wanglab/gogpt-training-data huggingface dataset:
Protein: Follistatin-related protein 3 (Follistatin-like protein 3) (Follistatin-related gene protein) (Q99PW7)
Organism: Rattus norvegicus (Rat)
Function: The secreted form is a binding and antagonizing protein for members of the TGF-beta family, such us activin, BMP2 and MSTN. Inhibits activin A-, activin B-, BMP2- and MSDT-induced cellular signaling; more effective on activin A than on activin B. Involved in bone formation; inhibits osteoclast differentiation. Involved in hematopoiesis; involved in differentiation of hemopoietic progenitor cells, increases hematopoietic cell adhesion to fibronectin and seems to contribute to the adhesion of hematopoietic precursor cells to the bone marrow stroma. The nuclear form is probably involved in transcriptional regulation via interaction with MLLT10 (By similarity).
Subcellular location: Secreted {ECO:0000250}. Nucleus {ECO:0000250}.
Interaction partners:
- Growth/differentiation factor 8
- Inhibin beta A chain
- Growth/differentiation factor 11
- Inhibin beta B chain
Sequence:
MRPGALWPLLWGALVWAVGSVGAVMGSGDSVPGGVCWLQQGKEATCSLVLKTQVSREECCASGNINTAWSNFTHPGNKISLLGFLGLVHCLPCKDSCDGVECGPGKACRMLGGRPHCECVSNCEGVPAGFQVCGSDGATYRDECELRTARCRGHPDLRVMYRGRCQKSCAQVVCPRPQSCLVDQTGSAHCVVCRAAPCPVPPNPGQELCGNNNVTYISSCHLRQATCFLGRSIGVRHPGICTGGPKVPAEEEENFV
Protein: Beta-1,3-N-acetylglucosaminyltransferase manic fringe (EC 2.4.1.222) (O-fucosylpeptide 3-beta-N-acetylglucosaminyltransferase) (O00587)
Organism: Homo sapiens (Human)
Function: Glycosyltransferase that initiates the elongation of O-linked fucose residues attached to EGF-like repeats in the extracellular domain of Notch molecules. Modulates NOTCH1 activity by modifying O-fucose residues at specific EGF-like domains resulting in inhibition of NOTCH1 activation by JAG1 and enhancement of NOTCH1 activation by DLL1 via an increase in its binding to DLL1 (By similarity).
Subcellular location: Golgi apparatus membrane {ECO:0000250}; Single-pass type II membrane protein {ECO:0000250}.
Interaction partners:
- Neurogenic locus notch homolog protein 3
- Neurogenic locus notch homolog protein 2
- Neurogenic locus notch homolog protein 1
- Neurogenic locus notch homolog protein 4
- Beta-1,3-N-acetylglucosaminyltransferase lunatic fringe
- Beta-1,3-N-acetylglucosaminyltransferase radical fringe
Sequence:
MQCRLPRGLAGALLTLLCMGLLCLRYHLNLSPQRVQGTPELSQPNPGPPKLQLHDVFIAVKTTRAFHRLRLELLLDTWVSRTREQTFVFTDSPDKGLQERLGSHLVVTNCSAEHSHPALSCKMAAEFDTFLASGLRWFCHVDDDNYVNPRALLQLLRAFPLARDVYVGRPSLNRPIHASEPQPHNRTRLVQFWFATGGAGFCINRKLALKMAPWASGSRFMDTSALIRLPDDCTMGYIIECKLGGRLQPSPLFHSHLETLQLLRTAQLPEQVTLSYGVFEGKLNVIKLQGPFSPEEDPSRFRSLHCLLYPDTPWCPQLGAR
Protein: Serpin-like protein HMSD (Minor histocompatibility protein HMSD) (Minor histocompatibility serpin domain-containing protein) (A8MTL9)
Organism: Homo sapiens (Human)
Function: Putative serine protease inhibitor.
Subcellular location: Secreted {ECO:0000305}.
Interaction partners:
Sequence:
MSISSALAMVFMGAKGNTAAQMSQALCFSKIGGEDGDIHRGFQSLLVAINRTDTEYVLRTANGLFGEKSYDFLTGFTDSCGKFYQATIKQLDFVNDTEKSTTRVNSWVADKTKGENILLFYFDNILNSFIVSSLQNCQI
Protein: pH-response regulator protein palI/RIM9 (O93956)
Organism: Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Function: Required for the proteolytic cleavage of the transcription factor pacC in response to alkaline ambient pH. Might be a pH sensor.
