wanglab/gogpt-training-data huggingface dataset:
Protein: GLABRA2 expression modulator (Q8S8F8)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Involved in the spatial control of cell division, patterning and differentiation of Arabidopsis root epidermal cells. Could be part of a complex that negatively modulates GLABRA2 and CAPRICE expression via the maintenance of a repressor histone H3 epigenetics status of the GL2 and CPC promoters.
Interaction partners:
- CDT1-like protein b
- CDT1-like protein a, chloroplastic
- GDSL esterase/lipase At2g27360
- Disease resistance protein RML1A
- GDSL esterase/lipase At5g03820
- Uncharacterized protein
- GDSL esterase/lipase At5g45670
- Lysine-specific demethylase JMJ27
- GDSL esterase/lipase At1g29660
- GDSL esterase/lipase At5g03610
Sequence:
MEPPKGDTVVKTEVPVKDPSLSVVDSKTKGVEDANTEIALSDEVEIETKGSDSTPVKAPSRTSSGSKKSVHWSPELVSGSQEPDQKAASSSSAGSNPYIARSPAETSDASLKDTMETVKGVLGRWGKRVAEAAKKTESLAGNTWQHLRTAPSFADAAMGRIAQSTKVFAEGGYEKIFRQTFETDPEEQLLNSFACYLSTSAGPVMGVLYISSAKLAYCSDNPLSYKNGDQTEWSYYKVVIPLHQLKAVNPSASIVNPAEKYIQVISVDNHEFWFMGFLNYDGAVTSLQDSLQAGALRSV
Protein: Nucleoporin-like protein (F4K465)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Probable calcium-binding protein CML17
- Calcium uptake protein, mitochondrial
- Vacuolar protein sorting-associated protein 53 A
- F-box/kelch-repeat protein At3g23880
- Binding protein
Sequence:
MATQGEATFSAAATTTSSYPTGGVGGKLKRQSARRHAATPYSRPTQNQVQRRPWISRIVDPAYRIISGGATRILPYFFSNAASAPALAAPPEDQNQHQGELQNNPQDNDPSVTPISNKPEPASIEVGGPSGTANVNEGNFSISAQRRGKAALNDDVAISELERLMEGKTFSQAEIDRLIEMISSRAIDLPDVKRDERNLEIPLREGAKKNMSLFDKAKEPIGGKDANSEIWATPTPLAKSIILDGDKIRDEVGLSPAELAKAYMGGQTSSSSSQGFVARNEKDCLDRSMLVGKSSLASPSSKPSACWPGIKSSEQSGFATPQSRRESYGLQNFPRTPYSRTILSNSKSKLMQLQNDSSKHLSNLQSPSQSVERRYGQLSKGRDGGLFGPSRRTRQSATPSMVSPYSRPSRGASRFENSAIMKSSEAGESSYLSRSQITTYGKHKEAEVGTLTVPTHSSQIARTILDHLERTQSQSTPKNKTAELKLATSWRHPQSSKTVEKSSSDVTNVKKDGSAKLHEDIQNIFSQNQPSSVLKPPATTTGDIQNGMNKTASATNGIFRGTQAASSGGNALQYEFGKPKGSLSRSMHDELGTSSQDAAKAVPYSFGGETANLPKPPSHSLGNNKPVLPSISVAKPFQKWAVPSGSNAGFTFPVSSSDGTTSSEPTTPSIMPFTTSPPVASGGGVAITNHHEARKDYEIPQFSFDGSNRRGDKSPLVFSFPSVSEEVVSEDDDARFGIKYTFGSEKPERISFSSAGSDGVCC
Protein: 60 kDa heat shock protein, mitochondrial (EC 5.6.1.7) (60 kDa chaperonin) (Chaperonin 60) (CPN60) (Heat shock protein 60) (HSP-60) (Hsp60) (Mitochondrial matrix protein P1) (P31081)
Organism: Bos taurus (Bovine)
Function: Chaperonin implicated in mitochondrial protein import and macromolecular assembly. Together with Hsp10, facilitates the correct folding of imported proteins. May also prevent misfolding and promote the refolding and proper assembly of unfolded polypeptides generated under stress conditions in the mitochondrial matrix. The functional units of these chaperonins consist of heptameric rings of the large subunit Hsp60, which function as a back-to-back double ring. In a cyclic reaction, Hsp60 ring complexes bind one unfolded substrate protein per ring, followed by the binding of ATP and association with 2 heptameric rings of the co-chaperonin Hsp10. This leads to sequestration of the substrate protein in the inner cavity of Hsp60 where, for a certain period of time, it can fold undisturbed by other cell components. Synchronous hydrolysis of ATP in all Hsp60 subunits results in the dissociation of the chaperonin rings and the release of ADP and the folded substrate protein.
