wanglab/gogpt-training-data huggingface dataset:
Protein: 3-ketosteroid 1-dehydrogenase helE (EC 1.3.-.-) (Helvolic acid biosynthesis cluster protein E) (Q4WR24)
Organism: Aspergillus fumigatus (strain ATCC MYA-4609 / CBS 101355 / FGSC A1100 / Af293) (Neosartorya fumigata)
Function: 3-ketosteroid 1-dehydrogenase; part of the gene cluster that mediates the biosynthesis of helvolic acid, an antibacterial nortriterpenoid. Protostadienol synthase helA cyclizes (3S)-oxidosqualene to (17Z)-protosta-17(20),24-dien-3-beta-ol (protostadienol). The synthesis of protostadienol is followed by several steps of monooxygenation, dehydrogenation, and acyl transfer to yield the final helvolic acid. Following the cyclization to the tetracyclic protostadienol by helA, cytochrome P450 monooxygenases helB1-mediated and helB2-mediated oxidation at C-4 and C-16, acyltransferase helD2-dependent acetylation of 16-OH, oxidation of C-21 by cytochrome P450 monooxygenase helB4, and short chain dehydrogenase helC-dependent oxidative decarboxylation yield the fusidane skeleton. This intermediate is further modified in three additional steps mediated by the cytochrome P450 monooxygenase helB3, the acyltransferase helD1, and the 3-ketosteroid 1-dehydrogenase helE to give helvolic acid. Compared with the late stages in the biosynthesis of helvolic acid, enzymes involved in the early stage modifications act in a relatively strict order. The hydroxylation of C-16 by helB1 and subsequent acetylation by helD2 should occur before the helB3-mediated oxidation of C-21. C-4 demethylation in fusidane-type antibiotics proceeds in an unusual manner though it is also achieved by oxidative decarboxylation. The methyl group at C-4 beta position is oxidized by helB1 and subsequently removed by the short chain dehydrogenase helC.
Interaction partners:
- Succinate dehydrogenase iron-sulfur subunit, mitochondrial
- Succinate dehydrogenase cytochrome b560 subunit
- Succinate dehydrogenase cytochrome b small subunit
- NADH-ubiquinone oxidoreductase 49 kDa subunit, putative
- NADH dehydrogenase flavoprotein 1, mitochondrial
- NADH-quinone oxidoreductase, 23 kDa subunit, putative
- fumarate hydratase
- Succinate dehydrogenase assembly factor 2, mitochondrial
- NADH-ubiquinone oxidoreductase 304 kDa subunit
- Cytochrome b-c1 complex subunit Rieske, mitochondrial
Sequence:
MAARQLRRLSLPTHLPLPIRPHVRHLGTAQTNCHRFDHETDILIVGSGAAGLTAALRSHFHGLSSLVIEKDAQIGGTSAYSGGGLWIPNNPLAVEAGIIDTPEQAMTYLISVIDADTAEDTDVRRASSPPRKRAFLTHGPHMVSFLRDRGFAFRLSPGCPDYYPQAHGALPTGGRSIEPDVFDARLLGLGEKWTEAIRQRPGRSLPLFTYEASSVTRMGASWRDVGTVLRVLLRGIYLSRVRGQIPVTMGKSLVAQLLWLHMQLDQGPVLTDTALRQLIATPEGVILGARVATPDGERSIRARCGVLLCAGGFAHNQGLRERYGPVPANAEWTSAARGDNGDAIVAGVRVGAATALMDEAWWGPTLRDPVRGMYYFALQERARPFGVIVDSSGKRFMNEAEPYTDAGHHQYAQKAVPAWFVFDWNHRKRYAVGSLMPRQQPPAQALDAGYIHRADTIAELARQIGVNEKGLEGTLARFNEMADCGVDSDFARGESAFDNYFGDPTVRPNPNLGAVRTPPFYAIPLVPGDLGTKGGLLTDEHARVIREDGTPVQGLYAAGNTTASVMGRTYPGAGATLGPAMTFAFIAIDHIASEHV
Protein: Mucin cell adhesion molecule MucCam (Q9EQG0)
Organism: Mus musculus (Mouse)
Interaction partners:
Sequence:
MKNEMFILGLLALTSYFMPGESHHKSRSSQFPVRKYLEDPRYPRYPRPHYSYGFIPSSPKFPKDNQWYKMCPPGTTLMLISRRSPKFLCIPKRQIISDKTKPNATTPAPTTKPTTNATTPAPTNRTTTNAITPAPTPKPTTNATTPATTTNATTPATTTKSTTKEPTTSPKPSTSTAIPTTTKSANSTSSTTTSTTIQTTAPTFAEVFWKFFQQIFRLKK
Protein: SLP adapter and CSK-interacting membrane protein (SLP65/SLP76, Csk-interacting membrane protein) (Q6UWF3)
Organism: Homo sapiens (Human)
Function: Lipid tetraspanin-associated transmembrane adapter/mediator that acts as a scaffold for Src-family kinases and other signaling proteins in immune cells. It is involved in major histocompatibility complex class II (MHC-II) signaling transduction in B cells, where it is required in generating the calcium response and enhancing ERK activity upon MHC-II stimulation. In dendritic cells, it is involved in sustaining CLEC7A/DECTIN1 signaling after CLEC7A activation by fungal beta-glucans (By similarity). It also acts as an agonist-inducible signaling adapter for TLR1, TLR2, TLR3, TLR4, and TLR7 by selectively enabling the expression of pro-inflammatory cytokines IL6 and IL12B in macrophages and acting as a scaffold for phosphorylation of Toll-like receptors by Src-family kinases (By similarity).
