wanglab/gogpt-training-data huggingface dataset:
Protein: UDP-2-acetamido-3-amino-2,3-dideoxy-D-glucuronate N-acetyltransferase (UDP-D-GlcNAc3NA N-acetyltransferase) (EC 2.3.1.201) (UDP-2-acetamido-3-amino-2,3-dideoxy-alpha-D-glucuronic acid 3-N-acetyltransferase) (G3XD01)
Organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Function: Plays a role in the biosynthesis of B-band O antigen for serotype O5. Catalyzes the transfer of an acetyl group to the C-3 amino position of UDP-2-acetamido-3-amino-2,3-dideoxy-alpha-D-glucuronate (UDP-D-GlcNAc3NA).
Interaction partners:
- UDP-2-acetamido-2-deoxy-3-oxo-D-glucuronate aminotransferase
- UDP-2,3-diacetamido-2,3-dideoxy-D-glucuronate 2-epimerase
- UDP-N-acetyl-2-amino-2-deoxy-D-glucuronate oxidase
- UDP-N-acetyl-D-glucosamine 6-dehydrogenase
- LPS biosynthesis protein WbpG
- O-antigen translocase
- Probable glycosyl transferase WbpJ
- Probable glycosyltransferase WbpH
- Putative imidazole glycerol phosphate synthase subunit hisF2
- O-antigen polymerase
Sequence:
MSYYQHPSAIVDDGAQIGSDSRVWHFVHICAGARIGAGVSLGQNVFVGNKVVIGDRCKIQNNVSVYDNVTLEEGVFCGPSMVFTNVYNPRSLIERKDQYRNTLVKKGATLGANCTIVCGVTIGEYAFVGAGAVINKNVPSYALMVGVPARQIGWMSEFGEQLQLNEQGEAVCSHSGARYVLNGKILSKVDV
Protein: Aldehyde dehydrogenase (EC 1.2.1.3) (EC 1.2.1.4) (NAD/NADP-dependent aldehyde dehydrogenase) (Q8GAK7)
Organism: Paenarthrobacter nicotinovorans (Arthrobacter nicotinovorans)
Function: Aldehyde dehydrogenase able to oxidize various aldehydes such as formaldehyde, glyceraldehyde, butyraldehyde, glutaraldehyde and benzaldehyde (in vitro). Is likely involved in the oxidative D-xylose degradation pathway, catalyzing the oxidation step of 2-oxoglutarate semialdehyde to 2-oxoglutarate. Is able to use both NAD(+) and NADP(+); however, shows a preference for NADP(+). Does not display succinate semialdehyde dehydrogenase activity.
Interaction partners:
Sequence:
MAIATIDPTTGITLKTFDAHTPEEVENRIARAEAAFRSLQNTSFEERARWMHKAADILESEADEVARLIATEMGKTLTTAKYEALKSATGMRHFADHAQRYLSPETPVPASEVNASNLHVQFDPLGVVLAVMPWNYPLWQAVRFAAPALMAGNTGLLKHASNVPQCALYLGDLFARGGFPEGAFQTLLVEGKDVIPLVDDARIRAVTLTGSVAAGSAIAEAAGRNIKRSVLELGGMDVFIVMPSADIEKAAAQAVIARLQNSGQSCIAAKRFYVHEDVYDRFEHLFVTGMAEAVAGDPLDESTSFGPLATERGRQDVHELVRDAREKGAAVQCGGEIPEGEGWYYPATVLTGVTEDMRIYREECFGPVACLYKVSSLQEAIALSNDSDFGLSSSVWTNDETEATEAARSIEAGGVFINGLTASFPAVPFGGLKDSGYGRELSAYGIREFVNIKTVWTS
Protein: Prune exopolyphosphatase 1 (Q5SZG1)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MDLKIGKATPKDSKYVEKLEALFPDLPKRNDIFDSLQKAKFDVSGLTTEQMLRKDQKTIYRQGVKVAISAIYMDLEICEVLERSHSPPLKLTPASSTHPNLHAYLQGNTQVSRKKLLPLLQEALSAYFDSMKIPSGQPETADVSREQVDKELDRASNSLISGLSQDEEDPPLPPTPMN
Protein: Delta(14)-sterol reductase TM7SF2 (Delta-14-SR) (EC 1.3.1.70) (3-beta-hydroxysterol Delta (14)-reductase) (C-14 sterol reductase) (Sterol C14-reductase) (Transmembrane 7 superfamily member 2) (E9PLS9)
Organism: Homo sapiens (Human)
Subcellular location: Endoplasmic reticulum membrane {ECO:0000256|RuleBase:RU369120}; Multi-pass membrane protein {ECO:0000256|RuleBase:RU369120}. Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}. Microsome membrane {ECO:0000256|RuleBase:RU369120}; Multi-pass membrane protein {ECO:0000256|RuleBase:RU369120}.
