wanglab/gogpt-training-data huggingface dataset:
Protein: Tissue alpha-L-fucosidase (EC 3.2.1.51) (Alpha-L-fucosidase I) (Alpha-L-fucoside fucohydrolase 1) (Alpha-L-fucosidase 1) (P04066)
Organism: Homo sapiens (Human)
Function: Alpha-L-fucosidase is responsible for hydrolyzing the alpha-1,6-linked fucose joined to the reducing-end N-acetylglucosamine of the carbohydrate moieties of glycoproteins.
Subcellular location: Lysosome {ECO:0000269|PubMed:9741689}.
Interaction partners:
- Plasma alpha-L-fucosidase
- Phosphoglucomutase-1
- Beta-galactosidase
- 6-phosphogluconate dehydrogenase, decarboxylating
- Adenylate kinase 2, mitochondrial
- Phosphopentomutase
- Alkaline phosphatase, tissue-nonspecific isozyme
Sequence:
MRAPGMRSRPAGPALLLLLLFLGAAESVRRAQPPRRYTPDWPSLDSRPLPAWFDEAKFGVFIHWGVFSVPAWGSEWFWWHWQGEGRPQYQRFMRDNYPPGFSYADFGPQFTARFFHPEEWADLFQAAGAKYVVLTTKHHEGFTNWPSPVSWNWNSKDVGPHRDLVGELGTALRKRNIRYGLYHSLLEWFHPLYLLDKKNGFKTQHFVSAKTMPELYDLVNSYKPDLIWSDGEWECPDTYWNSTNFLSWLYNDSPVKDEVVVNDRWGQNCSCHHGGYYNCEDKFKPQSLPDHKWEMCTSIDKFSWGYRRDMALSDVTEESEIISELVQTVSLGGNYLLNIGPTKDGLIVPIFQERLLAVGKWLSINGEAIYASKPWRVQWEKNTTSVWYTSKGSAVYAIFLHWPENGVLNLESPITTSTTKITMLGIQGDLKWSTDPDKGLFISLPQLPPSAVPAEFAWTIKLTGVK
Protein: Tropomyosin 2 (beta) (Tropomyosin beta chain isoform X7) (A0A0R4IAL5)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000256|ARBA:ARBA00004245}.
Interaction partners:
Sequence:
MASITSIEAVKRKIQTLQQQADDAEDRAEMLQREVDLERQCRERAEAEVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERGMKVIENRATKDEEKMEIQEMQLKEAKHIAEEADRKYEEVARKLVILEGELERSEERAEVAEARVRQLEEELRLMDQNLKSMMAGEEEYSTKEDKYEEEIRVLTDKLKEAETRAEFAERSVAKLEKTIDDLEEKVAQAKEENLNMHQVLDQTLLELNNL
Protein: Homeobox-leucine zipper protein HDG11 (HD-ZIP protein HDG11) (Homeodomain GLABRA 2-like protein 11) (Homeodomain transcription factor HDG11) (Protein ENHANCED DROUGHT TOLERANCE 1) (Protein HOMEODOMAIN GLABROUS 11) (Q9FX31)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Transcription factor which acts as positive regulator of drought stress tolerance. Can transactivate CIPK3, NCED3 and ERECTA. Transactivates several cell-wall-loosening protein genes by directly binding to HD motifs in their promoters. These target genes play important roles in coordinating cell-wall extensibility with root development and growth. Transactivates CYP74A/AOS, AOC3, OPR3 and 4CLL5/OPCL1 genes by directly binding to HD motifs in their promoters. These target genes are involved in jasmonate (JA) biosynthesis, and JA signaling affects root architecture by activating auxin signaling, which promotes lateral root formation. Acts as negative regulator of trichome branching. Required for the establishment of giant cell identity on the abaxial side of sepals. Seems to promote cell differentiation. May regulate cell differentiation and proliferation during root and shoot meristem development.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00108, ECO:0000269|PubMed:18451323}.
