wanglab/gogpt-training-data huggingface dataset:
Protein: Vacuolar protein sorting-associated protein 24 homolog 1 (AtVPS24-1) (Charged multivesicular body protein 3 homolog 1) (ESCRT-III complex subunit VPS24 homolog 1) (Q9FFB3)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Component of the ESCRT-III complex, which is required for multivesicular bodies (MVBs) formation and sorting of endosomal cargo proteins into MVBs. The ESCRT-III complex is probably involved in the concentration of MVB cargo (By similarity).
Subcellular location: Endosome {ECO:0000250}.
Interaction partners:
- Vacuolar protein sorting-associated protein 32 homolog 1
- Vacuolar protein sorting-associated protein 32 homolog 2
- Vacuolar protein sorting-associated protein 28 homolog 1
- Vacuolar protein sorting-associated protein 36
- Protein ELC-like
- Vacuolar protein sorting-associated protein 2 homolog 1
- AMSH-like ubiquitin thioesterase 3
- Vacuolar protein sorting-associated protein 28 homolog 2
- ESCRT-related protein CHMP1A
- ESCRT-related protein CHMP1B
Sequence:
MERVMNIIKPKPDPKQLLRDWQRKLRQECRNIERQIRDIQKEERNVQKAIKEAAKRNDMVSAKALAKEIVSSRRTVNRLYENKAQMNSISMHLGESVAIARTVGHLSKSAEVMKLVNNLMKAPQMAATMQEFSKEMTKAGVIEEFVNEAIDNALDSEDMEEEIDEEVDKVLTAIAGETAAELPVAVRKERIKVPAQKASTSREEEAVAEGVDDEEELEEIRARLAKVRS
Protein: Centrin-4 (Centrin4) (Q8K4K1)
Organism: Mus musculus (Mouse)
Function: Ca(2+)-binding protein that may be involved in basal body assembly or in a subsequent step of ciliogenesis.
Subcellular location: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole {ECO:0000269|PubMed:12802058, ECO:0000269|PubMed:15347651, ECO:0000269|PubMed:18269917}. Cytoplasm {ECO:0000269|PubMed:12802058, ECO:0000269|PubMed:15347651, ECO:0000269|PubMed:18269917}. Note=Accumulates at procentrioles during their elongation. Isoform 3 is not observed in the centriole.
Interaction partners:
- TBCC domain-containing protein 1
- Protein SFI1 homolog
Sequence:
MASSQRITLDQWKKKAAKVELNDTQKQEIKEAFDLFDIDGSGTIDLKELKIAMRALGFEPKKEEVKQLIAEIDKEGTGTICFEDFFAIMSVKMSEKDEKEEILKAFKLFDDDATGSISLNNIKRVAKELGENLTEDELQEMLDEADRDGDGEINEEEFLKMMKKTSLY
Protein: Centrosomal protein POC5 (Protein of centriole 5) (D6RDG4)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole {ECO:0000256|ARBA:ARBA00004114}.
Interaction partners:
Sequence:
MSSDEEKYSLPVVQNDSSRGSSVSSNLQEEYEELLHYAIVTPNIEPCASQSSHPKGELVPDVRISTIHDILHSQESSPVLSPRKPSHPVMDFFSSHLLADSSSPATNSSHTDAHEILVSDFLVSDENLQKMENVLDLWSSGLKTNIISELSKWRLNFIDWHRMEMRKEKEKHAAHLKQLCNQINELKELQKTFEISIGRKDEVISSLSHAIGKQKEKIELMRTFFHWRIGHVRARQDVYEGKLADQYYQRTLLKKVWKVWRSVVQKQWKDVVERACQARAEEVCIQISNDYEAKVAMLSGALENAKAEIQRMQHEKEHFEDSMKKAFMRGVCALNLEAMTIFQNRNDAGIDSTNNKKEEYGPGVQGKEHSAHLDPSAPPMPLPVTSPLLPSPPAAVGGASATAVPSAASMTSTRAASASSVHVPVSALGAGSAATAASEEMYVPRVVTSAQQKAGRTITARITGRCDFASKNRISSSLAIMGVSPPMSSVVVEKHHPVTVQTIPQATAAKYPRTIHPESSTSASRSLGTRSAHTQSLTSVHSIKVVD
Protein: Heat shock 70 kDa protein 4L (Heat shock 70-related protein APG-1) (Osmotic stress protein 94) (P48722)
Organism: Mus musculus (Mouse)
Function: Possesses chaperone activity in vitro where it inhibits aggregation of citrate synthase.
Subcellular location: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}. Note=May translocate to the nucleus after heat shock. {ECO:0000250}.