Subcellular location: Cell membrane; Multi-pass membrane protein.
Interaction partners:
- Uncharacterized protein
Sequence:
MLLKPATPLTILLLIAFVLLLLSVISTPIVKSIPLATFDNVEYGVFGYCKAGTCTAIHIGYTTEEIENTGSTDSDFNLPSDARRSLSSILIVHPIAAFLTLICLCLAAAAHLHAPSHSPRYLLALLILLLPTLLVSLLAFLVDILLFVPHLSWGGWIVLAATIILVTCGVVTCAMRRTLVSRKARKRRIAENAEMSGQNYYNRQNAAAAALNESKPIAPEAKETFVAATQSSESGPTFATFRTNTRSSDDDRTPLNNHSDPSAQDAGYQSRIPGDPVPYNAPRDDFGNPLPPGAYNSAPRMRTPGPPGPPPPDSRVRDQYSDPRRGPPTGFAPRGRGGYPPRGGYGRGGPYGGPYGPNSRAPLTGRGGYMGPMRGGPAGPMARGGYRPQPAAGGYGNARAMGEDEYGYRGPSSRQRTPGPMAAPAAPGPAGQAIEMMPQPRHEPDAQDEVPEQQQLHAISIDNQHEPVSPTSLYSRTQSYVPPRRNWGPQAYQSSEPNLPYQPNQPRHARSQSGSMYYEDEDPVYTSRNESAVGNSGVPSVLTPGNSAK
Protein: Telomeric repeat-binding factor (A0A8I5Y1U3)
Organism: Rattus norvegicus (Rat)
Subcellular location: Chromosome, telomere {ECO:0000256|ARBA:ARBA00004574}. Nucleus {ECO:0000256|PIRNR:PIRNR038016}.
Interaction partners:
Sequence:
MAGTVTSAAPGARSNAGGTSADSPEKEAARDDAELFDCRVQLGPPREEENAELVAEAEAVAAGWMLDFLCLSLCRAFRDGRCEDFRQTRDSAEAIIHGLPSLTAYQLKTVYICQFLTRVAAGKSLDAQFEVDERITPLESALMIWDSIEKEHDKLHEEIQNLIKIQPLERKLLKIISQKDVFHVLFQRFSYNLMMEKIQSYVECVLNEKSSTFLMKAATKVVENEKARTVASEDKAKATNTGTETEVNSNKGESVNGQQSVETESLVDTGSSVRSHKNALSPLKSRRLQPDFNRNEARTGTLQCEIATKRNRRTSGGNRLRISKNQPDTNEKHGRRKKQTWLWEEDRSLKCGVRKYGEGNWAKILSHYKFNNRTSVMLKDRWRTMRRLRLIS
Protein: CD40 ligand (CD40-L) (T-cell antigen Gp39) (TNF-related activation protein) (TRAP) (Tumor necrosis factor ligand superfamily member 5) (CD antigen CD154) [Cleaved into: CD40 ligand, membrane form; CD40 ligand, soluble form (sCD40L)] (P27548)
Organism: Mus musculus (Mouse)
Function: Cytokine that acts as a ligand to CD40/TNFRSF5 (By similarity). Costimulates T-cell proliferation and cytokine production (By similarity). Its cross-linking on T-cells generates a costimulatory signal which enhances the production of IL4 and IL10 in conjunction with the TCR/CD3 ligation and CD28 costimulation (By similarity). Induces the activation of NF-kappa-B (By similarity). Induces the activation of kinases MAPK8 and PAK2 in T-cells (By similarity). Mediates B-cell proliferation in the absence of co-stimulus as well as IgE production in the presence of IL4. Involved in immunoglobulin class switching.
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:P29965}; Single-pass type II membrane protein {ECO:0000250|UniProtKB:P29965}. Cell surface {ECO:0000250|UniProtKB:P29965}.; SUBCELLULAR LOCATION: [CD40 ligand, soluble form]: Secreted {ECO:0000250|UniProtKB:P29965}. Note=Release of soluble CD40L from platelets is partially regulated by GP IIb/IIIa, actin polymerization, and a matrix metalloproteinases (MMP) inhibitor-sensitive pathway. {ECO:0000250|UniProtKB:P29965}.