Subcellular location: Mitochondrion matrix {ECO:0000250|UniProtKB:P10809}.
Interaction partners:
- 10 kDa heat shock protein, mitochondrial
- Stress-70 protein, mitochondrial
- Toll-like receptor 4
- T-complex protein 1 subunit alpha
- Chaperonin 10
- ATP-dependent Clp protease proteolytic subunit, mitochondrial
- Heat shock 70 kDa protein 1A
- Lon protease homolog, mitochondrial
- Endoplasmic reticulum chaperone BiP
- Toll-like receptor 2
Sequence:
MLRLPAVLRQMRPVSRALALHLTRAYAKDVKFGADARALMLQGVDLLADAVAVTMGPKGRTVIIEQSWGSPRVTKDGVTVAKSIDLKDKYKNIGAKLVQDVANNTNEEAGDGTTTATVLARSIAKEGFEKISKGANPVEIRRGVMLAVDAVIVELKKQSKPVTTPEEIAQVATISANGDKEIGNIISDAMKKVGRKGVITVKDGKTLNDELEIIEGMKFDRGYISPYFINTSKGQKCEFQDAYVLLSEKKISSVQSIVPALEIANAHRKPLVIIAEDVDGEALSTLVLNRLKVGLQVVAVKAPGFGDNRKNQLKDMAIATGGAVFGEEGLNLNLEDVQPHDLGKVGEVIVTKDDAMLLKGKGDKAQIEKRIQEIIEQLDITTSEYEKEKLNERLAKLSDGVAVLKVGGTSDVEVNEKKDRVTDALNATRAAVEEGIVLGGDCALLRCIPALESITPANEDQKTGIEIIKKTLKIPAMTIAKNAGVEGSLIVEKIMQSSSEVGYDAMLGDFVNMVEKGIIDPTKVVRTALLDAAGVASLLTTAEVVVTEIPKEEKDPGMGGMGGMGGGMGGGMF
Protein: Pre-mRNA-splicing factor 18 (P33411)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Component of the U4/U5/U6 snRNP, binding principally to the u5 snRNP. It is not absolutely required for the second step of pre-mRNA splicing at low temperatures but is required at higher temperatures. It may stabilize a particular conformation of the U5 snRNP or orient the U5 snRNP within the U4/U5/U6 snRNP or within the spliceosome.
Subcellular location: Nucleus.
Interaction partners:
- Pre-mRNA-splicing factor SLU7
- Pre-mRNA-splicing factor CEF1
- Pre-mRNA-splicing helicase BRR2
- Pre-mRNA-splicing factor ATP-dependent RNA helicase PRP22
- Pre-mRNA-splicing factor BUD31
- Pre-mRNA-splicing factor 8
- Pre-mRNA-splicing factor SNU114
- Pre-mRNA-processing factor 17
- Pre-mRNA-splicing factor ATP-dependent RNA helicase PRP16
- Pre-mRNA-splicing factor ISY1
Sequence:
MDLDLASILKGEISKKKKELANSKGVQPPCTEKFQPHESANIDETPRQVEQESTDEENLSDNQSDDIRTTISKLENRPERIQEAIAQDKTISVIIDPSQIGSTEGKPLLSMKCNLYIHEILSRWKASLEAYHPELFLDTKKALFPLLLQLRRNQLAPDLLISLATVLYHLQQPKEINLAVQSYMKLSIGNVAWPIGVTSVGIHARSAHSKIQGGRNAANIMIDERTRLWITSIKRLITFEEWYTSNHDSLA
Protein: Probable serine/threonine-protein kinase PBL19 (EC 2.7.11.1) (PBS1-like protein 19) (Q9LTC0)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: May be involved in plant defense signaling.
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:O48814}; Lipid-anchor {ECO:0000250|UniProtKB:O48814}.