Interaction partners:
- Hsp70-binding protein 1
- BAG family molecular chaperone regulator 2
- BAG family molecular chaperone regulator 1
- Heat shock protein 105 kDa
- Stress-induced-phosphoprotein 1
- DnaJ homolog subfamily B member 1
- Heat shock protein HSP 90-alpha
- Heat shock 70 kDa protein 12A
- DnaJ homolog subfamily B member 4
- Endoplasmic reticulum chaperone BiP
Sequence:
MSVVGIDLGFLNCYIAVARSGGIETIANEYSDRCTPACISLGSRTRAIGNAAKSQIVTNVRNTIHGFKKLHGRSFDDPIVQTERIRLPYELQKMPNGSTGVKVRYLEEERPFAIEQVTGMLLAKLKETSENALKKPVADCVISIPSFFTDAERRSVMAAAQVAGLNCLRLMNETTAVALAYGIYKQDLPSLDEKPRNVVFIDMGHSAYQVSVCAFNKGKLKVLATTFDPYLGGRNFDEALVDYFCDEFKTKYKINVKENSRALLRLYQECEKLKKLMSANASDLPLNIECFMNDLDVSSKMNRAQFEQLCASLLARVEPPLKSVMDQANLQREDINSIEIVGGATRIPAVKEQVTRFFLKDISTTLNADEAVARGCALQCAILSPAFKVREFSITDLVPYSVTLRWKTSFEEGTGECEVFSKNHPAPFSKVITFHKKEPFELEAFYTNLHEVPYPDPRIGNFTIQNVFPQSDGDSSKVKVKVRINIHGIFSVASASVIEKQNLEGDHNDAAMETEAPKSEGKEDVDKMQVDQEEGGHQKCHAEHTPEEEIDHTGAKAKAPPSDKQDRINQTIKKGKIKSIDLPIQSSLYRQLTQDLLNSYIENEGKMIMQDKLEKERNDAKNAVEEYVYDFRDKLGTVYEKFITPEDMNKLSAMLEDTENWLYEEGEDQPKQVYVDRLQELKKYGQPIQMKYVEHEERPKALNDLGKKIQLVLKVIEAHRNKDERYDHLDPAEMERVEKYISDSMNWLNSKMNAQNKLSLTQDPVVKVSEIVTKSKELDNFCNPIVYKPKPKVEAPEDKAKTGSEHNGPMDGQSGSETSPDPPKGSSQHTDSGEMEVD
Protein: Plakophilin-4 (Armadillo-related protein) (Q68FH0)
Organism: Mus musculus (Mouse)
Function: Plays a role as a regulator of Rho activity during cytokinesis. May play a role in junctional plaques (By similarity).
Subcellular location: Cell junction, desmosome {ECO:0000250}. Cytoplasm, cytoskeleton, spindle {ECO:0000250}. Cytoplasm, cytoskeleton, spindle pole {ECO:0000250}. Midbody {ECO:0000250}. Cell membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Note=Associated with the pericentrosomal region in interphase and with spindle poles during mitosis. In anaphase, during chromosome segregation, is recruited to the central microtubule bundle, focussed at the spindle midzone and ultimately localizes to the midbody at cytokinesis. Constituent of the midbody cytoskeletal matrix. Colocalized with desmoplakin at desmosomal junctional plaques in cultured epithelial cells (By similarity). {ECO:0000250}.
Interaction partners:
- Junction plakoglobin
- Erbin
- Protein ECT2
- Desmoglein-2
- Desmoplakin
- Desmocollin-2
- Leucine-rich repeat-containing protein 7
Sequence:
MPAPEQGSLVEEGQPQTHQEAVSTGPGMEPETTATTILASVKEQELQFQRLTRELEVERQIVASQLERCRLGAESPSIASTSSTEKSFPWRSTDVPNPGVSKPRVSDTIHPNNYLIRTEPEQGTLYSPEQTSLHESEGSLGNSRSSTQMNSYSDSGYQEAGSFHNSQTVNKADSRQHPFTGSTSNHVVRTSRAEGQTLVQPSVANRAMRRVSSVPSRAQSPSYVTSTGVSPSRGSLRTSLGSGFGSPSVTDSRPLNPSAYSSSTLPAQRAASPYSQRPASPTAVRRVGSVTSRQTSNPNGPVPQYQTTTRVGSPLTLTDAQTRVASPSQGQVGSSSPKRSGMTAVPQHLGPSLQRTVHDMDQFGQQQYDIYERMVPPRPDSLTGLRSSYASQHSQLGQELRSAVSPDLHITPIYEGRTYYSPVYRSPNHGTVELQGSQTALYRTGSVGIGNLQRTSSQRSTLTYQRNNYALNTAATYAEPYRPVQYRVQECSYNRLQHTGPADDGATRSPSIDSIQKDPREFAWRDPELPEVIHMLQHQFPSVQANAAAYLQHLCFGDNKVKMEVYRLGGIKHLVDLLDHRVLEVQKNACGALRNLVFGKSTDENKIAMKNVGGIPALLRLLRKSIDAEVRELVTGVLWNLSSCDAVKMTIIRDALSTLTNTVIVPHSGWNNSSFDDDHKIKFQTSLVLRNTTGCLRNLSSAGEEARKQMRSCEGLVDSLLYVIHTCVNTSDYDSKTVENCVCTLRNLSYRLELEVPQARLLGLNELDDLLGKESPSKDSEPSCWGKKKKKKKRTPQEDQWDGVGPIPGLSKSPKGVEMLWHPSVVKPYLTLLAESSNPATLEGSAGSLQNLSAGNWKFAAYIRAAVRKEKGLPILVELLRMDNDRVVSSVATALRNMALDVRNKELIGKYAMRDLVNRLPGGNGPSILSDETVAAICCALHEVTSKNMENAKALADSGGIEKLVNITKGRGDRSSLKVVKAAAQVLNTLWQYRDLRSIYKKDGWNQNHFITPVSTLERDRFKSHPSLSTTNQQMSPIIQSVGSTSSSPALLGIREPRSEYDRTQPPMQYYNSQGDTTHKGLYPGSSKPSPIYISSYSSPAREQNRRLQHQQLYYQDDSTRKTLDAYRLYLQSPRSYEDPYCDDRVHFPASTDYSTQYGLKSTTNYVDFYSTKRPSYRAEQYPGSPDSWV
Protein: Alhambra, isoform F (A8JQU7)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MMMMDTMDTSQSQPMDVAPAVAVAATSGAALVDFTAAMVSMAATAEAESAESNNNHIDMAEYKEHRKNKKKKREKREREGKEHRHHKHRDREHREHRRHRDRDRDKERDREGHHHHPTHHHPNNSQHSTSASSSPSSASTTPSATIEYVGGSASASPSYLGGGATGTGAAVGATTTYPHNLKIRFLLSGQRTELSPPTHQTSATAEVNAPLASSTSASIAVTASATAASAPPATGTTTLGSSISGNAGSTSSGNSSGVSATGGAQSAVGSGGYPKTESSKSSGTASAGSGSGSSSNTSSTKHGSNIKDISSSSNQQASTASSSSAPSLYVSVPLSTANVPGINLPTSSTSSSTTSESHSASSRSSGAQSQHQQQLSNALVGPPMGGSAGAFHGGTTSAGSSSVIQQQSGKSSPALGTLVSGNSGGSIISASGFPLPSGNLTATTTESGNLKISYEKQTTRVQQLQEQEAPPARRSRSRSGESGSSHHHAHAHHHHHHPTHHNSHHQQNPQQQQQLHQQQQQNASSHMHACTNSSSSTSTSTTSSSLSGGTAPATSSSNSKGPSRSGKKRGAAMNKSESTSVATTATPATVAATPAEKQSRHSSPHYSATPTPPPTSTLPPVVSSPVVMLQSLSSSSIDSPPATAAAGATSNSRNTRNNSSNGNHNGEQTSSSSSSSSSSSSGGGGTSGAANVVNLLDSPVNMSASGNYRSSSNSTGNALPAASSNASQAKPLNKKMLRAQQTQLYQQQQQQQQYAPPARSISPTNLSSASASNSASLTHLQQQQQSHQQHEDLEILQFTNTNTTASSNTPTSKPNNRTLDLSTASASSSSPSAVPATTSPLVVLSNQLPLNSVAASSSTGGLKFTYESQTQMDVPMMPVSAIKDSPPSSPGSEIGSAMHSATTAPGSLTGASTAATAQPGNVRKRGRKAKDATIAAAAAAAAAAAALSNSQQDLKDVRILQNGASNTPGNPAGSTPTPPATPASSNAVSSASSIITHTAAHMLGNQINPNSSVAQKLSEQLHMEVQDHSIYTPDSMNSQYAGVPFPGKQRNSTAVPSNATPAQNPLQSMFSGGGMNGNMPIPQSLEQLLERQWEQGSQFLMEQAQHFDIASLLNCLHQLQSENLRLEEHVTSLIARRDHLLAVNARLQIPLSTIASNTKAEAHGK
Protein: Small ribosomal subunit protein uS9 (40S ribosomal protein S16) (Q6FR56)
Organism: Candida glabrata (strain ATCC 2001 / BCRC 20586 / JCM 3761 / NBRC 0622 / NRRL Y-65 / CBS 138) (Yeast) (Nakaseomyces glabratus)
Interaction partners:
- 60S ribosomal protein L28
- Large ribosomal subunit protein eL24
- Candida glabrata strain CBS138 chromosome D complete sequence
- Candida glabrata strain CBS138 chromosome K complete sequence
- Candida glabrata strain CBS138 chromosome J complete sequence
- L15
- Candida glabrata strain CBS138 chromosome M complete sequence
- 40S ribosomal protein S4
- Large ribosomal subunit protein uL30
- L17A
Sequence:
MSTVPSVQTFGKKKSATAVAHVKAGKGLIKVNGSPITLVEPEILRFKVYEPLLLVGLDKFANIDIRVRVTGGGHVSQVYAIRQAIAKGLVAYHQKFVDEQSKNELKKAFTSYDRTLLIADARRPEPKKFGGKGARARFQKSYR
Protein: Mushroom body defect, isoform H (Q8IR55)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
- G protein alpha i subunit subunit alpha 65A)
- LD33695p
- Atypical protein kinase C
- Inscuteable
- Bazooka, isoform B
- FI04457p
- Kinesin heavy chain 73, isoform E
- Chaperone Ric-8
- Aurora kinase