Interaction partners:
- Transcription factor MYB23
- Homeobox-leucine zipper protein ATHB-53
Sequence:
MSFVVGVGGSGSGSGGDGGGSHHHDGSETDRKKKRYHRHTAQQIQRLESSFKECPHPDEKQRNQLSRELGLAPRQIKFWFQNRRTQLKAQHERADNSALKAENDKIRCENIAIREALKHAICPNCGGPPVSEDPYFDEQKLRIENAHLREELERMSTIASKYMGRPISQLSTLHPMHISPLDLSMTSLTGCGPFGHGPSLDFDLLPGSSMAVGPNNNLQSQPNLAISDMDKPIMTGIALTAMEELLRLLQTNEPLWTRTDGCRDILNLGSYENVFPRSSNRGKNQNFRVEASRSSGIVFMNAMALVDMFMDCVKWTELFPSIIAASKTLAVISSGMGGTHEGALHLLYEEMEVLSPLVATREFCELRYCQQTEQGSWIVVNVSYDLPQFVSHSQSYRFPSGCLIQDMPNGYSKVTWVEHIETEEKELVHELYREIIHRGIAFGADRWVTTLQRMCERFASLSVPASSSRDLGGVILSPEGKRSMMRLAQRMISNYCLSVSRSNNTRSTVVSELNEVGIRVTAHKSPEPNGTVLCAATTFWLPNSPQNVFNFLKDERTRPQWDVLSNGNAVQEVAHISNGSHPGNCISVLRGSNATHSNNMLILQESSTDSSGAFVVYSPVDLAALNIAMSGEDPSYIPLLSSGFTISPDGNGSNSEQGGASTSSGRASASGSLITVGFQIMVSNLPTAKLNMESVETVNNLIGTTVHQIKTALSGPTASTTA
Protein: Muscleblind-like protein 2 isoform B (Muscleblind-like protein 2 isoform X11) (Muscleblind-like-splicing regulator 2) (A5YC70)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}. Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MALNIASIRDTKWLTLEVCRQFQRGTCSRSDEECKFAHPPKSCQVENGRVIACFDSLKGRCTRENCKYLHPPAHLKTQLEINGRNNLIQQKTAAAMLAQQMQFMIPGTTMQPVPTFPVSQGLGSNPGLSYAPYLTPMSHGMGLVPTEMLPSTPVIVPGSPPVSVPSSSSTQKLLRTDKLEVCREFQRGNCARGETDCRFAHPSDSPMIDTSDNTVTVCMDYIKSRCSREKCKYFHPPAHLQAKIKAAQHQANQTAVAAQAAAAAMAFPHGVLQPLPKRPALEKSNGASTLFNPSVLHYQQALASAQLQQPTAAFFPTATTPATSVPYATTAPANQIILK
Protein: Transmembrane emp24 domain-containing protein 3 (Membrane protein p24B) (p24 family protein gamma-4) (p24gamma4) (p26) (Q9Y3Q3)
Organism: Homo sapiens (Human)
Function: Potential role in vesicular protein trafficking, mainly in the early secretory pathway. Contributes to the coupled localization of TMED2 and TMED10 in the cis-Golgi network.
Subcellular location: Endoplasmic reticulum-Golgi intermediate compartment membrane {ECO:0000269|PubMed:12237308}; Single-pass type I membrane protein {ECO:0000255}. Golgi apparatus, cis-Golgi network membrane {ECO:0000269|PubMed:10852829, ECO:0000269|PubMed:12237308}; Single-pass type I membrane protein {ECO:0000255}. Golgi apparatus, Golgi stack membrane {ECO:0000250|UniProtKB:Q6AY25}; Single-pass type I membrane protein {ECO:0000255}. Endoplasmic reticulum membrane {ECO:0000269|PubMed:10852829}; Single-pass type I membrane protein {ECO:0000255}. Cytoplasmic vesicle, COPI-coated vesicle membrane {ECO:0000305|PubMed:16940185}; Single-pass type I membrane protein {ECO:0000255}. Note=Probably cycles between compartments of the early secretatory pathway. {ECO:0000269|PubMed:10852829}.