Interaction partners:
- Tumor necrosis factor receptor superfamily member 5
- Inducible T-cell costimulator
- T-lymphocyte activation antigen CD86
- T-lymphocyte activation antigen CD80
- T-cell surface glycoprotein CD4
- T-cell-specific surface glycoprotein CD28
- ICOS ligand
- CD70 antigen
- Tumor necrosis factor receptor superfamily member 13C
- Tumor necrosis factor ligand superfamily member 4
Sequence:
MIETYSQPSPRSVATGLPASMKIFMYLLTVFLITQMIGSVLFAVYLHRRLDKVEEEVNLHEDFVFIKKLKRCNKGEGSLSLLNCEEMRRQFEDLVKDITLNKEEKKENSFEMQRGDEDPQIAAHVVSEANSNAASVLQWAKKGYYTMKSNLVMLENGKQLTVKREGLYYVYTQVTFCSNREPSSQRPFIVGLWLKPSSGSERILLKAANTHSSSQLCEQQSVHLGGVFELQAGASVFVNVTEASQVIHRVGFSSFGLLKL
Protein: Lysine-ketoglutarate reductase/saccharopine dehydrogenase bifunctional enzyme (F4JVY8)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
Sequence:
MNSNGHEEEKKLGNGVVGILAETVNKWERRTPLTPSHCARLLHGGKDRTGISRIVVQPSAKRIHHDALYEDVGCEISDDLSDCGLILGIKQPELEMILPERAYAFFSHTHKAQKENMPLLDKILSERVTLCDYELIVGDHGKRLLAFGKYAGRAGLVDFLHGLGQRYLSLGYSTPFLSLGASYMYSSLAAAKAAVISVGEEIASQGLPLGICPLVFVFTGTGNVSLGAQEIFKLLPHTFVEPSKLPELFVKDKGISQNGISTKRVYQVYGCIITSQDMVEHKDPSKSFDKADYYAHPEHYNPVFHEKISPYTSVLVNCMYWEKRFPCLLSTKQLQDLTKKGLPLVGICDITCDIGGSIEFVNRATLIDSPFFRFNPSNNSYYDDMDGDGVLCMAVDILPTEFAKEASQHFGDILSGFVGSLASMTEISDLPAHLKRACISYRGELTSLYEYIPRMRKSNPEEAQDNIIANGVSSQRTFNILVSLSGHLFDKFLINEALDMIEAAGGSFHLAKCELGQSADAESYSELEVGADDKRVLDQIIDSLTRLANPNEDYISPHREANKISLKIGKVQQENEIKEKPEMTKKSGVLILGAGRVCRPAADFLASVRTISSQQWYKTYFGADSEEKTDVHVIVASLYLKDAKETVEGISDVEAVRLDVSDSESLLKYVSQVDVVLSLLPASCHAVVAKTCIELKKHLVTASYVDDETSMLHEKAKSAGITILGEMGLDPGIDHMMAMKMINDAHIKKGKVKSFTSYCGGLPSPAAANNPLAYKFSWNPAGAIRAGQNPAKYKSNGDIIHVDGKNLYDSAARFRVPNLPAFALECFPNRDSLVYGEHYGIESEATTIFRGTLRYEGFSMIMATLSKLGFFDSEANQVLSTGKRITFGALLSNILNKDADNESEPLAGEEEISKRIIKLGHSKETAAKAAKTIVFLGFNEEREVPSLCKSVFDATCYLMEEKLAYSGNEQDMVLLHHEVEVEFLESKRIEKHTATLLEFGDIKNGQTTTAMAKTVGIPAAIGALLLIEDKIKTRGVLRPLEAEVYLPALDILQAYGIKLMEKAE
Protein: SPRY domain-containing SOCS box protein 1 (SSB-1) (Q96BD6)
Organism: Homo sapiens (Human)
Function: Substrate recognition component of a SCF-like ECS (Elongin BC-CUL2/5-SOCS-box protein) E3 ubiquitin-protein ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins. Negatively regulates nitric oxide (NO) production and limits cellular toxicity in activated macrophages by mediating the ubiquitination and proteasomal degradation of NOS2. Acts as a bridge which links NOS2 with the ECS E3 ubiquitin ligase complex components ELOC and CUL5.
Subcellular location: Cytoplasm {ECO:0000305}. Cytoplasm, cytosol {ECO:0000269|PubMed:21199876}. Note=Exhibits a diffuse cytosolic localization. {ECO:0000269|PubMed:21199876}.
