wanglab/gogpt-training-data huggingface dataset:
Protein: Sepiapterin reductase (SPR) (SR) (EC 1.1.1.153) (Q54GP3)
Organism: Dictyostelium discoideum (Social amoeba)
Function: Catalyzes the production of D-threo-tetrahydrobiopterin (tetrahydrodictyopterin or DH4), also known as dictyopterin, and in a much smaller amount that of it's stereoisomer L-erythro-tetrahydrobiopterin ((6R)-L-erythro-5,6,7,8-tetrahydrobiopterin or BH4). Prefers 1-oxo-2-D-hydroxypropyl-tetrahydropterin to 6-pyruvoyltetrahydropterin (6-pyruvoyl-5,6,7,8-tetrahydropterin) as a substrate, thereby maintaining dominant production of DH4 over BH4 in sufficient supply of an aldose reductase-like enzyme. DH4 represents more than 95% of the total tetrahydrobiopterin production. It has a direct antioxidant function to protect mitochondria against oxidative stress. Essential for the last step of BH4 synthesis. Also catalyzes the conversion of sepiapterin to L-erythro-7,8-dihydrobiopterin, which is then reduced to BH4 by dihydrofolate reductase, constituting the salvage pathway of BH4.
Subcellular location: Cytoplasm {ECO:0000250}.
Interaction partners:
- 6-pyruvoyl tetrahydrobiopterin synthase
- Phenylalanine-4-hydroxylase
- Dihydropteridine reductase
- GTP cyclohydrolase 1
- dihydrofolate reductase
- Aldose reductase C
- Aldose reductase A
- Aldose reductase B
- MatA protein
- Large ribosomal subunit protein eL15
Sequence:
MSKVLAIVTGASKGFGKAIAQEIVKCNPNKNQLIDLVLFARSLDGLKSTKESIETISTNAKVIDLQSLDMSNIPDVELKFKSVLENIKWEEYSKICFFNNHGTLYHLGRIEDFSDFKNIQKDNDTNTTSFVVTTSLLVKKLKELGSQYSSEVTIVNSSSLCAIKAFPTWSLYCSSRAYRDMFFQALSLEYKLNDKFKVLNYSLGVLDTDMQSQVREECSEDDKSFYVGLKNDGKLINPNRSASICSNLVYSHKFETGSHLDYYDLDK
Protein: Nicotinic acetylcholine receptor alpha4, isoform D (Nicotinic acetylcholine receptor alpha4, isoform F) (M9NE13)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
Sequence:
MDEQQGSNVVAVGVDLSEFYMSVEWDILEVPAVRNEKFYTCCDEPYLDITFNITMRRKTLFYTVNIIIPCMGISFLTVLTFYLPSDSGEKVTLSISILISLHVFFLLVVEIIPPTSLVVPLLGKYLIFAMILVSISICVTVVVLNVHFRSPQTHKMAPWVKRVFIDFLPAFLFIKRPTYNFETSKLLLKDTHACFYPYYSATNIDRLVSSGYNNSLPKEDLSQSITANGPFGGSCQVHGPVPPLTHCSSDEIAAVPDMDIGPLGMKSPILNNPAFSHSKCLPKIHKSCFCVRFIAEHTKMQEDSTKVKEDWKYVAMVLDRLFLWIFTLAVVVGTAGIILQAPTLYDDRIPIIEQKDLDFSGTSAGRCRPPQ
Protein: Factor associated with metabolism and energy (Protein CCDC198) (Q9NVL8)
Organism: Homo sapiens (Human)
Subcellular location: Cell membrane {ECO:0000269|PubMed:37248239}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q9CPZ1}. Cytoplasmic vesicle {ECO:0000250|UniProtKB:Q9CPZ1}. Note=The localization of CCDC198 changes from membranous to vesicle-forming structures in the malignant tissue. {ECO:0000269|PubMed:37248239}.
Interaction partners:
Sequence:
MGLSHSKTHLRVIKVAPLQNKEVETPSAGRVDFAFNQNLEEKTSYSLARLQDQNKALEGQLPPLQENWYGRYSTASRDMYFDIPLEHRETSIIKRHPPQRLQKLEPIDLPRVITSGRLLSQREARTMHKAKQVLEKKMQTPMYTSENRQYLHKMQVLEMIRKRQEAQMELKKSLHGEARINKQSPRDHKAKKTLQSTPRNDDHDLLTMLPDEILNRGPGNSKNTEFLKHQAVNNYCPWKIGKMETWLHEQEAQGQLLWDSSSSDSDEQGKDEKKPRALVRTRTERIPLFDEFFDQE
Protein: Differentially expressed in FDCP 6 homolog (DEF-6) (IRF4-binding protein) (Q9H4E7)
Organism: Homo sapiens (Human)
Function: Phosphatidylinositol 3,4,5-trisphosphate-dependent guanine nucleotide exchange factor (GEF) which plays a role in the activation of Rho GTPases RAC1, RhoA and CDC42. Can regulate cell morphology in cooperation with activated RAC1 (By similarity). Involved in immune homeostasis by ensuring proper trafficking and availability of T-cell regulator CTLA-4 at T-cell surface. Plays a role in Th2 (T helper cells) development and/or activation, perhaps by interfering with ZAP70 signaling (By similarity).