Interaction partners:
- Transmembrane emp24 domain-containing protein 10
- Transmembrane emp24 domain-containing protein 2
- Transmembrane emp24 domain-containing protein 4
- Transmembrane emp24 domain-containing protein 9
- Coatomer subunit beta
- Coatomer subunit delta
- Coatomer subunit epsilon
- Coatomer subunit zeta-1
- Coatomer subunit zeta-2
- Coatomer subunit beta'
Sequence:
MGSTVPRSASVLLLLLLLRRAEQPCGAELTFELPDNAKQCFHEEVEQGVKFSLDYQVITGGHYDVDCYVEDPQGNTIYRETKKQYDSFTYRAEVKGVYQFCFSNEFSTFSHKTVYFDFQVGDEPPILPDMGNRVTALTQMESACVTIHEALKTVIDSQTHYRLREAQDRARAEDLNSRVSYWSVGETIALFVVSFSQVLLLKSFFTEKRPISRAVHS
Protein: Stress response kinase A (EC 2.7.11.1) (Serine/threonine protein kinase YihE) (Serine/threonine-protein kinase SrkA) (P0C0K3)
Organism: Escherichia coli (strain K12)
Function: A protein kinase that (auto)phosphorylates on Ser and Thr residues. Probably acts to suppress the effects of stress linked to accumulation of reactive oxygen species. Protects cells from stress by antagonizing the MazE-MazF TA module, probably indirectly as it has not been seen to phosphorylate MazE, MazF or MazG. Probably involved in the extracytoplasmic stress response.
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01497, ECO:0000305|PubMed:17302814}.
Interaction partners:
- Thiol:disulfide interchange protein DsbA
- Protein YihD
Sequence:
MNNSAFTFQTLHPDTIMDALFEHGIRVDSGLTPLNSYENRVYQFQDEDRRRFVVKFYRPERWTADQILEEHQFALQLVNDEVPVAAPVAFNGQTLLNHQGFYFAVFPSVGGRQFEADNIDQMEAVGRYLGRMHQTGRKQLFIHRPTIGLNEYLIEPRKLFEDATLIPSGLKAAFLKATDELIAAVTAHWREDFTVLRLHGDCHAGNILWRDGPMFVDLDDARNGPAVQDLWMLLNGDKAEQRMQLETIIEAYEEFSEFDTAEIGLIEPLRAMRLVYYLAWLMRRWADPAFPKNFPWLTGEDYWLRQTATFIEQAKVLQEPPLQLTPMY
Protein: Transcription factor TGAL11 (bZIP transcription factor 83) (OsbZIP83) (Q2QXL0)
Organism: Oryza sativa subsp. japonica (Rice)
Function: Transcriptional regulator involved in defense response.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00978}.
Interaction partners:
- BTB/POZ domain and ankyrin repeat-containing protein NPR3
- BTB/POZ domain and ankyrin repeat-containing protein NPR1
- BTB/POZ domain and ankyrin repeat-containing protein NPR5
- BTB/POZ domain and ankyrin repeat-containing protein NPR2
Sequence:
MGEARRGQNPHHVLGYGFHGTTLPNSMASANLFEQGGGGGGGAAYFGELEEALVHQVATLRRRAQQTATTTTSHHGHTTPFSTAAAAATATATARPPATLDIFPSWPMRRSSLPTPKDGCSNVTADTTDSESSSKNNGDQGAAAADMASQFDQIPQQQQKQHKKMAASSTHSDHRMTKTLDPKIMRRLAQNREAARKSRLRKKAYIQQLESSKLRLAQMEQDLERARSQGLLLGGSPGGNTSAGAAMFDAEYGRWLEDGGRRMAELHGGLHAHLPDGDLRAIVDDALAHYDELFRLRAAAAKADVFHLITGTWATPAERCFLWMGGFQPSDLLKTVAPQLDPLTEQQVVGICSLQQSSQQAEEALSQGLEQLHQSLAETVANGGSVVNEASLGSFMGYMALALGKLSNLEGFVIQADNLRQQTLHQMHRILTIRQAARCFLAIGEYHNRLRALSSLWASRPREILVADEGNCGELSIAAQPSESQFSAF
Protein: Succinate-CoA ligase ADP-forming subunit beta (A0A2R8Y6E6)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MAASMFYGRLVAVATLRNHRPRTAQRAAAQVLGSSGLFNNHGLQVQQQQQRNLSLHEYMSMELLQEAGVSVPKGYVAKSPDEAYAIAKKLGSKDVVIKAQVLAGGRGKGTFESGLKGGVKIVFSPEEAKAVSSQMIGKKLFTKQTGEKGRICNQVLVCERKYPRREYYFAITMERSFQGPVLIGSSHGGVNIEDVAAESPEAIIKEPIDIEEGIKKEQALQFSC
Protein: Cytoplasmic envelopment protein 3 (Q3KSR6)
Organism: Epstein-Barr virus (strain GD1) (HHV-4) (Human gammaherpesvirus 4)
Subcellular location: Virion tegument {ECO:0000256|HAMAP-Rule:MF_04042}. Virion membrane {ECO:0000256|HAMAP-Rule:MF_04042}; Lipid-anchor {ECO:0000256|HAMAP-Rule:MF_04042}. Host cell membrane {ECO:0000256|HAMAP-Rule:MF_04042}; Lipid-anchor {ECO:0000256|HAMAP-Rule:MF_04042}; Cytoplasmic side {ECO:0000256|HAMAP-Rule:MF_04042}. Host Golgi apparatus membrane {ECO:0000256|HAMAP-Rule:MF_04042}; Lipid-anchor {ECO:0000256|HAMAP-Rule:MF_04042}; Cytoplasmic side {ECO:0000256|HAMAP-Rule:MF_04042}. Note=Virion membrane-associated tegument protein. Associates with host membrane lipids rafts. During virion morphogenesis, this protein probably accumulates in the endosomes and trans-Golgi where secondary envelopment occurs. It is probably transported to the cell surface from where it is endocytosed and directed to the trans-Golgi network (TGN). {ECO:0000256|HAMAP-Rule:MF_04042}.
