wanglab/gogpt-training-data huggingface dataset:
Protein: Nuclear cap-binding protein subunit 2 (20 kDa nuclear cap-binding protein) (NCBP 20 kDa subunit) (CBP20) (B1WC40)
Organism: Rattus norvegicus (Rat)
Function: Component of the cap-binding complex (CBC), which binds co-transcriptionally to the 5' cap of pre-mRNAs and is involved in various processes such as pre-mRNA splicing, translation regulation, nonsense-mediated mRNA decay, RNA-mediated gene silencing (RNAi) by microRNAs (miRNAs) and mRNA export. The CBC complex is involved in mRNA export from the nucleus via its interaction with ALYREF/THOC4/ALY, leading to the recruitment of the mRNA export machinery to the 5' end of mRNA and to mRNA export in a 5' to 3' direction through the nuclear pore. The CBC complex is also involved in mediating U snRNA and intronless mRNAs export from the nucleus. The CBC complex is essential for a pioneer round of mRNA translation, before steady state translation when the CBC complex is replaced by cytoplasmic cap-binding protein eIF4E. The pioneer round of mRNA translation mediated by the CBC complex plays a central role in nonsense-mediated mRNA decay (NMD), NMD only taking place in mRNAs bound to the CBC complex, but not on eIF4E-bound mRNAs. The CBC complex enhances NMD in mRNAs containing at least one exon-junction complex (EJC) via its interaction with UPF1, promoting the interaction between UPF1 and UPF2. The CBC complex is also involved in 'failsafe' NMD, which is independent of the EJC complex, while it does not participate in Staufen-mediated mRNA decay (SMD). During cell proliferation, the CBC complex is also involved in microRNAs (miRNAs) biogenesis via its interaction with SRRT/ARS2, thereby being required for miRNA-mediated RNA interference. The CBC complex also acts as a negative regulator of PARN, thereby acting as an inhibitor of mRNA deadenylation. In the CBC complex, NCBP2/CBP20 recognizes and binds capped RNAs (m7GpppG-capped RNA) but requires NCBP1/CBP80 to stabilize the movement of its N-terminal loop and lock the CBC into a high affinity cap-binding state with the cap structure. The conventional cap-binding complex with NCBP2 binds both small nuclear RNA (snRNA) and messenger (mRNA) and is involved in their export from the nucleus (By similarity).
Subcellular location: Nucleus {ECO:0000250|UniProtKB:P52298}. Cytoplasm {ECO:0000250|UniProtKB:P52298}.
Interaction partners:
- Nuclear cap-binding protein subunit 1
- Phosphorylated adapter RNA export protein
- Small nuclear ribonucleoprotein Sm D3
- Aly/REF export factor
- Snurportin-1
- Eukaryotic translation initiation factor 4E
- Polyadenylate-binding protein 2
- RNA-binding protein 8A
- Arsenite-resistance protein 2
- GTP-binding nuclear protein Ran
Sequence:
MSGGLLKALRSDSYVELSEYRDQHFRGDNEEQEKLLKKSCTLYVGNLSFYTTEEQIYELFSKSGDIKKIIMGLDKMKKTACGFCFVEYYSRADAENAMRYINGTRLDDRIIRTDWDAGFKEGRQYGRGRSGGQVRDEYREDYDAGRGGYGKLAQKQ
Protein: UPF0336 protein Rv0504c (P9WFK3)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Interaction partners:
- (3R)-hydroxyacyl-ACP dehydratase subunit HadB
- Cyclopropane mycolic acid synthase 2
- Phosphoserine phosphatase SerB1
Sequence:
MTVPEEAQTLIGKHYRAPDHFLVGREKIREFAVAVKDDHPTHYSEPDAAAAGYPALVAPLTFLAIAGRRVQLEIFTKFNIPINIARVFHRDQKFRFHRPILANDKLYFDTYLDSVIESHGTVLAEIRSEVTDAEGKPVVTSVVTMLGEAAHHEADADATVAAIASI
Protein: Biotin-dependent long chain acyl-coenzyme A carboxylase beta4 subunit (EC 2.1.3.-) (O53578)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: Component of a biotin-dependent acyl-CoA carboxylase complex. This subunit transfers the CO2 from carboxybiotin to the CoA ester substrate. When associated with the alpha3 subunit AccA3, the beta5 subunit AccD5 and the epsilon subunit AccE5, forms the LCC complex, which is involved in the carboxylation of long chain acyl-CoA. The LCC complex can use C16-C24 substrates, the highest specific activity is obtained with carboxy-C20-CoA. Has low activity with acetyl-CoA and propionyl-CoA.