- Cyclin-dependent kinase 1
Sequence:
MDTRSWRKVLLQWIGECHFIESNYITLEQSDLDSFFSVFIQKIQETENVKGKNELQDQPTEQSPLVQEFLAHNYPEFIAQQDDKEVDLPLDCLYVYTLLLHYSCVKKPSLFFHNICNKLPELTQTCIASFFRETVDRLLTREYLSQAIANVAVVYRQGVSTSVSPCLPSSSLSPDPRSDDAPCPSTPSSSSSQPSSSTPQLRNHREQLRLNGCEMPPPSTPKTELLEQRTKELRGIRTQLEVVRYEKALLEEQQMEKDELIKVLNKEKMMAKMELEKLRNVKLTEEHHDNESHHIMPYEFEHMKGCLLKEIGLKESLIAEITDKLHDLRVENSELSEKLNLAGKRLLEYTDRIRFLESRVDDLTRIVSSRDVMISSLESDKQELDKCLKEARDDLHNRIEVLNASSDLLDCSLSPNTTPENLASSVIDKQLREKEHENAELKEKLLNLNNSQRELCQALSSFLQKHNIDHEFPVEWTSSSLLSTISAIESKFVNTLEKSTQMKKECDVQSVCVEKLLEKCKLLSVSLGCQPKELDGFEATIPEAMESGFESSRECETILSCCHMKVVDIASKNNDLELDNERLNDKCAELKSIIDRGDQHLADINLQLIEKEKQIKDVGAEIQELRKRNINLENMLSQIADKEASAASHAQHLKQCGELLRAKYEVCRNELIAKNAAQDELVRMMMVPDGETLNGRVRQLIDLEMMHDEHNKMYAQMLKQLNELSAKHDNMTHSHLDFVKRTEIELETKNAQIMAFDEHNNHFDRFLTRIFTLLRSRNCPKSTTMGSATNFLESMHIEKRFENIEMLIEGQLLSADDLKRELDDLRSKNEELAKQNINGIIKRNKFITSLEVNTEKVKQYITDLEEEAFKRKQKVVQLENTLSKEQSNAKEMAQRLDIAQQEIKDYHVEAIRFINTIRDRLQQDFNGVNTPQQLGTCMTEFLKMYDQMEVRYEESSSLVEKLTESQAKLEMQVAELQVELENKDTNQHSGALIKQLNDTIQNLEKVNAKLSEDNTVSHTVHSKLNESLLKAQKELDLRAKIIENLEASERNLSMKLCELKDLKNKLKSSDEKIAQIKETYEEQIKALQAKCDMEAKKNEHLERNQNQSLTQLKEDALENCVLMSTKLEELQAKLQEGQQLVDSQKLELDMNRKELALVKSAYEAQTKLSDDLQRQKESGQQLVDNLKVELEKERKELAHVNSAIGAQTKLSDDLECQKESGQQLVDNLKVELEKERKELAQVKSVIEAQTKLSDDLQREKESAQQLVDNLKVELDKERKELAQVNSAFEAQTKLSDDLQRQKESAQQLVDNLKVELDKERKELAQVNSAFEAQTKLSDDLQREKESAQQLVDNLKVELDKERKELAQVKSVIEAQTKLSDDLQRQKESAQQLVDNLKVELDKERKELAKVKSVIEAQTKLSDDLQRQKESAQQLEAQTKLSDDLQRQKESAQQLVDNLKVELDKERKELAQVKSVIEAQTKLSDDLQRQKESAQQLVDNLKMELDKERKELAQVKSAIGAQTKLSDDLECQKESVQQLVDNLKVELEKERKELAKVNSAFEAQTKLSDDLKLQKEDAQREVFLVKERLVKEKREFEVKLATLEDIIETLEMRCTQMEEERATAYEQINKLENRCQEKDNVKSSQLQVETFKVECLHHQLKSEMATHNSLVEDLNRKLAEKVSKLDFVQSRLMTEIAEHNQVKDQLAQITDIPKVVELQHRLEAETAEREEAQNKLAVVTGRLDEITRELDNARLEHGAQILRMEETAREVGNKNAELCELIEFYRNRVEALERLLLASNQELEELNSIQSNQAEGVRDLGDTYSAAEGRQTESDQDKERYQKLALDCKILQAKYRDAKDEIKRCEKKIKDQRLEMEGKLEKMKNKMRSLYTAEVTRMKEKQERDAAKSASELEALTAQNAKYEEHTRKLSNQIVRLNEKILEQQKQHAIISTNLRHLQMQPISETKPSSTTLTVSSSSSAPNDDWQPFKRPNVPSSNLAMEDEEGEVFNNTYLTDLKLGRVPADMTAEELIYRNSLQPPHLKSTYAAQYDLGSQDEDLKDGPHSLDDSMSALLSSSSTGTRKKSMGTHYKRPGPPTPSKNGGRLSFGSSEPPREILREFGDHNNTSKTPARFKFLTQRFSVGSSGLPRDEPIPQLPRRKRPNLLTGIHRRRLRHAVDIFCTSTPRKSRSYYDQQRMIGASDADKSEAVETEDEVIEVEPDAVPELEPLEDADQQGTPHLSTAALLALTKGNTRRLTGTTKSKKGRVSLSLHGNIFAKSRPASFVAGKRVQLRRKLRRDRIMGRFDEARHLDQMRLSHSAQAAKSPENNNYSLHNRNEEEHLPSENNVMGKTVVLVGKRRLSPVVSTTFNVEERSETSLLQQQFEHENCVTWAMHGGESVMMEETQNDWYFEQLCKETESTAPFQLQPLDYKPLDEEQVEPKFTQLVAASCSNITTTSCATNMTGASSCTVYSIGSVHMQPLPQINITYVQQPSDLQQRRPTRHRSLMAQCRRFLRHLSLGQRLVMGFALLVMVGLSLHLADKLVLVITGILSGMGLVFLTYSCPGRN
Protein: Synaptosomal-associated protein 23 (SNAP-23) (Syndet) (Vesicle-membrane fusion protein SNAP-23) (O09044)
Organism: Mus musculus (Mouse)
Function: Essential component of the high affinity receptor for the general membrane fusion machinery and an important regulator of transport vesicle docking and fusion.