Interaction partners:
Sequence:
MGALWSLCRRRVNSIGDVDGGIINLYNDYEEFNLETTKLIAVEEGRACGETNEGLEYDEDSENDELLFLPNKKPN
Protein: Oligopeptide transport ATP-binding protein OppD (EC 7.4.2.6) (P76027)
Organism: Escherichia coli (strain K12)
Function: Part of the binding-protein-dependent transport system for oligopeptides. Probably responsible for energy coupling to the transport system.
Subcellular location: Cell inner membrane {ECO:0000250|UniProtKB:P04285}; Peripheral membrane protein {ECO:0000250|UniProtKB:P04285}.
Interaction partners:
- Periplasmic oligopeptide-binding protein OppA
- Oligopeptide transport system permease protein OppB
- Oligopeptide transport ATP-binding protein OppF
- Oligopeptide transport system permease protein OppC
- Dipeptide transport system permease protein DppC
- Probable D,D-dipeptide transport system permease protein DdpC
- Nickel transport system permease protein NikC
- Glutathione transport system permease protein GsiD
- Periplasmic murein peptide-binding protein MppA
- Putrescine export system permease protein SapC
Sequence:
MSVIETATVPLAQQQADALLNVKDLRVTFSTPDGDVTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAANGRIGGSATFNGREILNLPEHELNKLRAEQISMIFQDPMTSLNPYMRVGEQLMEVLMLHKNMSKAEAFEESVRMLDAVKMPEARKRMKMYPHEFSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLVVVAGICDKVLVMYAGRTMEYGNARDVFYQPVHPYSIGLLNAVPRLDAEGETMLTIPGNPPNLLRLPKGCPFQPRCPHAMEICSSAPPLEEFTPGRLRACFKPVEELL
Protein: Superoxide dismutase [Mn] 3.1, mitochondrial (EC 1.15.1.1) (P09233)
Organism: Zea mays (Maize)
Function: Destroys superoxide anion radicals which are normally produced within the cells and which are toxic to biological systems.
Subcellular location: Mitochondrion matrix.
Interaction partners:
- Superoxide dismutase 4A
- Large ribosomal subunit protein uL23m
- Ribosomal protein S5 family protein
- Ribosomal protein S24/S35 mitochondrial
- Large ribosomal subunit protein mL46
- Translation elongation factor EF1B/ribosomal protein S6 family protein
- Large ribosomal subunit protein bL27c
- Small ribosomal subunit protein mS29
- Small ribosomal subunit protein uS14c
- Large ribosomal subunit protein uL5c
Sequence:
MALRTLASKKVLSFPFGGAGRPLAAAASARGVTTVTLPDLSYDFGALEPAISGEIMRLHHQKHHATYVANYNKALEQLETAVSKGDASAVVQLQAAIKFNGGGHVNHSIFWKNLKPISEGGGEPPHGKLGWAIDEDFGSFEALVKKMNAEGAALQGSGWVWLALDKEAKKVSVETTANQDPLVTKGASLVPLLGIDVWEHAYYLQYKNVRPDYLNNIWKVMNWKYAGEVYENVLA
Protein: Proteasome subunit alpha type-4 (Macropain subunit C9) (Multicatalytic endopeptidase complex subunit C9) (Proteasome component C9) (Proteasome subunit L) (Proteasome subunit alpha-3) (alpha-3) (Q9R1P0)
Organism: Mus musculus (Mouse)
Function: Component of the 20S core proteasome complex involved in the proteolytic degradation of most intracellular proteins. This complex plays numerous essential roles within the cell by associating with different regulatory particles. Associated with two 19S regulatory particles, forms the 26S proteasome and thus participates in the ATP-dependent degradation of ubiquitinated proteins. The 26S proteasome plays a key role in the maintenance of protein homeostasis by removing misfolded or damaged proteins that could impair cellular functions, and by removing proteins whose functions are no longer required. Associated with the PA200 or PA28, the 20S proteasome mediates ubiquitin-independent protein degradation. This type of proteolysis is required in several pathways including spermatogenesis (20S-PA200 complex) or generation of a subset of MHC class I-presented antigenic peptides (20S-PA28 complex).