Subcellular location: Cell membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000255}. Cell membrane {ECO:0000269|PubMed:21930792}; Lipid-anchor {ECO:0000269|PubMed:21930792}. Cytoplasmic vesicle, phagosome {ECO:0000250|UniProtKB:Q3UU41}. Cell projection, ruffle {ECO:0000250|UniProtKB:Q3UU41}. Cell projection, filopodium {ECO:0000250|UniProtKB:Q3UU41}. Note=Together with MHC-II, associates with lipid-enriched microdomains called tetraspanin-enriched microdomains (TEMs) (PubMed:21930792). Rapidly translocates into immunological synapse (IS) at cell-cell contacts between antigen-presenting cells (APCs) and T-cells (PubMed:21930792). Colocalized with tetraspanins CD37, CD53, and CD81 at the uropod (PubMed:21930792). Present at regions of cell-cell contacts but also at the leading edge of migrating cells (PubMed:21930792). Localizes to phagosomes in dendritic cells after exposure to particulate beta-glucan (By similarity). {ECO:0000250|UniProtKB:Q3UU41, ECO:0000269|PubMed:21930792}.
Interaction partners:
- Tyrosine-protein kinase CSK
- B-cell linker protein
Sequence:
MDTFTVQDSTAMSWWRNNFWIILAVAIIVVSVGLGLILYCVCKWQLRRGKKWEIAKPLKHKQVDEEKMYENVLNESPVQLPPLPPRNWPSLEDSSPQEAPSQPPATYSLVNKVKNKKTVSIPSYIEPEDDYDDVEIPANTEKASF
Protein: Dye-decolorizing peroxidase (MepDyP) (EC 1.11.1.19) (EC 1.11.1.7) (I2DBY3)
Organism: Mycena epipterygia (Yellow-stemmed mycena)
Function: Manganese-independent peroxidase that is able to convert a large number of compounds, but its physiological substrate is not known. In addition to classic peroxidase substrates (e.g. 2,6-dimethoxyphenol), oxidizes dyes such as Reactive Blue 5 and Reactive Black 5.
Subcellular location: Secreted {ECO:0000305|PubMed:23111597}.