Interaction partners:
- Biotin-dependent acyl-coenzyme A carboxylase alpha3 subunit
- Long-chain-fatty-acid--AMP ligase FadD32
- Polyketide synthase Pks13
- Biotin-dependent 3-methylcrotonyl-coenzyme A carboxylase alpha1 subunit
- Biotin-dependent 3-methylcrotonyl-coenzyme A carboxylase alpha1 subunit
- Biotin-dependent acetyl-/propionyl-coenzyme A carboxylase epsilon subunit
- Biotin-dependent acetyl-/propionyl-coenzyme A carboxylase beta6 subunit
- Biotin-dependent acetyl-/propionyl-coenzyme A carboxylase beta5 subunit
- Carboxylesterase/lipase Culp6
- Biotin--[acetyl-CoA-carboxylase] ligase
Sequence:
MTVTEPVLHTTAEKLAELRERLELAKEPGGEKAAAKRDKKGIPSARARIYELVDPGSFMEIGALCRTPGDPNALYGDGVVTGHGLINGRPVGVFSHDQTVFGGTVGEMFGRKVARLMEWCAMVGCPIVGINDSGGARIQDAVTSLAWYAELGRRHELLSGLVPQISIILGKCAGGAVYSPIQTDLVVAVRDQGYMFVTGPDVIKDVTGEDVSLDELGGADHQASYGNIHQVVESEAAAYQYVRDFLSFLPSNCFDKPPVVNPGLEPEITGHDLELDSIVPDSDNMAYDMHEVLLRIFDDGDFLDVAAQAGQAIITGYARVDGRTVGVVANQPMHMSGAIDNEASDKAARFIRFSDAFDIPLVFVVDTPGFLPGVEQEKNGIIKRGGRFLYAVVEADVPKVTITIRKSYGGAYAVMGSKQLTADLNFAWPTARIAVIGADGAAQLLMKRFPDPNAPEAQAIRKSFVENYNLNMAIPWIAAERGFIDAVIDPHETRLLLRKSMHLLRDKQLWWRVGRKHGLIPV
Protein: Helicase ATP-binding domain-containing protein (O50435)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Interaction partners:
- ATP-dependent helicase DinG
- Probable conserved transmembrane protein
- DNA-directed RNA polymerase subunit beta
- DNA-directed RNA polymerase subunit alpha
- DNA-directed RNA polymerase subunit omega
- Cullin, a subunit of E3 ubiquitin ligase
- DNA polymerase I
- 5'-3' exonuclease
- ERCC4 domain-containing protein
- CysO-cysteine peptidase
Sequence:
MDPHRDLESRAFAGNWRVYQQQALDAFDADVAAGDNRAYLVLPPGAGKTMIGLEAARRLGRRSLVLVPNTAVQAQWAAAWDNSFPSSDRSASKCGTERGLASAMNVLTYQSLAVIDAETDSTVRREVLRNRDQQALLDLLHPNGRAVIERAATLGPWTLVLDECHHLLATWGALVSALASVLGAQTALIGLTATPATELTAWQHTLHDELFGTADFVIPTPALVREGDLAPYQELVYLTQPTPEEQAWIGTHRARFADLMLALIDQKVGSMSLAAWLHTRIVDRATREGNQIAWSTFERAEPDLACSGLRFAYDGLIPLPDGVRLREQHRIAPDAQDWVNVLTDFSVGHLQQSADPRDAHALTAIKRVLPGLGYRLTSRGVRVATSPVDRLCALSESKIAATAHILDTEDAVLGARLRALVLCDFESMTGALPTSLKGAPVSEQSGSAQLVAAMLAASDHRRRTPLHALLVTGQTFACPAAIEDDLIAFCAERGALVTAEPLDAHPSLRVMRGTGGFTPRTWVALATEYFLAGRARVLVGTRSLLGEGWDCAAVNVNIDLTSATTQAAITQMRGRAIRNDPSDGHKVADNWSVCCIATEHPRGDADYLRLVRKHDGYYAATPQGLIESGVTHCDPSLSPYGPPVTDTHAITARALQRVAERAQARSWWRIGEPYEGVDVATIRVRSRQPLGVAAPRIPASALTPPVPGQFSPVRLARGAVAAVSVVGASTATAVASANLGMLAGAGTAGAIVAAGVGLVATAAAAESRRLDHAPNALEQLAAVVADALYAAGGAQRGSAALRLASDPEGWIRCQLDGVPTEQSLRFTAALDELLAPLAEPRYLIGRKILTPPARPVARRLFAVRAVVGLSLPGTVAWHAVPRWFARNKDRRQHLAQAWRKHIGPPRQLPADSPQGQAILDLFRGDNPLSVTTQLRTTWR
Protein: Lipopolysaccharide-binding protein (LBP) (Q61805)
Organism: Mus musculus (Mouse)
Function: Plays a role in the innate immune response. Binds to the lipid A moiety of bacterial lipopolysaccharides (LPS), a glycolipid present in the outer membrane of all Gram-negative bacteria. Acts as an affinity enhancer for CD14, facilitating its association with LPS (By similarity). Promotes the release of cytokines in response to bacterial lipopolysaccharide.