Subcellular location: Cytoplasm {ECO:0000269|PubMed:22078707}. Nucleus {ECO:0000269|PubMed:22078707}. Note=Translocated from the cytoplasm into the nucleus following interaction with AKIRIN2, which bridges the proteasome with the nuclear import receptor IPO9 (By similarity). Colocalizes with TRIM5 in the cytoplasmic bodies (PubMed:22078707). {ECO:0000250|UniProtKB:P25789, ECO:0000269|PubMed:22078707}.
Interaction partners:
- Proteasome subunit alpha type-2
- Proteasome subunit alpha type-6
- Proteasome subunit alpha type-7
- Proteasome subunit beta type-9
- Proteasome subunit beta type-7
- Proteasome subunit beta type-3
- Proteasome subunit beta type-5
- 26S proteasome non-ATPase regulatory subunit 4
- Proteasome subunit beta type-2
- Proteasome subunit alpha type-3
Sequence:
MSRRYDSRTTIFSPEGRLYQVEYAMEAIGHAGTCLGILANDGVLLAAERRNIHKLLDEVFFSEKIYKLNEDMACSVAGITSDANVLTNELRLIAQRYLLQYQEPIPCEQLVTALCDIKQAYTQFGGKRPFGVSLLYIGWDKHYGFQLYQSDPSGNYGGWKATCIGNNSAAAVSMLKQDYKEGEMTLKSALALAVKVLNKTMDVSKLSAEKVEIATLTRESGKTVIRVLKQKEVEQLIKKHEEEEAKAEREKKEKEQREKDK
Protein: Protein O-mannose kinase (POMK) (EC 2.7.1.183) (Protein kinase-like protein SgK196) (Sugen kinase 196) (Q5U3W1)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: Protein O-mannose kinase that specifically mediates phosphorylation at the 6-position of an O-mannose of the trisaccharide (N-acetylgalactosamine (GalNAc)-beta-1,3-N-acetylglucosamine (GlcNAc)-beta-1,4-mannose) to generate phosphorylated O-mannosyl trisaccharide (N-acetylgalactosamine-beta-1,3-N-acetylglucosamine-beta-1,4-(phosphate-6-)mannose). Phosphorylated O-mannosyl trisaccharide is a carbohydrate structure present in alpha-dystroglycan (dag1), which is required for binding laminin G-like domain-containing extracellular proteins with high affinity. Only shows kinase activity when the GalNAc-beta-3-GlcNAc-beta-terminus is linked to the 4-position of O-mannose, suggesting that this disaccharide serves as the substrate recognition motif (By similarity).
Subcellular location: Endoplasmic reticulum membrane {ECO:0000250}; Single-pass type II membrane protein {ECO:0000250}.
Interaction partners:
- UDP-GalNAc:beta-1,3-N-acetylgalactosaminyltransferase 2
- Fukutin.
- Protein O-linked-mannose beta-1,4-N-acetylglucosaminyltransferase 2
- Protein O-mannosyl-transferase 1
- Ribitol-5-phosphate xylosyltransferase 1
- Beta-1,4-glucuronyltransferase 1
- Protein O-mannosyl-transferase 2
- Ribitol-5-phosphate transferase
- Protein O-linked-mannose beta-1,2-N-acetylglucosaminyltransferase
- Dolichol-phosphate mannosyltransferase subunit 1
Sequence:
MGGTAVGGVIGVRCGVPAVLLCLGALLCANVLLYFYLDALYQNTNPPSAHTQCPPRHFKVGTMSSCSPWLKCPEIRSGVRRVKLIGQGAVKKVYLSEWQGQKVALSVLSSDQYADDFLHGLSMLRALQSSHVVTLVGVCEEDAVFVTEYHPLGSVLTLDTTLAQERYRWRNSWHTRLQLAIDYVAFLAYLHSSPAGIRVMCDSNDLHKTLSQFLLASDMRLLANDLDALPEVEKGGLGVKCGHHELTGDFVAPEQLWPYGEDFSFSDEAMPGYDEKTDIWKIPDVTRFLLGDVLGGDVIHFHLFQIYSECKRKEAHMRPTAREVLSVYRSVYDSMMESQSQRVRDML
Protein: Centrosomal protein 20 (I3NI25)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000256|ARBA:ARBA00004245}.