Subcellular location: Cytoplasm {ECO:0000269|PubMed:15023524}. Cell membrane {ECO:0000269|PubMed:15023524, ECO:0000305|PubMed:12651066}. Nucleus {ECO:0000269|PubMed:15023524}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:15023524}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:15023524}. Cell projection, filopodium {ECO:0000269|PubMed:15023524}. Note=Recruited to the plasma membrane upon binding phosphatidylinositol 3,4,5-trisphosphate (PubMed:15023524). Binds to actin filaments (PubMed:15023524). {ECO:0000269|PubMed:15023524}.
Interaction partners:
- Interferon regulatory factor 4
- Lys-63-specific deubiquitinase BRCC36
- Cell division control protein 42 homolog
- BRISC and BRCA1-A complex member 1
- BRISC and BRCA1-A complex member 2
- Ras-related C3 botulinum toxin substrate 2
Sequence:
MALRKELLKSIWYAFTALDVEKSGKVSKSQLKVLSHNLYTVLHIPHDPVALEEHFRDDDDGPVSSQGYMPYLNKYILDKVEEGAFVKEHFDELCWTLTAKKNYRADSNGNSMLSNQDAFRLWCLFNFLSEDKYPLIMVPDEVEYLLKKVLSSMSLEVSLGELEELLAQEAQVAQTTGGLSVWQFLELFNSGRCLRGVGRDTLSMAIHEVYQELIQDVLKQGYLWKRGHLRRNWAERWFQLQPSCLCYFGSEECKEKRGIIPLDAHCCVEVLPDRDGKRCMFCVKTANRTYEMSASDTRQRQEWTAAIQMAIRLQAEGKTSLHKDLKQKRREQREQRERRRAAKEEELLRLQQLQEEKERKLQELELLQEAQRQAERLLQEEEERRRSQHRELQQALEGQLREAEQARASMQAEMELKEEEAARQRQRIKELEEMQQRLQEALQLEVKARRDEESVRIAQTRLLEEEEEKLKQLMQLKEEQERYIERAQQEKEELQQEMAQQSRSLQQAQQQLEEVRQNRQRADEDVEAAQRKLRQASTNVKHWNVQMNRLMHPIEPGDKRPVTSSSFSGFQPPLLAHRDSSLKRLTRWGSQGNRTPSPNSNEQQKSLNGGDEAPAPASTPQEDKLDPAPEN
Protein: Glial cell line-derived neurotrophic factor (zGDNF) (Q98TU0)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: Neurotrophic factor that enhances survival and morphological differentiation of dopaminergic neurons and increases their high-affinity dopamine uptake (By similarity). Essential for the development of the enteric nervous system, but appears dispensable for the development of the kidney and primary motor neuron.
Subcellular location: Secreted {ECO:0000250|UniProtKB:P39905}.
Interaction partners:
- GDNF family receptor alpha-1
- Proto-oncogene tyrosine-protein kinase receptor Ret
- Brain-derived neurotrophic factor
- GDNF family receptor alpha
- Neurotrophin-3
- Gdnf family receptor alpha 1a.
- GDNF family receptor alpha-like.
- GDNF family receptor alpha 2b.
- Syndecan
- END domain-containing protein.
Sequence:
MKLWDILATCLLLLSSVSTRPLFHKLQPSKRAVVRSESPALDPIIDSQPETSNPKQASMEEQYDLTGLYPEQFEDVMDFIEATLGRLRRSSDVEPQMKRDRVRQKAAANTEKSGGRGRGERKRSRGRARSRDDRVKGQGRGCLLKEIHLNVTDLDLGYRTKEELIFRYCSGPCHDAETNYDKILNNLTHNKKLDKDTPSRTCCRPIAFDDDISFLDDSLEYHTLKKHSAKKCACV
Protein: Dual adapter for phosphotyrosine and 3-phosphotyrosine and 3-phosphoinositide (hDAPP1) (B lymphocyte adapter protein Bam32) (B-cell adapter molecule of 32 kDa) (Q9UN19)
Organism: Homo sapiens (Human)
Function: May act as a B-cell-associated adapter that regulates B-cell antigen receptor (BCR)-signaling downstream of PI3K.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:10770799}. Membrane {ECO:0000269|PubMed:10770799}; Peripheral membrane protein {ECO:0000269|PubMed:10770799}. Note=Membrane-associated after cell stimulation leading to its translocation.
