wanglab/gogpt-training-data huggingface dataset:
Protein: CDK5 regulatory subunit-associated protein 3 (CDK5 activator-binding protein C53) (Q9JLH7)
Organism: Rattus norvegicus (Rat)
Function: Substrate adapter for ufmylation, the covalent attachment of the ubiquitin-like modifier UFM1 to substrate proteins, in response to endoplasmic reticulum stress (By similarity). Negatively regulates NF-kappa-B-mediated gene transcription through the control of RELA phosphorylation. Probable tumor suppressor initially identified as a CDK5R1 interactor controlling cell proliferation. Also regulates mitotic G2/M transition checkpoint and mitotic G2 DNA damage checkpoint. Through its interaction with CDKN2A/ARF and MDM2 may induce MDM2-dependent p53/TP53 ubiquitination, stabilization and activation in the nucleus, thereby promoting G1 cell cycle arrest and inhibition of cell proliferation. May also play a role in the rupture of the nuclear envelope during apoptosis. May regulate MAPK14 activity by regulating its dephosphorylation by PPM1D/WIP1 (By similarity). Required for liver development (By similarity).
Subcellular location: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q96JB5}. Cytoplasm {ECO:0000250|UniProtKB:Q96JB5}. Nucleus {ECO:0000250|UniProtKB:Q96JB5}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250|UniProtKB:Q96JB5}. Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:Q96JB5}. Note=Tethered to the endoplasmic reticulum membrane as part of the UFM1 ribosome E3 ligase (UREL) complex. Colocalizes and associates with microtubules. {ECO:0000250|UniProtKB:Q96JB5}.
Interaction partners:
- E3 UFM1-protein ligase 1
- DDRGK domain-containing protein 1
- Ufm1-specific protease 2
- Ubiquitin-fold modifier-conjugating enzyme 1
- Ubiquitin-like modifier-activating enzyme 5
Sequence:
MQDHQHVPIDIQTSKLLDWLVDRRHCNLKWQSLVLTIREKINTAIQDMPESQEIAQLLSGSYIHYFHCLRIVDLLKGTEASTKNIFGRYSSQRMKDWQEIISLYEKDNTYLVELSSLLVRNVNYEIPSLKKQIAKCQQLQQDYSRKEEEGQAGAAEMREQFYHSCKQYGITGDNVRRELLALVKDLPSQLAEIGAGAQSLGEAIDLYQACVEFVCDSPTEQVLPMLRYVQPKGNSTVYEWRTGTEPSVVERPQLEDPPEQVQEDEIDWGDFGLEAVSDSGNIISAETPGIDWGISLESESKDAGADKIDWGDNAVASEITVLETGTEAPEGVARGSDALTLLEYPETRNQFIDELMELEIFLSQRAVEMSEEADILSVSQFQLAPAILQGQTKEKMLSLVSTLQHLIGQLTSLDLQHLFMILASPRYVDRVTELLQQKLKQSQLLALKKDLMVEKQQEALQEQAALEPKLDLLLEKTRELQKLIEADISKRYNGRPVNLMGTSV
Protein: Phytoene dehydrogenase (Q9RW08)
Organism: Deinococcus radiodurans (strain ATCC 13939 / DSM 20539 / JCM 16871 / CCUG 27074 / LMG 4051 / NBRC 15346 / NCIMB 9279 / VKM B-1422 / R1)
Interaction partners:
- Phytoene synthase
- Uncharacterized carotenoid cyclase DR_0801
- Carotenoid biosynthesis protein
- Dehydrogenase, putative
Sequence:
MTSALPRPAPSPYARRKTALVIGAGFGGLALGIRLQSLGFDTTILERLDGPGGRAYQKRTPDGYVFDMGPTVLTVPHFIEELFALERDRAGLDAPDYPPEVLSGERVKEGVSGGPHTSRYVTLVPILPFYRIVFHDGTYFDYDGDPESTRRQIAELAPGDLAGYERFHADAEAIFRRGFLELGYTHFGDVPTMLRVVPDLLKLDAVRTLFSFTSKYFQSDKLRQVFSFETLLVGGNPLSVPAIYAMIHFVEKTWGIHYAMGGTGALVRGLVQKFEELGGAIRYGAGVDEVLVDGNLPGKRTARGVRLESGEELRADLVASNGDWANTYLKRVRPSARLVNSDLRVKAASESMSLLVVYFGFRGGDDLPLKHHNILLGPRYEALLSEIFGTKRLGEDFSQYLHVPTLTDPALAPAGHHAAYTLVPVPHNGSGIDWDVEGPKLAEAALADIERRGLIPGLRERLTHFEFITPDYFAGTLDSYLGNAFGPEPRLVQSAFFRPHNRSEDLHNFYLVGAGAQPGAGTPSVMMSAKMTARLIAEDFGIHADIRR
Protein: Calnexin (pp90) (P24643)
Organism: Canis lupus familiaris (Dog) (Canis familiaris)
Function: Calcium-binding protein that interacts with newly synthesized monoglucosylated glycoproteins in the endoplasmic reticulum. It may act in assisting protein assembly and/or in the retention within the ER of unassembled protein subunits. It seems to play a major role in the quality control apparatus of the ER by the retention of incorrectly folded proteins. Associated with partial T-cell antigen receptor complexes that escape the ER of immature thymocytes, it may function as a signaling complex regulating thymocyte maturation. Additionally it may play a role in receptor-mediated endocytosis at the synapse (By similarity).