Interaction partners:
- F2J10.10 protein
- 16S rRNA
- Beta-glucosidase 14
- Proteasome subunit beta type-3-B
- Ethylene-responsive transcription factor ERF026
Sequence:
MNCLFLFKSKKPRKQQKDNNKNKRKGKELLQNSAPELTNRSETSSFNLQTPRSLPSPRSIKDLYTEREQNLRVFSYEELSKATYVFSRKLVIGEGGFGIVYKGKILSNGDSSDPPLVVAIKKLNRQGLQGHKQWLAEVQFLGVVNHPNVVKLIGYCSEDGETGIERLLVYEYMSNRSLEDHLFPRRSHTLPWKKRLEIMLGAAEGLTYLHDLKVIYRDFKSSNVLLDDQFCPKLSDFGLAREGPDGDNTHVTTARVGTHGYAAPEYVQTGHLRLKSDVYSFGVVLYEIITGRRTIERNKPVAERRLLDWVKEYPADSQRFSMIVDPRLRNNYPAAGARSLAKLADLCLKKNDKERPTMEIVVERLKKIIEESDSEDYPMATTTTKESSQVRRRQVAKPEKQSLRGVSVRG
Protein: Tetrahydromethanopterin S-methyltransferase subunit D (EC 7.2.1.4) (N5-methyltetrahydromethanopterin--coenzyme M methyltransferase subunit D) (P80183)
Organism: Methanothermobacter marburgensis (strain ATCC BAA-927 / DSM 2133 / JCM 14651 / NBRC 100331 / OCM 82 / Marburg) (Methanobacterium thermoautotrophicum)
Function: Part of a complex that catalyzes the formation of methyl-coenzyme M and tetrahydromethanopterin from coenzyme M and methyl-tetrahydromethanopterin. This is an energy-conserving, sodium-ion translocating step.
Subcellular location: Cell membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
- Tetrahydromethanopterin S-methyltransferase subunit C
- Tetrahydromethanopterin S-methyltransferase subunit G
- Tetrahydromethanopterin S-methyltransferase subunit B
- Tetrahydromethanopterin S-methyltransferase subunit A 1
- Tetrahydromethanopterin S-methyltransferase subunit E
- Tetrahydromethanopterin S-methyltransferase subunit H
- Tetrahydromethanopterin S-methyltransferase subunit A 2
- Tetrahydromethanopterin S-methyltransferase subunit F
- Methyl-coenzyme M reductase I operon protein D
- Methyl-coenzyme M reductase I operon protein C
Sequence:
MDPLLLIGAITAGGVLIGGGVHFVPVGGAPAAMATATGVGTGTAMLAAGAGLTGLITAAAMTGQSPLMIMAAGAVGSMLMIGITMLVGNLIYVFGVGTVPVSAKVSVDPITGMEQEKYVTPGTEGHGLPTVCFVSGIIGGALGGIGGGLIYWALNEALKTLSYGAMGAAGVAAIFAVGIFFINAVIASYNIGGTIEGFHDPKFKRIGRGIVACLIASIVAGALSTLLVYGGVF
Protein: Zinc finger protein 77 (ZNFpT1) (Q15935)
Organism: Homo sapiens (Human)
Function: May be involved in transcriptional regulation.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- P2X purinoceptor 3
- P2X purinoceptor 2
Sequence:
MDCVIFEEVAVNFTPEEWALLDHAQRSLYRDVMLETCRNLASLDCYIYVRTSGSSSQRDVFGNGISNDEEIVKFTGSDSWSIFGENWRFDNTGDQHQIPQRHLRSQLGRLCESNEGHQCGETLSQTANLLVHKSYPTEAKPSECTKCGKAFENRQRSHTGQRPCKECGQACSCLSCQSPPMKTQTVEKPCNCQDSRTASVTYVKSLSSKKSYECQKCGKAFICPSSFRGHVNSHHGQKTHACKVCGKTFMYYSYLTRHVRTHTGEKPYECKECGKAFSCPSYFREHVRTHTGEKPYECKHCGKSFSCYSSFRDHVRTHTGEKPCQCKHCGKAFTCYSSLREHGRTHSGEKPYECKECGKAFRYPSSLRAHMRMHTGEKPYVCKQCGKAFGCPTYFRRHVKTHSGVKPYQCKECGKAYSFSSSLRIHVRTHTGEKPFECKHCGKAFSCHSSLREHVRTHSGEKPYECNQCGKAFSHAQYFQKHVRSHSGVKPYECTECGKAYSCSSSLRVHVRTHTGERPYECKQCGKTFRYLASLQAHVRTHAGA
Protein: VIP peptides [Cleaved into: Intestinal peptide PHI-27 (Peptide histidine isoleucinamide 27); Vasoactive intestinal peptide (VIP) (Vasoactive intestinal polypeptide)] (P81401)
Organism: Bos taurus (Bovine)
Function: VIP causes vasodilation, lowers arterial blood pressure, stimulates myocardial contractility, increases glycogenolysis and relaxes the smooth muscle of trachea, stomach and gall bladder.
Subcellular location: Secreted.