Interaction partners:
Sequence:
MFHLLLAARSGPARLLGPPASLPGLEVLWSPRALLLWLAWLGLQAALYLLPARKVAEGQELKDKSRLRYPINGNPIYDFFLGRELNPRICFFDFKYFCELRPGLIGWVLINLALLMKEAELRGSPSLAMWLVNGFQLLYVGDALWHEEAVLTTMDITHDGFGFMLAFGDMAWVPFTYSLQAQFLLHHPQPLGLPMASVICLINATGYYIFRGANSQKNTFRKNPSDPRVAGLETISTATGRKLLVSGWWGMVRHPNYLGDLIMALAWSLPC
Protein: Geranyltranstransferase (Farnesyldiphosphate synthase) (A0A0H2UXE9)
Organism: Shigella flexneri
Interaction partners:
Sequence:
MDFPQQLEACVKQANQALSRFIAPLPFQNTPVVETMQYGALLGGKRLRPFLVYATGHMFGVSTNTLDAPAAAVECIHAYSLIHDDLPAMDDDDLRRGLPTCHVKFGEANAILAGDALQTLAFSILSDANMPEVSDRDRISMISELASASGIAGMCGGQALDLDAEGKHVPLDALERIHRHKTGALIRAAVRLGALSAGDKGRRALPVLDKYAESIGLAFQVQDDILDVVGDTATLGKRQGADQQLGKSTYPALLGLEQARKKARDLIDDARQALKQLAEQSLDTSALEALADYIIQRNK
Protein: AP-3 complex subunit beta (Adaptor-related protein complex 3 subunit beta) (Beta-3-adaptin) (Clathrin assembly protein complex 3 beta large chain) (Clathrin assembly protein large beta chain) (P46682)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Part of the AP-3 complex, an adaptor-related complex which is not clathrin-associated. The complex is associated with the Golgi region as well as more peripheral structures. It facilitates the budding of vesicles from the Golgi membrane and may be directly involved in trafficking to the vacuole. Required for the transport via the ALP pathway, which directs the transport of the cargo proteins PHO8 and VAM3 to the vacuole.
Subcellular location: Golgi apparatus {ECO:0000269|PubMed:10559961, ECO:0000269|PubMed:14562095}. Cytoplasmic vesicle, clathrin-coated vesicle membrane {ECO:0000269|PubMed:10559961}; Peripheral membrane protein {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Note=Component of the coat surrounding the cytoplasmic face of coated vesicles located at the Golgi complex. {ECO:0000269|PubMed:10559961}.
Interaction partners:
- AP-3 complex subunit mu
- AP-3 complex subunit sigma
- AP-3 complex subunit delta
- AP-1 complex subunit gamma-1
- AP-2 complex subunit alpha
- AP-1 complex subunit beta-1
- AP-2 complex subunit beta
- AP-1 complex subunit mu-1-I
- AP-2 complex subunit mu
- AP-1 complex subunit sigma-1
Sequence:
MVDSIHRIASALDTAKVITREAAAVATSKLGESSYTYYSQNINPQQLVTLLNSRNSREVRDAMKRIISIMASDDDSIDVQLYFADVVKNITTNDTKVKRLIHLYLLRFAENDPNLTLLSINSLQKSLSDSNSELRCFALSALSDMKMSSLAPIILHTVKKLVTDPSAMVRGEVALAIIKLYRAGKNDYHEELLDILKELMADTDPKVISCAVLAYKECYADHLELLHGHFRRYCRIIKQLDSWSQSYLIELLIKYCKQYLPKPTVVDKSSEGSPRSCPLPDKYNEIEYPSYEVVNDPDLDLFLQSLNCLIYSSNPTVILSCCNALYQLASPLQMKNTKFIEALVRTVTMTENQGNKEMLLQAIHFLSILDQTLFLPYTKKFYVFPKDPIVASIWKIQILSTLINESNVKEIFKELKYYVASAHFPENVVIMAVKSLSRCGQLSTSWESHVMKWLIDHMESHNLSASVLDAYVNVIRMLVQKNPTKHLRIIFKLADLLTVQTSLADNARAGIVWLFGEIASIEFKICPDVLRRLIQNFSNEGPETRCQILVLSAKLLSYDIDNFKQAQVTGSEENNQNPPYYDFSGSRISQMYNAVLYLAKYDDEFDIRDRARMISSLFDSGKYEIVSLLLQAPKPTARSDDFIVSARLETHTPEIKEFFRMLPWNTEITEVGETGNDIREGAELKDYNKYKKSFSSQSFITNNSARSFTSSSNAKLTGINDGDSNSISGKGNVNTFTSQNGKKYRLQSLDEFFSDIPERKSKPRKIIKVVEESSDEDEDESEESSDDDEYSDSSLGTSSSGTSSSHLEL
Protein: Zinc finger protein ZIC 5 (Zinc finger protein of the cerebellum 5) (Q96T25)
Organism: Homo sapiens (Human)
Function: Essential for neural crest development, converting cells from an epidermal fate to a neural crest cell fate. Binds to DNA (By similarity).