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:22045338}; Single-pass type I membrane protein {ECO:0000255}. Mitochondrion membrane {ECO:0000269|PubMed:22045338}; Single-pass type I membrane protein {ECO:0000255}. Melanosome membrane {ECO:0000250|UniProtKB:P27824}; Single-pass type I membrane protein {ECO:0000255}. Note=The palmitoylated form preferentially localizes to the perinuclear rough ER (By similarity). Localizes to endoplasmic reticulum mitochondria-associated membrane (MAMs) that connect the endoplasmic reticulum and the mitochondria (PubMed:22045338). {ECO:0000250|UniProtKB:P27824, ECO:0000269|PubMed:22045338}.
Interaction partners:
- Protein disulfide-isomerase.
- Endoplasmin
- Calreticulin
- Heat shock protein family A
- Early endosome antigen 1.
- Epstein-Barr virus induced 3.
- Tetraspanin.
- Calreticulin.
- Thioredoxin domain-containing protein.
- SEC31 homolog A, COPII coat complex component.
Sequence:
MEGKWLLCMLLVLGTTIVQAHEGHDDDMIDIEDDLDDVIEEVEDSKSKPDTSAPTSPKVTYKAPVPTGEVYFADSFDRGTLSGWILSKAKKDDTDDEIAKYDGKWEVDEMKETKLPGDKGLVLMSRAKHHAISAKLNKPFLFDTKPLIVQYEVNFQNGIECGGAYVKLLSKTPELNLDQFHDKTPYTIMFGPDKCGEDYKLHFIFRHKNPKTGVYEEKHAKRPDADLKTYFTDKKTHLYTLILNPDNSFEILVDQSIVNSGNLLNDMTPPVNPSREIEDPEDQKPEDWDERPKIPDPDAVKPDDWNEDAPAKIPDEEATKPDGWLDDEPEYVPDPDAEKPEDWDEDMDGEWEAPQIANPKCESAPGCGVWQRPMIDNPNYKGKWKPPMIDNPNYQGIWKPRKIPNPDFFEDLEPFKMTPFSAIGLELWSMTSDIFFDNFIVCGDRRVVDDWANDGWGLKKAADGAAEPGVVGQMIEAAEERPWLWVVYVLTVALPVFLVILFCCSGKKQSSPVEYKKTDAPQPDVKEEEEEKEEEKDKGDEEEEGEEKLEEKQKSDAEEDGGTASQEEDDRKPKAEEDEILNRSPRNRKPRRE
Protein: 4-hydroxyproline 2-epimerase (4Hyp 2-epimerase) (4HypE) (EC 5.1.1.8) (A1BBM5)
Organism: Paracoccus denitrificans (strain Pd 1222)
Function: Catalyzes the epimerization of trans-4-hydroxy-L-proline (t4LHyp) to cis-4-hydroxy-D-proline (c4DHyp). Is likely involved in a degradation pathway that converts t4LHyp to alpha-ketoglutarate, which would allow P.denitrificans to grow on t4LHyp as a sole carbon source. Also seems to be involved in an alternative catabolic pathway that degrades trans-4-hydroxy-L-proline betaine (tHyp-B) to alpha-ketoglutarate; this pathway would permit the utilization of tHyp-B as a sole carbon and nitrogen source.