Interaction partners:
- Tyrosine-protein kinase Lyn
- 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase gamma-2
- Ras-related C3 botulinum toxin substrate 2
- Ras-related C3 botulinum toxin substrate 3
- Pleckstrin
- Phosphoinositide 3-kinase adapter protein 1
Sequence:
MGRAELLEGKMSTQDPSDLWSRSDGEAELLQDLGWYHGNLTRHAAEALLLSNGCDGSYLLRDSNETTGLYSLSVRAKDSVKHFHVEYTGYSFKFGFNEFSSLKDFVKHFANQPLIGSETGTLMVLKHPYPRKVEEPSIYESVRVHTAMQTGRTEDDLVPTAPSLGTKEGYLTKQGGLVKTWKTRWFTLHRNELKYFKDQMSPEPIRILDLTECSAVQFDYSQERVNCFCLVFPFRTFYLCAKTGVEADEWIKILRWKLSQIRKQLNQGEGTIRSRSFIFK
Protein: MutS protein homolog 1 (O13921)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Involved in mitochondrial DNA repair.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:10759889}. Mitochondrion {ECO:0000305}.
Interaction partners:
- Putative MutL protein homolog 1
- DNA mismatch repair protein pms1
- DNA mismatch repair protein msh6
- DNA mismatch repair protein msh3
- Exodeoxyribonuclease 1
- UPF0589 protein C32H8.01c
- N-acetyltransferase eso1
- Putative anion/proton exchange transporter C19C7.11
- Proliferating cell nuclear antigen
- ATP-dependent DNA helicase pfh1
Sequence:
MPTWRYIFSLRSKSSFTKTWVPFTQIRNSSKSPKVGQKPILQGALGPPLDFIRPKEKVTLPPLLKEVSFQQKKFADCVLLTKVGNFYEMYFEQAEKIGPLLNLRVSKKKTSKSDVSMAGFPFFKLDRYLKILVEDLKKCVALSEEVIRPVDDLSSKNMYIRSVTRVITPGTLIDENFMNPYESNYILTVVFDPNFFSSDISNQGTAEDKDCFADCKIGLSWLDLSTGEFFTQDSNLQRLAGDLTRISPREIVLDESLKSFTTHPIYSFIQERKYFLSYVENRYQSLDCWNKFLEKEIDPSFIKYCTKLEVTAGCTLISYIADRLQNSHPNIQPPIRVSLNEYMIIGESAMKGLEIRSSLYQNRYTGSLLHAINKTVTKSGSRLLTRRLCAPSTNIVEINNRLDLVEKFKLLPELCSKVINLLKKSNDTHRILQHLLMGRGNSYDLLKMADNFSITKEIHSLLSPLESSSAFRLLLLNMHPHDELKQLINNAVDENALMKQKINEEEETEVIAQEAEEILQDENAQVEIVKKSLSSEFDIRQSFKENWVVKSNFNNNLRKLHEKLQSLFASYDKLQEDLSKRLGKKATLRKSPAKLYYVHLKLSGNETIERFIKKFTQAVLFQSTKSTASFQLPGWTSLGMDLENTKLHIHQEEQRVLKSITDEIVSHHKTLRSLANALDELDISTSLATLAQEQDFVRPVVDDSHAHTVIQGRHPIVEKGLSHKLIPFTPNDCFVGNGNVNIWLITGPNMAGKSTFLRQNAIISILAQIGSFVPASNARIGIVDQIFSRIGSADNLYQQKSTFMVEMMETSFILKNATRRSFVIMDEIGRGTTASDGIAIAYGCLKYLSTINHSRTLFATHAHQLTNLTKSFKNVECYCTNLSIDRDDHTFSFDYKLKKGVNYQSHGLKVAEMAGIPKNVLLAAEEVLTLLPNTSKPTSMK
Protein: E3 ubiquitin-protein ligase RNF43 (EC 2.3.2.27) (RING finger protein 43) (RING-type E3 ubiquitin transferase RNF43) (Q68DV7)
Organism: Homo sapiens (Human)
Function: E3 ubiquitin-protein ligase that acts as a negative regulator of the Wnt signaling pathway by mediating the ubiquitination, endocytosis and subsequent degradation of Wnt receptor complex components Frizzled. Acts on both canonical and non-canonical Wnt signaling pathway. Along with RSPO2 and ZNRF3, constitutes a master switch that governs limb specification (By similarity).