Subcellular location: Cell membrane; Peripheral membrane protein. Cell membrane {ECO:0000250}; Lipid-anchor {ECO:0000250}. Synapse, synaptosome. Note=Mainly localized to the plasma membrane.
Interaction partners:
- Vesicle-associated membrane protein 2
- Syntaxin-3
- Vesicle-associated membrane protein 7
- Syntaxin-4
- Vesicle-associated membrane protein 3
- Vesicle-associated membrane protein 8
- Syntaxin-11
- Syntaxin-2
- Syntaxin-1A
- Vesicle-trafficking protein SEC22b
Sequence:
MDNLSPEEVQLRAHQVTDESLESTRRILGLAIESQDAGIKTITMLDEQGEQLNRIEEGMDQINKDMREAEKTLTELNKCCGLCICPCNRTKNFESGKNYKATWGDGGDNSPSNVVSKQPSRITNGQPQQTTGAASGGYIKRITNDAREDEMEENLTQVGSILGNLKNMALDMGNEIDAQNQQIQKITEKADTNKNRIDIANTRAKKLIDS
Protein: Phosphoglycerate kinase (EC 2.7.2.3) (P00560)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Subcellular location: Cytoplasm {ECO:0000269|PubMed:11502169}. Mitochondrion {ECO:0000269|PubMed:16823961}.
Interaction partners:
- Fructose-bisphosphate aldolase
- Triosephosphate isomerase
- Glyceraldehyde-3-phosphate dehydrogenase 3
- Glyceraldehyde-3-phosphate dehydrogenase 2
- Glyceraldehyde-3-phosphate dehydrogenase 1
- Phosphoglycerate mutase 1
- Enolase 2
- Glucose-6-phosphate isomerase
- Enolase 1
- Pyruvate kinase 1
Sequence:
MSLSSKLSVQDLDLKDKRVFIRVDFNVPLDGKKITSNQRIVAALPTIKYVLEHHPRYVVLASHLGRPNGERNEKYSLAPVAKELQSLLGKDVTFLNDCVGPEVEAAVKASAPGSVILLENLRYHIEEEGSRKVDGQKVKASKEDVQKFRHELSSLADVYINDAFGTAHRAHSSMVGFDLPQRAAGFLLEKELKYFGKALENPTRPFLAILGGAKVADKIQLIDNLLDKVDSIIIGGGMAFTFKKVLENTEIGDSIFDKAGAEIVPKLMEKAKAKGVEVVLPVDFIIADAFSADANTKTVTDKEGIPAGWQGLDNGPESRKLFAATVAKAKTIVWNGPPGVFEFEKFAAGTKALLDEVVKSSAAGNTVIIGGGDTATVAKKYGVTDKISHVSTGGGASLELLEGKELPGVAFLSEKK
Protein: Uncharacterized protein YnbB (P76091)
Organism: Escherichia coli (strain K12)
Subcellular location: Cell membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
- Uncharacterized protein YnbD
- Inner membrane protein YnbA
- Uncharacterized protein YnbC
- Phosphatidate cytidylyltransferase
- Uncharacterized protein YdbD
- CDP-diacylglycerol--glycerol-3-phosphate 3-phosphatidyltransferase
- 1-acyl-sn-glycerol-3-phosphate acyltransferase
- CDP-diacylglycerol pyrophosphatase
- CDP-diacylglycerol--serine O-phosphatidyltransferase PssA
- Diacylglycerol kinase
Sequence:
MLEKSLATLFALLILATLINRFLLWRLPERKGGEVTLRIRTWWGIVICFSMVISGPRWMTLTFFALISFLALKEYCTLISVHFPRWLYWGIPLNYLLIGFNCFELFLLFIPLAGFLILATGQVLVGDPSGFLHTVSAIFWGWIMTVFALSHAAWLLMLPTTNIQGGALLVLFLLALTESNDIAQYLWGKSCGRRKVVPKVSPGKTLEGLMGGVITIMIASLIIGPLLTPLNTLQALLAGLLIGISGFCGDVVMSAIKRDIGVKDSGKLLPGHGGLLDRIDSLIFTAPVFFYFIRYCCY
Protein: CCN family member 1 (3CH61) (Cellular communication network factor 1) (Cysteine-rich angiogenic inducer 61) (Insulin-like growth factor-binding protein 10) (IBP-10) (IGF-binding protein 10) (IGFBP-10) (Protein CYR61) (P18406)
Organism: Mus musculus (Mouse)
