wanglab/gogpt-training-data huggingface dataset:
Protein: Protective antigen (PA) (Anthrax toxins translocating protein) (PA-83) (PA83) [Cleaved into: Protective antigen PA-20 (PA-20) (PA20); Protective antigen PA-63 (PA-63) (PA63)] (P13423)
Organism: Bacillus anthracis
Function: Protective antigen constitutes one of the three proteins composing the anthrax toxin; it mediates attachment to host cells and translocation of edema factor (EF) and lethal factor (LF) into the host cytoplasm. PA associated with LF forms the lethal toxin (LeTx) and causes death when injected; PA associated with EF forms the edema toxin (EdTx) and produces edema. PA induces immunity to infection with anthrax.
Subcellular location: [Protective antigen]: Secreted {ECO:0000269|PubMed:11207581, ECO:0000269|PubMed:12606539}. Host cell membrane {ECO:0000269|PubMed:11700562, ECO:0000269|PubMed:14507921}. Note=Secreted through the Sec-dependent secretion pathway (PubMed:12606539). Therefore, PA is translocated across the membrane in an unfolded state and then it is folded into its native configuration on the trans side of the membrane, prior to its release to the environment (PubMed:12606539). PA requires the extracellular chaperone PrsA for efficient folding (PubMed:12606539). It circulates in the host blood and binds host cell receptors at the cell surface (PubMed:11700562, PubMed:14507921). {ECO:0000269|PubMed:11700562, ECO:0000269|PubMed:12606539, ECO:0000269|PubMed:14507921}.; SUBCELLULAR LOCATION: [Protective antigen PA-63]: Host cell membrane {ECO:0000305|PubMed:16051798, ECO:0000305|PubMed:25778700}; Multi-pass membrane protein {ECO:0000269|PubMed:25778700, ECO:0000269|PubMed:32047164}. Host endosome membrane {ECO:0000305|PubMed:10085027}; Multi-pass membrane protein {ECO:0000269|PubMed:25778700, ECO:0000269|PubMed:32047164}. Note=Following attachment to host cell receptors at the cell surface and cleavage by FURIN, homooligomerizes to form ring-shaped oligomers that are in a pre-pore conformation, and associates with EF and LF (PubMed:15313199). Loaded complexes are then endocytosed in a clathrin-dependent process, followed by a conformational change of oligomerized PA-63 from the pre-pore to pore state, which is triggered by the low pH in the endosome (PubMed:10085027, PubMed:15326297). {ECO:0000269|PubMed:10085027, ECO:0000269|PubMed:15313199, ECO:0000269|PubMed:15326297}.
Interaction partners:
Sequence:
MKKRKVLIPLMALSTILVSSTGNLEVIQAEVKQENRLLNESESSSQGLLGYYFSDLNFQAPMVVTSSTTGDLSIPSSELENIPSENQYFQSAIWSGFIKVKKSDEYTFATSADNHVTMWVDDQEVINKASNSNKIRLEKGRLYQIKIQYQRENPTEKGLDFKLYWTDSQNKKEVISSDNLQLPELKQKSSNSRKKRSTSAGPTVPDRDNDGIPDSLEVEGYTVDVKNKRTFLSPWISNIHEKKGLTKYKSSPEKWSTASDPYSDFEKVTGRIDKNVSPEARHPLVAAYPIVHVDMENIILSKNEDQSTQNTDSQTRTISKNTSTSRTHTSEVHGNAEVHASFFDIGGSVSAGFSNSNSSTVAIDHSLSLAGERTWAETMGLNTADTARLNANIRYVNTGTAPIYNVLPTTSLVLGKNQTLATIKAKENQLSQILAPNNYYPSKNLAPIALNAQDDFSSTPITMNYNQFLELEKTKQLRLDTDQVYGNIATYNFENGRVRVDTGSNWSEVLPQIQETTARIIFNGKDLNLVERRIAAVNPSDPLETTKPDMTLKEALKIAFGFNEPNGNLQYQGKDITEFDFNFDQQTSQNIKNQLAELNATNIYTVLDKIKLNAKMNILIRDKRFHYDRNNIAVGADESVVKEAHREVINSSTEGLLLNIDKDIRKILSGYIVEIEDTEGLKEVINDRYDMLNISSLRQDGKTFIDFKKYNDKLPLYISNPNYKVNVYAVTKENTIINPSENGDTSTNGIKKILIFSKKGYEIG
Protein: BCL2 associated X, apoptosis regulator b (Bax2) (Bcl2-associated X protein, b) (Q5EAR7)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
Sequence:
MACEASQDYQIGEALLIGVVRQELMEVMEVTEGNAAPPALPEAKPISNSQDQILVQQLANTIKVIGDKLDQDQAFNDMIDGLVKVADKSSFWKLVEKVFTDGQINWGRIIVLFYSVGKLSAKMVVARLPRIVSDILSLSLDYFKRNLLQWILTVGGWMNSIPALACFSVDQFSGSSMRKYSPYVGVVFAFTGGLLLGGFIVSRFQKT
Protein: Protein EMSY-LIKE 1 (AtEML1) (Q9C7C4)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Probably involved in the regulation of chromatin states (Probable). Contributes to RPP7-mediated and basal immunity, especially against Hyaloperonospora arabidopsidis isolate Hiks1. Regulates negatively EDM2-dependent floral transition.
