2 complex member HPS6
- BLOC-2 complex member HPS3
- BLOC-3 complex member HPS4
- Biogenesis of lysosome-related organelles complex 1 subunit 6
- Biogenesis of lysosome-related organelles complex 1 subunit 3
- Dysbindin
- Biogenesis of lysosome-related organelles complex 1 subunit 5
- SNARE-associated protein Snapin
- Biogenesis of lysosome-related organelles complex 1 subunit 2
- Biogenesis of lysosome-related organelles complex 1 subunit 1
Sequence:
MAFVPVIPESYSHVLAEFESLDPLLSALRLDSSRLKCTSIAVSRKWLALGSSGGGLHLIQKEGWKHRLFLSHREGAISQVACCLHDDDYVAVATSQGLVVVWELNQERRGKPEQMYVSSEHKGRRVTALCWDTAILRVFVGDHAGKVSAIKLNTSKQAKAAAAFVMFPVQTITTVDSCVVQLDYLDGRLLISSLTRSFLCDTEREKFWKIGNKERDGEYGACFFPGRCSGGQQPLIYCARPGSRMWEVNFDGEVISTHQFKKLLSLPPLPVITLRSEPQYDHTAGSSQSLSFPKLLHLSEHCVLTWTERGIYIFIPQNVQVLLWSEVKDIQDVAVCRNELFCLHLNGKVSHLSLISVERCVERLLRRGLWNLAARTCCLFQNSVIASRARKTLTADKLEHLKSQLDHGTYNDLISQLEELILKFEPLDSACSSRRSSISSHESFSILDSGIYRIISSRRGSQSDEDSCSLHSQTLSEDERFKEFTSQQEEDLPDQCCGSHGNEDNVSHAPVMFETDKNETFLPFGIPLPFRSPSPLVSLQAVKESVSSFVRKTTEKIGTLHTSPDLKVRPELRGDEQSCEEDVSSDTCPKEEDTEEEKEVTSPPPEEDRFQELKVATAEAMTKLQDPLVLFESESLRMVLQEWLSHLEKTFAMKDFSGVSDTDNSSMKLNQDVLLVNESKKGILDEDNEKEKRDSLGNEESVDKTACECVRSPRESLDDLFQICSPCAIASGLRNDLAELTTLCLELNVLNSKIKSTSGHVDHTLQQYSPEILACQFLKKYFFLLNLKRAKESIKLSYSNSPSVWDTFIEGLKEMASSNPVYMEMEKGDLPTRLKLLDDEVPFDSPLLVVYATRLYEKFGESALRSLIKFFPSILPSDIIQLCHHHPAEFLAYLDSLVKSRPEDQRSSFLESLLQPESLRLDWLLLAVSLDAPPSTSTMDDEGYPRPHSHLLSWGYSQLILHLIKLPADFITKEKMTDICRSCGFWPGYLILCLELERRREAFTNIVYLNDMSLMEGDNGWIPETVEEWKLLLHLIQSKSTRPAPQESLNGSLSDGPSPINVENVALLLAKAMGPDRAWSLLQECGLALELSEKFTRTCDILRIAEKRQRALIQSMLEKCDRFLWSQQA
Protein: Battenin (A0A1B0GW90)
Organism: Homo sapiens (Human)
Subcellular location: Endomembrane system {ECO:0000256|ARBA:ARBA00004127}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004127}.
Interaction partners:
Sequence:
VFKGLLWYIVPLVVVYFAEYFINQGLFELLFFWNTSLSHAQQYRWYQMLYQAGVFASRSSLRCCRIRFTWALALLQVINSLAVYRHRETDFGVGVRDHPGQHGKTPSPQKLDNLIIIIIGFLRRYTFNVLFCTSCLCVSFLKTIFWSRNGHDGSMDVQQRAWRSNRSRQKGLRSICMHTKKRVSSFRGNKIGLKDVITLRRHVETKVRAKIRKRKVTTKINRHDKINGKRKTARKQKMFQRAQELRRRAEDYHKCKIPPSARKPLCNWVRMAAAEHCHSSGLPYWLYLTAETLKNRMGRQPPPPTQQHSITDNSLSLKTPPECLLTPLPPSVDDNIKECPLAPLPPSPLPPSVDDNLKECLFVPLPPSPL
Protein: Flagellar calcium-binding protein TB-44A (Q57UL8)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Cell projection, cilium, flagellum {ECO:0000256|ARBA:ARBA00004230}.