Interaction partners:
Sequence:
MATVAELKAVLKDTLEKKGVLGHLKARIRAEVFNALDDDREPRPSLSHENLLINELIREYLEFNKYKYTASVLIAAHCILRLLGSSSSPASASRVPGTTESGQPVVPLDRQFLIHELNAFEESKDNTIPLLYGILAHFLRGTKDGIQNAFLKGPSLQPSDPSLGRQPSRRKPMDDHLRKEEQKSTNIEDLHVSQAVNR
Protein: Katanin p80 WD40 repeat-containing subunit B1 (Katanin p80 subunit B1) (p80 katanin) (Q9NHF0)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000256|ARBA:ARBA00004245, ECO:0000256|HAMAP-Rule:MF_03022}. Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03022}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000256|HAMAP-Rule:MF_03022}. Cytoplasm, cytoskeleton, spindle pole {ECO:0000256|HAMAP-Rule:MF_03022}. Cytoplasm, cytoskeleton, spindle {ECO:0000256|HAMAP-Rule:MF_03022}. Note=Predominantly cytoplasmic. Localized to the interphase centrosome and mitotic spindle poles. {ECO:0000256|HAMAP-Rule:MF_03022}.
Interaction partners:
Sequence:
MALPRKLISKIYDIKAHDSRVTSLDLGETGRVLVTGGEDRNVNLWAIGQNECFMSLTGHNRSIDCVRFAYKDNFVYSADDIGIIRRWDLNSQKIYSTLNGHMKSGRTLDFNPSGEYVVSGSNDTTVRLWDVQNENNCIKVCRGHMSHVNSVKFSPDGLWIASAGLEGSILIWDIRKSKQIMEFIADPPVTAITCVQFHPFEFLLAAGRVDGTVSIYDLEHQQLVSQTTHFYGQAIRCITFSDNGECLFVGSSSGISVIGWEPDRELDHIKSTWSFLADMKVVNNKLICGCHEIDTVSINTISLDRVIPFYQPPNSLPNFKHNSTNRKSFTRGNQKFRLSVGGAKPAQVQEEHEGDKSGLSSPNYSLEVVNERLLEVAGRLSSKWSSGCHLSTWLPNGRIRRRNLAPHHVVYGGAIDSALRQGKYSRVPDNMASYGSSYGAIDTRLMSLNEPSSLHKPDIYNLYPLDKNEEADVQQLEFNLNDSNPPILNNYDNYEMAEDFPVNQNLNYITNNYKPVPQPPRSTPRPSRSRRPLPPPLHKRTTNNMAGAKQTSTGIFGGSKLSQVSSVSSMELHKLDDNMVLKKSSSSNVVNKNKRPMGSAQSQFSKENNQQKNINVEIITKPPMRSRTTLDMRTSHQAKTQEKQIHQQQPMNNRIIMDDHDFDMLSRSHEAVLQELSNRQSSLDLLRHATRSHDVLGALRQARSCGKSIFIDLLGAILEKPSSWNLDFCMFVLPEIYELLQSQHKFHFTRACDTLRIILSNFLPTIQENLDSWAANGLGVDVTREDRQRKCAECQRWLLQIKNLPESTHFGSTLSQLQNIIIF
Protein: Keratin-associated protein 29-1 (Keratin-associated protein 29.2) (A8MX34)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MADGCCPGNTTAIPAVPTITTYPVKGGFRHALCLPSSCHSRMWQLVTCQESCQPSIGAPSGCDPASCQPTRLPATSCVGFVCQPMCSHAACYQSGTGQSPCLVSSCQPSCSESTCCQEKCCDASPCQQSSCQESVCMSGSCQAACGQSVCCDAGSCQPSCSEVTSCPETSCLPTICTASPCQPTWCQGSSCQPVSGEGQPCKSTYYQPICYIFKPCQSALYMPVPCQPSTCVFSSCNTTCCVPSHCQPPHCQLVPSTCFIYQPVANCQAPCSTKNCCKPASCDTVISGQPTCDGPPSYNQSGCKSACCVTGLGTSPSSGSNCLPTSCQPSCESSFCKATLC
Protein: Copper-exporting P-type ATPase (EC 7.2.2.8) (Copper-exporting P-type ATPase A) (P9WPU1)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: Involved in copper export. Could be involved in the copper detoxification of mycobacterial cells.