Subcellular location: Nucleus {ECO:0000269|PubMed:21830950}.
Interaction partners:
- Protein ENHANCED DOWNY MILDEW 2
- Uncharacterized methyltransferase At1g78140, chloroplastic
- Pollen Ole e 1 allergen and extensin family protein
- L10-interacting MYB domain-containing protein
- Protein SAWADEE HOMEODOMAIN HOMOLOG 2
- Uncharacterized GPI-anchored protein At3g06035
- Serine/threonine-protein kinase GRIK1
- 26S proteasome regulatory subunit 10B homolog A
Sequence:
METQIHQLEQEAYTAVLRAFKAQSDAISWEKESLITELRKELRVSDDEHRELLSRVNKDDTIQRIRDWRQGGASQITRHATIQPFDVLPSPTFSAARKKQKTFPSYNPSIGATGNRSFNNRLVSSGISGNESAEALIGRKVWTKWPEDNHFYEAIITQYNADEGRHALVYDIHAANETWEWVDLKEIPPEDIRWDGEESGVALNIGHGSASFRGNRRGQIHGGRGRGPRIHQPRRELVPPPTQQNGSGGRRTSSDDIELFNTDSLVKEVERVFDSTHPDPLELDKAKKMLKEHEQALIAAIARLADTSDGEMDGDPPYSHDHPMPQG
Protein: Cripto, FRL-1, cryptic family 1 (F1LV65)
Organism: Rattus norvegicus (Rat)
Interaction partners:
- Activin receptor type-2B
- Activin receptor type-1B
Sequence:
MELGYQREGDGAREISYLLSPKLPGTTLDGTLSSSSRKNDSQEGAHPSEALSGSNTLEESAVPGSRCCHNGGTCVLGSFCVCPAHFTGRYCEHDQRHRDCGALGHGAWTLHSCRLCRCIFSALYCLPRQTFSHCDLKSFLSSGARGSRACSIPRLLLLVLCLLLQVVCGW
Protein: Translocon-associated protein subunit delta (Signal sequence receptor subunit delta) (A6NLM8)
Organism: Homo sapiens (Human)
Subcellular location: Endoplasmic reticulum membrane {ECO:0000256|ARBA:ARBA00004115}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004115}.
Interaction partners:
Sequence:
MAAMASLGALALLLLSSLSRCSAEACLEPQITPSYYTTSDAVISTETVFIVEISLTCKNRVQVSWSLDHKSAHAGTYEVRFFDEESYSLLRKAQRNNEDISIIPPLFTVSVDHRGTWNGPWVSTEVLAAAIGLVIYYLAFSAKSHIQA
Protein: Troponin T, slow skeletal muscle (TnTs) (Slow skeletal muscle troponin T) (sTnT) (P13805)
Organism: Homo sapiens (Human)
Function: Troponin T is the tropomyosin-binding subunit of troponin, the thin filament regulatory complex which confers calcium-sensitivity to striated muscle actomyosin ATPase activity.
Interaction partners:
- Troponin I, fast skeletal muscle
- Troponin I, cardiac muscle
- Troponin I, slow skeletal muscle
- Troponin C, skeletal muscle
- Troponin C, slow skeletal and cardiac muscles
- Tropomyosin alpha-1 chain
- Tropomyosin beta chain
- Tropomyosin alpha-3 chain
- Myosin light chain 1/3, skeletal muscle isoform
- Troponin T, cardiac muscle
Sequence:
MSDTEEQEYEEEQPEEEAAEEEEEAPEEPEPVAEPEEERPKPSRPVVPPLIPPKIPEGERVDFDDIHRKRMEKDLLELQTLIDVHFEQRKKEEEELVALKERIERRRSERAEQQRFRTEKERERQAKLAEEKMRKEEEEAKKRAEDDAKKKKVLSNMGAHFGGYLVKAEQKRGKRQTGREMKVRILSERKKPLDIDYMGEEQLRARSAWLPPSQPSCPAREKAQELSDWIHQLESEKFDLMAKLKQQKYEINVLYNRISHAQKFRKGAGKGRVGGRWK
Protein: Protein GOLVEN 7 (CLAVATA3/ESR (CLE)-related protein CLEL3) (CLE-Like protein 3) (Root meristem growth factor 3) (AtRGF3) [Cleaved into: GLV7p] (Q6ID76)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Signaling peptide (root growth factor) that maintains the postembryonic root stem cell niche. Regulates the pattern of root growth and lateral root development by modulating the length and the number of cortical cells in the root apical meristem (RAM), and the anticlinal asymmetric cell divisions in lateral root initiation cells (By similarity).