Function: Promotes cell proliferation, chemotaxis, angiogenesis and cell adhesion. Appears to play a role in wound healing by up-regulating, in skin fibroblasts, the expression of a number of genes involved in angiogenesis, inflammation and matrix remodeling including VEGA-A, VEGA-C, MMP1, MMP3, TIMP1, uPA, PAI-1 and integrins alpha-3 and alpha-5 (By similarity). CCN1-mediated gene regulation is dependent on heparin-binding (By similarity). Down-regulates the expression of alpha-1 and alpha-2 subunits of collagen type-1 (By similarity). Promotes cell adhesion and adhesive signaling through integrin alpha-6/beta-1, cell migration through integrin alpha-1/beta-5 and cell proliferation through integrin alpha-v/beta-3 (By similarity).
Subcellular location: Secreted.
Interaction partners:
- Integrin alpha-V
- Ankyrin repeat domain-containing protein 1
- Serine/threonine-protein kinase LATS1
- Transcription factor Jun
- Early growth response protein 1
- Angiomotin-like protein 2
- Transcriptional coactivator YAP1
- Fibronectin
- WW domain-containing transcription regulator protein 1
- Transcriptional enhancer factor TEF-1
Sequence:
MSSSTFRTLAVAVTLLHLTRLALSTCPAACHCPLEAPKCAPGVGLVRDGCGCCKVCAKQLNEDCSKTQPCDHTKGLECNFGASSTALKGICRAQSEGRPCEYNSRIYQNGESFQPNCKHQCTCIDGAVGCIPLCPQELSLPNLGCPNPRLVKVSGQCCEEWVCDEDSIKDSLDDQDDLLGLDASEVELTRNNELIAIGKGSSLKRLPVFGTEPRVLFNPLHAHGQKCIVQTTSWSQCSKSCGTGISTRVTNDNPECRLVKETRICEVRPCGQPVYSSLKKGKKCSKTKKSPEPVRFTYAGCSSVKKYRPKYCGSCVDGRCCTPLQTRTVKMRFRCEDGEMFSKNVMMIQSCKCNYNCPHPNEASFRLYSLFNDIHKFRD
Protein: Leucine-rich repeat and immunoglobulin-like domain containing-NOGO receptor-interacting protein 4 (Leucine-rich repeat neuronal protein 6D) (Q149C3)
Organism: Mus musculus (Mouse)
Subcellular location: Membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}.
Interaction partners:
Sequence:
MDAATAPKQAWLPWSPLLFLLLLPGGSISSCPTVCDCTSQTRAVFCAHRRLDTIPGGLPLDTELLDLSGNRLWGLQRGMLSRLGQLQELDLSYNQLSTLEPGAFHGLQSLLTLRLQGNRLRIVGPGIFSGLTALTLLDLRLNQIVLFLDGAFSELGSLQQLEVGDNHLVFVAPGAFAGLAKLSTITLERCNLSTVPGLALAQLPALVALRLRELDIERLPAGALRGLGQLKELEIHHWPSLEALDPGSLVGLNLSSLAITRCNLSSVPFQALHHLSFLRILDLSQNPISAIPARRLSPLVRLQELRLSGACLTSIAAHAFHGLTAFHLLDVADNALQTLEETAFPSPDKLVTLRLSGNPLTCDCRLLWLLRLRRRLDFGTSPPACAGPQHVQGKSLREFSDILPPGHFTCKPALIRKSGPRWVIAEEGGHAVFSCSGDGDPAPTVSWMRPQGAWLGRVGRVRVLEDGTLEIRSVQLRDRGAYVCVVSNVAGNDSLRTWLEVIQVEPPNGTLSDPNITMPGIPGPFFLDSRGVAMVLAVGFLPFLTSVTLCFGLIALWSKGKGRVKHHMTFDFVAPRPSGDKNSGGNRVTAKLF
Protein: CTD small phosphatase-like protein (CTDSP-like) (EC 3.1.3.16) (Carboxy-terminal domain RNA polymerase II polypeptide A small phosphatase 3) (NIF-like protein) (Nuclear LIM interactor-interacting factor 1) (NLI-interacting factor 1) (Protein YA22) (hYA22) (RBSP3) (Small C-terminal domain phosphatase 3) (SCP3) (Small CTD phosphatase 3) (O15194)
Organism: Homo sapiens (Human)
Function: Recruited by REST to neuronal genes that contain RE-1 elements, leading to neuronal gene silencing in non-neuronal cells (By similarity). Preferentially catalyzes the dephosphorylation of 'Ser-5' within the tandem 7 residue repeats in the C-terminal domain (CTD) of the largest RNA polymerase II subunit POLR2A. Negatively regulates RNA polymerase II transcription, possibly by controlling the transition from initiation/capping to processive transcript elongation.