Interaction partners:
Sequence:
MRKSISTFILLSVLSVGQLVAARPRSTNAPPRRRTPQPRRTTSLFINPPALPDLPTVQAVDKLDDALDIDNIQSDILVGMKKTKELFFFFGVEDAATFKSKLASDILPLITTTTEILSTDTQPITAVNIAFSHTGLVALGVNDDIGDTDFVSGQFSEATTVGDRPTLWDPAFAGTKIHGVFLLASNTTEDINTELANIQSILGSSITEIHRLQGAARPGAEEGHEHFGFLDGISQPAVNGFTDTVLPGQTPVDPGLFLLGESGDPSQDSRPSWAVDGSFLVFRQLQQFVPEFNQFLADHPLDIPGRTAEEGSELLGARMVGRWKSGAPVFLSPTQDDPVLGADKNRNNDFNYLVASDPDPGTENHFNQTACPFGAHIRKVHPRGDLSPSAENPHFIIRSSIPYGPEVTDAEAASSTTSVDRGLAFVSYQSNIFNGFVFLQSIWINNVNFIFGKVDPTIGVDPIIGTLGGGPHNISGLNPLIPVNETVDFQDDPWNDVVIPRDFVVSHGGEYFFSPSLSGISAIAAA
Protein: HAD superfamily, subfamily IIIB acid phosphatase (Putative vegetative storage protein) (Vegetative storage protein-like) (Q9FNC4)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Large ribosomal subunit protein uL18y
- At1g43860
- Translation elongation factor EF1B/ribosomal protein S6 family protein
- Small ribosomal subunit protein uS14z/uS14y/uS14x
- Large ribosomal subunit protein uL5c
- Large ribosomal subunit protein eL42z/eL42y
- Large ribosomal subunit protein bL28c
- Large ribosomal subunit protein uL24c
- Large ribosomal subunit protein eL38z/eL38y
- Small ribosomal subunit protein eS30z/eS30y/eS30x
Sequence:
MARSLLLSLTLTFLFAGIVSARDWNILSQLKGTTTTTKTSQTGVTSLKAPNLNGYCESWRVNVELNNIRDFKVVPQECVWFVQKYMTSSQYEDDVERAVDEAILYLGKTCCEKKTCDGMDAWIFDIDDTLLSTIPYHKSNGCFGGEQLNTTKFEEWQNSGKAPAVPHMVKLYHEIRERGFKIFLISSRKEYLRSATVENLIEAGYHSWSNLLLRGEDDEKKSVSQYKADLRTWLTSLGYRVWGVMGAQWNSFSGCPVPKRTFKLPNSIYYVA
Protein: Estrogen receptor (ER) (ER-alpha) (Estradiol receptor) (Nuclear receptor subfamily 3 group A member 1) (Q800Q2)
Organism: Zoarces viviparus (Viviparous eelpout) (Blennius viviparus)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|PIRNR:PIRNR002527}.
Interaction partners:
Sequence:
MYPEESRGSGGVTTVDFLEGTYDYAAPTPAPTPLYSHSTPGFYSAPLDSHRPPSDGSLQSLGSGPTSPIVFVPSSPRLSPFLHPPSHHYLETTSTHVYSVPSSQQSVSREDQCGTSDESYSLVESGAGAGAGGFEMAKETRFCAVCSDYASGYHYGVWSCEGCKAFFKRSIQGHNDYMCPATNQCTIDRNRRKSCQACRLRKCYEVGMMKGGVRKDRGHVLRRDKRRSDLSDRDKASKDLEHRTVPSQDRRKRSSISSACVGGKSMLTSMPPDQVLLLLQCAEPPILCSRQKLSRPYTEVTMMTLLTSMADKELVHMIAWAKKLPGFLQLGLHDQVQLLESSWLEVLMIGLIWRSIHCPGKLIFAQDLILDRNEGDCVEGMAEIFDMLLATTSRFRLLKLKPEEFVCLKAIILLNSGAFSFCTATMEPLHDTAAVQHMLDTITDTLIHHIGQSGCSVQQQSRRQAQLLLLLSHIRHMSNKGMEHLYSMKCKNKVPLYDLLLEMLDAHRLHRPDKPGESWFPADGETLCTTSDNISSGGSGSGPRVSHDSPSRAPTVLQYGGSISDCTHIL
Protein: non-specific serine/threonine protein kinase (EC 2.7.11.1) (B6TGM8)
Organism: Zea mays (Maize)
Interaction partners:
Sequence:
MAGPAPDRAALTVGPGMDMPIMHDSDRYELVRDIGSGNFGVARLMRDRRTSELVAVKYIERGEKIDENVQREIINHRSLKHPNIIRFKEVILTPTHLAIVMEYASGGELFERICKNVRFSEDEARYFFQQLISGVSYCHSMQVCHRDLKLENTLLDGSDAPRLKICDFGYSKSSVLHSQPKSTVGTPAYIAPEVLLKKEYDGKIADVWSCGVTLYVMVVGAYPFEDPEEPKNFRKTIQRILNVQYAIPDNVNISPECRHLISRIFVGDPATRITIPEIRNHSWFLKNLPADLMDDDSMSNQYEEPDQPMQTMDQIMQILTEATIPPACSRSINVLADGLDMDDDMDDLDSDSDLDVDSSGEIVYAM
Protein: Autophagy-related protein 30 (I6LAD1)
Organism: Komagataella pastoris (Yeast) (Pichia pastoris)
Function: Acts as the peroxisome receptor for pexophagy. Required for both micropexophagy and macropexophagy, but not for the cytoplasm to vacuole transport (Cvt) or autophagy pathways. Required for functional micropexophagic apparatus (MIPA) and relocation of ATG11 to the peroxisome-sequestering arms of the vacuole.