Interaction partners:
Sequence:
MTQYIFPCIDGHTCGNPVRLVAGGAPRLEGATMLEKRAHFLREFDWIRTGLMFEPRGHDMMSGAILYPPTRGDCDVAVLYIETSGCLPMCGHGTIGTITMGIENGLIVPRTPGRLSIETPAGKVDIEYRQEGRHVEEVRLTNVPGFLYAEGLTAEVEGLGEIVVDVAYGGNFYAIVEPQKNFRDMADHTAGELIGWSLTLRAALNQKYEFTHPEHPQINGLSHIQWTGAPTVPGAHARNAVFYGDKAIDRSPCGTGTSARMAQLAARGRLGVGDEFWHESIIGSIFKGRIEAAATVAGRDAIIPSIAGWARQTGLNTIFIDAERDPFAHGFVVK
Protein: Transcription factor SOX-2 (P48431)
Organism: Homo sapiens (Human)
Function: Transcription factor that forms a trimeric complex with OCT4 on DNA and controls the expression of a number of genes involved in embryonic development such as YES1, FGF4, UTF1 and ZFP206 (By similarity). Binds to the proximal enhancer region of NANOG (By similarity). Critical for early embryogenesis and for embryonic stem cell pluripotency. Downstream SRRT target that mediates the promotion of neural stem cell self-renewal (By similarity). Keeps neural cells undifferentiated by counteracting the activity of proneural proteins and suppresses neuronal differentiation (By similarity). May function as a switch in neuronal development (By similarity).
Subcellular location: Nucleus speckle {ECO:0000250|UniProtKB:Q05066}. Cytoplasm {ECO:0000250|UniProtKB:Q05738}. Nucleus {ECO:0000250|UniProtKB:Q05738}. Note=Acetylation contributes to its nuclear localization and deacetylation by HDAC3 induces a cytoplasmic delocalization (By similarity). Colocalizes in the nucleus with ZNF208 isoform KRAB-O and tyrosine hydroxylase (TH) (By similarity). Colocalizes with SOX6 in speckles. Colocalizes with CAML in the nucleus (By similarity). Nuclear import is facilitated by XPO4, a protein that usually acts as a nuclear export signal receptor (By similarity). {ECO:0000250|UniProtKB:Q05066, ECO:0000250|UniProtKB:Q05738}.
Interaction partners:
- POU domain, class 5, transcription factor 1
- Homeobox protein NANOG
- Krueppel-like factor 4
- Catenin beta-1
- Sal-like protein 4
- Protein lin-28 homolog A
- Paired box protein Pax-6
- POU domain, class 2, transcription factor 1
- Histone deacetylase 1
- PR domain zinc finger protein 14
Sequence:
MYNMMETELKPPGPQQTSGGGGGNSTAAAAGGNQKNSPDRVKRPMNAFMVWSRGQRRKMAQENPKMHNSEISKRLGAEWKLLSETEKRPFIDEAKRLRALHMKEHPDYKYRPRRKTKTLMKKDKYTLPGGLLAPGGNSMASGVGVGAGLGAGVNQRMDSYAHMNGWSNGSYSMMQDQLGYPQHPGLNAHGAAQMQPMHRYDVSALQYNSMTSSQTYMNGSPTYSMSYSQQGTPGMALGSMGSVVKSEASSSPPVVTSSSHSRAPCQAGDLRDMISMYLPGAEVPEPAAPSRLHMSQHYQSGPVPGTAINGTLPLSHM
Protein: Alpha box domain-containing protein (G5EAT5)
Organism: Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Subcellular location: Nucleus {ECO:0000256|RuleBase:RU003516}.
Interaction partners:
- MAT2 proteinMating type HMG-box protein
Sequence:
MENALSPLQRAFNAFLLSMPPQQLDDLVKHIQDVKAQEQKPPVFRNEIPAIRANTTQDAHHTFPTFPSSKHRPASSRGRRVHDGKRRPLNSFIAFRSFYSAIFPDITQKSKSGILRFLWQNDPFKAKWTILAKAYSIIRDKHDDEVSLESFLTLNAELIGVTQPDRYLDAMGWELTLNDQQQYTMARVKSPVATEAQLSTHFSVDDLIKHCYATGYVTEDKRKKEIRGHNAPVMTFATQPALVIHKNNSLQISGNHTVVSTNGSESVTKETPAFEPTEATELPYPSDIVSPVTGDTSFESTDATRIYQRPQSRTSLAENYLDMANMQFHTWDDQTALLPYNTGPLMQESFDALDFKPFLNI