Subcellular location: Secreted {ECO:0000250|UniProtKB:P18428}. Cytoplasmic granule membrane {ECO:0000250|UniProtKB:P17213}. Note=Membrane-associated in polymorphonuclear Leukocytes (PMN) granules. {ECO:0000250|UniProtKB:P17213}.
Interaction partners:
- Monocyte differentiation antigen CD14
- Lymphocyte antigen 96
- Toll-like receptor 4
- Bactericidal permeability-increasing protein
- C-reactive protein
- Apolipoprotein A-I
Sequence:
MKAGTGPLLSTLLGLLFLSIQGTGGVNPGVVARITDKGLAYAAKEGLVALQRELYKITLPDFSGDFKIKAVGRGQYEFHSLEIQNCELRGSSLKLLPGQGLSLAISDSSIGVRGKWKVRKSFLKLHGSFDLDVKGVTISVDLLLGMDPSGRPTVSASGCSSRICDLDVHISGNVGWLLNLFHNQIESKLQKVLENKVCEMIQKSVTSDLQPYLQTLPVTAEIDNVLGIDYSLVAAPQAKAQVLDVMFKGEIFNRNHRSPVATPTPTMSLPEDSKQMVYFAISDYAFNIASRVYHQAGYLNFSITDDMLPHDSGIRLNTKAFRPFTPQIYKKYPDMKLELLGTVVSAPILNVSPGNLSLAPQMEIEGFVILPTSAREPVFRLGVVTNVFASLTFNNSKVTGMLHPDKAQVRLIESKVGMFNVNLFQAFLNYYLLNSLYPDVNAELAQGFPLPLPRHIQLHDLDFQIRKDFLYLGANVQYMRV
Protein: DNA-directed RNA polymerase III subunit RPC7-like (RNA polymerase III subunit C7-like) (DNA-directed RNA polymerase III subunit G-like) (RNA polymerase III 32 kDa beta subunit) (RPC32-beta) (Q9BT43)
Organism: Homo sapiens (Human)
Function: DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Specific peripheric component of RNA polymerase III which synthesizes small RNAs, such as 5S rRNA and tRNAs.
Subcellular location: Nucleus {ECO:0000269|PubMed:20154270}.
Interaction partners:
- DNA-directed RNA polymerase III subunit RPC6
- DNA-directed RNA polymerase III subunit RPC3
- DNA-directed RNA polymerase III subunit RPC1
- DNA-directed RNA polymerase III subunit RPC2
- DNA-directed RNA polymerase III subunit RPC4
- DNA-directed RNA polymerase III subunit RPC8
- DNA-directed RNA polymerase III subunit RPC5
- DNA-directed RNA polymerases I and III subunit RPAC1
- DNA-directed RNA polymerase III subunit RPC9
- DNA-directed RNA polymerases I and III subunit RPAC2
Sequence:
MASRGGGRGRGRGQLTFNVEAVGIGKGDALPPPTLQPSPLFPPLEFRPVPLPSGEEGEYVLALKQELRGAMRQLPYFIRPAVPKRDVERYSDKYQMSGPIDNAIDWNPDWRRLPRELKIRVRKLQKERITILLPKRPPKTTEDKEETIQKLETLEKKEEEVTSEEDEEKEEEEEKEEEEEEEYDEEEHEEETDYIMSYFDNGEDFGGDSDDNMDEAIY
Protein: Chondrolectin (Transmembrane protein MT75) (Q9H9P2)
Organism: Homo sapiens (Human)
Function: May play a role in the development of the nervous system such as in neurite outgrowth and elongation. May be involved in motor axon growth and guidance.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:22042635}. Membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}.; SUBCELLULAR LOCATION: [Isoform 2]: Endoplasmic reticulum {ECO:0000269|PubMed:12621022}. Endoplasmic reticulum membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}.; SUBCELLULAR LOCATION: [Isoform 3]: Cytoplasm {ECO:0000269|PubMed:12621022}.