Subcellular location: Vacuole lumen {ECO:0000269|PubMed:18331717}. Preautophagosomal structure {ECO:0000269|PubMed:18331717}. Peroxisome membrane {ECO:0000269|PubMed:18331717}; Peripheral membrane protein {ECO:0000269|PubMed:18331717}. Note=Surrounds the peroxisome cluster, but a small amount is also inside the vacuole in methanol-grown cells. Upon induction of micropexophagy, localizes inside the vacuolar lumen. Also localizes near peroxisomes during early stages of micropexophagy.
Interaction partners:
Sequence:
MFSRKQVQKRNNELSSLHCSNSSNSLNRIHKNEETAKGTVGVNARGNNRSDNVASPGQLRPRTSSILTDNSEWILFSPENAEGEYVITSSDGIRRTNSNHYYYNYNEDDILSSSRRSSEDVYDAEQEYTEQPVNNHVQVEDEEDDDSIINDLTHVVDDYDYEEEDDKQDLTTRIDNWRKKQVSELLNELNHDDDLDPVLNRDKIDLIQSWGIENEKLNTKPRAKKRQRKSKRASFYGQDLLSKYSMEDLKIIKQIVAQLRDDLDKVKHDKPSSPLPNYHNTLKQAPSSNSQNPSFISYYSNYLTKNNSQQTPNSQSTSGSLLNNPNLEKYLPLFLKNLLYEDSNGSHQHPETSEKEHFWDNDLKSVNSSILTLSSNSKLKQEIL
Protein: Nip100p (A0A1D8PSM7)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Subcellular location: Cytoplasm, cytoskeleton, spindle {ECO:0000256|ARBA:ARBA00004186}.
Interaction partners:
- Microtubule-binding protein
- Dynein heavy chain, cytoplasmic
- Kinesin-like protein
Sequence:
MSFEIGQSVVVKNDIGSIKYIGTTKFAPGVWYGIELLQPKGKNNGSVQGVKYFDCKEDDNGFYGIFVKGSMLNALEDNKNSKSEDVAQYNKTIEKLKSKLKAVTDESIRHREKLIAIQSELQTKIEIMKSMESKLEMQTVENEYLKSIKLDLEEKLRQLSVEHQELKNEFELIQEELEINREIEREMESLDSDHYSPGDVRMIFEKNRRLEDTLALLTRNSKETEIKLKHELEHLQSEQLNMNELQKKLDQAESVVRMLQERIETTEDMDKMMERLTVENEDLTNKIHTLMMTIDDLNEIHELDKKLEEDQKQVELDLRQEIDSLQQIIRQDKLKINELESNRLAQLPHTDKSLESPSRSDQESELQVLRQTISDLRLKSRSDSVQLKLVKARYEILQQRIVYSQASMKFPGLIDLIFMLKLGCSDIAVVKDSISLKSLHQLFANTFLSLIENFLKLLITLLEFNYSAESINELLSELTVKVKACNLCLGDIINVFLSDDLHMNIPHNLHQSFQKLQDNNLDITVTLDLSFSAPRFVYECKECLKLVASSSQLETSFFFDVWKHLRLQTNNADPTITALIKEGDDNLARIKGQVEALKDISHVEEGHDVTFSSAMPDFKEMVSQIGILVKLYDLVKSDGLDINVDSLNKMIELTQVVESLYNLDTEVHSFEITVPSIYEYKSESILQQPSIDDGGLQNKLAQREREVTDLKLNIALLEQNMSSLASQNTQYITELTQKLQSLKKEEEDSSRVISQLEQDKKDLVSELNAVNRNTVSTTSFANLKSQQDYNNSLTIMEKIVHLKRLTKTIDKEQVDDFAWLQPQSKRQFWTEASSVHNLSKSLQSLALNAKPVSINDGNSYKWTKKKDSSKFAALVLEENYNKYKTMRTNLLCSEK
Protein: IP12902p (IP13102p) (Uncharacterized protein, isoform A) (Uncharacterized protein, isoform B) (Q9VCL2)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Don juan like
- Uncharacterized protein, isoform A
- Reticulon-like protein
- AT30637p
- AT04270p
- FI08238p
- GH08353p
- Glycerol-3-phosphate dehydrogenase
- FI23334p1
- FI08446p
Sequence:
MKKKSRRDRTPKVEQPEPSRVVNTEPIRLNVEPQSQEIDDQAAPFILVDCAKYEDRSDLEAMLSSIEKERMKKVQADIEQQYFPLLEDEEPPPELDMPINLSSQALAVLNDADNERRFKEDLESLSIAGLEEKDTSISITNMKIEDSKLLFRTMPGMNQICCTLEQMKNVHGKIGPAEPTPQARCTSLIPLSGLRRQDTFEIKRKKNQKIRYPEVSTKSAISERKHLPLIAKGGKCEKVISETDKIFSQIGDLLVKLQLQHEGSKVLNKGSSYSYMVNIKPAGGASNCSVYALTKLKSHEVEETHAENLRTSHAPLINILYPGRGGLMETSELSTTARCIDGSSIGSMSLRETPSSKIKPSFLRKRPSSHLRAPNPVKFCHGRKKN
Protein: CCAAT/enhancer-binding protein beta (C/EBP beta) (AGP/EBP) (Interleukin-6-dependent-binding protein) (IL-6DBP) (Liver-enriched transcriptional activator) (LAP) (P28033)
Organism: Mus musculus (Mouse)