Subcellular location: [GLV7p]: Secreted {ECO:0000250|UniProtKB:Q3E880}.
Interaction partners:
- LRR receptor-like serine/threonine-protein kinase RGI3
- Protein GOLVEN 11
- Protein GOLVEN 10
- Protein GOLVEN 3
- Protein GOLVEN 9
- Protein GOLVEN 6
- Protein GOLVEN 1
- Protein GOLVEN 2
- Root meristem growth factor 10
- CLAVATA3/ESR
Sequence:
MTTLSKILCVLIILLLCFSFRYSLHEDGNQQSSRDFVSTAKAIKYGDVMKKMIRGRKLMMASGEKEEAETKMKRGNRETERNSSKSVEEDGLVAYTADYWRAKHHPPKNN
Protein: Palmitoyltransferase erf2 (EC 2.3.1.225) (DHHC cysteine-rich domain-containing protein erf2) (Meiotically up-regulated gene 142 protein) (Ras protein acyltransferase) (O74384)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: The erf2-erf4 complex is a palmitoyltransferase with a major role in driving sexual development. Palmitoylates ras1. Palmitoylates isp3. Palmitoylates rho3.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q06551}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q06551}. Golgi apparatus, Golgi stack membrane {ECO:0000269|PubMed:16823372}; Multi-pass membrane protein {ECO:0000269|PubMed:16823372}.
Interaction partners:
- Ras modification protein erf4
- Protein-S-isoprenylcysteine O-methyltransferase
- Spore wall structural constituent isp3
- Serine palmitoyltransferase 1
- Serine palmitoyltransferase 2
- Uncharacterized membrane protein C23A1.05
- GTP-binding protein rho3
Sequence:
MSYEKHSDAKASRYAWNQPWNPFEVTLSDPTYPMNLEEKNQIPYRFQSVPDDVPEVPHIESRYKNLPGNNIYLCCGRLQMSSQYKAFLISLFALILPGVLFFIFSAFWLWHHVSPAVPITFAYLYALAVVSMFKCSTADPGILPRNAYSLTYNPAHPWSVIPEDRKVLVGSTRSDSVFVNTVYCHTCHLYRPPRASHCHLCDNCVEYLDHHCIWLNTCIGRRNYRYYFIFLLSVVLSALYLTGLGFYTSIGSFHESTDTNFAAHLRRPWAGVSFFLGIYGALGAILPGILFCYQCYLISVGQNVHEYLRAKSTETEDVHPFHDSIWLNFLVVLCRPKNVSYVRPTRKSYV
Protein: Phospholipase A2 (EC 3.1.1.4) (Group IB phospholipase A2) (PLA2-Ib) (Phosphatidylcholine 2-acylhydrolase 1B) (Q9Z0Y2)
Organism: Mus musculus (Mouse)
Function: Secretory calcium-dependent phospholipase A2 that primarily targets dietary phospholipids in the intestinal tract (By similarity). Hydrolyzes the ester bond of the fatty acyl group attached at sn-2 position of phospholipids (phospholipase A2 activity) with preference for phosphatidylethanolamines and phosphatidylglycerols over phosphatidylcholines (By similarity). May play a role in the biosynthesis of N-acyl ethanolamines that regulate energy metabolism and inflammation in the intestinal tract. Hydrolyzes N-acyl phosphatidylethanolamines to N-acyl lysophosphatidylethanolamines, which are further cleaved by a lysophospholipase D to release N-acyl ethanolamines (By similarity). May act in an autocrine and paracrine manner. Upon binding to the PLA2R1 receptor can regulate podocyte survival and glomerular homeostasis (By similarity). Has anti-helminth activity in a process regulated by gut microbiota. Upon helminth infection of intestinal epithelia, directly affects phosphatidylethanolamine contents in the membrane of helminth larvae, likely controlling an array of phospholipid-mediated cellular processes such as membrane fusion and cell division while providing for better immune recognition, ultimately reducing larvae integrity and infectivity.