Subcellular location: Nucleus {ECO:0000250}.
Interaction partners:
- Zinc finger protein ZIC 2
Sequence:
MEPPLSKRNPPALRLADLATAQVQPLQNMTGFPALAGPPAHSQLRAAVAHLRLRDLGADPGVATTPLGPEHMAQASTLGLSPPSQAFPAHPEAPAAAARAAALVAHPGAGSYPCGGGSSGAQPSAPPPPAPPLPPTPSPPPPPPPPPPPALSGYTTTNSGGGGSSGKGHSRDFVLRRDLSATAPAAAMHGAPLGGEQRSGTGSPQHPAPPPHSAGMFISASGTYAGPDGSGGPALFPALHDTPGAPGGHPHPLNGQMRLGLAAAAAAAAAELYGRAEPPFAPRSGDAHYGAVAAAAAAALHGYGAVNLNLNLAAAAAAAAAGPGPHLQHHAPPPAPPPPPAPAQHPHQHHPHLPGAAGAFLRYMRQPIKQELICKWIDPDELAGLPPPPPPPPPPPPPPPAGGAKPCSKTFGTMHELVNHVTVEHVGGPEQSSHVCFWEDCPREGKPFKAKYKLINHIRVHTGEKPFPCPFPGCGKVFARSENLKIHKRTHTGEKPFKCEFDGCDRKFANSSDRKKHSHVHTSDKPYYCKIRGCDKSYTHPSSLRKHMKIHCKSPPPSPGPLGYSSVGTPVGAPLSPVLDPARSHSSTLSPQVTNLNEWYVCQASGAPSHLHTPSSNGTTSETEDEEIYGNPEVVRTIH
Protein: NADH dehydrogenase [ubiquinone] iron-sulfur protein 5 (Complex I-15 kDa) (CI-15 kDa) (NADH-ubiquinone oxidoreductase 15 kDa subunit) (Q99LY9)
Organism: Mus musculus (Mouse)
Function: Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed not to be involved in catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone.
Subcellular location: Mitochondrion inner membrane {ECO:0000269|PubMed:38575788}; Peripheral membrane protein {ECO:0000269|PubMed:38575788}. Mitochondrion intermembrane space {ECO:0000269|PubMed:38575788}.
Interaction partners:
- NADH-ubiquinone oxidoreductase 75 kDa subunit, mitochondrial
- NADH dehydrogenase flavoprotein 1, mitochondrial
- NADH dehydrogenase iron-sulfur protein 3, mitochondrial
- NADH dehydrogenase 1 alpha subcomplex subunit 13
- NADH dehydrogenase 1 alpha subcomplex subunit 1
- NADH dehydrogenase flavoprotein 2, mitochondrial
- NADH dehydrogenase 1 alpha subcomplex subunit 7
- NADH dehydrogenase 1 alpha subcomplex subunit 5
- NADH dehydrogenase iron-sulfur protein 7, mitochondrial
- NADH dehydrogenase 1 beta subcomplex subunit 10
Sequence:
MPFLDIQKKLGISLDRHFMFLSAEQPYKNAARCHAFEKEWIECAHGIGGTRAKKECKIEFDDFEECLLRYKTMRRMHDIKKQREKLMKEGKYTPPPHHSGREEPRP
Protein: Radial spoke head 1 homolog (Male meiotic metaphase chromosome-associated acidic protein) (Meichroacidin) (Testis-specific gene A2 protein) (Q8VIG3)
Organism: Mus musculus (Mouse)
Function: The specific expression during male germ cell development and its characteristic localization suggest that it may play an important role in male meiosis. It is necessary for proper building of the axonemal central pair and radial spokes (By similarity).