Function: Important transcription factor regulating the expression of genes involved in immune and inflammatory responses. Also plays a significant role in adipogenesis, as well as in the gluconeogenic pathway, liver regeneration, and hematopoiesis. The consensus recognition site is 5'-T[TG]NNGNAA[TG]-3'. Its functional capacity is governed by protein interactions and post-translational protein modifications. During early embryogenesis, plays essential and redundant roles with CEBPA. Has a promitotic effect on many cell types such as hepatocytes and adipocytes but has an antiproliferative effect on T-cells by repressing MYC expression, facilitating differentiation along the T-helper 2 lineage. Binds to regulatory regions of several acute-phase and cytokines genes and plays a role in the regulation of acute-phase reaction and inflammation. Also plays a role in intracellular bacteria killing. During adipogenesis, is rapidly expressed and, after activation by phosphorylation, induces CEBPA and PPARG, which turn on the series of adipocyte genes that give rise to the adipocyte phenotype. The delayed transactivation of the CEBPA and PPARG genes by CEBPB appears necessary to allow mitotic clonal expansion and thereby progression of terminal differentiation. Essential for female reproduction because of a critical role in ovarian follicle development. Restricts osteoclastogenesis. Together with NFE2L1; represses expression of DSPP during odontoblast differentiation (By similarity).
Subcellular location: Nucleus {ECO:0000269|PubMed:16585579, ECO:0000269|PubMed:19015024}. Cytoplasm {ECO:0000250|UniProtKB:P17676}. Note=In T-cells when sumoylated drawn to pericentric heterochromatin thereby allowing proliferation (PubMed:16585579). Translocates to the nucleus when phosphorylated at Ser-288 (By similarity). {ECO:0000250|UniProtKB:P17676, ECO:0000269|PubMed:16585579}.
Interaction partners:
- Histone-lysine N-methyltransferase PRDM16
- Histone deacetylase 1
- Peroxisome proliferator-activated receptor gamma
- CCAAT/enhancer-binding protein alpha
- Cyclic AMP-dependent transcription factor ATF-4
- Signal transducer and activator of transcription 3
- DNA damage-inducible transcript 3 protein
- Mitogen-activated protein kinase 14
- CCAAT/enhancer-binding protein delta
- CCAAT/enhancer-binding protein gamma
Sequence:
MHRLLAWDAACLPPPPAAFRPMEVANFYYEPDCLAYGAKAARAAPRAPAAEPAIGEHERAIDFSPYLEPLAPAADFAAPAPAHHDFLSDLFADDYGAKPSKKPADYGYVSLGRAGAKAAPPACFPPPPPAALKAEPGFEPADCKRADDAPAMAAGFPFALRAYLGYQATPSGSSGSLSTSSSSSPPGTPSPADAKAAPAACFAGPPAAPAKAKAKKTVDKLSDEYKMRRERNNIAVRKSRDKAKMRNLETQHKVLELTAENERLQKKVEQLSRELSTLRNLFKQLPEPLLASAGHC
Protein: Aminodeoxychorismate synthase (ADC synthase) (EC 2.6.1.85) (P-aminobenzoic acid synthase) (PABA synthase) (Para-aminobenzoate synthase) (P37254)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Catalyzes the biosynthesis of 4-amino-4-deoxychorismate (ADC) from chorismate and glutamine. Required for the synthesis of 4-aminobenzoate (PABA), an important component in tetrahydrofolate biosynthesis.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:14562095}.