Interaction partners:
- Vasoactive intestinal polypeptide receptor 1
- Vasoactive intestinal polypeptide receptor 2
- Adrenocorticotropic hormone receptor
- Pituitary adenylate cyclase-activating polypeptide type I receptor
- Calcitonin receptor-stimulating peptide 1
- Guanylate cyclase
- Tachykinin 1
- Glucagon like peptide 1 receptor
- Lutropin-choriogonadotropic hormone receptor
- D
Sequence:
METRSKPQLLVFLTLFSVLFSQTLAWPLFGAPSALRMGDRIPFEGANEPDQVSLKADTDILQDALAENDTPYYDVSRNVRHADGVFTSDYSRLLGQLSAKKYLESLIGKRVSNSISEDQGPIKRHSDAVFTDNYTRLRKQMAVKKYLNSILNGKRSSEGESPDFLEELEK
Protein: Glucuronoxylan 4-O-methyltransferase 2 (EC 2.1.1.112) (Q9T0F7)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Methyltransferase catalyzing 4-O-methylation of glucuronic acid side chains on xylan.
Subcellular location: Golgi apparatus membrane {ECO:0000269|PubMed:23045523}; Single-pass membrane protein {ECO:0000269|PubMed:23045523}.
Interaction partners:
- Pollen Ole e 1 allergen and extensin family protein
- At5g05500
- Endoglucanase 5
- Xyloglucan endotransglucosylase/hydrolase protein 14
- Protein SEED AND ROOT HAIR PROTECTIVE PROTEIN
- Peroxidase 44
- Proline-rich extensin-like family protein
- RING-type E3 ubiquitin transferase
- Probable pectinesterase/pectinesterase inhibitor 46
- Probable galacturonosyltransferase 12
Sequence:
MRNKSQSFISSKLIFICCSILVLFILFLKRASFSSNSTATIRDEYHQKSKCPSTPQQCTKLPTSLSDALVHYVTSEITPQQTFDEVSVSKRVLDKKSPCNFLVFGLGHDSLMWASLNHGGRTLFLEEDEAWIETVTKKFPNLESYHVVYDTKVKDSNKLMELKRTEDCKAVSDPRDSKCALSLKGFPADVYETQWDVIMVDAPTGYHDEAPGRMSAIYTAGLLARNRYDGGETDVFVHDINRPVEDEFSVAFLCGGYMKEQQGRLRHFNIPSHRASFGTPFCPADISRRF
Protein: Myelin protein P0 (Myelin peripheral protein) (MPP) (Myelin protein zero) (P25189)
Organism: Homo sapiens (Human)
Function: Is an adhesion molecule necessary for normal myelination in the peripheral nervous system. It mediates adhesion between adjacent myelin wraps and ultimately drives myelin compaction.
Subcellular location: Cell membrane {ECO:0000269|PubMed:18337304}; Single-pass type I membrane protein.; SUBCELLULAR LOCATION: [Isoform L-MPZ]: Myelin membrane {ECO:0000269|PubMed:22457349}; Single-pass type I membrane protein {ECO:0000269|PubMed:22457349}.
Interaction partners:
Sequence:
MAPGAPSSSPSPILAVLLFSSLVLSPAQAIVVYTDREVHGAVGSRVTLHCSFWSSEWVSDDISFTWRYQPEGGRDAISIFHYAKGQPYIDEVGTFKERIQWVGDPRWKDGSIVIHNLDYSDNGTFTCDVKNPPDIVGKTSQVTLYVFEKVPTRYGVVLGAVIGGVLGVVLLLLLLFYVVRYCWLRRQAALQRRLSAMEKGKLHKPGKDASKRGRQTPVLYAMLDHSRSTKAVSEKKAKGLGESRKDKK
Protein: V-type proton ATPase subunit G 1 (V-ATPase subunit G 1) (V-ATPase 13 kDa subunit 1) (Vacuolar proton pump subunit G 1) (Vacuolar proton pump subunit M16) (O75348)
Organism: Homo sapiens (Human)
Function: Subunit of the V1 complex of vacuolar(H+)-ATPase (V-ATPase), a multisubunit enzyme composed of a peripheral complex (V1) that hydrolyzes ATP and a membrane integral complex (V0) that translocates protons. V-ATPase is responsible for acidifying and maintaining the pH of intracellular compartments and in some cell types, is targeted to the plasma membrane, where it is responsible for acidifying the extracellular environment. In aerobic conditions, involved in intracellular iron homeostasis, thus triggering the activity of Fe(2+) prolyl hydroxylase (PHD) enzymes, and leading to HIF1A hydroxylation and subsequent proteasomal degradation.