Subcellular location: Cytoplasm {ECO:0000269|PubMed:9578619}. Chromosome {ECO:0000269|PubMed:9578619}. Cytoplasm, cytoskeleton, cilium axoneme {ECO:0000269|PubMed:32203505, ECO:0000269|PubMed:34871179}. Cytoplasm, cytoskeleton, flagellum axoneme {ECO:0000269|PubMed:36417862}. Note=Cytoplasmic in late spermatocytes, secondary spermatocytes and round spermatids. Gathered around metaphase chromosomes during meiotic divisions. {ECO:0000269|PubMed:9578619}.
Interaction partners:
- Radial spoke head protein 9 homolog
- Radial spoke head protein 4 homolog A
- Zinc finger MYND domain-containing protein 10
- Radial spoke head protein 3 homolog B
- Dynein axonemal assembly factor 19
- Axonemal dynein light intermediate polypeptide 1
- Radial spoke head protein 6 homolog A
- Methyl-CpG-binding protein 2
- Dynein axonemal intermediate chain 2
- Coiled-coil domain-containing protein 39
Sequence:
MSDLGSEELEEEGENDLGEYEGERNEVGERHGHGKARLPNGDTYEGSYEFGKRHGQGTYKFKNGARYTGDYVKNKKHGQGTFIYPDGSRYEGEWADDQRHGQGVYYYVNNDTYTGEWFNHQRHGQGTYLYAETGSKYVGTWVHGQQEGAAELIHLNHRYQGKFMNKNPVGPGKYVFDIGCEQHGEYRLTDTERGEEEEEEETLVNIVPKWKALNITELALWTPTLSEEQPPPEGQGQEEPQGLTGVGDPSEDIQAEGFEGELEPRGADEDVDTFRQESQENSYDIDQGNLNFDEEPSDLQD
Protein: Cytokine receptor common subunit beta (GM-CSF/IL-3/IL-5 receptor common beta subunit) (CD antigen CD131) (P26955)
Organism: Mus musculus (Mouse)
Function: High affinity receptor for interleukin-3, interleukin-5 and granulocyte-macrophage colony-stimulating factor.
Subcellular location: Membrane; Single-pass type I membrane protein.
Interaction partners:
- Interleukin-3
- Granulocyte-macrophage colony-stimulating factor receptor subunit alpha
- Interleukin-5
- Interleukin-3 receptor subunit alpha
- Granulocyte-macrophage colony-stimulating factor
- Interleukin-5 receptor subunit alpha
- Tyrosine-protein kinase JAK2
- Erythropoietin receptor
- Interleukin-3 receptor class 2 subunit beta
- GTPase KRas
Sequence:
MDQQMALTWGLCYMALVALCWGHGVTEAEETVPLKTLQCYNDYTNHIICSWADTEDAQGLINMTLYHQLEKKQPVSCELSEELMWSECPSSHRCVPRRCVIPYTRFSITNEDYYSFRPDSDLGIQLMVPLAQNVQPPLPKNVSISSSEDRFLLEWSVSLGDAQVSWLSSKDIEFEVAYKRLQDSWEDAYSLHTSKFQVNFEPKLFLPNSIYAARVRTRLSPGSSLSGRPSRWSPEVHWDSQPGDKAQPQNLQCFFDGIQSLHCSWEVWTQTTGSVSFGLFYRPSPVAPEEKCSPVVKEPPGASVYTRYHCSLPVPEPSAHSQYTVSVKHLEQGKFIMSYNHIQMEPPTLNLTKNRDSYSLHWETQKMAYSFIEHTFQVQYKKKSDSWEDSKTENLDRAHSMDLSQLEPDTSYCARVRVKPISNYDGIWSKWSEEYTWKTDWVMPTLWIVLILVFLILTLLLILRFGCVSVYRTYRKWKEKIPNPSKSLLFQDGGKGLWPPGSMAAFATKNPALQGPQSRLLAEQQGESYAHLEDNNVSPLTIEDPNIIRVPPSGPDTTPAASSESTEQLPNVQVEGPTPNRPRKQLPSFDFNGPYLGPPQSHSLPDLPDQLGSPQVGGSLKPALPGSLEYMCLPPGGQAQLVPLSQVMGQGQAMDVQCGSSLETSGSPSVEPKENPPVELSMEEQEARDNPVTLPISSGGPEGSMMASDYVTPGDPVLTLPTGPLSTSLGPSLGLPSAQSPSLCLKLPRVPSGSPALGPPGFEDYVELPPSVSQAAKSPPGHPAPPVASSPTVIPGEPREEVGPASPHPEGLLVLQQVGDYCFLPGLGPGSLSPHSKPPSPSLCSETEDLVQDLSVKKFPYQPMPQAPAIQFFKSLKHQDYLSLPPWDNSQSGKVC
Protein: 3-oxosteroid 1-dehydrogenase (EC 1.3.99.4) (3-keto-Delta(4)-steroid Delta(1)-dehydrogenase) (KSDD) (3-oxo-Delta(4)-steroid 1-dehydrogenase) (KSTD) (A0R4S9)
Organism: Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) (Mycobacterium smegmatis)
Function: Catalyzes the elimination of the C-1 and C-2 hydrogen atoms of the A-ring from the polycyclic ring structure of 3-ketosteroids. Is also involved in the formation of 1,4-androstadiene-3,17-dione (ADD) from 4-androstene-3,17-dione (AD) to.