Subcellular location: Secreted {ECO:0000250|UniProtKB:P04054}. Note=Secreted from pancreatic acinar cells in its inactive form. {ECO:0000250|UniProtKB:P04054}.
Interaction partners:
- Group XIIA secretory phospholipase A2
- Group XIIB secretory phospholipase A2-like protein
- Group 3 secretory phospholipase A2
- Cytochrome P450 2E1
- Group IIC secretory phospholipase A2
- Group 10 secretory phospholipase A2
- Phospholipase A and acyltransferase 3
- Phospholipase A2 group V
- Group IIE secretory phospholipase A2
- Polyunsaturated fatty acid 5-lipoxygenase
Sequence:
MKLLLLAALLTAGAAAHSISPRAVWQFRNMIKCTIPGSDPLKDYNNYGCYCGLGGWGTPVDDLDRCCQTHDHCYSQAKKLESCKFLIDNPYTNTYSYSCSGSEITCSAKNNKCEDFICNCDREAAICFSKVPYNKEYKNLDTGKFC
Protein: Olfactory receptor (Q8VEY9)
Organism: Mus musculus (Mouse)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004651, ECO:0000256|RuleBase:RU363047}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651, ECO:0000256|RuleBase:RU363047}.
Interaction partners:
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein G
Sequence:
MEAENHTAIVHFLLIGLSEDPKIQSVLFGLFLSMFLITMLGNFLIVLVTSCDSHLHTPMYFFLCNLSFVDICLTSTTIPKMLVNIYMHTMKISYTECLTQVYFFNNFLGMDNFLLTIMAYDRFVAICHPLNYTVIMNPRICGLLVLLSWIIMFWVSLIHMLLMKQLNFSTSTEIPHFFCELTELLRVARSDTHINNIFLYLVTAVLGMFPVIGIAFSYFHIVSALMKMSSIKNKYKAFSTCGSHLCVVSMFYGTGFVVHLSSAVAHSSKRNTITSIMYTVVTPMLNPFIYSLRNKDVKGALVRLLRRVKFCP
Protein: At4g29110 (Cotton fiber protein) (Q9SZE0)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
Sequence:
MESSVPKRGLYMEMEQNAQVAAKRLWKVVRIVFCVLKTGTVKNKLMLDLNLMLKRGNKAITNLRRRSSSTGSHDVSSSSRVRDYDPFAFISKRKRRVHGGYDNEEDAVEAAVKKVFELLGENDKKTVATESARESPLIMSPAVRQLRVTDSPFPLDDGGDHDHVVDKAAEEFIKKFYKNLKLQKKMTNALESPYHDGWVR
Protein: Protein disulfide isomerase-like 2-3 (OsPDIL2-3) (EC 5.3.4.1) (Protein disulfide isomerase-like 5-1) (OsPDIL5-1) (Q67UF5)
Organism: Oryza sativa subsp. japonica (Rice)
Function: Acts as a protein-folding catalyst that interacts with nascent polypeptides to catalyze the formation, isomerization, and reduction or oxidation of disulfide bonds. May play a role in storage protein biogenesis.
Subcellular location: Endoplasmic reticulum lumen {ECO:0000269|PubMed:21278127}. Note=Localizes on the surface of ER-derived type-I protein bodies in the endosperm. {ECO:0000269|PubMed:21278127}.
Interaction partners:
- Endoplasmic oxidoreductin 1, putative, expressed
- Nitrate reductase
- Nitrate reductase 1
- Nitrate reductase
- Probable 5'-adenylylsulfate reductase 1, chloroplastic
- Protein disulfide isomerase-like 1-1
- Protein disulfide isomerase-like 1-4
- Protein disulfide isomerase-like 2-1
- Protein disulfide isomerase-like 2-2
- Protein disulfide isomerase-like 1-2
Sequence:
MRPAVAAALLLVAAAVAASPVSALYSAGSPVLQFNPNNFKSKVLNSNGVVLVEFFAPWCGHCQQLTPIWEKAAGVLKGVATVAALDADAHKELAQEYGIRGFPTIKVFVPGKPPVDYQGARDVKPIVEFALSQVKALLRDRLNGKTSAGSGGKKSGGSSEKTEPSASIELNSQNFDKLVTKSKDLWIVEFFAPWCGHCKKLAPEWKKAAKNLKGQVKLGHVDCDAEKSLMSKYKVEGFPTILVFGADKESPFPYQGARVASAIESFALEQLEANAAPPEVSELTGPDAMEEKCASAAICFVSFLPDILDSKAEGRNKYLELLLSVAEKFKKSPYSFVWTAAGKQADLEKQVGVGGYGYPAMVALNVKKGAYAPLRSAFQLDEITEFVKEAGRGGKGNLPLDGTPTIVQSEPWDGKDGEVIEEDEFSLEELMADNSPVNDEL
Protein: 5'-methylthioadenosine nucleosidase (MTA nucleosidase) (EC 3.2.2.16) (5'-methylthioadenosine nucleosidase 1) (AtMTAN1) (MTA nucleosidase 1) (Q9T0I8)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Enzyme of the methionine cycle that catalyzes the irreversible cleavage of the glycosidic bond in 5'-methylthioadenosine (MTA) to adenine and 5'-methylthioribose. Contributes to the maintenance of AdoMet homeostasis and is required to sustain high rates of ethylene synthesis. Inactive towards S-adenosylhomocysteine (SAH/AdoHcy).