Subcellular location: Apical cell membrane {ECO:0000269|PubMed:29993276}.
Interaction partners:
- V-type proton ATPase catalytic subunit A
- V-type proton ATPase subunit B, brain isoform
- V-type proton ATPase subunit F
- V-type proton ATPase subunit E 1
- V-type proton ATPase subunit D
- V-type proton ATPase subunit d 1
- V-type proton ATPase subunit H
- V-type proton ATPase subunit B, kidney isoform
- V-type proton ATPase 21 kDa proteolipid subunit c''
- V-type proton ATPase subunit C 1
Sequence:
MASQSQGIQQLLQAEKRAAEKVSEARKRKNRRLKQAKEEAQAEIEQYRLQREKEFKAKEAAALGSRGSCSTEVEKETQEKMTILQTYFRQNRDEVLDNLLAFVCDIRPEIHENYRING
Protein: Adenine phosphoribosyltransferase (APRT) (EC 2.4.2.7) (P63544)
Organism: Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4)
Function: Catalyzes a salvage reaction resulting in the formation of AMP, that is energically less costly than de novo synthesis.
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00004}.
Interaction partners:
Sequence:
MNLKDYIATIENYPKEGITFRDISPLMADGNAYSYAVREIVQYATDKKVDMIVGPEARGFIVGCPVAFELGIGFAPVRKPGKLPREVISADYEKEYGVDTLTMHADAIKPGQRVLIVDDLLATGGTVKATIEMIEKLGGVMAGCAFLVELDELNGREKIGDYDYKVLMHY
Protein: Cystathionine beta-synthase (EC 4.2.1.22) (Q9VRD9)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- cystathionine gamma-lyase
- Adenosylhomocysteinase
- Serine hydroxymethyltransferase
- Betaine-homocysteine S-methyltransferase
- Adenosylhomocysteinase-like 1
- Adenosylhomocysteinase-like 2
- FI01821p
- Phosphoserine phosphatase
- Alanine--glyoxylate aminotransferase
- Cysteine--tRNA ligase
Sequence:
MPQPKPYERPADFIDPGKPSKCKWHLGTAEKSPHIHRGIAHRQQITPNILEVIGCTPLVKLNNIPASDGIECEMYAKCEFLNPGGSVKDRIGYRMVQDAEEQGLLKPGYTIIEPTSGNTGIGLAMACAVKGYKCIIVMPEKMSNEKVSALRTLGAKIIRTPTEAAYDSPEGLIYVAQQLQRETPNSIVLDQYRNAGNPLAHYDGTAAEILWQLDNKVDMIVVSAGTAGTISGIGRKIKEQVPSCQIVGVDPYGSILARPAELNKTDVQFYEVEGIGYDFPPTVFDDTVVDVWTKIGDSDCFPMSRRLNAEEGLLCGGSSGGAMHAALEHARKLKKGQRCVVILPDGIRNYMTKFVSDNWMEARNFKEPVNEHGHWWWSLAIAELELPAPPVILKSDATVGEAIALMKKHRVDQLPVVDQDDGSVLGVVGQETLITQIVSMNRQQSDPAIKALNKRVIRLNESEILGKLARVLEVDPSVLILGKNPAGKVELKALATKLDVTTFIAAGKQKPKANGTTNGGSH
Protein: ATP-dependent 6-phosphofructokinase subunit beta (EC 2.7.1.11) (ATP-dependent 6-phosphofructokinase) (ATP-PFK) (Phosphofructokinase 2) (Phosphohexokinase) (P16862)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Catalyzes the phosphorylation of D-fructose 6-phosphate to fructose 1,6-bisphosphate by ATP, the first committing step of glycolysis.
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03184, ECO:0000269|PubMed:18313953}. Mitochondrion outer membrane; Peripheral membrane protein; Cytoplasmic side {ECO:0000269|PubMed:16962558}.