Interaction partners:
- Elongin-C
- PRKC apoptosis WT1 regulator protein
- Cytokine-inducible SH2-containing protein
- Elongin-B
- Cullin-5
- Nitric oxide synthase, inducible
Sequence:
MGQKVTGGIKTVDMRDPTYRPLKQELQGLDYCKPTRLDLLLDMPPVSYDVQLLHSWNNNDRSLNVFVKEDDKLIFHRHPVAQSTDAIRGKVGYTRGLHVWQITWAMRQRGTHAVVGVATADAPLHSVGYTTLVGNNHESWGWDLGRNRLYHDGKNQPSKTYPAFLEPDETFIVPDSFLVALDMDDGTLSFIVDGQYMGVAFRGLKGKKLYPVVSAVWGHCEIRMRYLNGLDPEPLPLMDLCRRSVRLALGRERLGEIHTLPLPASLKAYLLYQ
Protein: Serine/threonine-protein phosphatase (EC 3.1.3.16) (E2CWF2)
Organism: Rattus norvegicus (Rat)
Interaction partners:
Sequence:
MSGRRPQFSTTERVIKAVPFPPTRRLTLKEVFENGKPKMDVLKNHLVKEGRVEEDVALKIINDGAAILKQEKTMLEVEAPITVCGDVHGQFFDLMKLFEVGGSPSNTRYLFLGDYVDRGYFSIECVLYLWSLKINHPKTLFLLRGNHECRHLTEYFTFKQECRIKYSELVYEACMHTFDCLPLAALLNQQFLCVHGGMSPEITCLDDIRKLDRFAEPPAFGPVCDLLWSDPLEDYGSEKTLEHYTHNTVRGCSYFFSCSIEI
Protein: Troponin T, slow skeletal muscle (TnTs) (Slow skeletal muscle troponin T) (sTnT) (Q7TNB2)
Organism: Rattus norvegicus (Rat)
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, slow skeletal muscle
- Troponin I, fast skeletal muscle
- Troponin C, skeletal muscle
- Troponin C, slow skeletal and cardiac muscles
- Troponin I, cardiac muscle
- Myosin light chain 1/3, skeletal muscle isoform
- Tropomyosin beta chain
- Troponin T, fast skeletal muscle
- Troponin T, cardiac muscle
- Tropomyosin alpha-1 chain
Sequence:
MSDTEEQEYEEEQAEDEEAVEEEAPEEPEPVAEREEERPKPSRPVVPPLIPPKIPEGERVDFDDIHRKRMEKDLLELQTLIDVHFEQRKKEEEELIALKDRIERRRAERAEQQRFRTEKERERQAKLAEEKMRKEEEEAKKRAEDDAKKKKVLSNMGAHFGGYLVKAEQKRGKRQTGREMKLRILSERKKPLNIDYMGEDQLREKAQELSEWIHQLESEKFDLMEKLKQQKYEINVLYNRISHAQKFRKGAGKGRVGGRWK
Protein: Fibrinogen alpha chain [Cleaved into: Fibrinopeptide A; Fibrinogen alpha chain] (P02671)
Organism: Homo sapiens (Human)
Function: Cleaved by the protease thrombin to yield monomers which, together with fibrinogen beta (FGB) and fibrinogen gamma (FGG), polymerize to form an insoluble fibrin matrix. Fibrin has a major function in hemostasis as one of the primary components of blood clots. In addition, functions during the early stages of wound repair to stabilize the lesion and guide cell migration during re-epithelialization. Was originally thought to be essential for platelet aggregation, based on in vitro studies using anticoagulated blood. However, subsequent studies have shown that it is not absolutely required for thrombus formation in vivo. Enhances expression of SELP in activated platelets via an ITGB3-dependent pathway. Maternal fibrinogen is essential for successful pregnancy. Fibrin deposition is also associated with infection, where it protects against IFNG-mediated hemorrhage. May also facilitate the immune response via both innate and T-cell mediated pathways.
Subcellular location: Secreted {ECO:0000269|PubMed:19296670, ECO:0000269|PubMed:9628725}.