Interaction partners:
Sequence:
MSRVVSLLLGAALLCGHGAFCRRVVSGQKVCFADFKHPCYKMAYFHELSSRVSFQEARLACESEGGVLLSLENEAEQKLIESMLQNLTKPGTGISDGDFWIGLWRNGDGQTSGACPDLYQWSDGSNSQYRNWYTDEPSCGSEKCVVMYHQPTANPGLGGPYLYQWNDDRCNMKHNYICKYEPEINPTAPVEKPYLTNQPGDTHQNVVVTEAGIIPNLIYVVIPTIPLLLLILVAFGTCCFQMLHKSKGRTKTSPNQSTLWISKSTRKESGMEV
Protein: Acetolactate synthase large subunit IlvG (ALS) (EC 2.2.1.6) (Acetohydroxy-acid synthase large subunit) (AHAS) (P9WG39)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: Catalyzes the conversion of 2 pyruvate molecules into acetolactate in the first common step of the biosynthetic pathway of the branched-amino acids such as leucine, isoleucine, and valine.
Interaction partners:
- Putative acetolactate synthase small subunit
- Ketol-acid reductoisomerase
- 3-isopropylmalate dehydrogenase
- L-threonine dehydratase biosynthetic IlvA
- 2-isopropylmalate synthase
- Putative acetolactate synthase large subunit IlvB2
- Acetolactate synthase large subunit IlvB1
- Putative acetolactate synthase large subunit IlvX
- 2-oxoglutarate oxidoreductase subunit KorA
- 2-oxoglutarate oxidoreductase subunit KorB
Sequence:
MSTDTAPAQTMHAGRLIARRLKASGIDTVFTLSGGHLFSIYDGCREEGIRLIDTRHEQTAAFAAEGWSKVTRVPGVAALTAGPGITNGMSAMAAAQQNQSPLVVLGGRAPALRWGMGSLQEIDHVPFVAPVARFAATAQSAENAGLLVDQALQAAVSAPSGVAFVDFPMDHAFSMSSDNGRPGALTELPAGPTPAGDALDRAAGLLSTAQRPVIMAGTNVWWGHAEAALLRLVEERHIPVLMNGMARGVVPADHRLAFSRARSKALGEADVALIVGVPMDFRLGFGGVFGSTTQLIVADRVEPAREHPRPVAAGLYGDLTATLSALAGSGGTDHQGWIEELATAETMARDLEKAELVDDRIPLHPMRVYAELAALLERDALVVIDAGDFGSYAGRMIDSYLPGCWLDSGPFGCLGSGPGYALAAKLARPQRQVVLLQGDGAFGFSGMEWDTLVRHNVAVVSVIGNNGIWGLEKHPMEALYGYSVVAELRPGTRYDEVVRALGGHGELVSVPAELRPALERAFASGLPAVVNVLTDPSVAYPRRSNLA
Protein: UDP-glycosyltransferase 71B6 (EC 2.4.1.-) (Abscisic acid glycosyltransferase) (Q9LSY6)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Glucosyltransferase that glucosylates the (+) enantiomer of abscisic acid ((+)-ABA). Is not active on structural analogs with alterations to the 8'- and 9'- methyl groups.
Interaction partners:
- Abscisic acid 8'-hydroxylase 1
- Glycosyltransferase
- Abscisic acid 8'-hydroxylase 3
Sequence:
MKIELVFIPSPAISHLMATVEMAEQLVDKNDNLSITVIIISFSSKNTSMITSLTSNNRLRYEIISGGDQQPTELKATDSHIQSLKPLVRDAVAKLVDSTLPDAPRLAGFVVDMYCTSMIDVANEFGVPSYLFYTSNAGFLGLLLHIQFMYDAEDIYDMSELEDSDVELVVPSLTSPYPLKCLPYIFKSKEWLTFFVTQARRFRETKGILVNTVPDLEPQALTFLSNGNIPRAYPVGPLLHLKNVNCDYVDKKQSEILRWLDEQPPRSVVFLCFGSMGGFSEEQVRETALALDRSGHRFLWSLRRASPNILREPPGEFTNLEEILPEGFFDRTANRGKVIGWAEQVAILAKPAIGGFVSHGGWNSTLESLWFGVPMAIWPLYAEQKFNAFEMVEELGLAVEIKKHWRGDLLLGRSEIVTAEEIEKGIICLMEQDSDVRKRVNEISEKCHVALMDGGSSETALKRFIQDVTENIAWSETES
Protein: Suppressor of IKBKE 1 (Suppressor of IKK-epsilon) (Q9BRV8)
Organism: Homo sapiens (Human)
Function: Physiological suppressor of IKK-epsilon and TBK1 that plays an inhibitory role in virus- and TLR3-triggered IRF3. Inhibits TLR3-mediated activation of interferon-stimulated response elements (ISRE) and the IFN-beta promoter. May act by disrupting the interactions of IKBKE or TBK1 with TICAM1/TRIF, IRF3 and RIGI. Does not inhibit NF-kappa-B activation pathways.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16281057}.