Interaction partners:
- ATP-dependent 6-phosphofructokinase subunit alpha
- Glucose-6-phosphate isomerase
- Fructose-bisphosphate aldolase
- Fructose-1,6-bisphosphatase
- Transketolase 1
- Hexokinase-2
- 6-phosphofructo-2-kinase 2
- Transaldolase
- Glucokinase-1
- N-acetylglucosamine kinase
Sequence:
MTVTTPFVNGTSYCTVTAYSVQSYKAAIDFYTKFLSLENRSSPDENSTLLSNDSISLKILLRPDEKINKNVEAHLKELNSITKTQDWRSHATQSLVFNTSDILAVKDTLNAMNAPLQGYPTELFPMQLYTLDPLGNVVGVTSTKNAVSTKPTPPPAPEASAESGLSSKVHSYTDLAYRMKTTDTYPSLPKPLNRPQKAIAVMTSGGDAPGMNSNVRAIVRSAIFKGCRAFVVMEGYEGLVRGGPEYIKEFHWEDVRGWSAEGGTNIGTARCMEFKKREGRLLGAQHLIEAGVDALIVCGGDGSLTGADLFRSEWPSLIEELLKTNRISNEQYERMKHLNICGTVGSIDNDMSTTDATIGAYSALDRICKAIDYVEATANSHSRAFVVEVMGRNCGWLALLAGIATSADYIFIPEKPATSSEWQDQMCDIVSKHRSRGKRTTIVVVAEGAIAADLTPISPSDVHKVLVDRLGLDTRITTLGHVQRGGTAVAYDRILATLQGLEAVNAVLESTPDTPSPLIAVNENKIVRKPLMESVKLTKAVAEAIQAKDFKRAMSLRDTEFIEHLNNFMAINSADHNEPKLPKDKRLKIAIVNVGAPAGGINSAVYSMATYCMSQGHRPYAIYNGWSGLARHESVRSLNWKDMLGWQSRGGSEIGTNRVTPEEADLGMIAYYFQKYEFDGLIIVGGFEAFESLHQLERARESYPAFRIPMVLIPATLSNNVPGTEYSLGSDTALNALMEYCDVVKQSASSTRGRAFVVDCQGGNSGYLATYASLAVGAQVSYVPEEGISLEQLSEDIEYLAQSFEKAEGRGRFGKLILKSTNASKALSATKLAEVITAEADGRFDAKPAYPGHVQQGGLPSPIDRTRATRMAIKAVGFIKDNQAAIAEARAAEENFNADDKTISDTAAVVGVKGSHVVYNSIRQLYDYETEVSMRMPKVIHWQATRLIADHLVGRKRVD
Protein: Carbohydrate sulfotransferase 4 (EC 2.8.2.-) (Galactose/N-acetylglucosamine/N-acetylglucosamine 6-O-sulfotransferase 3) (GST-3) (High endothelial cells N-acetylglucosamine 6-O-sulfotransferase) (HEC-GlcNAc6ST) (L-selectin ligand sulfotransferase) (LSST) (N-acetylglucosamine 6-O-sulfotransferase 2) (GlcNAc6ST-2) (Gn6st-2) (Q8NCG5)
Organism: Homo sapiens (Human)
Function: Sulfotransferase involved in SELL/L-selectin ligand biosynthesis pathway. Catalyzes the transfer of the sulfate group from 3'-phospho-5'-adenylyl sulfate (PAPS) onto the hydroxyl group at C-6 position of the non-reducing N-acetylglucosamine (GlcNAc) residue within O-linked mucin-type glycans. Contributes to generate sialyl 6-sulfo Lewis X determinant (also known as MECA-79 epitope) for SELL recognition, a prerequisite for continuous lymphocyte homing into peripheral lymph nodes and antigen immune surveillance. Transfers the sulfate group primarily on core 2 GlcNAcbeta1-6(Galbeta1-3)GalNAcalphaSer/Thr and extended core 1 GlcNAcbeta1-3Galbeta1-3GalNAcalphaSer/Thr based O-linked glycans on CD34 and GLYCAM1 peripheral node addressins (PNAds) expressed on the lumenal side of high endothelial venules (HEVs). The recognition of PNAds by SELL initiates a multistep process comprising tethering and rolling of blood lymphocytes on HEVs against the blood flow, followed by chemokine signaling, integrin-mediated lymphocyte adhesion onto endothelial cells and lymphocyte transendothelial migration. Modulates rolling velocity and differential T and B lymphocyte recruitment into peripheral lymph nodes, with a major role in B lymphocyte homing. Might be redundant in sulfation of MADCAM1 and lymphocyte trafficking to mesenteric lymph nodes (By similarity). Can also sulfonate core 3 GlcNAcbeta1-3GalNAc-R based glycans as well as GlcNAcbeta1-3Galbeta1-Glc, GlcNAcbeta1-6ManOMe and GlcNAcbeta1-2Man oligosaccharides, which might be ectopically expressed during tumorigenesis.
Subcellular location: Golgi apparatus membrane {ECO:0000269|PubMed:12855678}; Single-pass type II membrane protein {ECO:0000269|PubMed:12855678}.