Interaction partners:
- Multifunctional tryptophan biosynthesis protein
- Anthranilate phosphoribosyltransferase
- Tryptophan synthase
- Aminodeoxychorismate lyase
- Folic acid synthesis protein FOL1
- Chorismate mutase
- Chorismate synthase ARO2
- N-
- Anthranilate synthase component 1
- Dihydrofolate synthetase
Sequence:
MLSDTIDTKQQQQQLHVLFIDSYDSFTYNVVRLIEQQTDISPGVNAVHVTTVHSDTFQSMDQLLPLLPLFDAIVVGPGPGNPNNGAQDMGIISELFENANGKLDEVPILGICLGFQAMCLAQGADVSELNTIKHGQVYEMHLNDAARACGLFSGYPDTFKSTRYHSLHVNAEGIDTLLPLCTTEDENGILLMSAQTKNKPWFGVQYHPESCCSELGGLLVSNFLKLSFINNVKTGRWEKKKLNGEFSDILSRLDRTIDRDPIYKVKEKYPKGEDTTYVKQFEVSEDPKLTFEICNIIREEKFVMSSSVISENTGEWSIIALPNSASQVFTHYGAMKKTTVHYWQDSEISYTLLKKCLDGQDSDLPGSLEVIHEDKSQFWITLGKFMENKIIDNHREIPFIGGLVGILGYEIGQYIACGRCNDDENSLVPDAKLVFINNSIVINHKQGKLYCISLDNTFPVALEQSLRDSFVRKKNIKQSLSWPKYLPEEIDFIITMPDKLDYAKAFKKCQDYMHKGDSYEMCLTTQTKVVPSAVIEPWRIFQTLVQRNPAPFSSFFEFKDIIPRQDETPPVLCFLSTSPERFLKWDADTCELRPIKGTVKKGPQMNLAKATRILKTPKEFGENLMILDLIRNDLYELVPDVRVEEFMSVQEYATVYQLVSVVKAHGLTSASKKTRYSGIDVLKHSLPPGSMTGAPKKITVQLLQDKIESKLNKHVNGGARGVYSGVTGYWSVNSNGDWSVNIRCMYSYNGGTSWQLGAGGAITVLSTLDGELEEMYNKLESNLQIFM
Protein: CKLF-like MARVEL transmembrane domain-containing protein 3 (Chemokine-like factor superfamily member 3) (Q96MX0)
Organism: Homo sapiens (Human)
Subcellular location: Membrane; Multi-pass membrane protein.
Interaction partners:
- CKLF-like MARVEL transmembrane domain-containing protein 1
- CKLF-like MARVEL transmembrane domain-containing protein 2
- Chemokine-like factor
- CKLF-like MARVEL transmembrane domain-containing protein 4
- CKLF-like MARVEL transmembrane domain-containing protein 7
- CKLF-like MARVEL transmembrane domain-containing protein 8
- CKLF-like MARVEL transmembrane domain-containing protein 6
Sequence:
MWPPDPDPDPDPEPAGGSRPGPAVPGLRALLPARAFLCSLKGRLLLAESGLSFITFICYVASSASAFLTAPLLEFLLALYFLFADAMQLNDKWQGLCWPMMDFLRCVTAALIYFAISITAIAKYSDGASKAAGVFGFFATIVFATDFYLIFNDVAKFLKQGDSADETTAHKTEEENSDSDSD
Protein: Ribokinase (RK) (EC 2.7.1.15) (E9AD19)
Organism: Leishmania major
Function: Catalyzes the phosphorylation of ribose at O-5 in a reaction requiring ATP and magnesium. The resulting D-ribose-5-phosphate can then be used either for sythesis of nucleotides, histidine, and tryptophan, or as a component of the pentose phosphate pathway. Specifically phosphorylates D-ribose. Fails to phosphorylate 4, 5 or 6 D-carbon sugars (erythrose, threose, xylulose, arabinose, fructose and glucose).
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03215}. Nucleus {ECO:0000255|HAMAP-Rule:MF_03215}.