Interaction partners:
- Striatin-3
- Sarcolemmal membrane-associated protein
- Striatin-interacting protein 1
- Programmed cell death protein 10
- Striatin-interacting protein 2
- Striatin
- MOB-like protein phocein
- FGFR1 oncogene partner 2
- Serine/threonine-protein kinase 25
- Striatin-4
Sequence:
MSCTIEKILTDAKTLLERLREHDAAAESLVDQSAALHRRVAAMREAGTALPDQYQEDASDMKDMSKYKPHILLSQENTQIRDLQQENRELWISLEEHQDALELIMSKYRKQMLQLMVAKKAVDAEPVLKAHQSHSAEIESQIDRICEMGEVMRKAVQVDDDQFCKIQEKLAQLELENKELRELLSISSESLQARKENSMDTASQAIK
Protein: Cyclin-dependent kinase-like 5 (A0A8I5ZVL4)
Organism: Rattus norvegicus (Rat)
Interaction partners:
Sequence:
MKIPNIGNVMNKFEILGVVGEGAYGVVLKCRHKETHEIVAIKKFKDSEENEEVKETTLRELKMLRTLKQENIVELKEAFRRRGKLYLVFEYVEKNMLELLEEMPNGVPPEKVKSYIYQLIKAIHWCHKNDIVHRDIKPENLLISHNDVLKLCDFGFARNLSEGNNANYTEYVATRWYRSPELLLGAPYGKSVDMWSVGCILGELSDGQPLFPGESEIDQLFTIQKVLGPLPSEQMKLFYSNPRFHGLRFPAVNHPQSLERRYLGILNSVLLDLMKNLLKLDPADRYLTEQCLNHPTFQTQRLLDRSPSRSTKRKPYHVESSTLSNRSQSTKGGALQTHHRSNSKDIQNLSVGLPRAEEGLPANESFLNGNLAGATLSPMHTKTYQASTQPGSSSKDLTNNNIPHLLSPKEAKSKTEFDFNIDPKPSEGPGTKYLKSSTRSQQNRHSFMESSQSKAGTLQPSEKQSRHSYIDTIPQSSRSPSYRTKAKSHGALSDSKSVSNLSEARAQITETNTSRYFPSSCLDLNSPTSPTPTRHTDTRTLLSPSGRNNRNEGTLDSRRTTTRHSKTMEELKLPEHMDSSHSHSLSAPHESFSYGLGYTSPFSSQQRPHRHSMYVTRDKVRAKGIDGSLSIGQGMAARANSLQLLSPQPGEQLPPEMTVARPSVKESSREGTSSFHTRQKSEGGVYHDPHSDDGTAPKENRHLYNDPVPRRVGSFYRVPSPRPDNSFHENNVSTRVSSLPSDSSSGTNHSKRQPGFDPWKSPENISHSDQLKEKEKQGFFRSMKKKKKKTQTTDSTNGENPSIKKSLFPLFNSKNHLKHSSSLKKLPVVTPPMVPNTDGPDLLTLQKAIHSSSTASSRPKEWRPEKLSDLQTQSQPLKSLRKLLHLSSSTNHPASSDPRFQPLTAQQAKNSFSEIRIHPLSQASGGSSNIRQEPTPKGRPALQLPGLHQESF
Protein: SH3 domain-containing protein (C7FZZ0)
Organism: Dictyostelium discoideum (Social amoeba)
Interaction partners:
Sequence:
MSNAKKQQNPGIEITLKTINNLKVNSPPLFTEVIKAANKYQQQAQALSQAGLVLADTLTRLTIHNGGDFGEGFKKLADAIKDLENRRDDVAKVLLNEFITPNKQAIEDDQKAIATFEKNYKKDRDQMRQDILKLEAKTRKAGKKTTPEVLKQQITELNDKIKESEQLNANKLRDVVLMERRKHATFLSQFNQFLEKEIELSADTMSKFSTNLNTHRDLINSQSQLPLEMESMISKQERTLVQIQPQGDTGSDAYRISYAPGTIQTTGGGDQYYESYESYDNYDNYDNYDDGGSGGLGGSELQARALYDYESAEPSDLNLKAGDIISVIQQDDGSGWTKGRNYEGNEGIFPSTYIEYV
Protein: Platelet basic protein (PBP) (C-X-C motif chemokine 7) (Leukocyte-derived growth factor) (LDGF) (Macrophage-derived growth factor) (MDGF) (Small-inducible cytokine B7) [Cleaved into: Connective tissue-activating peptide III (CTAP-III) (LA-PF4) (Low-affinity platelet factor IV); TC-2; Connective tissue-activating peptide III(1-81) (CTAP-III(1-81)); Beta-thromboglobulin (Beta-TG); Neutrophil-activating peptide 2(74) (NAP-2(74)); Neutrophil-activating peptide 2(73) (NAP-2(73)); Neutrophil-activating peptide 2 (NAP-2); TC-1; Neutrophil-activating peptide 2(1-66) (NAP-2(1-66)); Neutrophil-activating peptide 2(1-63) (NAP-2(1-63))] (P02775)
Organism: Homo sapiens (Human)
Function: LA-PF4 stimulates DNA synthesis, mitosis, glycolysis, intracellular cAMP accumulation, prostaglandin E2 secretion, and synthesis of hyaluronic acid and sulfated glycosaminoglycan. It also stimulates the formation and secretion of plasminogen activator by human synovial cells. NAP-2 is a ligand for CXCR1 and CXCR2, and NAP-2, NAP-2(73), NAP-2(74), NAP-2(1-66), and most potent NAP-2(1-63) are chemoattractants and activators for neutrophils. TC-1 and TC-2 are antibacterial proteins, in vitro released from activated platelet alpha-granules. CTAP-III(1-81) is more potent than CTAP-III desensitize chemokine-induced neutrophil activation.