Interaction partners:
- Protein N-terminal asparagine amidohydrolase
- Carbohydrate sulfotransferase 2
- L-selectin
Sequence:
MLLPKKMKLLLFLVSQMAILALFFHMYSHNISSLSMKAQPERMHVLVLSSWRSGSSFVGQLFGQHPDVFYLMEPAWHVWMTFKQSTAWMLHMAVRDLIRAVFLCDMSVFDAYMEPGPRRQSSLFQWENSRALCSAPACDIIPQDEIIPRAHCRLLCSQQPFEVVEKACRSYSHVVLKEVRFFNLQSLYPLLKDPSLNLHIVHLVRDPRAVFRSRERTKGDLMIDSRIVMGQHEQKLKKEDQPYYVMQVICQSQLEIYKTIQSLPKALQERYLLVRYEDLARAPVAQTSRMYEFVGLEFLPHLQTWVHNITRGKGMGDHAFHTNARDALNVSQAWRWSLPYEKVSRLQKACGDAMNLLGYRHVRSEQEQRNLLLDLLSTWTVPEQIH
Protein: Formylglycine-generating enzyme (FGE) (EC 1.8.3.7) (C-alpha-formylglycine-generating enzyme 1) (Sulfatase-modifying factor 1) (Q8NBK3)
Organism: Homo sapiens (Human)
Function: Oxidase that catalyzes the conversion of cysteine to 3-oxoalanine on target proteins, using molecular oxygen and an unidentified reducing agent. 3-oxoalanine modification, which is also named formylglycine (fGly), occurs in the maturation of arylsulfatases and some alkaline phosphatases that use the hydrated form of 3-oxoalanine as a catalytic nucleophile. Known substrates include GALNS, ARSA, STS and ARSE.
Subcellular location: Endoplasmic reticulum lumen {ECO:0000269|PubMed:15657036, ECO:0000269|PubMed:15962010, ECO:0000269|PubMed:18266766, ECO:0000269|PubMed:21224894}.
Interaction partners:
- Inactive C-alpha-formylglycine-generating enzyme 2
- N-acetylgalactosamine-6-sulfatase
- Arylsulfatase A
- Arylsulfatase B
- N-sulphoglucosamine sulphohydrolase
- Iduronate 2-sulfatase
- Endoplasmic reticulum resident protein 44
- Arylsulfatase G
- Steryl-sulfatase
- Inositol 1,4,5-trisphosphate-gated calcium channel ITPR1
Sequence:
MAAPALGLVCGRCPELGLVLLLLLLSLLCGAAGSQEAGTGAGAGSLAGSCGCGTPQRPGAHGSSAAAHRYSREANAPGPVPGERQLAHSKMVPIPAGVFTMGTDDPQIKQDGEAPARRVTIDAFYMDAYEVSNTEFEKFVNSTGYLTEAEKFGDSFVFEGMLSEQVKTNIQQAVAAAPWWLPVKGANWRHPEGPDSTILHRPDHPVLHVSWNDAVAYCTWAGKRLPTEAEWEYSCRGGLHNRLFPWGNKLQPKGQHYANIWQGEFPVTNTGEDGFQGTAPVDAFPPNGYGLYNIVGNAWEWTSDWWTVHHSVEETLNPKGPPSGKDRVKKGGSYMCHRSYCYRYRCAARSQNTPDSSASNLGFRCAADRLPTMD
Protein: Peptide deformylase 1B, chloroplastic/mitochondrial (AtDEF2) (AtPDF1B) (PDF 1B) (EC 3.5.1.88) (Polypeptide deformylase) (Q9FUZ2)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Removes the formyl group from the N-terminal Met of newly synthesized proteins. Has a preferred substrate specificity towards the photosystem II (PS II) D1 polypeptide.
Subcellular location: Plastid, chloroplast stroma. Mitochondrion. Note=Reported to be localized to chloroplast and mitochondria based on transient GFP expression in a heterologous system. {ECO:0000269|PubMed:11060042}.