Interaction partners:
- Prothrombin
- Fibrinogen beta chain
- Fibrinogen gamma chain
- Alpha-2-HS-glycoprotein
- Antithrombin-III
- Integrin beta-3
- Albumin
- Alpha-2-antiplasmin
- Plasminogen
- Coagulation factor XIII B chain
Sequence:
MFSMRIVCLVLSVVGTAWTADSGEGDFLAEGGGVRGPRVVERHQSACKDSDWPFCSDEDWNYKCPSGCRMKGLIDEVNQDFTNRINKLKNSLFEYQKNNKDSHSLTTNIMEILRGDFSSANNRDNTYNRVSEDLRSRIEVLKRKVIEKVQHIQLLQKNVRAQLVDMKRLEVDIDIKIRSCRGSCSRALAREVDLKDYEDQQKQLEQVIAKDLLPSRDRQHLPLIKMKPVPDLVPGNFKSQLQKVPPEWKALTDMPQMRMELERPGGNEITRGGSTSYGTGSETESPRNPSSAGSWNSGSSGPGSTGNRNPGSSGTGGTATWKPGSSGPGSTGSWNSGSSGTGSTGNQNPGSPRPGSTGTWNPGSSERGSAGHWTSESSVSGSTGQWHSESGSFRPDSPGSGNARPNNPDWGTFEEVSGNVSPGTRREYHTEKLVTSKGDKELRTGKEKVTSGSTTTTRRSCSKTVTKTVIGPDGHKEVTKEVVTSEDGSDCPEAMDLGTLSGIGTLDGFRHRHPDEAAFFDTASTGKTFPGFFSPMLGEFVSETESRGSESGIFTNTKESSSHHPGIAEFPSRGKSSSYSKQFTSSTSYNRGDSTFESKSYKMADEAGSEADHEGTHSTKRGHAKSRPVRDCDDVLQTHPSGTQSGIFNIKLPGSSKIFSVYCDQETSLGGWLLIQQRMDGSLNFNRTWQDYKRGFGSLNDEGEGEFWLGNDYLHLLTQRGSVLRVELEDWAGNEAYAEYHFRVGSEAEGYALQVSSYEGTAGDALIEGSVEEGAEYTSHNNMQFSTFDRDADQWEENCAEVYGGGWWYNNCQAANLNGIYYPGGSYDPRNNSPYEIENGVVWVSFRGADYSLRAVRMKIRPLVTQ
Protein: Spore development regulator RYP2 (B2CQK0)
Organism: Ajellomyces capsulatus (Darling's disease fungus) (Histoplasma capsulatum)
Function: Component of the RYP2-RYP3 heterodimeric complex that plays a dual role in activating genes associated with spore maturation and repressing certain development-associated genes (By similarity). The complex binds DNA through the DNA-binding domain of vosA that recognizes an 11-nucleotide consensus sequence 5'-CTGGCCGCGGC-3' consisting of two motifs in the promoters of key developmental regulatory genes (By similarity). Required for viable spore production and regulation of sporulation in response to temperature and for the switch to yeast-form in the presence of host cells.
Subcellular location: Nucleus {ECO:0000250|UniProtKB:Q5BBX1}.
Interaction partners:
Sequence:
MSAPTFAEDPVTQRPALQSADFRLTVRQNPERARVAGGKEKERKAVDPPPIIQLKIDESKDPGQNYLQSPFYFMCCTLYNATEDTPATTAQSTALAGTLVSSLHRLKDTDNMEGGFFVFGDLSVKIEGEFRLKFNLFEMREVKRCGGSRDEVVYIKSILSKPFTVLPPKNFPGMTESTWLSRSFADQGVKLRIRKEARTLLKRPLNRAEPDYPAPPTQPRTPERSGASSQQMVAAYQTNRDYPFYNGPDAKRPRSSVDMSGRGLYEGDARYSYPPHAANPYQGQTYQQGMMQGYPTAGAGVSDYAIRQAQQGSTPTPFGSADESIGSIRSPGAGGYIGQPRYQSYSGAQMPYNLASSTQMSQMGESTPGRTGQAANMGGIVSGQSFSQSAGHMQSPSQVPPAWG
Protein: Tubulin-folding cofactor B (AtTFCB) (Protein EMBRYO DEFECTIVE 2804) (Q67Z52)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Involved in control of cell division. Regulates probably the availability of alpha-tubulin for dimerization of alpha-/beta-tubulin, which is required for proper microtubule biogenesis. Decreased expression of TFCB results in enlarged mesophyll cells and leaf epidermal cells with bulged nuclei, increased ploidy and increased numbers of spindles and phragmoplasts.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16928693}. Note=Not associated with microtubular arrays.