Interaction partners:
- deoxyribose-phosphate aldolase
- Transketolase
- Phosphomannomutase-like protein
- phosphoglucomutase
- ribose-phosphate diphosphokinase
- ribose-phosphate diphosphokinase
- Putative ribose-phosphate pyrophosphokinase
- ribose-phosphate diphosphokinase
- Putative ribose 5-phosphate isomerase
- Transaldolase
Sequence:
MHRVQNVQSHVGEYAPDILVVGSCFLDYVGYVDHMPQVGETMHSESFHKGFGGKGANQAVAAGRLGAKVAMVSMVGTDGDGSDYIKELERNGVHTAYMLRTGKSSTGLAMILVDTKSSNNEIVICPNATNYFTPELLRAQTSNYEKILHTGLKYLICQNEIPLPTTLDTIKEAHSRGVYTVFNSAPAPKPAEVEQIKPFLPYVSLFCPNEVEAALITGMKVTDTESAFRAIKALQQLGVRDVVITLGAAGFALSENGAEPVHVTGKHVKAVDTTGAGDCFVGSMVYFMSRGRNLLEACKRANECAAISVTRKGTQLSYPHPSELPAGVT
Protein: Myosin-1 (Myosin heavy chain 1) (Myosin heavy chain 2x) (MyHC-2x) (Myosin heavy chain IIx/d) (MyHC-IIx/d) (Myosin heavy chain, skeletal muscle, adult 1) (P12882)
Organism: Homo sapiens (Human)
Function: Muscle contraction.
Subcellular location: Cytoplasm, myofibril. Note=Thick filaments of the myofibrils.
Interaction partners:
- Myosin-2
- Myosin light chain 1/3, skeletal muscle isoform
- Myosin regulatory light chain 11
- Myosin-7
- Myosin regulatory light chain 2, ventricular/cardiac muscle isoform
- Myosin-13
- Myosin-8
- Myosin light chain 3
- Myosin-6
- Myosin-14
Sequence:
MSSDSEMAIFGEAAPFLRKSERERIEAQNKPFDAKTSVFVVDPKESFVKATVQSREGGKVTAKTEAGATVTVKDDQVFPMNPPKYDKIEDMAMMTHLHEPAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGESGAGKTVNTKRVIQYFATIAVTGEKKKEEVTSGKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGKLASADIETYLLEKSRVTFQLKAERSYHIFYQIMSNKKPDLIEMLLITTNPYDYAFVSQGEITVPSIDDQEELMATDSAIEILGFTSDERVSIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAAYLQNLNSADLLKALCYPRVKVGNEYVTKGQTVQQVYNAVGALAKAVYDKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWTFIDFGMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYEQHLGKSNNFQKPKPAKGKPEAHFSLIHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSAMKTLALLFVGATGAEAEAGGGKKGGKKKGSSFQTVSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVLNASAIPEGQFIDSKKASEKLLGSIDIDHTQYKFGHTKVFFKAGLLGLLEEMRDEKLAQLITRTQAMCRGFLARVEYQKMVERRESIFCIQYNVRAFMNVKHWPWMKLYFKIKPLLKSAETEKEMANMKEEFEKTKEELAKTEAKRKELEEKMVTLMQEKNDLQLQVQAEADSLADAEERCDQLIKTKIQLEAKIKEVTERAEDEEEINAELTAKKRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDETIAKLTKEKKALQEAHQQTLDDLQAEEDKVNTLTKAKIKLEQQVDDLEGSLEQEKKIRMDLERAKRKLEGDLKLAQESTMDIENDKQQLDEKLKKKEFEMSGLQSKIEDEQALGMQLQKKIKELQARIEELEEEIEAERASRAKAEKQRSDLSRELEEISERLEEAGGATSAQIEMNKKREAEFQKMRRDLEEATLQHEATAATLRKKHADSVAELGEQIDNLQRVKQKLEKEKSEMKMEIDDLASNMETVSKAKGNLEKMCRALEDQLSEIKTKEEEQQRLINDLTAQRARLQTESGEYSRQLDEKDTLVSQLSRGKQAFTQQIEELKRQLEEEIKAKSALAHALQSSRHDCDLLREQYEEEQEAKAELQRAMSKANSEVAQWRTKYETDAIQRTEELEEAKKKLAQRLQDAEEHVEAVNAKCASLEKTKQRLQNEVEDLMIDVERTNAACAALDKKQRNFDKILAEWKQKCEETHAELEASQKESRSLSTELFKIKNAYEESLDQLETLKRENKNLQQEISDLTEQIAEGGKRIHELEKIKKQVEQEKSELQAALEEAEASLEHEEGKILRIQLELNQVKSEVDRKIAEKDEEIDQMKRNHIRIVESMQSTLDAEIRSRNDAIRLKKKMEGDLNEMEIQLNHANRMAAEALRNYRNTQAILKDTQLHLDDALRSQEDLKEQLAMVERRANLLQAEIEELRATLEQTERSRKIAEQELLDASERVQLLHTQNTSLINTKKKLETDISQIQGEMEDIIQEARNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKNLEQTVKDLQHRLDEAEQLALKGGKKQIQKLEARVRELEGEVESEQKRNVEAVKGLRKHERKVKELTYQTEEDRKNILRLQDLVDKLQAKVKSYKRQAEEAEEQSNVNLSKFRRIQHELEEAEERADIAESQVNKLRVKSREVHTKIISEE
Protein: Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit STT3A (EC 2.4.99.18) (Q9VRE0)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Endoplasmic reticulum membrane {ECO:0000256|ARBA:ARBA00004477}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004477}.