Interaction partners:
- Trigger factor-like protein TIG, Chloroplastic
- Methionine aminopeptidase 1A
- Large ribosomal subunit protein bL28c
- Large ribosomal subunit protein uL11c
- Ribosomal protein L25/Gln-tRNA synthetase, anti-codon-binding domain-containing protein
- Methionine aminopeptidase 1D, chloroplastic/mitochondrial
- Methionine aminopeptidase 1C, chloroplastic/mitochondrial
- Large ribosomal subunit protein bL21c
- Large ribosomal subunit protein bL31c
- Translation elongation factor EF1B/ribosomal protein S6 family protein
Sequence:
MAVCNCFLQAPPLSRILLPVLSRRATTLSAGYGRLKSTVTFCSTVNRTSPLTSSVRAEVKRVSRKDDKVASATDVQFETPLKIVEYPDPILRAKNKRIDIFDENLKNLVDAMFDVMYKTDGIGLSAPQVGLNVQLMVFNPAGEPGEGKEIVLVNPKIKKYSDKLVPFDEGCLSFPGIYAEVVRPQSVKIDARDITGERFSISLSRLPARIFQHEYDHLEGVLFFDRMTDQVLDSIREELEALEKKYEEKTGLPSPERVEARQKRKAGVGFGKR
Protein: Erythrocyte membrane protein band 4.1 like 1 (Q4VXN5)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MTTETGPDSEVKKAQEEAPQQPEAAAAVTTPVTPAGHGHPEANSNEKHPSQQDTRPAEQSLDMEEKDYSEADGLSERTTPSKAQKSPQKIAKKYKSAICRVTLLDASEYECEVEKHGRGQVLFDLVCEHLNLLEKDYFGLTFCDADSQKNWLDPSKEIKKQIRSSPWNFAFTVKFYPPDPAQLTEDIT
Protein: Matrilin-2 (O08746)
Organism: Mus musculus (Mouse)
Function: Involved in matrix assembly.
Subcellular location: Secreted.
Interaction partners:
- Lumican
Sequence:
MEKMLVGCLLMLGQLFLVLPVDGRERPQARFPSRGRHVRMYPQTALLESSCENKRADLVFIIDSSRSVNTYDYAKVKEFILDILQFLDIGPDVTRVGLLQYGSTVKNEFSLKTFKRKSEVERAVKRMRHLSTGTMTGLAIQYALNIAFSEAEGARPLRENVPRIIMIVTDGRPQDSVAEVAAKARNTGILIFAIGVGQVDLNTLKAIGSEPHKDHVFLVANFSQIESLTSVFQNKLCTVHMCSVLEHNCAHFCLNTPGSYICKCKQGYILSTDQKTCRIQDLCATEDHGCEQLCVNMLGSFVCQCYSGYTLAEDGKRCTAVDYCASENHGCEHECVNAESSYLCRCHEGFALNSDKKTCSKIDYCASSNHGCQHECVNAQTSALCRCLKGFMLNPDRKTCRRINYCALNKPGCEHECVNTEEGHYCRCRQGYNLDPNGKTCSRVDHCAQQDHGCEQLCLNTEESFVCQCSEGFLINDDLKTCSRADYCLLSNHGCEYSCVNTDKSFACQCPEGHVLRSDGKTCAKLDSCALGDHGCEHSCVSSEDSFVCQCFEGYILRDDGKTCRRKDVCQDVNHGCEHLCVNSGESYVCKCLEGFRLAEDGKRCRRKNVCKSTQHGCEHMCVNNGNSYLCRCSEGFVLAEDGKHCKRCTEGPIDLVFVIDGSKSLGEENFETVKHFVTGIIDSLAVSPKAARVGLLQYSTQVRTEFTLRGFSSAKEMKKAVTHMKYMGKGSMTGLALKHMFERSFTQVEGARPPSTQVPRVAIVFTDGRAQDDVSEWASKAKANGITMYAVGVGKAIEEELQEIASEPIDKHLFYAEDFSTMGEISEKLKEGICEALEDSGGRQDSAAWDLPQQAHQPTEPEPVTIKIKDLLSCSNFAVQHRFLFEEDNLSRSTQKLFHSTKSSGNPLEESQDQCKCENLILFQNVANEEVRKLTQRLEEMTQRMEALENRLKYR
Protein: LIM-domain binding factor 3a (Ldb3a protein) (Q7ZVD3)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Cytoplasm, myofibril, sarcomere, Z line {ECO:0000256|ARBA:ARBA00004216}.
Interaction partners:
Sequence:
MTSYNVSLSGPPPWGFRLQGGKDFNMPLTVSRITPGSKAASSNLIQGDIIVAIDGVSTDGMTHLEAQNKIKSANFNLALTMQRSKRPTPVPMATPRIESPMPVIPHQKVITHAPANNEFLPSFNPIALKDTALSTNKPIEVKGPGGKATIIHAQYNTPISMYSQDAIMDAIAGQSQARGSEMSGNETDSQLSNLPVKERVIDSASPVYQAVIPSEIDQLGPADWARRAAQLQSKSFRVLAHITGTEYMQDPDEEALRKSRERFESEAKGPRFAKLKNWHNGLSAQILNVPQ