Subcellular location: Nucleus {ECO:0000250}.
Interaction partners:
- Cell division cycle-associated protein 3
- Carboxy-terminal domain RNA polymerase II polypeptide A small phosphatase 1
- Myelin basic protein
- General transcription factor IIF subunit 1
- RNA polymerase II subunit A C-terminal domain phosphatase
- RE1-silencing transcription factor
Sequence:
MDGPAIITQVTNPKEDEGRLPGAGEKASQCNVSLKKQRSRSILSSFFCCFRDYNVEAPPPSSPSVLPPLVEENGGLQKGDQRQVIPIPSPPAKYLLPEVTVLDYGKKCVVIDLDETLVHSSFKPISNADFIVPVEIDGTIHQVYVLKRPHVDEFLQRMGQLFECVLFTASLAKYADPVADLLDRWGVFRARLFRESCVFHRGNYVKDLSRLGRELSKVIIVDNSPASYIFHPENAVPVQSWFDDMTDTELLDLIPFFEGLSREDDVYSMLHRLCNR
Protein: 3-keto-steroid reductase/17-beta-hydroxysteroid dehydrogenase 7 (17-beta-hydroxysteroid dehydrogenase 7) (17-beta-HSD 7) (3-keto-steroid reductase) (EC 1.1.1.270) (Dihydrotestosterone oxidoreductase) (EC 1.1.1.210) (Estradiol 17-beta-dehydrogenase 7) (EC 1.1.1.62) (Short chain dehydrogenase/reductase family 37C member 1) (P56937)
Organism: Homo sapiens (Human)
Function: Bifunctional enzyme involved in steroid-hormone metabolism and cholesterol biosynthesis. Catalyzes the NADP(H)-dependent reduction of estrogens and androgens and regulates the biological potency of these steroids. Converts estrone (E1) to a more potent estrogen, 17beta-estradiol (E2). Converts dihydrotestosterone (DHT) to its inactive form 5a-androstane-3b,17b-diol. Converts moderately progesterone to 3beta-hydroxypregn-4-ene-20-one, leading to its inactivation. Additionally, participates in the post-squalene cholesterol biosynthesis, as a 3-ketosteroid reductase.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:12829805}; Single-pass membrane protein {ECO:0000255}.
Interaction partners:
- Methylsterol monooxygenase 1
- Lathosterol oxidase
- Sterol-4-alpha-carboxylate 3-dehydrogenase, decarboxylating
- Lanosterol 14-alpha demethylase
- Squalene synthase
- Lanosterol synthase
- 17-beta-hydroxysteroid dehydrogenase type 1
- Dehydrogenase/reductase SDR family member 11
- Ergosterol biosynthetic protein 28 homolog
- Delta
Sequence:
MRKVVLITGASSGIGLALCKRLLAEDDELHLCLACRNMSKAEAVCAALLASHPTAEVTIVQVDVSNLQSVFRASKELKQRFQRLDCIYLNAGIMPNPQLNIKALFFGLFSRKVIHMFSTAEGLLTQGDKITADGLQEVFETNVFGHFILIRELEPLLCHSDNPSQLIWTSSRSARKSNFSLEDFQHSKGKEPYSSSKYATDLLSVALNRNFNQQGLYSNVACPGTALTNLTYGILPPFIWTLLMPAILLLRFFANAFTLTPYNGTEALVWLFHQKPESLNPLIKYLSATTGFGRNYIMTQKMDLDEDTAEKFYQKLLELEKHIRVTIQKTDNQARLSGSCL
Protein: NADH kinase pos5, mitochondrial (EC 2.7.1.86) (Q9UT98)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Phosphorylates both NADH and NAD(+), with a preference for NADH. Anti-oxidant factor and key source of the cellular reductant NADPH (By similarity).
Subcellular location: Mitochondrion {ECO:0000269|PubMed:16823372}.