Interaction partners:
- Methyltransferase type 11 domain-containing protein
Sequence:
MGCSASKDTTNSKDGAASKGGKDGKTTADRKVAWERIRCAIPRDKDAESKSRRIELFKRFDTNGTGKLSFREVLDGCYSILKLDEFTTHLPGIVQRAFDKAKDLGNKVKGVGEEDLVEFLEFRLMLCYIYDIFELTVMFDTMDKDGSLLIELQEFKEALPKLKEWGVDITDATTVFNEIDTNGSGVVTFDEFSCWAVTKKLQVCGDPDGEGAAKTTADRKVAWERIRCAIPRDKDAESKSRRIELFKQFDTNGTGKLGFREVLDGCYSVLKLDEFTTHLPDIVQRAFDKAKDLGNRVKGVGEEDLVEFLEFRLMLCYIYDIFELTVMFDTMDKDGSLLLELQEFKEALPKLKEWGVDITDATTVFNEIDTNGSGVVTFDEFSCWAVTKKLQVCGDPDGEENGANEGN
Protein: Spinalin (O45025)
Organism: Hydra vulgaris (Hydra) (Hydra attenuata)
Interaction partners:
Sequence:
MVIAQAALVLLLVAVDARPWGPGCADGSYGYGGCGHHQANGYGGAHHAAGCCNGLAHGGHHGGAYGQAAHHAGGYGGAYGGHHEDHGEDVKVETHGVHHIASHGGIHHEHGGLRGGHHGAYGGHGAHEAGNFGHVHGGHYGLGGNHYGGSDYGHGHHGGYVHEPCHTPCHTVGGCGGCGGYGHLGGVGGYGTGLGGVGGVGGLHVYKKETVKGKKVQQVTKAEEENEDDDDDESEDAEAESGNSSDEDMPNGGD
Protein: Exosome complex component RRP4 (Ribosomal RNA-processing protein 4) (P38792)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Non-catalytic component of the RNA exosome complex which has 3'->5' exoribonuclease activity and participates in a multitude of cellular RNA processing and degradation events. In the nucleus, the RNA exosome complex is involved in proper maturation of stable RNA species such as rRNA, snRNA and snoRNA, in the elimination of RNA processing by-products and non-coding 'pervasive' transcripts, such as antisense RNA species and cryptic unstable transcripts (CUTs), and of mRNAs with processing defects, thereby limiting or excluding their export to the cytoplasm. In the cytoplasm, the RNA exosome complex is involved in general mRNA turnover and in RNA surveillance pathways, preventing translation of aberrant mRNAs. The catalytic inactive RNA exosome core complex of 9 subunits (Exo-9) is proposed to play a pivotal role in the binding and presentation of RNA for ribonucleolysis, and to serve as a scaffold for the association with catalytic subunits and accessory proteins or complexes. RRP4 as peripheral part of the Exo-9 complex is thought to stabilize the hexameric ring of RNase PH-domain subunits.
Subcellular location: Cytoplasm. Nucleus, nucleolus.
Interaction partners:
- Exosome complex component MTR3
- M-phase phosphoprotein 6 homolog
- Exosome complex component SKI6
- Exosome complex component RRP45
- Exosome complex protein LRP1
- Exosome complex component RRP43
- Exosome complex component CSL4
- Exosome complex exonuclease RRP6
- Exosome complex exonuclease DIS3
- Exosome complex component RRP42
Sequence:
MSEVITITKRNGAFQNSSNLSYNNTGISDDENDEEDIYMHDVNSASKSESDSQIVTPGELVTDDPIWMRGHGTYFLDNMTYSSVAGTVSRVNRLLSVIPLKGRYAPETGDHVVGRIAEVGNKRWKVDIGGKQHAVLMLGSVNLPGGILRRKSESDELQMRSFLKEGDLLNAEVQSLFQDGSASLHTRSLKYGKLRNGMFCQVPSSLIVRAKNHTHNLPGNITVVLGVNGYIWLRKTSQMDLARDTPSANNSSSIKSTGPTGAVSLNPSITRLEEESSWQIYSDENDPSISNNIRQAICRYANVIKALAFCEIGITQQRIVSAYEASMVYSNVGELIEKNVMESIGSDILTAEKMRGNGN