Subcellular location: Cell membrane; Single-pass type I membrane protein. Endoplasmic reticulum membrane; Single-pass type I membrane protein. Nucleus envelope. Note=According to a report, may be secreted. {ECO:0000269|PubMed:15492824}.
Interaction partners:
- R-spondin-1
- Leucine-rich repeat-containing G-protein coupled receptor 5
- Leucine-rich repeat-containing G-protein coupled receptor 4
- R-spondin-2
- Frizzled-5
- R-spondin-4
- R-spondin-3
- Frizzled-8
- A-kinase anchor protein 8-like
- Frizzled-1
Sequence:
MSGGHQLQLAALWPWLLMATLQAGFGRTGLVLAAAVESERSAEQKAIIRVIPLKMDPTGKLNLTLEGVFAGVAEITPAEGKLMQSHPLYLCNASDDDNLEPGFISIVKLESPRRAPRPCLSLASKARMAGERGASAVLFDITEDRAAAEQLQQPLGLTWPVVLIWGNDAEKLMEFVYKNQKAHVRIELKEPPAWPDYDVWILMTVVGTIFVIILASVLRIRCRPRHSRPDPLQQRTAWAISQLATRRYQASCRQARGEWPDSGSSCSSAPVCAICLEEFSEGQELRVISCLHEFHRNCVDPWLHQHRTCPLCMFNITEGDSFSQSLGPSRSYQEPGRRLHLIRQHPGHAHYHLPAAYLLGPSRSAVARPPRPGPFLPSQEPGMGPRHHRFPRAAHPRAPGEQQRLAGAQHPYAQGWGLSHLQSTSQHPAACPVPLRRARPPDSSGSGESYCTERSGYLADGPASDSSSGPCHGSSSDSVVNCTDISLQGVHGSSSTFCSSLSSDFDPLVYCSPKGDPQRVDMQPSVTSRPRSLDSVVPTGETQVSSHVHYHRHRHHHYKKRFQWHGRKPGPETGVPQSRPPIPRTQPQPEPPSPDQQVTRSNSAAPSGRLSNPQCPRALPEPAPGPVDASSICPSTSSLFNLQKSSLSARHPQRKRRGGPSEPTPGSRPQDATVHPACQIFPHYTPSVAYPWSPEAHPLICGPPGLDKRLLPETPGPCYSNSQPVWLCLTPRQPLEPHPPGEGPSEWSSDTAEGRPCPYPHCQVLSAQPGSEEELEELCEQAV
Protein: SUN domain-containing protein 2 (AtSUN2) (Q9SG79)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Component of SUN-protein-containing multivariate complexes also called LINC complexes which link the nucleoskeleton and cytoskeleton by providing versatile outer nuclear membrane attachment sites for cytoskeletal filaments. Required for the maintenance and/or formation of polarized nuclear shape in root hairs. Modulates the anchoring and mobility of WIP proteins in the nuclear envelope (NE). In association with SUN1, may be involved in telomere attachment to nuclear envelope in the prophase of meiosis. As component of the SUN-WIP-WIT2-KAKU1 complex, mediates the transfer of cytoplasmic forces to the nuclear envelope (NE), leading to nuclear shape changes.
Subcellular location: Nucleus inner membrane {ECO:0000269|PubMed:19807882, ECO:0000269|PubMed:21294795, ECO:0000269|PubMed:24667841, ECO:0000269|PubMed:25412930}; Single-pass type II membrane protein {ECO:0000255}. Cytoplasm, cytoskeleton, phragmoplast {ECO:0000269|PubMed:21294795}. Endoplasmic reticulum membrane {ECO:0000269|PubMed:21294795}; Single-pass type II membrane protein {ECO:0000255}. Nucleus envelope {ECO:0000269|PubMed:22270916}. Note=Dynamic localization during mitosis and meiosis, tightly coupled with nuclear envelope (NE) dynamics. Localized with the nuclear envelope during meiotic prophase I. NE re-formation during metaphase is temporally and spatially coordinated with plant-specific microtubule structures such as phragmoplasts. During anaphase, after NE breakdown (NEBD), predominantly localized with the endoplasmic reticulum, in the outside of the segregated chromosomes and not in between segregated chromosomes. {ECO:0000269|PubMed:21294795, ECO:0000269|PubMed:25412930}.