Subcellular location: Secreted.
Interaction partners:
- C-X-C motif chemokine 10
- C-X-C chemokine receptor type 2
- C-X-C motif chemokine 11
- Stromal cell-derived factor 1
- C-C motif chemokine 21
- C-C motif chemokine 5
- C-X-C chemokine receptor type 1
- C-C motif chemokine 13
- C-X-C motif chemokine 9
- C-X-C motif chemokine 6
Sequence:
MSLRLDTTPSCNSARPLHALQVLLLLSLLLTALASSTKGQTKRNLAKGKEESLDSDLYAELRCMCIKTTSGIHPKNIQSLEVIGKGTHCNQVEVIATLKDGRKICLDPDAPRIKKIVQKKLAGDESAD
Protein: Peptidyl-prolyl cis-trans isomerase FKBP20-1 (PPIase FKBP20-1) (EC 5.2.1.8) (FK506-binding protein 20-1) (AtFKBP20-1) (Immunophilin FKBP20-1) (Rotamase) (Q9M2S7)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides (By similarity).
Interaction partners:
- Peptidyl-prolyl cis-trans isomerase FKBP16-3, chloroplastic
- Peptidyl-prolyl cis-trans isomerase FKBP43
- Peptidyl-prolyl cis-trans isomerase FKBP17-3, chloroplastic
- Protein ROOT HAIR DEFECTIVE 3 homolog 1
- Protein ROOT HAIR DEFECTIVE 3 homolog 2
- Peptidyl-prolyl cis-trans isomerase FKBP42
- Peptidyl-prolyl cis-trans isomerase FKBP18, chloroplastic
- Peptidyl-prolyl cis-trans isomerase FKBP17-2, chloroplastic
- Peptidyl-prolyl cis-trans isomerase FKBP20-2, chloroplastic
- Peptidyl-prolyl cis-trans isomerase FKBP13, chloroplastic
Sequence:
MGDAIDLSGDGGVLKKIVRSAKPDAISPSDDLPVVDVHYEGILAEDEKVFDTTREDNLVFSFELGTGSVIRSWDIALKTMKVGEVAKITCKPEYAYGRAGSPPDIPPDATLIFEVELVACRPRKGASVGSVSEERARLEDLKKQREIAAAAKEDDKKKREEAKAAAAARIQAKLDAKKGPGKGKGKGKAK
Protein: CG9893 protein (CG9893-PA) (Dynactin 3, p24 subunit, isoform A) (Dynactin 3, p24 subunit, isoform B) (LD16285p) (Q9W1V8)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Dynactin subunit 2
- Dynactin subunit 6
- Actin-related protein 10, isoform A
- Dynactin subunit 4
- Actin-related protein 1
- Dynactin subunit 1
- Dynactin subunit 5
- Dynactin subunit 1
- F-actin-capping protein subunit beta
- F-actin-capping protein subunit alpha
Sequence:
MEALDILEKRIDALTRVLGPVQDSEVGEGVVDALCSAHAILGEATTGSAALQQCVKRSDELEKYLDPNFLEEHQQVRSKEVYLQAVAPELHTQAEQLERIKQLEPALGAEYFRSIPAECLEQLKGITQNNGEYAQQSELIEESLVLAMKRYGEIQAGLLSSLDAMSERLDQVEERMEQRKRAELSKDVPPKD
Protein: Uncharacterized protein (Q385Y4)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MEQPSQMSVSAPPAPSIKRPAAPKLTYEEVRRAARLSVLEDFTSQRDHRQRVARASALGTDVHVIPAAAGGPLSKEGSTRLLKEHTSASWSVYLYQWSIFGLTGVSSISTAMGFYLTIYHNRMFLPVGPMMAVVTWRLWSSLESAWEEQRFIDNAASIRESRKGNPMNLVVKRVVVNDEEAEEPAEGMV
Protein: Ferric reductase transmembrane component 6 (EC 1.16.1.9) (Ferric-chelate reductase 6) (Q12473)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Metalloreductase responsible for reducing vacuolar iron and copper prior to transport into the cytosol. Catalyzes the reduction of Fe(3+) to Fe(2+) and Cu(2+) to Cu(+), respectively, which can then be transported by the respective vacuolar efflux systems to the cytosol.