Protein: EG:22E5.12 protein (FI16619p1) (Uncharacterized protein, isoform A) (Uncharacterized protein, isoform B) (Q9XZS4)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MGRNNVICTICSERFRTSDNIQAGSCGHAFHEDCLDHWRKQSRTCPICRSQDAAYFQLYLDFEEFPESASAQGGSWGGHNRSQGHSSSSSSCSSNNNNSNDNSSSDDYIGIMREYENLLYETGVYREEIEYLNQRIGALTVLNAELSKLHECSDSDVD
Protein: TRPL translocation defect 14, isoform C (A8DYI2)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MATLLSNGQQSVMASTSNGQEQQRHQDEPEQQQQVEIRKSSSPKPGAMPSLKLNRMGSVSPKDKRVYKIVLTGGPCGGKTTGQSRLCTFFENLGWKVFRVPETATVLLSGGVKFSDLTEKEDPPTPTTFVYKDLPFAAPEHSLIDLTASCPRCLAKAASRPNGSEAYKFQENLIRTMVQIENTYFELGNSSNRNCLIICDRGVMDASAYISKDKWEKMMAGNNWNPVEMRDNRYNQILHLVSAANGAEDFYSTEDHACRSEGVDLARELDYKSAAAWVGHPYFDVIDNSTNFETKMNRMIESVCQKLGIDIGDRLQATSRKLKYLVALLPPDSEFPPFQDFDVVHHYLQSAGPKVQARLRKRGQKNHWSYIHTQRRPNVHGQARIEVKTQLTHRDYMNLLAQRDDAHFTIYKKRRCFLINNQYFQLDIYKEPGHPRCKGLVLLETYSSLTGDALKNCMPKFLNIVKEVTGDPDYSMFNLSLKEDWSTTKKFCRSATHVKGAANGVSSTPLLLNGQ
Protein: Twenty-four, isoform B (Twenty-four, isoform C) (Twenty-four, isoform I) (Twenty-four, isoform J) (Twenty-four, isoform N) (Q9W4M7)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Ataxin-2 homolog
- LSM12 homolog A
- Polyadenylate-binding protein
- Protein timeless
- LSM12 homolog B
- RE28271p
- GH27708p
Sequence:
MNNEQTPSSSDTPADRVASGGAAAKLPTIIPDTPIVSIAAGTMSESTTTTTVTKTTPTPFPQEQLMTMMSDHVAKADAQLDEACRNQGAKDEDSQGAAPVAANHVATSGSSSRGNDPKKSSSPSNSHSSGNHAATADAAKGSAAEAAAGDTSFSQVFAMLKDSPSAELSRPNRRVLQYGATAKGKTQDDQNVGKRQKKKKTKYDTWEDSDFNDLDDASLKKLLEEAYWYRNPGDRKNKSERFLQMLKKAEYDEEISYRAIKSCLTINPSALTSSAATGSSGGSSSSAGHNSSYNSTNHRSTDPGQRHKQGGSLQDLVEAAHRSELATTSAAAAAAATAAATQRFNCDYQLSGRSNRRQQQQQQQHNQNATSSASASKKIKNLNVSGRQREGGSLPSSVNFEPASSAMEAKQNKQQAQPSTEAAGGSFSGSVGNKHHHRSSTGSCSSLITQSRDTEANNQFDLDMDDATGVGASAVVGASGDQDDNMLEQLDPQNPSMKFLIDALNDTPLEARYTGAGKKFLIDDRLHFSVLELSARRKLQQQAQYLAALTGQFGLGLEEEKRKVEAGYVSLNDNYTACSSVYGGGAGSPAAVEGSKPSTSSSAVSGGSNCGASSDALSSDLRPAKIGRMVPAAAAVAAAPMGGKTTTRQLDENGNALGDGFGGSAASGSSGASGASAAASSSNGNGNANQFTALITPTVGSSVPTSTVAHRQNSVSTLLSTGTNTTTTAMAAAAVAASYSQLQQAPVGGAAGTVSGIGIGMQQPTKQKTKKKSQQERNTTTVDVESVAGYRGNDPVEQLVKYIENDVNGGGNSAAGQRKKERKKQNKLKKSNSLEELRTCSKMEVDDLKRQSATTEMMRHKKGTNNASSGGSSSTASGSSNSGKHNSASVADINKNCNKEQQQQSTPTVQVRNSNNPGTQQRKGERRSWGTEELQYLGDHQEISAAWSELETVGQKELPLALPALARMSELDALNTVLSETAEFHVVTKKKKPKKQRAVTMDDAAVAAAAVTGGNLQRMQQITKSASSNIMSQRMHYYTPYNSNNGGGSVNYKQQQQQSQQYQEHYQAPQGQHHHHHHHHHHHHHHHSGSAVSNQVDSSRRKSTSSMPPSEKSDSSDLDSVHSLPIQTGKKKSLGGGNNKQRGAPSASQRQAKQNNNAAAPISYADIARNKQEALNNATASDTELELGDKMQIKSGGKSKSRPDFPELPGAVTAVAASGGAANQATVVSSQNTPPSSSSSISYSQSLNATPPSSSSDAESTNSPELLAQVQIPAYSMITPTLTASMISSVSSSVASTSSTSCSPPALQKSKSVEHDTSYSCNSSNLDQQYPALEKTVKRHSTNNVSVAVAASTSASASSSLYNFAAAAKQQLTENTHSAVSPPAAVTTTSTAVAASAPAPTTVTVPAAVTVPCYSSSSTHGSTQTSTSTASSAIAALPSGKAKAKPKELSPSSSCSKKPTKPSQDVPSISLSISTTPRATTSTSTTTTQKTTAATQTEGAKKLIGGIHKLPSSSCIAKGAGAVLEATAGRRAVIILNDDREAGRSNNEFIFGDFNEDELKLFDDNLDDEEEGQHKQSSNKKQQTEGESDVTQDDTEDVDQDLDKELECLGRRPEKKQERQQDISASSDQHLNDSGAASDAVNSSASLDMLSISAEAAQSSPNAGATATSSSVASPINSSTPSGASSASASTSTSSSSVSISSSSGGNGAACLASVSGMLGGVANQSGDSGIYAAANTSIKEHVNTFLSKASSSEETLPSPNSISMQQLETCNDIEAAIIAAARAAAAARSTSCSRSNSQEQDALQPQVKTKATPNPEAKMVLPVFVTYNNNNNDDDDDEEDDESLQELSFMADLKADAATEDIAMQPPPPSCPAMMTNTELIVDYIAKTWNAIANSKYVTYYNEQEQEQET