Interaction partners:
- Protein CROWDED NUCLEI 1
- Zinc finger protein WIP3
- SUN domain-containing protein 4
- SUN domain-containing protein 3
- SUN domain-containing protein 5
- Protein SINE1
- WPP domain-interacting tail-anchored protein 1
- Protein SINE2
- TIR domain-containing protein
- Protein KAKU4
Sequence:
MSASTVSITASPRTIRRTPVLSGEKKSNFDFPPSESHANAAIGESSAGTNKDLIRAEAAGERSNTYDVGPVTRKSGSTATGTNTTTTQRRTRKSQGNKIDRGKWKTVVRVFAKQFGALLLLVGLIQLIRKLTLKDSSLSSSNFPIETEMVLSELESRISAVDGLVKTTTKMMQVQVEFLDKKMDSESRALRQTIDSTSSVLHSELKKVESKTERLQVSVDELNAKPLVSREELERVYEELKKGKVGDSDVNIDKLRAYARDIVEKEIGKHVADGLGRVDYALASGGAFVMGHSDPFLVGNGRNWFGTSRRRVHSKAVKMLTPSFGEPGQCFPLKGSNGYVLVRLRAPIIPEAVTLEHVSKAVAYDRSSAPKDCRVSGWLGDIDMETETMPLLTEFSYDLDRSNAQTFDIADSAHSGLVNTVRLDFNSNHGSSSHTCIYRFRVHGRELDSVSVAHA
Protein: Bifunctional polynucleotide phosphatase/kinase (DNA 5'-kinase/3'-phosphatase) (Polynucleotide kinase-3'-phosphatase) [Includes: Polynucleotide 3'-phosphatase (EC 3.1.3.32) (2'(3')-polynucleotidase); Polynucleotide 5'-hydroxyl-kinase (EC 2.7.1.78)] (Q9JLV6)
Organism: Mus musculus (Mouse)
Function: Plays a key role in the repair of DNA damage, functioning as part of both the non-homologous end-joining (NHEJ) and base excision repair (BER) pathways. Through its two catalytic activities, PNK ensures that DNA termini are compatible with extension and ligation by either removing 3'-phosphates from, or by phosphorylating 5'-hydroxyl groups on, the ribose sugar of the DNA backbone.
Subcellular location: Nucleus {ECO:0000250|UniProtKB:Q96T60}.
Interaction partners:
- DNA repair protein XRCC1
- DNA polymerase beta
- DNA ligase 3
- DNA repair protein XRCC4
- Tyrosyl-DNA phosphodiesterase 1
- Endonuclease 8-like 1 lyase Neil1)
- Endonuclease 8-like 2 lyase Neil2)
- Aprataxin and PNK-like factor
- X-ray repair cross-complementing protein 6
- Bifunctional 3'-5' exonuclease/ATP-dependent helicase WRN
Sequence:
MSQLGSRGRLWLQSPTGGPPPIFLPSDGQALVLGRGPLTQVTDRKCSRNQVELIADPESRTVAVKQLGVNPSTVGVHELKPGLSGSLSLGDVLYLVNGLYPLTLRWEELSTSGSQPDAPPDTPGDPEEGEDTEPQKKRVRKSSLGWESLKKLLVFTASGVKPQGKVAAFDLDGTLITTRSGKVFPTSPSDWRILYPEIPKKLQELAAEGYKLVIFTNQMGIGRGKLPAEVFKGKVEAVLEKLGVPFQVLVATHAGLNRKPVSGMWDHLQEQANEGIPISVEDSVFVGDAAGRLANWAPGRKKKDFSCADRLFALNVGLPFATPEEFFLKWPAARFELPAFDPRTISSAGPLYLPESSSLLSPNPEVVVAVGFPGAGKSTFIQEHLVSAGYVHVNRDTLGSWQRCVSSCQAALRQGKRVVIDNTNPDVPSRARYIQCAKDAGVPCRCFNFCATIEQARHNNRFREMTDPSHAPVSDMVMFSYRKQFEPPTLAEGFLEILEIPFRLQEHLDPALQRLYRQFSEG
Protein: Co-chaperonin GroES (10 kDa chaperonin) (Chaperonin-10) (Cpn10) (P0A6F9)
Organism: Escherichia coli (strain K12)
Function: Together with the chaperonin GroEL, plays an essential role in assisting protein folding. The GroEL-GroES system forms a nano-cage that allows encapsulation of the non-native substrate proteins and provides a physical environment optimized to promote and accelerate protein folding, probably by preventing aggregation and by entropically destabilizing folding intermediates. GroES binds to the apical surface of the GroEL ring, thereby capping the opening of the GroEL channel. Regulates the ATPase activity of GroEL.
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00580, ECO:0000269|PubMed:22380631}. Note=Exclusively localized in foci, usually near 1 cell pole in mid-to-late exponential phase; polar localization depends on the minCDE operon. Foci form near midcell.