Interaction partners:
- Methylthioribose kinase
- 1-aminocyclopropane-1-carboxylate synthase 9
- Spermidine synthase 1
- Spermidine synthase 2
- Spermine synthase
- Calcineurin B-like protein 3
- 1-aminocyclopropane-1-carboxylate synthase 8
- 1-aminocyclopropane-1-carboxylate synthase 11
- 1-aminocyclopropane-1-carboxylate synthase 7
- 1-aminocyclopropane-1-carboxylate synthase 4
Sequence:
MAPHGDGLSDIEEPEVDAQSEILRPISSVVFVIAMQAEALPLVNKFGLSETTDSPLGKGLPWVLYHGVHKDLRINVVCPGRDAALGIDSVGTVPASLITFASIQALKPDIIINAGTCGGFKVKGANIGDVFLVSDVVFHDRRIPIPMFDLYGVGLRQAFSTPNLLKELNLKIGRLSTGDSLDMSTQDETLIIANDATLKDMEGAAVAYVADLLKIPVVFLKAVTDLVDGDKPTAEEFLQNLTVVTAALEGTATKVINFINGRNLSDL
Protein: Hexosyltransferase GAUT11 (EC 2.4.1.43) (Galacturonosyltransferase 11) (Q949Q1)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Glycosyltransferase involved in pectin and/or xylans biosynthesis in cell walls (By similarity). Required for the biosynthesis of pectin in seed coat epidermal (SCE) cells. Collaboratively with MUCI70, essential for the accumulation of seed mucilage, a gelatinous wall rich in unbranched rhamnogalacturonan I (RG I), and for shaping the surface morphology of seeds. Catalyzes homogalacturonan (HG) elongation by acting as an HG alpha-1,4 galacturonic acid transferase.
Subcellular location: Golgi apparatus membrane {ECO:0000250}; Single-pass type II membrane protein {ECO:0000255}.
Interaction partners:
- Trifunctional UDP-glucose 4,6-dehydratase/UDP-4-keto-6-deoxy-D-glucose 3,5-epimerase/UDP-4-keto-L-rhamnose-reductase RHM2
- Granule-bound starch synthase 1, chloroplastic/amyloplastic
- Alkaline-phosphatase-like family protein
- Rhamnogalacturonan I rhamnosyltransferase 1
- Beta-galactosidase 6
- UDP-D-xylose:L-fucose alpha-1,3-D-xylosyltransferase 3
- Galactan beta-1,4-galactosyltransferase GALS3
- Protein trichome birefringence-like 10
- UDP-D-xylose:L-fucose alpha-1,3-D-xylosyltransferase
- Pectinesterase inhibitor 6
Sequence:
MRRWPVDHRRRGRRRLSSWIWFLLGSFSVAGLVLFIVQHYHHQQDPSQLLLERDTRTEMVSPPHLNFTEEVTSASSFSRQLAEQMTLAKAYVFIAKEHNNLHLAWELSSKIRSCQLLLSKAAMRGQPISFDEAKPIITGLSALIYKAQDAHYDIATTMMTMKSHIQALEERANAATVQTTIFGQLVAEALPKSLHCLTIKLTSDWVTEPSRHELADENRNSPRLVDNNLYHFCIFSDNVIATSVVVNSTVSNADHPKQLVFHIVTNRVSYKAMQAWFLSNDFKGSAIEIRSVEEFSWLNASYSPVVKQLLDTDARAYYFGEQTSQDTISEPKVRNPKYLSLLNHLRFYIPEIYPQLEKIVFLDDDVVVQKDLTPLFSLDLHGNVNGAVETCLEAFHRYYKYLNFSNPLISSKFDPQACGWAFGMNVFDLIAWRNANVTARYHYWQDQNRERTLWKLGTLPPGLLSFYGLTEPLDRRWHVLGLGYDVNIDNRLIETAAVIHYNGNMKPWLKLAIGRYKPFWLKFLNSSHPYLQDCVTA
Protein: Lysine-specific demethylase hairless (EC 1.14.11.65) ([histone H3]-dimethyl-L-lysine(9) demethylase hairless) (Q61645)
Organism: Mus musculus (Mouse)
Function: Histone demethylase that specifically demethylates both mono- and dimethylated 'Lys-9' of histone H3. May act as a transcription regulator controlling hair biology (via targeting of collagens), neural activity, and cell cycle.