Protein: Zinc finger protein ZPR1 (Zinc finger protein 259) (O75312)
Organism: Homo sapiens (Human)
Function: Acts as a signaling molecule that communicates proliferative growth signals from the cytoplasm to the nucleus. It is involved in the positive regulation of cell cycle progression. Plays a role for the localization and accumulation of the survival motor neuron protein SMN1 in sub-nuclear bodies, including gems and Cajal bodies. Induces neuron differentiation and stimulates axonal growth and formation of growth cone in spinal cord motor neurons. Plays a role in the splicing of cellular pre-mRNAs. May be involved in H(2)O(2)-induced neuronal cell death.
Subcellular location: Nucleus. Nucleus, nucleolus. Nucleus, gem. Nucleus, Cajal body. Cytoplasm, perinuclear region. Cytoplasm. Cell projection, axon {ECO:0000250}. Cell projection, growth cone {ECO:0000250}. Note=Colocalized with SMN1 in Gemini of coiled bodies (gems), Cajal bodies, axon and growth cones of neurons (By similarity). Localized predominantly in the cytoplasm in serum-starved cells growth arrested in G0 of the mitotic cell cycle. Localized both in the nucleus and cytoplasm at the G1 phase of the mitotic cell cycle. Accumulates in the subnuclear bodies during progression into the S phase of the mitotic cell cycle. Diffusely localized throughout the cell during mitosis. Colocalized with NPAT and SMN1 in nuclear bodies including gems (Gemini of coiled bodies) and Cajal bodies in a cell cycle-dependent manner. Translocates together with EEF1A1 from the cytoplasm to the nucleolus after treatment with mitogens. Colocalized with EGFR in the cytoplasm of quiescent cells. Translocates from the cytoplasm to the nucleus in a epidermal growth factor (EGF)-dependent manner. {ECO:0000250}.
Interaction partners:
- Epidermal growth factor receptor
- BUD13 homolog
- Elongation factor 1-alpha 1
- Apolipoprotein A-V
- Zinc finger FYVE domain-containing protein 1
- Zinc finger protein 91
- Zinc finger protein 37 homolog
- Zinc finger protein ZIC 4
- E3 ubiquitin-protein ligase RNF103
- DnaJ homolog subfamily C member 2
Sequence:
MAASGAVEPGPPGAAVAPSPAPAPPPAPDHLFRPISAEDEEQQPTEIESLCMNCYCNGMTRLLLTKIPFFREIIVSSFSCEHCGWNNTEIQSAGRIQDQGVRYTLSVRALEDMNREVVKTDSAATRIPELDFEIPAFSQKGALTTVEGLITRAISGLEQDQPARRANKDATAERIDEFIVKLKELKQVASPFTLIIDDPSGNSFVENPHAPQKDDALVITHYNRTRQQEEMLGLQEEAPAEKPEEEDLRNEVLQFSTNCPECNAPAQTNMKLVQIPHFKEVIIMATNCENCGHRTNEVKSGGAVEPLGTRITLHITDASDMTRDLLKSETCSVEIPELEFELGMAVLGGKFTTLEGLLKDIRELVTKNPFTLGDSSNPGQTERLQEFSQKMDQIIEGNMKAHFIMDDPAGNSYLQNVYAPEDDPEMKVERYKRTFDQNEELGLNDMKTEGYEAGLAPQR
Protein: Lysozyme E (EC 3.2.1.17) (1,4-beta-N-acetylmuramidase E) (P37159)
Organism: Drosophila melanogaster (Fruit fly)
Function: Unlikely to play an active role in the humoral immune defense. May have a function in the digestion of bacteria in the food.