Interaction partners:
- 3-ketosteroid-9-alpha-monooxygenase, oxygenase component
- 3-ketosteroid-9-alpha-monooxygenase, ferredoxin reductase component
- Rieske-type oxygenase
- Steroid delta-isomerase
- Nuclear transport factor 2
- Peroxisomal multifunctional enzyme type 2
- Succinate dehydrogenase
- 3-ketosteroid-delta4
- Oxidoreductase, NAD/FAD-binding
- SnoaL-like domain-containing protein
Sequence:
MFYMTGQEYDVVVVGSGAAGMVAALTAAHQGLSTVVVEKAPHYGGSTARSGGGVWIPNNEILKRDGVKDTPDEARKYLHAIIGDVVPAEKIDTYLDRGPEMLSFVLKHSPLKLCWVPGYSDYYPETPGGKPTGRSVEPKPFDANKLGPDLKGLEPPYGKVPMNMVVMQQDYVRLNQLKRHPRGVLRSLKVGIRATWGKVSGKNLVGMGRALIAPLRIGLREAGVPVLLNTALTDLYVEDGRVLGIYVRDTTAGDDAEPRLIRARHGVILGSGGFEHNEQMRVKYQRAPITTEWTVGAVANTGDGIVAAEKLGAALELMEDAWWGPTVPLVGAPWFALSERNSPGSIIVNMSGKRFMNESMPYVEACHHMYGGQYGQGPGPGENIPAWLIFDQQYRDRYIFAGLQPGQRIPSKWLESGVIVKADTLVELAEKTGLPADQFTSTIERFNGFARSGVDEDFHRGESAYDRYYGDPTNKPNPNLGEIKHGPFYAAKMVPGDLGTKGGIRTDVRGRALRDDDSVIEGLYAAGNVSSPVMGHTYPGPGGTIGPAMTFGYLAALDIAATAAASRKG
Protein: A-kinase anchor protein 5 (AKAP-5) (A-kinase anchor protein 79 kDa) (AKAP 79) (H21) (cAMP-dependent protein kinase regulatory subunit II high affinity-binding protein) (P24588)
Organism: Homo sapiens (Human)
Function: Multivalent scaffold protein that anchors the cAMP-dependent protein kinase/PKA to cytoskeletal and/or organelle-associated proteins, targeting the signal carried by cAMP to specific intracellular effectors. Association with the beta2-adrenergic receptor (beta2-AR) not only regulates beta2-AR signaling pathway, but also the activation by PKA by switching off the beta2-AR signaling cascade. Plays a role in long term synaptic potentiation by regulating protein trafficking from the dendritic recycling endosomes to the plasma membrane and controlling both structural and functional plasticity at excitatory synapses.
Subcellular location: Postsynaptic recycling endosome membrane {ECO:0000269|PubMed:21771783, ECO:0000269|PubMed:25589740}; Lipid-anchor {ECO:0000269|PubMed:21771783}. Cell projection, dendrite {ECO:0000250|UniProtKB:D3YVF0}. Postsynaptic cell membrane {ECO:0000250|UniProtKB:D3YVF0}; Lipid-anchor. Note=Associates with lipid rafts. {ECO:0000269|PubMed:21771783}.