Subcellular location: Vacuole membrane {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:17553781, ECO:0000269|PubMed:17681937}; Multi-pass membrane protein {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:17553781, ECO:0000269|PubMed:17681937}.
Interaction partners:
- Probable ferric reductase transmembrane component 8
- Iron-regulated transcriptional activator AFT1
- Iron transport multicopper oxidase FET5
- Copper transport protein CTR2
- Iron transporter FTH1
- Iron transporter SMF3
- Siderophore iron transporter ARN1
- Iron transport multicopper oxidase FET3
- Protein CCC1
- Iron-regulated transcriptional activator AFT2
Sequence:
MHRTLLFLTWLISLTKAFNIKLPHTEKKDHLESNAVLACASYINTLKWSFDSSVVPGFYSTICSYSPAFDTWSLCIFNSLTDQIIPMDNTSFEESLGNVRKTCSFVDKKFSNISLEQYYSSLNNASSHALEDYGSIESLSTSIRVDRETRSRWIRAFHAHAYNLDISSVYGAYLTYYFVIVGIIAVFFHMSHYNGLNRALFASRFVNYIRGHFVLPTFLVDKHANHFKFLNVEVFTGLMPNSLEAWIIFGYTLANIIFLSISYIIDPYNLIFNSHLSQFTRLLADRSGILAFTQFPLIIIFTARNSFLEFLTGVKFNSFISFHKWIGRIMVLNATIHSLSYSLFAIINHAFKISNKQLYWKFGIASITVLCVLLVLSLGIVRKRHYEFFLYTHIILALLFFYCCWQHVKIFNGWKEWIVVSLLIWGLEKLFRIWNILQFRFPKATLINLNTSNNPHDEMFKVIIPKYNRRWHSKPGQYCFIYFLHPLVFWQCHPFTIIDEGEKCVLVIKPKSGLTRFIYNHILQSLNGKLQLRVAIEGPYGPSNLHLDKFDHLLLLSGGTGLPGPLDHAIKLSRNPDKPKSIDLIMAIKNPSFLNGYKSEILELKNSRSHVNVQVYLTQKTAVTKAANARDQLIHFDDIMTELTSFAHIGNARPNFSNVIENAIKSTPPGDSLAVVCCGPPVLVDDVRNTVSQKLLGYPERIIEYFEEYQCW
Protein: Histidinol-phosphatase (HolPase) (EC 3.1.3.15) (Histidinol-phosphate phosphatase) (P95189)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: Catalyzes the dephosphorylation of histidinol-phosphate to histidinol, the direct precursor of histidine.