Interaction partners:
- Lysozyme S
- Lysozyme P
- Venom allergen-1
- trypsin
- Jonah 25Bi
- LP07116p
Sequence:
MKAFIVLVALAMAAPALGRTLDRCSLAREMSNLGVPRDQLARWACIAEHESSYRTGVVGPENYNGSNDYGIFQINNYYWCAPPSGRFSYNECGLSCNALLTDDITHSVRCAQKVLSQQGWSAWSTWHYCSGWLPSIDGCF
Protein: Succinate--CoA ligase [ADP/GDP-forming] subunit alpha, mitochondrial (EC 6.2.1.4) (EC 6.2.1.5) (Succinyl-CoA synthetase subunit alpha) (SCS-alpha) (P53597)
Organism: Homo sapiens (Human)
Function: Succinyl-CoA synthetase functions in the citric acid cycle (TCA), coupling the hydrolysis of succinyl-CoA to the synthesis of either ATP or GTP and thus represents the only step of substrate-level phosphorylation in the TCA. The alpha subunit of the enzyme binds the substrates coenzyme A and phosphate, while succinate binding and specificity for either ATP or GTP is provided by different beta subunits.
Subcellular location: Mitochondrion {ECO:0000255|HAMAP-Rule:MF_03222}.
Interaction partners:
- Succinate dehydrogenase iron-sulfur subunit, mitochondrial
- Succinate dehydrogenase flavoprotein subunit, mitochondrial
- Succinate dehydrogenase cytochrome b560 subunit, mitochondrial
- Succinate--CoA ligase [GDP-forming] subunit beta, mitochondrial
- Succinate--CoA ligase subunit beta, mitochondrial
- 2-oxoglutarate dehydrogenase complex component E1
- Dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex, mitochondrial
- ATP-citrate synthase
- Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex, mitochondrial
- Succinate dehydrogenase cytochrome b small subunit, mitochondrial
Sequence:
MTATLAAAADIATMVSGSSGLAAARLLSRSFLLPQNGIRHCSYTASRQHLYVDKNTKIICQGFTGKQGTFHSQQALEYGTKLVGGTTPGKGGQTHLGLPVFNTVKEAKEQTGATASVIYVPPPFAAAAINEAIEAEIPLVVCITEGIPQQDMVRVKHKLLRQEKTRLIGPNCPGVINPGECKIGIMPGHIHKKGRIGIVSRSGTLTYEAVHQTTQVGLGQSLCVGIGGDPFNGTDFIDCLEIFLNDSATEGIILIGEIGGNAEENAAEFLKQHNSGPNSKPVVSFIAGLTAPPGRRMGHAGAIIAGGKGGAKEKISALQSAGVVVSMSPAQLGTTIYKEFEKRKML
Protein: Delta-like protein 4 (Drosophila Delta homolog 4) (Delta4) (Q9NR61)
Organism: Homo sapiens (Human)
Function: Involved in the Notch signaling pathway as Notch ligand. Activates NOTCH1 and NOTCH4. Involved in angiogenesis; negatively regulates endothelial cell proliferation and migration and angiogenic sprouting. Essential for retinal progenitor proliferation. Required for suppressing rod fates in late retinal progenitors as well as for proper generation of other retinal cell types (By similarity). During spinal cord neurogenesis, inhibits V2a interneuron fate.
Subcellular location: Cell membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}.