Subcellular location: Nucleus.
Interaction partners:
Sequence:
MESMPSFLKDTPAWEKTAPVNGIVGQEPGTSPQDGLRHGALCLGEPAPFWRGVLSTPDSWLPPGFLQGPKDTLSLVEGEGPRNGERKGSWLGGKEGLRWKEAMLAHPLAFCGPACPPRYGPLIPEHSGGHPKSDPVAFRPLHCPFLLETKILERAPFWVPTCLPPYLMSSLPPERPYDWPLAPNPWVYSGSQPKVPSAFGLGSKGFYHKDPNILRPAKEPLAESGMLGLAPGGHLQQACESEGPSLHQRDGETGAGRQQNLCPVFLGYPDTVPRAPWPSCPPGLVHSLGNIWAGPGSNSLGYQLGPPATPRCPSPGPPTPPGGCCSSHLPAREGDLGPCRKCQDSPEGGSSGPGESSEERNKADSRACPPSHHTKLKKTWLTRHSEQFECPGGCSGKEESPATGLRALKRAGSPEVQGASRGPAPKRPSHPFPGTGRQGARAWQETPETIIGSKAEAEQQEEQRGPRDGRIRLQESRLVDTSCQHHLAGVTQCQSCVQAAGEVGVLTGHSQKSRRSPLEEKQLEEEDSSATSEEGGGGPGPEASLNKGLAKHLLSGLGDRLCRLLRKEREALAWAQREGQGPAMTEDSPGIPHCCSRCHHGLFNTHWRCSHCSHRLCVACGRIAGAGKNREKTGSQEQHTDDCAQEAGHAACSLILTQFVSSQALAELSTVMHQVWAKFDIRGHCFCQVDARVWAPGDGGQQKEPTEKTPPTPQPSCNGDSNRTKDIKEETPDSTESPAEDGAGRSPLPCPSLCELLASTAVKLCLGHDRIHMAFAPVTPALPSDDRITNILDSIIAQVVERKIQEKALGPGLRAGSGLRKGLSLPLSPVRTRLSPPGALLWLQEPRPKHGFHLFQEHWRQGQPVLVSGIQKTLRLSLWGMEALGTLGGQVQTLTALGPPQPTNLDSTAFWEGFSHPETRPKLDEGSVLLLHRTLGDKDASRVQNLASSLPLPEYCAHQGKLNLASYLPLGLTLHPLEPQLWAAYGVNSHRGHLGTKNLCVEVSDLISILVHAEAQLPPWYRAQKDFLSGLDGEGLWSPGSQTSTVWHVFRAQDAQRIRRFLQMVCPAGAGTLEPGAPGSCYLDAGLRRRLREEWGVSCWTLLQAPGEAVLVPAGAPHQVQGLVSTISVTQHFLSPETSALSAQLYHQGASLPPDHRMLYAQMDRAVFQAVKAAVGALQEAK
Protein: Polypeptide N-acetylgalactosaminyltransferase 4 (EC 2.4.1.41) (Polypeptide GalNAc transferase 4) (GalNAc-T4) (pp-GaNTase 4) (Protein-UDP acetylgalactosaminyltransferase 4) (UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 4) (Q8N4A0)
Organism: Homo sapiens (Human)
Function: Catalyzes the initial reaction in O-linked oligosaccharide biosynthesis, the transfer of an N-acetyl-D-galactosamine residue to a serine or threonine residue on the protein receptor. Has a highest activity toward Muc7, EA2 and Muc2, with a lowest activity than GALNT2. Glycosylates 'Thr-57' of SELPLG.
Subcellular location: Golgi apparatus membrane {ECO:0000305|PubMed:9804815}; Single-pass type II membrane protein {ECO:0000305|PubMed:9804815}.