Interaction partners:
- Aspartate aminotransferase, mitochondrial
- Glutathione S-transferase omega-like 2
- Uncharacterized protein PB1E7.11c
- General alpha-glucoside permease
- Inositol phosphoceramide mannosyltransferase 1
Sequence:
MIRAANGFRISVRNTAVCLAPNFRQLKGFSIINLGSLQYFRYNSVYSKSIRLVNTLENRIVPVYKECASPQSIGGKSNLKQLQWPKPPKNILILKKRMDERVDHCFETLVQHLQQTYPDICIITETDVAKKFSYLNLYTWTEISDLEQKVDAIITVGGDGTILHAASLFARSGMPPILSFSLGTLGFLLPFDFGSFQTAFADFYNSRSFVLMRMRLRVAMKTKLYNESIYAMNEMHIHRGLSPHMAVLKVFVNDKFLTEAVADGLIISTPTGSTAYSLSSGGPIVHPSINALLLTPICPNSLSFRPVLFPDTFKISIETSNKSRVRPQLSIDGRPLGLTDIGQRIDITSVKDNAIPCIIRSHKEDDWVSDIVSLLRWNHPFHRKGW
Protein: Procollagen-lysine,2-oxoglutarate 5-dioxygenase 1 (EC 1.14.11.4) (Lysyl hydroxylase 1) (A8WIN7)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Rough endoplasmic reticulum membrane {ECO:0000256|ARBA:ARBA00037819}; Peripheral membrane protein {ECO:0000256|ARBA:ARBA00037819}; Lumenal side {ECO:0000256|ARBA:ARBA00037819}.
Interaction partners:
- Procollagen galactosyltransferase 1
- Collagen beta
- Cerebral endothelial cell adhesion molecule
- procollagen galactosyltransferase
- Si:ch211-13f8.2.
- procollagen-lysine 5-dioxygenase
- procollagen-lysine 5-dioxygenase
- Calmodulin-lysine N-methyltransferase.
- Procollagen, type V, alpha 1.
- Collagen, type IV, alpha 1.
Sequence:
MRGVLAFLACLFASFPPLHCNQQGSIPEGDLLVLTVATQETDGFRRFLRSAKHFNYTIKVLGRGETWRGGDYMTAPGGGQKVRLLKSALEDIQEEKKVILFVDSYDVIFSSGPKELLKKFQQAKHKVVFSAETLIWPDRHLEDKHPHVREGKRFLGAGGFIGYAANLKKMLSDWSGADGDSDQLFYTKIYINKEKRKSINITLDSKCRLFQNLHGALDEVVLKFEDGRVRARNVLYDTLPVIIHGNGPTKLQINYLGNYIPNLWTFETGCTMCNQDRRLLSGLQESEYPVVVIGIFIQQPTPFVTVFFERLFNLKYPKNRLKLFIYNQETHHEQHIHAFLDSHESEYQGVKLIGPEEDIDPVSSRNLGFDMCREDIDCEYFFSIDVDVVLKNEDTLRILIEHNKPFIAPMLTKPGRLWTNFWGALSADGFYARSEDYVDIVQGHRVGLWNVPYVSHIFLIKADTLRTDLKDPDLFKSTTLDPDMAFCEKIRNKGVFMFVTNMDTFGRVLSTDNYQTNHLHNDLWQIFENPVEWEERYIHPNYSRVLKDEFIETPCPDVYWFPIFSEVACDHLVEEMENFGQWSGGANVDNRIQGGYENVPTIDIHMNQVGYEKEWQKFLLDYIAPVTEKMFPGYYTRAQFDLAFVVRYKPDEQPSLRPHHDASTFTINIALNHVGIDFQGGGCRFLRYDCSIRSPRKGWAFMHPGRLTHYHEGLPTTEGVRYIAVSFVDP
Protein: SoxXA-binding protein SoxK (Q8KDM6)
Organism: Chlorobaculum tepidum (strain ATCC 49652 / DSM 12025 / NBRC 103806 / TLS) (Chlorobium tepidum)
Interaction partners:
- L-cysteine S-thiosulfotransferase subunit SoxA
- Sulfur oxidation protein SoxX
- Sulfide dehydrogenase, flavoprotein subunit
Sequence:
MKKVLSLLSMLVLTPSASLLLAEPAPAAPAASSSPLIEQAEAARKEADALGYEWRDTAKILDSAREALQRGDQAESDKLASKALFQARAAKAQAQFMDKNWQMMIPKN
Protein: Rho GTPase activating protein at 5A, isoform B (SD02309p) (Q961S1)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MPRNTEAGAGNANTGGSGGVGGAPEPSSPVQKVWKPELYKLQLEAPAPCPLRCQRTLPLPPAKSTAEAVEANNLAGRLYGSEYHGLMGHLEAEQLLANARDGSYFVRRSPQSDGYYTLSLRFNKRPKHYKLLYKPGVGHYLRGQDKRFDTVHDMVADGLINFHMQLHASPIIQQINQQTKNCYQQSPYMTLNGRKLRALSNELGKAAAKESKESPAEEKEQKQEEPPPPAVDPMPLVYEKPHHFKVHTFKGLNWCEFCANFLWGFTAQGVKCEACGFVAHSKCSELVPPKCVPDLKRIRGVFGTDLTTMVQLEPHHQIPFVVRRCVEEVEARGMLQEGIYRVSGFADEIEALKLALDREGEKTDMSETAYGNVNVIAGTLKLYLRLLPVPLITFQAYPSFMAAGRTGKQAEQRQLMAEAVRRLPPAHHSCLQYMLEHLKR