Interaction partners:
- Chaperone protein DnaK
- Chaperonin GroEL
- Protein GrpE
- Chaperone protein HtpG
- Chaperone protein DnaJ
- Chaperone protein ClpB
- ATP-dependent protease ATPase subunit HslU
- ATP-dependent protease subunit HslV
- ATP-dependent Clp protease proteolytic subunit
- Trigger factor
Sequence:
MNIRPLHDRVIVKRKEVETKSAGGIVLTGSAAAKSTRGEVLAVGNGRILENGEVKPLDVKVGDIVIFNDGYGVKSEKIDNEEVLIMSESDILAIVEA
Protein: Probable ubiquitin carboxyl-terminal hydrolase 7 (EC 3.4.19.12) (Deubiquitinating enzyme 7) (Ubiquitin thioesterase 7) (Ubiquitin-specific-processing protease 7) (Q9P7S5)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Interaction partners:
- Ubiquitin carboxyl-terminal hydrolase 14
- Putative ubiquitin thioesterase otu1
- Probable mRNA-splicing protein ubp10
- Ubiquitin thioesterase otu2
- AMSH-like protease sst2
- Probable ubiquitin carboxyl-terminal hydrolase 2
- Probable ubiquitin carboxyl-terminal hydrolase 9
- Ubiquitin carboxyl-terminal hydrolase 6
- Probable ubiquitin carboxyl-terminal hydrolase 1
- Probable ubiquitin carboxyl-terminal hydrolase 1
Sequence:
MPHSNTLIVPSTNPFDDPSSIKNGLNNLTSSELVNQMKKESLAASVKTPSTPPKECSHLKKGVKLSHLKGNARALRDPSKHLCFICTTEKIKREDYELTLCANCGYLFCCNHESDHSRKHFEKNKKHCVFVNIITLKCHCYSCDADIVIFDKKNLVVRDVQQFICSNLVSSLTKAPNVLKSNSSHFKKEKKSKHSSGKSSKKYKVISPGLKNLGATCFFNSTLQVLCACEALHDVISPFQYSHSSVIVRKLTKSPESSLLSAFIKFLETFYKSDGTISVYRPTTFFGEFRRLHPQFSESVQQDAHELLRLLLDDLISEEFRVLRFNLNSVSRSLQLSPCLTDDEQLSKSLTSFKQVNVTDASLSPNSHNTSDNEQNNEDYVSVSSLVGSETEDITYSKELSQSSDSSQHQHDSFLPANSSPLAASSTKSLPSSELLDSSSDKGQQVFKGQHEVAGTNSFEDPNSHFNVSNSSNHEEASPKKEVLKSPQFQRRSLDILRLGELSSDDMMLDKATMDEFSSSLVIKSIFTGRLTSVVMCQSCNEITNTPEPIQDLSIPIHYPSSRVSRRHRFHRALRSRFSRSPKKSSVKIVVDNANDDTDQAPTTNSSSLNENLLGGHASENDKSLKQSPFQKLTRRLSDLSVNSSGQISKQDFDNSNSIFSESSLSSPIIEEPKTLIDCLKNFTHVEELSGENMFACENCCNQPNEVGSPAKGGLTSDNDKYSFNNSVYRNAYKRMLLDDPLPPVFIIHLKRFFQEISHDGYANPKKISDFIEFEQELDLNEFVMPHLRASSSFRYRLFGVIVHSGTLNYGHYVAYVLSHKFLDLSAPSTNSKDFRSEAGIPERRWLYISDNIVRESSWDEVSKVEAYMLFYERV
Protein: Heat shock protein 90 (Q0Q0I7)
Organism: Triticum aestivum (Wheat)
Interaction partners:
- Cysteine and histidine-rich domain-containing protein RAR1
- Cysteine and histidine-rich domain-containing protein RAR1
- HSP70
- Protein SGT1 homolog
- Protein SGT1 homolog
- Cysteine and histidine-rich domain-containing protein RAR1
- peptidylprolyl isomerase
- peptidylprolyl isomerase
- peptidylprolyl isomerase
- peptidylprolyl isomerase
Sequence:
MATETETFAFQAEINQLLSLIINTFYSNKEIFLRELISNSSDALDKIRFESLTDKSKLDAQPELFIHIIPDKATNTLTIVDSGIGMTKSDLVNNLGTIARSGTKEFMEALAAGADVSMIGQFGVGFYSAYLVAERVVVTTKHNDDEQYVWESQAGGSFTVTRDTSGEQLGRGTKMVLYLKDDQMEYLEERRIKDLVKKHSEFISYPISLWTEKTTEKEISDDEDEEEKKDTEEGKVEDVDEEKEEKEKKKKKIKEVSHEWNLVNKQKPIWMRKPEEINKEEYAAFYKSLTNDWEEHLAVKHFSVEGQLEFKAVLFVPKRAPFDLFDNKKKANNIKLYVRRVFIMDNCEELIPEYLSFVKGIVDSEDLPLNISRETLQQNKILKVIRKNLVKKCIELFFEIAENKEDYNKFYEAFSKNLKLGIHEDSQNRTKIAELLRYHSTKSGDELTSLKDYVTRMKEGQNEIYYITGESKKAVENSPFLEKLKKKGYEVIYMVDAIDEYAIGQLKEFEGKKLVSATKEGLKLDESEDEKKKQEELKEKFEGLCKVIKEVLGDKVEKVIVSDRVVDSPCCLVTGEYGWTANMERIMKAQALRDSSMAGYMSSKKTMEINPENAIMDELRKRADADKNDKSVKDLVMLLFETSLLTSGFSLEDPNTFGTRIHRMLKLGLSIDEDDEAPENDTDMPPLEDDAGESKMEEVD