Interaction partners:
- cAMP-dependent protein kinase catalytic subunit beta
- cAMP-dependent protein kinase catalytic subunit alpha
- cAMP-dependent protein kinase catalytic subunit gamma
- cAMP-dependent protein kinase type II-beta regulatory subunit
- Calmodulin-1
- Adenylate cyclase type 5
- Disks large homolog 1
- Ras GTPase-activating-like protein IQGAP1
- A-kinase anchor protein 1, mitochondrial
- Disks large homolog 4
Sequence:
METTISEIHVENKDEKRSAEGSPGAERQKEKASMLCFKRRKKAAKALKPKAGSEAADVARKCPQEAGASDQPEPTRGAWASLKRLVTRRKRSESSKQQKPLEGEMQPAINAEDADLSKKKAKSRLKIPCIKFPRGPKRSNHSKIIEDSDCSIKVQEEAEILDIQTQTPLNDQATKAKSTQDLSEGISRKDGDEVCESNVSNSTTSGEKVISVELGLDNGHSAIQTGTLILEEIETIKEKQDVQPQQASPLETSETDHQQPVLSDVPPLPAIPDQQIVEEASNSTLESAPNGKDYESTEIVAEETKPKDTELSQESDFKENGITEEKSKSEESKRMEPIAIIITDTEISEFDVTKSKNVPKQFLISAENEQVGVFANDNGFEDRTSEQYETLLIETASSLVKNAIQLSIEQLVNEMASDDNKINNLLQ
Protein: Tyrosine-protein kinase Fer (EC 2.7.10.2) (Feline encephalitis virus-related kinase FER) (Fujinami poultry sarcoma/Feline sarcoma-related protein Fer) (Proto-oncogene c-Fer) (Tyrosine kinase 3) (p94-Fer) (P16591)
Organism: Homo sapiens (Human)
Function: Tyrosine-protein kinase that acts downstream of cell surface receptors for growth factors and plays a role in the regulation of the actin cytoskeleton, microtubule assembly, lamellipodia formation, cell adhesion, cell migration and chemotaxis. Acts downstream of EGFR, KIT, PDGFRA and PDGFRB. Acts downstream of EGFR to promote activation of NF-kappa-B and cell proliferation. May play a role in the regulation of the mitotic cell cycle. Plays a role in the insulin receptor signaling pathway and in activation of phosphatidylinositol 3-kinase. Acts downstream of the activated FCER1 receptor and plays a role in FCER1 (high affinity immunoglobulin epsilon receptor)-mediated signaling in mast cells. Plays a role in the regulation of mast cell degranulation. Plays a role in leukocyte recruitment and diapedesis in response to bacterial lipopolysaccharide (LPS). Plays a role in synapse organization, trafficking of synaptic vesicles, the generation of excitatory postsynaptic currents and neuron-neuron synaptic transmission. Plays a role in neuronal cell death after brain damage. Phosphorylates CTTN, CTNND1, PTK2/FAK1, GAB1, PECAM1 and PTPN11. May phosphorylate JUP and PTPN1. Can phosphorylate STAT3, but the biological relevance of this depends on cell type and stimulus.
Subcellular location: Cytoplasm. Cytoplasm, cytoskeleton. Cell membrane; Peripheral membrane protein; Cytoplasmic side. Cell projection. Cell junction. Membrane; Peripheral membrane protein; Cytoplasmic side. Nucleus. Cytoplasm, cell cortex. Note=Associated with the chromatin. Detected on microtubules in polarized and motile vascular endothelial cells. Colocalizes with F-actin at the cell cortex. Colocalizes with PECAM1 and CTNND1 at nascent cell-cell contacts.