Interaction partners:
- Histidinol dehydrogenase
- Probable pyruvate formate lyase activating protein PflA
- Histidinol-phosphate aminotransferase
- Histidinol-phosphate aminotransferase Rv2231c
- Aromatic amino acid aminotransferase
- Probable NADPH quinone oxidoreductase FadB4
- Conserved protein
- 3'-phosphoadenosine 5'-phosphate phosphatase
- Phosphoribosyl isomerase A
- Uncharacterized PPE family protein PPE50
Sequence:
MSHDDLMLALALADRADELTRVRFGALDLRIDTKPDLTPVTDADRAVESDVRQTLGRDRPGDGVLGEEFGGSTTFTGRQWIVDPIDGTKNFVRGVPVWASLIALLEDGVPSVGVVSAPALQRRWWAARGRGAFASVDGARPHRLSVSSVAELHSASLSFSSLSGWARPGLRERFIGLTDTVWRVRAYGDFLSYCLVAEGAVDIAAEPQVSVWDLAALDIVVREAGGRLTSLDGVAGPHGGSAVATNGLLHDEVLTRLNAG
Protein: U2 small nuclear ribonucleoprotein auxiliary factor 35 kDa subunit-related protein 1 (CCCH type zinc finger, RNA-binding motif and serine/arginine rich protein 1) (U2(RNU2) small nuclear RNA auxiliary factor 1-like 1) (Q15695)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
Sequence:
MAALEKMTFPKKMTFPEKPSHKKYRAALKKEKRKKRRQELARLRDSGLSQEEEEDTFIEEQQLEEEKLLERERERLHEEWLLREQKAQEEFRIKKEKEEAAKKWLEEQERKLKEQWKEQQRKEREEEEQKQQEKKEKEEAVQKMLDQAENDLENSTTWQNPEPPVDFRVMEKDRANCPFYSKTGACRFGDRCSRKHNFPTSSPTLLIKSMFTTFGMEQCRRDDYDPDASLEYSEEETYQQFLDFYEDVLPEFKNVGKVIQFKVSCNLEPHLRGNVYVQYQSEEECQAALSLFNGRWYAGRQLQCEFCPVTRWKMAICGLFEIQQCPRGKHCNFLHVFRNPNNEFWEANRDIYLSSDQTGSSFGKNSERREKMGHHDHYYSRQRGRRNPSPDHTYKRNGESERKKSSHRGKKSHKRTSKSRERHNSPSRGRNRHRSWDQGRRSQSRRSHRSRSQSSSRCRSRGRRKSGNRDRTVQSPQSK
Protein: Meprin A subunit beta (EC 3.4.24.63) (Endopeptidase-2) (Meprin B) (Q61847)
Organism: Mus musculus (Mouse)
Function: Membrane metallopeptidase that sheds many membrane-bound proteins. Exhibits a strong preference for acidic amino acids at the P1' position. Known substrates include: FGF19, VGFA, IL1B, IL18, procollagen I and III, E-cadherin, KLK7, gastrin, ADAM10, tenascin-C. The presence of several pro-inflammatory cytokine among substrates implicate MEP1B in inflammation. It is also involved in tissue remodeling due to its capability to degrade extracellular matrix components (By similarity).
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:Q16820}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:Q16820}. Secreted {ECO:0000250|UniProtKB:Q16820}. Note=Homodimers are essentially membrane bound but may also be shed from the surface by ADAM-10 and ADAM-17. {ECO:0000250|UniProtKB:Q16820}.
Interaction partners:
- Meprin A subunit alpha
- Dipeptidyl peptidase 4
- Neprilysin
- Angiotensin-converting enzyme 2
- Lysosomal Pro-X carboxypeptidase
Sequence:
MDARHQPWFLVFATFLLVSGLPAPEKFVKDIDGGIDQDIFDINQGLGLDLFEGDIKLEANGKNSIIGDHKRWPHTIPYVLEDSLEMNAKGVILNAFERYRLKTCIDFKPWSGEANYISVFKGSGCWSSVGNIHAGKQELSIGTNCDRIATVQHEFLHALGFWHEQSRADRDDYVIIVWDRIQPGKEHNFNIYNDSVSDSLNVPYDYTSVMHYSKTAFQNGTESTIVTRISEFEDVIGQRMDFSDYDLLKLNQLYNCTSSLSFMDSCDFELENICGMIQSSGDSADWQRVSQVLSGPESDHSKMGQCKDSGFFMHFNTSILNEGATAMLESRLLYPKRGFQCLEFYLYNSGSGNDQLNIYTREYTTGQQGGVLTLQRQIKEVPIGSWQLHYVTLQVTKKFRVVFEGLRGPGTSSGGLSIDDINLSETRCPHHIWHIQNFTQILGGQDTSVYSPPFYSSKGYAFQIYMDLRSSTNVGIYFHLISGANDDQLQWPCPWQQATMTLLDQNPDIRQRMFNQRSITTDPTMTSDNGSYFWDRPSKVGVTDVFPNGTQFSRGIGYGTTVFITRERLKSREFIKGDDIYILLTVEDISHLNSTSAVPDPVPTLAVHNACSEVVCQNGGICVVQDGRAECKCPAGEDWWYMGKRCEKRGSTRDTVIIAVSSTVTVFAVMLIITLVSVYCTRRKYRKKARANTAAMTLENQHAF