Interaction partners:
- Beta-1,3-galactosyl-O-glycosyl-glycoprotein beta-1,6-N-acetylglucosaminyltransferase
- Alpha-N-acetylgalactosaminide alpha-2,6-sialyltransferase 1
- Mucin-1
- Acetylgalactosaminyl-O-glycosyl-glycoprotein beta-1,3-N-acetylglucosaminyltransferase
- Glycoprotein-N-acetylgalactosamine 3-beta-galactosyltransferase 1
- Beta-1,4 N-acetylgalactosaminyltransferase 1
- C1GALT1-specific chaperone 1
- Mucin-2
- C1GALT1-specific chaperone 1-like protein
- N-acetylgalactosaminyltransferase 7
Sequence:
MAVRWTWAGKSCLLLAFLTVAYIFVELLVSTFHASAGAGRARELGSRRLSDLQKNTEDLSRPLYKKPPADSRALGEWGKASKLQLNEDELKQQEELIERYAINIYLSDRISLHRHIEDKRMYECKSQKFNYRTLPTTSVIIAFYNEAWSTLLRTIHSVLETSPAVLLKEIILVDDLSDRVYLKTQLETYISNLDRVRLIRTNKREGLVRARLIGATFATGDVLTFLDCHCECNSGWLEPLLERIGRDETAVVCPVIDTIDWNTFEFYMQIGEPMIGGFDWRLTFQWHSVPKQERDRRISRIDPIRSPTMAGGLFAVSKKYFQYLGTYDTGMEVWGGENLELSFRVWQCGGKLEIHPCSHVGHVFPKRAPYARPNFLQNTARAAEVWMDEYKEHFYNRNPPARKEAYGDISERKLLRERLRCKSFDWYLKNVFPNLHVPEDRPGWHGAIRSRGISSECLDYNSPDNNPTGANLSLFGCHGQGGNQFFEYTSNKEIRFNSVTELCAEVPEQKNYVGMQNCPKDGFPVPANIIWHFKEDGTIFHPHSGLCLSAYRTPEGRPDVQMRTCDALDKNQIWSFEK
Protein: Interleukin-12 subunit alpha (IL-12A) (O60595)
Organism: Homo sapiens (Human)
Subcellular location: Secreted {ECO:0000256|ARBA:ARBA00004613, ECO:0000256|RuleBase:RU363133}.
Interaction partners:
Sequence:
MWPPGSASQPPPSPAAATGLHPAARPVSLQCRLSMCPARSLLLVATLVLLDHLSLARNLPVATPDPGMFPCLHHSQNLLRAVSNMLQKARQTLEFYPCTSEEIDHEDITKDKTSTVEACLPLELTKNESCLNSRETSFITNGSCLASRKTSFMMALCLSSIYEDLKMYQVEFKTMNAKLLMDPKRQIFLDQNMLAVIDELMQALNFNSETVPQKSSLEEPDFYKTKIKLCILLHAFRIRAVTIDRVMSYLNAS
Protein: LIM zinc-binding domain-containing protein (Q3S1I9)
Organism: Caenorhabditis elegans
Interaction partners:
Sequence:
MNKDWHSDHFCCWQCDQTLTGQRYIMRDEQPYCIKCYEDVFANQCDECAKPIGIDSKDLSYKDKHWHEHCFLCSMCKISLVDMPFGSKNDRIFCSNCYDQAFATRCDGCNEIFRAGMKKMEYKGKQWHDKCFCCAHCKLAIGTKSFIPKNDDVFCGPCYEEKFATRCSKCKKVITAGGVTYKNEPWHRECFCCTNCNSSLAGQRFTSKDEKPYCANCYGDLFAKRCNACTKPITGIGGAKFISFEDRHWHNDCFICAQCTTSLVGKGFITDGHEILCPECAKARLMAANS
Protein: GTPase ERA1, chloroplastic (Zm-ERA1) (GTP-binding protein ERA1) (K7UTH7)
Organism: Zea mays (Maize)
Function: Nuclear genome-encoded probable GTPase involved in ribosome biogenesis in chloroplasts. Plays a role in 16S rRNA maturation in plastids and may contribute to the assembly of the small (30S) ribosomal subunit.
Subcellular location: Plastid, chloroplast stroma, chloroplast nucleoid {ECO:0000269|PubMed:22065420}.