Interaction partners:
- Neurogenic locus notch homolog protein 1
- Neurogenic locus notch homolog protein 2
- Neurogenic locus notch homolog protein 4
- Neurogenic locus notch homolog protein 3
- Delta-like protein 1
- Delta-like protein 3
- Recombining binding protein suppressor of hairless
- Ephrin-B2
- Vascular endothelial growth factor receptor 3
- Vascular endothelial growth factor receptor 2
Sequence:
MAAASRSASGWALLLLVALWQQRAAGSGVFQLQLQEFINERGVLASGRPCEPGCRTFFRVCLKHFQAVVSPGPCTFGTVSTPVLGTNSFAVRDDSSGGGRNPLQLPFNFTWPGTFSLIIEAWHAPGDDLRPEALPPDALISKIAIQGSLAVGQNWLLDEQTSTLTRLRYSYRVICSDNYYGDNCSRLCKKRNDHFGHYVCQPDGNLSCLPGWTGEYCQQPICLSGCHEQNGYCSKPAECLCRPGWQGRLCNECIPHNGCRHGTCSTPWQCTCDEGWGGLFCDQDLNYCTHHSPCKNGATCSNSGQRSYTCTCRPGYTGVDCELELSECDSNPCRNGGSCKDQEDGYHCLCPPGYYGLHCEHSTLSCADSPCFNGGSCRERNQGANYACECPPNFTGSNCEKKVDRCTSNPCANGGQCLNRGPSRMCRCRPGFTGTYCELHVSDCARNPCAHGGTCHDLENGLMCTCPAGFSGRRCEVRTSIDACASSPCFNRATCYTDLSTDTFVCNCPYGFVGSRCEFPVGLPPSFPWVAVSLGVGLAVLLVLLGMVAVAVRQLRLRRPDDGSREAMNNLSDFQKDNLIPAAQLKNTNQKKELEVDCGLDKSNCGKQQNHTLDYNLAPGPLGRGTMPGKFPHSDKSLGEKAPLRLHSEKPECRISAICSPRDSMYQSVCLISEERNECVIATEV
Protein: FI18055p1 (Secreted decoy of InR, isoform A) (Secreted decoy of InR, isoform B) (Q9VFE2)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cell envelope {ECO:0000256|ARBA:ARBA00004196}.
Interaction partners:
- Insulin-like peptide 1
Sequence:
MGHLHPVPNPLPIPISIAVPLILLFLGASSPVLASSDDQTACGSLEINKIADLRKLQNCTHVVGHVRLAYVDLTDVSGNYSLDSLASNVTEISDYLMVYRCTGLISLQSIFPRLRIIRGQELLFDQYSLVVYENRNLRELGLVELLRIQSGFIRVESNPLLCFVETVDWIYLMGNATRQHFSLKHNRPQSQCPLCGSLSADFEFIRNSSERCWNVNTTQLRPQPPRLKDCPIACGLNGCDSAGKCCDHNCVTGCYSQNCSLCANYQGRMGCVNQCVASYELNKRRCIGHRECRELGRIPLIRGYQCVKKCPGNQKEILVAKGIIHCQVECNGDFHVKSAADLEVLQDCVTINGSLTIELTNIKEKIVDALENALASVKEITGYLKVIHSAQLMSLTFLQNLDAIRGDKLVENKYALYVVNNYHLEHIWPPNHLVIIQRGTLFFHLNPRLCYEKIHQLQGSLKSGENISVADVSPNSNGERVICGDAVRSLNPKVEDLNSTAVRIILDYMDWEGMETLIGYSYHYKEAPVQNVTMYDGRHGCGHDNWLMDVVPNQSRRHVISGLKPYTQYAYFVKTLTRTEYHIQIDAYSKIGYFQTLPDRPSPVLRIYGSSEISSQILLHWWPPRRPNGVIKNYFVTAEKYNATKEAKDKNYVNVELENAKDIDCECAGVLPYYSGPQPDDEDYYNKEQITYEDALPNLIYVSRNHDYRRKEFEKVINYEHLLSIKKDEEPTRPPTTTPAPTNATLAKERLAAINYENYRLNSEKKQRDLQDLDQHKYTIRHALPKCQNSHASVVQQVEEKCVAEEPLSGYELPGTQHFYCLSQLEPETHYRITIRACVEGVVNGCSTPAEAVIKTASIQLERFIKGV
Protein: Neutrophil defensin 3 (Defensin, alpha 3) (HNP-3) (HP-3) (HP3) [Cleaved into: HP 3-56; Neutrophil defensin 2 (HNP-2) (HP-2) (HP2)] (P59666)
Organism: Homo sapiens (Human)
Function: Effector molecule of the innate immune system that acts via antibiotic-like properties against a broad array of infectious agents including bacteria, fungi, and viruses. Possesses the ability to neutralize bacterial toxins such as B. anthracis lethal factor, Clostridium difficile cytotoxin B as well as leukocidin produced by Staphylococcus aureus. Blocks also herpes simplex virus infection by interacting with envelope glycoprotein B and thus preventing its binding to heparan sulfate, the receptor for attachment.
Subcellular location: Secreted {ECO:0000269|PubMed:29282039}.