Subcellular location: Cell membrane {ECO:0000269|PubMed:25967101}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Cation-transporting P-type ATPase B
Sequence:
MTTAVTGEHHASVQRIQLRISGMSCSACAHRVESTLNKLPGVRAAVNFGTRVATIDTSEAVDAAALCQAVRRAGYQADLCTDDGRSASDPDADHARQLLIRLAIAAVLFVPVADLSVMFGVVPATRFTGWQWVLSALALPVVTWAAWPFHRVAMRNARHHAASMETLISVGITAATIWSLYTVFGNHSPIERSGIWQALLGSDAIYFEVAAGVTVFVLVGRYFEARAKSQAGSALRALAALSAKEVAVLLPDGSEMVIPADELKEQQRFVVRPGQIVAADGLAVDGSAAVDMSAMTGEAKPTRVRPGGQVIGGTTVLDGRLIVEAAAVGADTQFAGMVRLVEQAQAQKADAQRLADRISSVFVPAVLVIAALTAAGWLIAGGQPDRAVSAALAVLVIACPCALGLATPTAMMVASGRGAQLGIFLKGYKSLEATRAVDTVVFDKTGTLTTGRLQVSAVTAAPGWEADQVLALAATVEAASEHSVALAIAAATTRRDAVTDFRAIPGRGVSGTVSGRAVRVGKPSWIGSSSCHPNMRAARRHAESLGETAVFVEVDGEPCGVIAVADAVKDSARDAVAALADRGLRTMLLTGDNPESAAAVATRVGIDEVIADILPEGKVDVIEQLRDRGHVVAMVGDGINDGPALARADLGMAIGRGTDVAIGAADIILVRDHLDVVPLALDLARATMRTVKLNMVWAFGYNIAAIPVAAAGLLNPLVAGAAMAFSSFFVVSNSLRLRKFGRYPLGCGTVGGPQMTAPSSA
Protein: Beta-nerve growth factor (Beta-NGF) (P01139)
Organism: Mus musculus (Mouse)
Function: Nerve growth factor is important for the development and maintenance of the sympathetic and sensory nervous systems. Extracellular ligand for the NTRK1 and NGFR receptors, activates cellular signaling cascades to regulate neuronal proliferation, differentiation and survival. The immature NGF precursor (proNGF) functions as ligand for the heterodimeric receptor formed by SORCS2 and NGFR, and activates cellular signaling cascades that lead to inactivation of RAC1 and/or RAC2, reorganization of the actin cytoskeleton and neuronal growth cone collapse. In contrast to mature NGF, the precursor form (proNGF) promotes neuronal apoptosis (in vitro). Inhibits metalloproteinase-dependent proteolysis of platelet glycoprotein VI (By similarity). Binds lysophosphatidylinositol and lysophosphatidylserine between the two chains of the homodimer. The lipid-bound form promotes histamine relase from mast cells, contrary to the lipid-free form.
Subcellular location: Secreted {ECO:0000269|PubMed:1284621}. Endosome lumen {ECO:0000269|PubMed:20036257}. Note=ProNGF is endocytosed after binding to the cell surface receptor formed by SORT1 and NGFR. {ECO:0000269|PubMed:20036257}.