Protein: Starch-binding domain-containing protein 1 (Genethonin-1) (Glycophagy cargo receptor stbd1) (Q8C7E7)
Organism: Mus musculus (Mouse)
Function: Acts as a cargo receptor for glycogen. Delivers its cargo to an autophagic pathway called glycophagy, resulting in the transport of glycogen to lysosomes.
Subcellular location: Preautophagosomal structure membrane {ECO:0000250|UniProtKB:Q5FVN1, ECO:0000305|PubMed:20810658}; Single-pass type III membrane protein {ECO:0000250|UniProtKB:O95210}. Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:O95210}; Single-pass type III membrane protein {ECO:0000250|UniProtKB:O95210}. Cell membrane, sarcolemma, T-tubule {ECO:0000250|UniProtKB:O95210}. Note=Also detected near the junctional sarcoplasmic reticulum (By similarity). Concentrates at perinuclear structures (PubMed:20810658). {ECO:0000250|UniProtKB:O95210, ECO:0000269|PubMed:20810658}.
Interaction partners:
- Gamma-aminobutyric acid receptor-associated protein-like 1
- Glycogen debranching enzyme
Sequence:
MGAVWSALLVGGGLAGALILWLLRGDSGAPGKDGVAEPPQKGAPPGEAAAPGDGPGGGGSGGLSPEPSDRELVSKAEHLRESNGHLISESKDLGNLPEAQRLQNVGADWVNAREFVPVGKIPDTHSRADSEAARNQSPGSHGGEWRLPKGQETAVKVAGSVAAKLPSSSLLVDRAKAVSQDQAGHEDWEVVSRHSSWGSVGLGGSLEASRLSLNQRMDDSTNSLVGGRGWEVDGKVASLKPQQVSIQFQVHYTTNTDVQFIAVTGDHESLGRWNTYIPLHYCKDGLWSHSVFLPADTVVEWKFVLVENKEVTRWEECSNRFLQTGHEDKVVHGWWGIH
Protein: Group XIIA secretory phospholipase A2 (GXII sPLA2) (sPLA2-XII) (EC 3.1.1.4) (Phosphatidylcholine 2-acylhydrolase 12A) (Q9BZM1)
Organism: Homo sapiens (Human)
Function: PA2 catalyzes the calcium-dependent hydrolysis of the 2-acyl groups in 3-sn-phosphoglycerides. Does not exhibit detectable activity toward sn-2-arachidonoyl- or linoleoyl-phosphatidylcholine or -phosphatidylethanolamine.
Subcellular location: Secreted {ECO:0000269|PubMed:12522102}. Cytoplasm {ECO:0000269|PubMed:12522102}.
Interaction partners:
- Group 10 secretory phospholipase A2
- Group 3 secretory phospholipase A2
- Group IID secretory phospholipase A2
- Phospholipase A2, membrane associated
- Cytochrome P450 2E1
- Group IIE secretory phospholipase A2
- Group IIF secretory phospholipase A2
- Phospholipase A2 group V
- Phospholipase A and acyltransferase 3
- Lysosomal phospholipase A and acyltransferase
Sequence:
MALLSRPALTLLLLLMAAVVRCQEQAQTTDWRATLKTIRNGVHKIDTYLNAALDLLGGEDGLCQYKCSDGSKPFPRYGYKPSPPNGCGSPLFGVHLNIGIPSLTKCCNQHDRCYETCGKSKNDCDEEFQYCLSKICRDVQKTLGLTQHVQACETTVELLFDSVIHLGCKPYLDSQRAACRCHYEEKTDL
Protein: Dystrophin-related protein 2 (DRP-2) (Q9EPA0)
Organism: Rattus norvegicus (Rat)
Function: Required for normal myelination and for normal organization of the cytoplasm and the formation of Cajal bands in myelinating Schwann cells. Required for normal PRX location at appositions between the abaxonal surface of the myelin sheath and the Schwann cell plasma membrane. Possibly involved in membrane-cytoskeleton interactions of the central nervous system.