Interaction partners:
- Tubulin-folding cofactor D
- Tubulin-folding cofactor E
- ADP-ribosylation factor-like protein 2
- Tubulin-folding cofactor A
- GPN-loop GTPase QQT2
- Tubulin alpha-3 chain
- Trafficking protein particle complex subunit
- Tubulin alpha-1 chain
Sequence:
MATSRLQLEGDDSVHLHITHANLKSFSADARFSPQMSVEAVKEKLWKKCGTSVNSMALELYDDSGSKVAVLSDDSRPLGFFSPFDGFRLHIIDLDPSSVTTGGWLEDTSLVEKYNISEEDYAKRTDSFRKFKEKRVSQNPVAAEAKTKENYMEDLCANIKVGDRCQVEPGEKRGMVKYVGRAESLGPGYWVGIQYDEPLGKHDGMVKGTRFFECPRLQGGMVRPDKVKVGDYPERDPFEEDEI
Protein: GTP-binding elongation factor Tu family, putative (Q586X7)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MADGSHDREAALFLVLSEPEAMTVGQWLKEVAEKHLMPPVVHAMLYNVSEACGKSSSNNNNSNSNGRAASGGSEGNGCFQNALTRVLNEFHHSGKHGVPMTSMRVLVVALFWDGQSESAKAEFARLRELADETNKQASDPQVNADKANNSGSDGKQKLPSLIGSNVHIVLQALNAKKSNEKLVETLDAVVCSLRKKLQSACGPSEHVDPTRIDAAASRRVDKVTVTQKEKGSQNGTGDGGSGNNVIGVEDLSDSAVAGRVEEGQGECFIVISGTTMEEFQKRVWELKASAARIGVGCSPVLAEPREVQTSNSGTKTKVFAQEFLVRQGASVEQHIEMRIAMCGNVDSGKSTLTSVLTRGCRDNGRGSARAFVFKHKHEAATGRTSSVSENHLGFSEAGEVVNYVVAGAKHSLGGVSLGEETPNDGGGGGGGGDGPIGNKPVTINSHQLGQEVAAKSSKVLTLYDLAGHERYLKTTVLGMTRNIPDYACVVISANNGIQRMTKEHVALCLALKIPFFVVITRIDSTPENIRQETLASVHKLLKVPTVRKLPYPVRRVDDVVLSAKNLRNDRITPIFEISNVSGEGLQSLVRFLNLLPMRKDWRNARQLPREMVIDSTFFVAGVGTVVGGIVTQGVFNVNDAVLLGPDASGGFRTVQIKSIHVKGVEQQRAVAGCDASFCLKKEKRRGIRKGNILTDPKHPVEAYWQFEADVVILYHSTTILVNYEPVIHSTTVRQSARIVFVEKEVLRTGDRSLVRFHFLYRPEFMKVGQQLIFREGRTKGIGTVTNLIGPREGSLLAKRLKHKET
Protein: H-2 class II histocompatibility antigen, A-U alpha chain (P14438)
Organism: Mus musculus (Mouse)
Subcellular location: Membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}.
Interaction partners:
Sequence:
DHVGSYGIVVYQSPGDIGQYTFEFDGDELFYVDLDKKETIWMLPEFAQLRSFDPQGGLQNIATGKHNLGVLTKRSNSTPATNEAPQATVFPKSPVLLGQPNTLICFVDNIFPPVINITWLRNSKSVADGVYETSFFVNRDYSFHKLSYLTFIPSDDDIYDCKVEHWGLEEPVLKHWEPEIPAPMSELTETVVCALGLSVGLVGIVVGTIFIIQGLRSGGTSRHPGPL
Protein: Ube2n protein (Ubiquitin-conjugating enzyme E2N (EC 6.3.2.19)) (Q803J2)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
- Ubiquitin-conjugating enzyme E2 variant 2
- Ubiquitin-conjugating enzyme E2 variant 1.
- TNF receptor-associated factor 6
- Ubiquitin-ribosomal protein eS31 fusion protein
- Ubiquitin-ribosomal protein eL40 fusion protein
- Polyubiquitin-C
- Polyubiquitin-B
- Si:ch211-202a12.4.
- Mitogen-activated protein kinase kinase kinase 7.