Interaction partners:
- Tumor necrosis factor receptor superfamily member 16
- BDNF/NT-3 growth factors receptor
- High affinity nerve growth factor receptor
- NT-3 growth factor receptor
- Kallikrein 1-related peptidase-like b4
- Sortilin
- VPS10 domain-containing receptor SorCS2
- GDNF family receptor alpha-1
- Kallikrein 1-related peptidase b3
- Neurotrophic factor BDNF precursor form
Sequence:
MSMLFYTLITAFLIGVQAEPYTDSNVPEGDSVPEAHWTKLQHSLDTALRRARSAPTAPIAARVTGQTRNITVDPRLFKKRRLHSPRVLFSTQPPPTSSDTLDLDFQAHGTIPFNRTHRSKRSSTHPVFHMGEFSVCDSVSVWVGDKTTATDIKGKEVTVLAEVNINNSVFRQYFFETKCRASNPVESGCRGIDSKHWNSYCTTTHTFVKALTTDEKQAAWRFIRIDTACVCVLSRKATRRG
Protein: Histidinol-phosphate aminotransferase 1, chloroplastic (EC 2.6.1.9) (Gene duplicate 1-B protein) (Imidazole acetol-phosphate transaminase) (Protein EMBRYO DEFECTIVE 2196) (Protein HISTIDINE BIOSYNTHESIS 6A) (B9DHD3)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Plastid, chloroplast {ECO:0000305}.
Interaction partners:
- Imidazoleglycerol-phosphate dehydratase 1, chloroplastic
- Imidazoleglycerol-phosphate dehydratase 2, chloroplastic
- Histidinol dehydrogenase, chloroplastic
- Arogenate dehydrogenase 1, chloroplastic
- Arogenate dehydrogenase 2, chloroplastic
- Bifunctional phosphatase IMPL2, chloroplastic
- Histidine biosynthesis bifunctional protein hisIE, chloroplastic
- 1-
- ATP phosphoribosyltransferase 2, chloroplastic
- ATP phosphoribosyltransferase 1, chloroplastic
Sequence:
MGVINVQGSPSFSIHSSESNLRKSRALKKPFCSIRNRVYCAQSSSAAVDESKNITMGDSFIRPHLRQLAAYQPILPFEVLSAQLGRKPEDIVKLDANENPYGPPPEVFEALGNMKFPYVYPDPQSRRLRDALAQDSGLESEYILVGCGADELIDLIMRCVLDPGEKIIDCPPTFSMYVFDAAVNGAGVIKVPRNPDFSLNVDRIAEVVELEKPKCIFLTSPNNPDGSIISEDDLLKILEMPILVVLDEAYIEFSGVESRMKWVKKYENLIVLRTFSKRAGLAGLRVGYGAFPLSIIEYLWRAKQPYNVSVAGEVAALAALSNGKYLEDVRDALVRERERLFGLLKEVPFLNPYPSYSNFILCEVTSGMDAKKLKEDLAKMGVMVRHYNSQELKGYVRVSAGKPEHTDVLMECLKQFY
Protein: Vacuolar proton pump subunit B (V-ATPase subunit B) (Vacuolar proton pump subunit B) (D3ZZS8)
Organism: Rattus norvegicus (Rat)
Interaction partners:
- V-type proton ATPase subunit D
- V-type proton ATPase subunit a
- V-type proton ATPase subunit E 1
- V-type proton ATPase subunit d 2
- V-type proton ATPase catalytic subunit A
- V-type proton ATPase subunit
- ATPase H+ transporting V1 subunit E2
- V-type proton ATPase subunit F
- V-type proton ATPase 116 kDa subunit a 1
- V-type proton ATPase 16 kDa proteolipid subunit c
Sequence:
MATQVDGRPSGFTSNSCDPGTAREHVQVVTRNYITHPRVTYRTVCSVNGPLVVLDQVKFAQYAEIVNFTLPDGTQRSGQVLEVAGTKAIVQVFEGTSGIDSQKTTCEFTGDILRTPVSEDMLGRIFNGSGKPIDKGPAVMAEDFLDINGQPINPHDRIYPEEMIQTGISPIDVMNSIARGQKIPIFSAAGLPHNEIAAQICRQAGLVKKSKAVLDYHEDNFAIVFAAMGVNMETARFFKSDFEQNGTMGNVCLFLNLANDPTIERIITPRLALTTAEFLAYQCEKHVLVILTDMSSYAEALREVSAAREEVPGRRGFPGYMYTDLATIYERAGRVEGRGGSITQIPILTMPNDDITHPIPDLTGFITEGQIYVDRQLHNRQVYPPINVLPSLSRLMKSAIGEGMTRKDHGDVSNQLYACYAIGKDVQAMKAVVGEEALTSEDLLYLEFLQKFEKNFINQGPYENRTVFESLDLGWKLLRIFPKEMLKRIPQSVTDEFYSRQGAQQDPASDTAL