Interaction partners:
- Dolichyl-diphosphooligosaccharide--protein glycosyltransferase 48 kDa subunit
- Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit 2
- Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit DAD1
- GH11935p
- Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit 1
- DSec61alpha
- Mannosyl-oligosaccharide glucosidase
- dolichyl-diphosphooligosaccharide--protein glycotransferase
- Protein transport protein Sec61 subunit beta
- Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit 4
Sequence:
MTLDVGGVARGLLTWDKQEHLVKLAILILAAVLSFATRLFSVLRFESVIHEFDPYFNYRTTRFLAEQGFYKFHNWFDDRAWYPLGRIIGGTIYPGLMLTSAALYRLMWLLNVTIDIRNVCVFLAPFFSSLTTLVTYALTKEIHSTGAGLVAAALISIVPGYISRSVAGSYDNEGIAIFCMLFTYYLWIKAVKTGTIFWSAMSALAYFYMVSSWGGYVFLINLIPLHVLALMITGRFSHRIYIAYSTLYCVGTILSMQISFVGFQPIQSSEHMLALGTFGLCQIHAFVDYLRSRIPKDHFDLLFKTLVSSVLTVVFVVGTLLTLTGKVSPWTGRFYSLLDPSYAKNHIPIIASVSEHQPTSWSSFYFDLQILVFLFPAGLYFCFSKLTDSNIFIILYGVTSIYFAGVMVRLMLVLAPVMCVLSGIAISHLLAKYIKSVDAGSSSKQGVESKRQHKKLEQQTGGVKSEVAIGFVGVITLMLIVYTLHCTWVTSEAYSSPSIVLSARSHDGGRIIFDDFREAYYWLQMNTPEDARIMSWWDYGYQITAMANRTILVDNNTWNNTHISRVGQAMASSEEKAYEIMRELDVDYVLVIFGGLTGYSSDDINKFLWMVRIGGSTDRGAHIREKDYYAANGEFRVDKEGSPTLLNCLMYKMCYYRFGQMYTEGGKAQGYDRVRAAEIGNKDFELDVMEEAYTTEHWLVRIYKVKDLPNRGV
Protein: Cathepsin Z (EC 3.4.18.1) (Q9WUU7)
Organism: Mus musculus (Mouse)
Function: Exhibits carboxy-monopeptidase as well as carboxy-dipeptidase activity (By similarity). Capable of producing kinin potentiating peptides (By similarity).
Subcellular location: Lysosome.
Interaction partners:
- Apoptosis regulator Bcl-2
- Bcl-2-like protein 1
- BH3-interacting domain death agonist
- Angiotensinogen
- Legumain
- Cathepsin D
- N-acetylglucosamine-6-sulfatase
- Vesicle-trafficking protein SEC22a
- Lysosomal protective protein
- Baculoviral IAP repeat-containing protein 5
Sequence:
MASSGSVQQLPLVLLMLLLASAARARLYFRSGQTCYHPIRGDQLALLGRRTYPRPHEYLSPADLPKNWDWRNVNGVNYASVTRNQHIPQYCGSCWAHGSTSAMADRINIKRKGAWPSILLSVQNVIDCGNAGSCEGGNDLPVWEYAHKHGIPDETCNNYQAKDQDCDKFNQCGTCTEFKECHTIQNYTLWRVGDYGSLSGREKMMAEIYANGPISCGIMATEMMSNYTGGIYAEHQDQAVINHIISVAGWGVSNDGIEYWIVRNSWGEPWGEKGWMRIVTSTYKGGTGDSYNLAIESACTFGDPIV