- E3 ubiquitin-protein ligase rnf8
Sequence:
MAGLPRRIIKETQRLLAEPVPGIKAEPDEGNARYFHVVIAGPQDSPFEGGTFKLELFLPEEYPMAAPKVRFMTKIYHPNVDKLGRICLDILKDKWSPALQIRTVLLSIQALLSAPNPDDPLANDVAEQWKTNEAQAIETARTWTRLYAGNNIEV
Protein: KIB1-4 beta-propeller domain-containing protein (Q9FLW7)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Putative F-box protein At5g55150
- Probable F-box protein At4g22030
- F-box protein At2g16300
- Protein DETOXIFICATION 4
- Protein DETOXIFICATION 3
- Putative F-box protein At4g22180
- Putative F-box protein At2g16290
- Probable F-box protein At1g65740
- F-box/kelch-repeat protein At1g57790
- Protein DETOXIFICATION 1
Sequence:
MAMLLSRLRLGKPVFVRSSLLHSNALSNSLLQNPPYHVFTADPSGPRYPDLGKLIIFEANGYDSTHLEKKVPMELVDGKARVTIGSSHGWVATLKDDGIVRLQDDLNLVASDTDPKRIPLPPLVTLPHCQTKVVTNVAMSSSSPEDEDCVVALKFLGPQLSLCRPAQRNSEWTNIRIENPCFYSSPVMFSKKDGTFRILGSGGHLIGSWDLHKHKNKPKIQRLRFKNLPELTKTKRELLHSCCTSQHLVESTTTNETFLVKWYRKDTSNGVVKMKTRAVMVFKLYEEGKAVYTQDIGDLCIFLSKSEPFCVTASSFPGMCPNEVHTLDVDEHALVDLSDSSIISGICTFGSPYYFPPPKIDS
Protein: Interferon alpha-21 (IFN-alpha-21) (Interferon alpha-F) (LeIF F) (P01568)
Organism: Homo sapiens (Human)
Function: Produced by macrophages, IFN-alpha have antiviral activities. Interferon stimulates the production of two enzymes: a protein kinase and an oligoadenylate synthetase.
Subcellular location: Secreted.
Interaction partners:
- Interferon alpha/beta receptor 1
- Interferon alpha-14
- Interferon alpha-4
- Interferon alpha-1/13
- Ubiquitin-like protein ISG15
- Interleukin-2
- Interferon alpha-16
- Interferon alpha/beta receptor 2
- Interferon alpha-10
- Interferon alpha-6
Sequence:
MALSFSLLMAVLVLSYKSICSLGCDLPQTHSLGNRRALILLAQMGRISPFSCLKDRHDFGFPQEEFDGNQFQKAQAISVLHEMIQQTFNLFSTKDSSATWEQSLLEKFSTELNQQLNDLEACVIQEVGVEETPLMNVDSILAVKKYFQRITLYLTEKKYSPCAWEVVRAEIMRSFSLSKIFQERLRRKE
Protein: Triosephosphate isomerase (TIM) (TPI) (EC 5.3.1.1) (Triose-phosphate isomerase) (Q59182)
Organism: Borreliella burgdorferi (strain ATCC 35210 / DSM 4680 / CIP 102532 / B31) (Borrelia burgdorferi)
Function: Involved in the gluconeogenesis. Catalyzes stereospecifically the conversion of dihydroxyacetone phosphate (DHAP) to D-glyceraldehyde-3-phosphate (G3P).
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00147}.