Interaction partners:
- Catenin delta-1
- Catenin beta-1
- Tyrosine-protein kinase Yes
- Fms-related tyrosine kinase 3 ligand
Sequence:
MGFGSDLKNSHEAVLKLQDWELRLLETVKKFMALRIKSDKEYASTLQNLCNQVDKESTVQMNYVSNVSKSWLLMIQQTEQLSRIMKTHAEDLNSGPLHRLTMMIKDKQQVKKSYIGVHQQIEAEMIKVTKTELEKLKCSYRQLIKEMNSAKEKYKEALAKGKETEKAKERYDKATMKLHMLHNQYVLALKGAQLHQNQYYDITLPLLLDSLQKMQEEMIKALKGIFDEYSQITSLVTEEIVNVHKEIQMSVEQIDPSTEYNNFIDVHRTTAAKEQEIEFDTSLLEENENLQANEIMWNNLTAESLQVMLKTLAEELMQTQQMLLNKEEAVLELEKRIEESSETCEKKSDIVLLLSQKQALEELKQSVQQLRCTEAKFSAQKELLEQKVQENDGKEPPPVVNYEEDARSVTSMERKERLSKFESIRHSIAGIIRSPKSALGSSALSDMISISEKPLAEQDWYHGAIPRIEAQELLKKQGDFLVRESHGKPGEYVLSVYSDGQRRHFIIQYVDNMYRFEGTGFSNIPQLIDHHYTTKQVITKKSGVVLLNPIPKDKKWILSHEDVILGELLGKGNFGEVYKGTLKDKTSVAVKTCKEDLPQELKIKFLQEAKILKQYDHPNIVKLIGVCTQRQPVYIIMELVSGGDFLTFLRRKKDELKLKQLVKFSLDAAAGMLYLESKNCIHRDLAARNCLVGENNVLKISDFGMSRQEDGGVYSSSGLKQIPIKWTAPEALNYGRYSSESDVWSFGILLWETFSLGVCPYPGMTNQQAREQVERGYRMSAPQHCPEDISKIMMKCWDYKPENRPKFSELQKELTIIKRKLT
Protein: Adult cuticle protein 1 (dACP-1) (Q26416)
Organism: Drosophila melanogaster (Fruit fly)
Function: Component of the cuticle of the adult fruit fly. Could be involved in thickening of the hard adult cuticle.
Interaction partners:
- Uncharacterized protein, isoform B
- Adult cuticle protein 65Aa
- HL02931p
- Cuticular protein 92F
- GEO07736p1
- HL02234p
- Cuticular protein 49Ae
Sequence:
MKFAVAVIFTLALAMGVQSSVIPLLSQVAGHGLSYTAVSGPAVVASPWAVPAAHWPAAVNVASWPPAAIHAAAPAVLAAPAPAVVAAHAPSVVVAPVAHSGVYTAQTRGAIHTAPLAGHIQSVASINAAPAPGTL
Protein: Otospiralin (Organ of Corti 10 kDa protein) (Q8R448)
Organism: Mus musculus (Mouse)
Function: May be essential for the survival of the neurosensory epithelium of the inner ear.
Subcellular location: Secreted {ECO:0000305}.
Interaction partners:
Sequence:
MQACVLWWLALGMLLGIPAGAKPMPEEADPHTQPPAMPYWPFSTSDFWNYVQYFQTQGAYPQIEDMARTFFAHFPLGSTLGFHVPYQED
Protein: Bifunctional enzyme CysN/CysC [Includes: Sulfate adenylyltransferase subunit 1 (EC 2.7.7.4) (ATP-sulfurylase large subunit) (Sulfate adenylate transferase) (SAT); Adenylyl-sulfate kinase (EC 2.7.1.25) (APS kinase) (ATP adenosine-5'-phosphosulfate 3'-phosphotransferase)] (O50274)
Organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Function: With CysD forms the ATP sulfurylase (ATPS) that catalyzes the adenylation of sulfate producing adenosine 5'-phosphosulfate (APS) and diphosphate, the first enzymatic step in sulfur assimilation pathway. APS synthesis involves the formation of a high-energy phosphoric-sulfuric acid anhydride bond driven by GTP hydrolysis by CysN coupled to ATP hydrolysis by CysD.
Interaction partners:
- Sulfate transport system permease protein CysT
- Adenosine 5'-phosphosulfate reductase
- Sulfite reductase
- Sulfate transport system permease protein CysW
- Sulfate/thiosulfate import ATP-binding protein CysA
- Sulfate adenylyltransferase subunit 2
- Sulfate-binding protein
- Thiosulfate-binding protein
- 3'
- Adenylyl-sulfate kinase
Sequence:
MSHQSDLISEDILAYLGQHERKELLRFLTCGNVDDGKSTLIGRLLHDSKMIYEDHLEAITRDSKKVGTTGDDVDLALLVDGLQAEREQGITIDVAYRYFSTAKRKFIIADTPGHEQYTRNMATGASTCDLAIILIDARYGVQTQTRRHSFIASLLGIRHIVVAINKMDLKDFDQGVFEQIKADYLAFAEKIGLKTSSLHFVPMSALKGDNVVNKSERSPWYAGQSLMEILETVEIAADRNLDDMRFPVQYVNRPNLNFRGFAGTLASGVVRKGDEVVALPSGKGSKVKSIVTFEGELEQAGPGQAVTLTLEDEIDVSRGDMLVHADNRPLVTDGFDAMLVWMAEEPMLPGKKYDIKRATSYVPGSIPSIVHKVDVNTLERTPGSELKLNEIARVKVSLDAPIALDGYEQNRTTGAFIVIDRLTNGTVGAGMIVSAPPAAHGSSAHHGSNAHVTREERAGRFGQQPATVLFSGLSGAGKSTLAYAVERKLFDMGRAVYVLDGQNLRHDLNKGLPQDRAGRTENWLRTAHVAKQFNEAGLISLCAFVAPSAEGREQARALIGAERLITVYVQASPQVCRERDPQGLYAAGEDNIPGESFPYDVPLDADLVIDTQALSVEDGVKQVLDLLRERQAI