Interaction partners:
- Neutrophil defensin 1
- Defensin alpha 4
- Beta-defensin 1
- Defensin beta 4A
- Beta-defensin 103
- T-cell surface glycoprotein CD4
- Beta-defensin 104
- Beta-defensin 107
Sequence:
MRTLAILAAILLVALQAQAEPLQARADEVAAAPEQIAADIPEVVVSLAWDESLAPKHPGSRKNMDCYCRIPACIAGERRYGTCIYQGRLWAFCC
Protein: Bromodomain PHD finger transcription factor (A0A140LHY5)
Organism: Mus musculus (Mouse)
Interaction partners:
Sequence:
EELKRDLKMKREREMAQAVQANAASVPTPSVPAPVPAPAPAAPPAPPRSPPPSTHSLPPAGHPTAPLPVTSQKRKREEEKDSKSKKKKMISTTSKEAKKDTRLYCICKTPYDESKFYIGCDLCTNWYHGECVGITEKEAKKMDVYICNDCKRAQEGSSEELYCICRTPYDESQFYIGCDRCQNWYHGRCVGILQSEADLIDEYVCPQCQSTEDAMTVLTPLTEKDYEGLKRVLRSLQAHKMAWPFLEPVDPNDAPDYYGVIKEPMDLATMEERIQKRYYEKLTEFVADMTKIFDNCRYYNPRDTPFYQCAEVLESFFVQKLKGFKASRL
Protein: Para-Rep C1 (Rep1) (EC 2.7.7.-) (EC 3.1.21.-) (EC 3.6.1.-) (ATP-dependent helicase C1) (Replication-associated protein of non-essential DNA C1) (Q66862)
Organism: Faba bean necrotic yellows C1 alphasatellite (FBNYC1A)
Function: Initiates and terminates the replication only of its own subviral DNA molecule. The closed circular ssDNA genome is first converted to a superhelical dsDNA. Rep binds a specific hairpin at the genome origin of replication. Introduces an endonucleolytic nick within the intergenic region of the genome, thereby initiating the rolling circle replication (RCR). Following cleavage, binds covalently to the 5'-phosphate of DNA as a tyrosyl ester. The cleavage gives rise to a free 3'-OH that serves as a primer for the cellular DNA polymerase. The polymerase synthesizes the (+) strand DNA by rolling circle mechanism. After one round of replication, a Rep-catalyzed nucleotidyl transfer reaction releases a circular single-stranded virus genome, thereby terminating the replication. Displays origin-specific DNA cleavage, nucleotidyl transferase, ATPase and helicase activities.
Subcellular location: Host nucleus {ECO:0000305}.
Interaction partners:
Sequence:
MACSNWVFTRNFQGALPLLSFDERVQYAVWQHERGTHDHIQGVIQLKKKARFSTVKEIIGGNPHVEKMKGTIEEASAYVQKEETRVAGPWSYGDLLKRGSHRRKTMERYLEDPEEMQLKDPDTALRCNAKRLKEDFMKEKTKLQLRPWQKELHDLILTEPDDRTIIWVYGPDGGEGKSMFAKELIKYGWFYTAGGKTQDILYMYAQDPERNIAFDVPRCSSEMMNYQAMEMMKNRCFASTKYRSVDLCCNKNVHLVVFANVAYDPTKISEDRIVIINC
Protein: Thioredoxin domain-containing protein 12 (EC 1.8.4.2) (Q498E0)
Organism: Rattus norvegicus (Rat)
Function: Protein-disulfide reductase of the endoplasmic reticulum that promotes disulfide bond formation in client proteins through its thiol-disulfide oxidase activity.
Subcellular location: Endoplasmic reticulum lumen {ECO:0000255|PROSITE-ProRule:PRU10138, ECO:0000269|PubMed:12930873}.
Interaction partners:
- Glutathione hydrolase 6
- Glutathione hydrolase 7
- Glutathione hydrolase 5 proenzyme
- Glutathione synthetase
- Putative glutathione-specific gamma-glutamylcyclotransferase 2
- Glutathione-specific gamma-glutamylcyclotransferase 1
- Glutathione S-transferase A6
- Glutathione S-transferase alpha-3
- Glutathione S-transferase Mu 4
- Glutathione S-transferase theta-2
Sequence:
MSLRFGATCLLSFSFLLLITSSDGRTGLGKGFGDHIHWRTLEDGKKEAAASGLPLMVIIHKSWCGACKALKPKFAESTEISELSHNFVMVNLEDEEEPRDEDFSPDGGYIPRILFLDPSGKVRPEIINESGNPSYKYFYVSAEQVVQGMKEAQVRLTGDAFREKHFQDEL