Interaction partners:
- Glyceraldehyde-3-phosphate dehydrogenase
- Phosphoglycerate kinase
- Glucose-6-phosphate isomerase
- Fructose-bisphosphate aldolase
- Enolase
- 2,3-bisphosphoglycerate-dependent phosphoglycerate mutase
- Pyruvate kinase
- ATP-dependent 6-phosphofructokinase
- Probable protein-export membrane protein SecG
- Glucose-6-phosphate 1-dehydrogenase
Sequence:
MRKTFLAGNWKMHYTSAEASIVAKKIATEVKTLKDDVVIMITPPFTALSKVSECIKGSNILLGAQNMSYMESGARTSEISPSMLLEFGVEYVILGHSECRLYLAETDEIINKKILAGLKHPFKYLILCVGETLDERDSGKTLEVVLNQVKKGLNCVSESDIQRIILAYEPVWAIGTGKTATKEEAEEVHKAIRLEITKLYSKSASDNIIIQYGGSVNSNNVKELMNEPNIDGALIGGASLKAESFLSIINNVL
Protein: SWIB/MDM2 domain superfamily protein (Q9SYZ4)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Single-stranded DNA-binding protein WHY2, mitochondrial
- Heat shock 70 kDa protein 9, mitochondrial
- NADH-cytochrome b5 reductase-like protein
- Chaperone DnaJ-domain superfamily protein
- Chromatin structure-remodeling complex protein BSH
- Shewanella-like protein phosphatase 2
Sequence:
MALSSGIFSTTFLCVDTAPLRSSMLSPSSLRLSPNHPTNLRMVRAVTSAAAASSDPTTTTKTREPRGIMKPRPVSQAMQDVVGVPEIPRTQALKRIWAYIKEHDLQDPQNKRDILCDEKLKKIFEGKERVGFLEIAKLIGPHFL
Protein: Glutamate receptor (H7BYG7)
Organism: Homo sapiens (Human)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004651}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}. Postsynaptic cell membrane {ECO:0000256|RuleBase:RU367118}; Multi-pass membrane protein {ECO:0000256|RuleBase:RU367118}.
Interaction partners:
Sequence:
MEHGTLLAQPGLWTRDTSWALLYFLCYILPQTAPQVLRIGGIFETVENEPVNVEELAFKFAVTSINRNRTLMPNTTLTYDIQRINLFDSFEASRRACDQLALGVAALFGPSHSSSVSAVQSICNALEVPHIQTRWKHPSVDNKDLFYINLYPDYAAISRAILDLVLYYNWKTVTVVYEDSTGLIRLQELIKAPSRYNIKIKIRQLPSGNKDAKPLLKEMKKGKEFYVIFDCSHETAAEILKQILFMGMMTEYYHYFFTTLDLFALDLELYRYSGVNMTGFRLLNIDNPHVSSIIEKWSMERLQAPPRPETGLLDGMMTTEAALMYDAVYMVAIASHRASQLTVSSLQCHRHKPWRLGPRFMNLIKEARWDGLTGHITFNKTNGLRKDFDLDIISLKEEGTEKAAGEVSKHLYKVWKKIGIWNSNSGLNMTDSNKDKSSNITDSLANRTLIVTTILEEPYVMYRKSDKPLYGNDRFEGYCLDLLKELSNILGFIYDVKLVPDGKYGAQNDKGEWNGMVKELIDHRADLAVAPLTITYVREKVIDFSKPFMTLGISILYRKPNGTNPGVFSFLNPLSPDIWMYVLLACLGVSCVLFVIARFTPYEWYNPHPCNPDSDVVENNFTLLNSFWFGVGALMQQGSELMPKALSTRIVGGIWWFFTLIIISSYTANLAAFLTVERMESPIDSADDLAKQTKIEYGAVRDGSTMTFFKKSKISTYEKMWAFMSSRQQTALVRNSDEGIQRVLTTDYALLMESTSIEYVTQRNCNLTQIGGLIDSKGYGVGTPIGSPYRDKITIAILQLQEEGKLHMMKEKWWRGNGCPEEDNKEASALGVENIGGIFIVLAAGLVLSVFVAIGEFIYKSRKNNDIEQHY
Protein: Zgc:193816 protein (B3DGY9)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Chromosome, telomere {ECO:0000256|ARBA:ARBA00004574}. Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MAELEPWIEKLIQNFGQNQTETVVKASVIGTCEISDSQRMDRTDACMLFLSDGIAMIPAVLSDAAWERLQELEDLDSFTSLLNHVAFIRSFELEFDMKPDLGSCQFYLKVNQMNTFCIALKRQQPPSCTTLQSVRDQIEKTWRSRGGGSESSVSGVSLSSLLDVWHSDIIVSILNDAMEKINVSATYSPSVATPTHWHRERLQRRAQEQFAIPVPFLLIPEEQRELMTADPGADSETPTGLAPPYEEPHPISTQSANQAVAVQDDAISDLCPDEGPSTLVQTRPEVLCGTGDLSRDTTSPWDMFTEEPGLLGRSTSSGSNATSTQFSKQVSAGPSADGITLSQRPKPTQFSLSRSIGRSIRDPSQEQDKEPAQSPPSWLIHNTAPPSAPPPPRTKPSTPAPSKTRRVHSDGAPFSYLYHPKPQVASALSHFQVPGHLIQWAVCYLGTSDCADINAEAGS