Subcellular location: Postsynaptic density {ECO:0000269|PubMed:11083927}. Cell projection, dendrite {ECO:0000269|PubMed:11083927}. Perikaryon {ECO:0000269|PubMed:11083927}. Cell membrane {ECO:0000269|PubMed:11430802, ECO:0000305|PubMed:11083927}; Peripheral membrane protein {ECO:0000305}. Note=Detected in Schwann cells at periaxonal myelin membranes. {ECO:0000269|PubMed:11430802}.
Interaction partners:
- Periaxin
- Sarcospan
Sequence:
MQPLVMQGCPYTLPRCHEWHAADRFHHSSSLRNTCPQPQVRAAVTIPAPPWDGAGDPCLSPKLLNGSVGAVGPLEPSAMNLCWNEIKKKSHNLRARLEAFSDHSGKLQLPLQEIIDWLSQKDEELSAQLPLQGDVALVQQEKETHAAFMEEVKSKGPYIYSVLESAQAFLSQHPFEELEESHSESKDTSPRQRIQNLSRFVWKQATVASELWEKLTARCVDQHRHIEHTLEHLLEIQGAMEELSSTLTQAEGVRATWEPIGDLFIDSLPEHIQAIKLFKEEFSPVKDGVKLVNDLAHQLAISDVHLSMENSRALEQINVRWKQLQVSVAERLKQLQDAHRDFGPGSQHFLSTSVQVPWERAISPNKVPYYINHQAQTTCWDHPKMTELYQTLADLNNIKFSAYRTAMKLRRVQKALRLDLVTLTTALEIFNEHDLQASEHVMDVVEVIHCLTALYERLEEERGILVNVPLCVDMSLNWLLNVFDSGRSGKMRALSFKTGIACLCGTEVKEKLQYLFSQVANSGSQCDQRHLGALLHEAIQVPRQLGEVAAFGGSNVEPSVRSCFRFSTGKPVIEASQFLEWVNLEPQSMVWLAVLHRVTVAEQVKHQTKCSICRQCPIKGFRYRSLKQFNVDICQTCFLTGKASKGNKLHYPIMEYYTPTTSSENMRDFATTLKNKFRSKQYFSKHPQRGYLPVQSVLESDCSETPASSPMLPHADTHSRIEHFASRLAEMESQNCSFFNDSLSPDDSIDEDQYLLRHSSPITDREPAFGQQAPCSMATESKGELEKILAHLEDENRILQGELRRLKWQHEEAVEAPTLAEGSAEATPDHRNEELLAEARILRQHKSRLETRMQILEDHNKQLESQLQRLRELLLQPPTESDGNGSAGSSLASSPRQSEGSHPREKGQTTPDTEAADDVGSKSQDVSLCLEDIMEKLRHAFPSVRSSDVTANTLLAS
Protein: Protein ECM11 (Extracellular mutant protein 11) (Q04110)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: May be involved in cell wall organization and biogenesis.
Subcellular location: Nucleus {ECO:0000269|PubMed:11678331}.
Interaction partners:
- Grand meiotic recombination cluster protein 2
- Synaptonemal complex protein ZIP1
- Protein RED1
- MutS protein homolog 4
- Meiosis-specific protein SPO11
- Sporulation-specific protein 22
- Chromosome stability protein 9
- Protein ZIP2
- Ubiquitin-like protein SMT3
- Meiosis-specific transcription factor NDT80
Sequence:
MTVIKTEPTTEVTLYSPPSKESLSKDDAHRKKQNNKPPSSINSRSGPNKHKLAAKAPEKKINNTDKQDLSAFLLNPSLIVKPSESKKKENIVAYNDTPGIKTEHTAFQPLTPISKKRALKEKAASEKCDSFDLSRDEKPYIQKKSKTLSSVTEINSSEYKLSLNGENTSSPAKEKSQEPIENPGSYQKTRNYLFEKPDPLDTCLQDYSSMLPSNVAEEDQEYFISVADSTLEEWTNKGQEIIDQQFQLYQEIIKKRIELSYKFKGIISVINDRADALEEQGQQLEGKIKKVKTLANEILNII