Protein: Actin-related protein 3-A (Q801P7)
Organism: Xenopus laevis (African clawed frog)
Function: ATP-binding component of the Arp2/3 complex, a multiprotein complex that mediates actin polymerization upon stimulation by nucleation-promoting factor (NPF). The Arp2/3 complex mediates the formation of branched actin networks in the cytoplasm, providing the force for cell motility. Seems to contact the pointed end of the daughter actin filament (By similarity). In addition to its role in the cytoplasmic cytoskeleton, the Arp2/3 complex also promotes actin polymerization in the nucleus, thereby regulating gene transcription and repair of damaged DNA (Probable). The Arp2/3 complex promotes homologous recombination (HR) repair in response to DNA damage by promoting nuclear actin polymerization, leading to drive motility of double-strand breaks (DSBs) (By similarity).
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000269|PubMed:17178911}. Cell projection {ECO:0000269|PubMed:17178911}. Nucleus {ECO:0000269|PubMed:29925947}.
Interaction partners:
- Actin-related protein 2/3 complex subunit 4
- Actin-related protein 2
- Actin-related protein 2
- Actin-related protein 2/3 complex subunit 2-A
- Actin-related protein 2/3 complex subunit 3-B
- Actin-related protein 2/3 complex subunit 2-B
- Actin-related protein 2/3 complex subunit 1A-A
- Actin-related protein 2/3 complex subunit 3-A
- Actin-related protein 2/3 complex subunit 5-A
- Uncharacterized protein.
Sequence:
MAARLPACVVDCGTGYTKLGYAGNTEPQFIIPSCIAIKESAKVGDQAQRRLMKGVDDLDFHIGDEAIDKPTYATKWPIRHGIVEDWDLMERFMEQIIFKYLRAEPEDHYFLLTEPPLNTPENREYTAEIMFESFNVPGLYIAVQAVLALAASWTSRQVGERTLTGTVIDSGDGVTHVIPVAEGYVIGSCIKHIPIAGRDITYFIQQLLRDREVGIPPEQSLETAKAVKEKFSYVCPDLVKEFSKYDTDGAKWIKQYMGVNAVSKKEFSIDVGYERFLGPEIFFHPEFANPDFTQPISEVVDEVIQNCPIDVRRPLYKNIVLSGGSTMFRDFGRRLQRDVKRTVDARLKLSEELSGGRLKPKPIDVQVITHHMQRYAVWFGGSMLASTPEFYQVCHTKKDYEEIGPSICRHNPVFGVMS
Protein: Annexin (Q5T3N0)
Organism: Homo sapiens (Human)
Subcellular location: Apical cell membrane {ECO:0000256|ARBA:ARBA00004221}. Basolateral cell membrane {ECO:0000256|ARBA:ARBA00004187}. Cell membrane {ECO:0000256|ARBA:ARBA00004296}; Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004296}; Extracellular side {ECO:0000256|ARBA:ARBA00004296}. Cell projection, cilium {ECO:0000256|ARBA:ARBA00004138}. Cell projection, phagocytic cup {ECO:0000256|ARBA:ARBA00004231}. Cytoplasmic vesicle membrane {ECO:0000256|ARBA:ARBA00004284}; Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004284}. Cytoplasmic vesicle, secretory vesicle lumen {ECO:0000256|ARBA:ARBA00004263}. Endosome membrane {ECO:0000256|ARBA:ARBA00004481}; Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004481}. Lateral cell membrane {ECO:0000256|ARBA:ARBA00004124}. Nucleus {ECO:0000256|ARBA:ARBA00004123}. Secreted, extracellular exosome {ECO:0000256|ARBA:ARBA00004550}.
Interaction partners:
Sequence:
MAMVSEFLKQAWFIENEEQEYVQTVKSSKGGPGSAVSPYPTFNPSSDVAALHKAIMVKGVDEATIIDILTKRNNAQRQQIKAAYLQETGKPLDETLKKALTGHLEEVVLALLKTP