Interaction partners:
- Small ribosomal subunit protein mS29
- Ribosomal protein S5 family protein
- Translation elongation factor EF1B/ribosomal protein S6 family protein
- Small ribosomal subunit protein uS9c
- Ribosomal protein S5 domain 2-like superfamily protein
- Ribosomal protein S24/S35 mitochondrial
- Small ribosomal subunit protein uS14c
- 30S ribosomal protein S16
- Small ribosomal subunit protein bS16c
- 30S ribosomal protein S16
Sequence:
MELGLALRLVAPPPLLPCLSRRALSLPPDFVSSRVLRGRRIHASRLKHGAGVVCNAIMTYSGVEEEEMVEEEMEEEAEPAVSTRPRLELIEKPDRSLALLDEYESEELGTSLCANHRSGYVAVLGKPNVGKSTLINQMVGQKLSIVTDKPQTTRHRILGICSEPEYQIILYDTPGVIKKEMHKLDSMMMKNVRSAIGSADCVLVVADACKTPEKIDEMLEEGVGNKDIGLPVLLVLNKKDLIKPGEIAKKLEWYQKFTNVDDVIPISAKFGHGVDDIKEWILSKLPLGPAYYPKDIASEHPERFFVGEIVREKIFVQYRQEIPYSCQVNVVSYKSRPAAKDFIQVEILVEKESQRGIILGKDGKSIKMLATASRLDIEDFLQKKVYLEVEVKVKENWRQDERLLKRYGYGGEIQAL
Protein: Synovial sarcoma, X breakpoint 2 interacting protein a isoform X1 (Synovial sarcoma, X breakpoint 2-interacting protein a) (X1WH62)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Cell junction, adherens junction {ECO:0000256|ARBA:ARBA00004536}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriolar satellite {ECO:0000256|ARBA:ARBA00004607}.
Interaction partners:
- Actinin, alpha 4.
- Actinin, alpha 1
- Afadin, adherens junction formation factor a.
- Afadin- and alpha-actinin-binding protein
- Ribonuclease T2
- Vitellogenin 7.
- Vitellogenin 6.
- Vitellogenin 5.
- Vitellogenin 4.
Sequence:
MGDWWSPAMMPDPTLDTKELSSISGISMSPSRQNSQHSLHSTMVLPKSTYSVLSAFCTEENISQCVTYINQEVCSLGLSAVSVECKSGSVSAVPVLNLLYEVLQLQRRAQRGLQELETQQIKNCSDLEHLQNNNCRLKDQLEHTRRENSGLHEGERQLQLKIKTLQNCLKSEKEEVQKLQSIISSRATQYNHDLKRKERDFTKLKDRLNQLLMDKRDKKLSIEVSNYVGRSDGKRGLWKTGKMEARHEGEMYKALLTDYEARQRSLMLENSELKKVLQHMKKDMIAILSPKKPCVKAELADDSLEQAGSECEDEAGESSRETLEQSCEQAREQLTNSIRLQWRKLKSHMERLDSQASLVASQEREAEELISRKEQEEELQRMRLELQQCKEFIHMQQQLLQQQISSPCDEETAALLNDCYTLEEKERLKEEWRLFNEQKRNFERERKNFTEAAIRLGHERKVFEEDRAAWLKTQFLNMTPFVDRKRPALSEPHSALSVGTEPEAKLHLTPPLFTKSLSNSVFCTPKAAPVKMPTTADLYRTLNLIPESRGQGKCQSAEMLSRSRLRNSSSDCSVISLVRDENGSV
Protein: AMP deaminase (EC 3.5.4.6) (Q9VY76)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MQSYADALSAKGYRSFGFDTDMEMDMDMGCTTMRRIEKRKGGDLADSPVDEKAEADVEVTNEISAPYEVPQFPIEQIEKKLQIQRHLNEKQATGPRPVATAAVLATNRESSSSTEGRESAVTMERNDADINFQRVSISGEDTSGVPLEDLERASTLLIEALRLRSHYMAMSDQSFPSTTARFLKTVKLKDRINNLPVKEVSDVHLRHSPMKITNPWNVEFPNDEDFKIKPLNGVFHIYENDDESSEIKYEYPDMSQFVNDMQVMCNMIADGPLKSFCYRRLCYLSSKYQMHVLLNELRELAAQKAVPHRDFYNTRKVDTHIHAASCMNQKHLLRFIKKTLKNNANEVVTVTNGQQMTLAQVFQSMNLTTYDLTVDMLDVHADRNTFHRFDKFNSKYNPIGESRLREVFLKTDNYLNGKYFAQIIKEVAFDLEESKYQNAELRLSIYGKSPDEWYKLAKWAIDNDVYSSNIRWLIQIPRLFDIFKSNKMMKSFQEILNNIFLPLFEATARPSKHPELHRFLQYVIGFDSVDDESKPENPLFDNDVPRPEEWTYEENPPYAYYIYYMYANMTVLNKFRQSRNMNTFVLRPHCGEAGPVQHLVCGFLMAENISHGLLLRKVPVLQYLYYLTQIGIAMSPLSNNSLFLNYHRNPLPEYLARGLIISLSTDDPLQFHFTKEPLMEEYSIAAQVWKLSSCDMCELARNSVMMSGFPHAIKQQWLGPIYYEDGIMGNDITRTNVPEIRVAYRYETLLDELSNIFKVNQTCSIADMNAT