wanglab/gogpt-training-data huggingface dataset:
Protein: Long-chain-fatty-acid--CoA ligase ACSBG2 (EC 6.2.1.3) (Acyl-CoA synthetase bubblegum family member 2) (Arachidonate--CoA ligase ACSBG2) (EC 6.2.1.15) (Bubblegum-related protein) (PRTD-NY3) (Q5FVE4)
Organism: Homo sapiens (Human)
Function: Catalyzes the conversion of fatty acids such as long chain and very long-chain fatty acids to their active form acyl-CoAs for both synthesis of cellular lipids, and degradation via beta-oxidation. Can activate diverse saturated, monosaturated and polyunsaturated fatty acids. Has increased ability to activate oleic and linoleic acid. May play a role in spermatogenesis.
Subcellular location: Cytoplasm. Membrane; Peripheral membrane protein.
Interaction partners:
- Fatty acid synthase
- Palmitoyl-protein thioesterase 1
- Lysosomal thioesterase PPT2
- Lipoprotein lipase
- Monoglyceride lipase
- Carnitine O-palmitoyltransferase 1, liver isoform
- Fatty acid CoA ligase Acsl3
- Long-chain-fatty-acid--CoA ligase 5
- Long-chain-fatty-acid--CoA ligase 4
- Carnitine O-palmitoyltransferase 1, muscle isoform
Sequence:
MTGTPKTQEGAKDLEVDMNKTEVTPRLWTTCRDGEVLLRLSKHGPGHETPMTIPEFFRESVNRFGTYPALASKNGKKWEILNFNQYYEACRKAAKSLIKLGLERFHGVGILGFNSAEWFITAVGAILAGGLCVGIYATNSAEVCQYVITHAKVNILLVENDQQLQKILSIPQSSLEPLKAIIQYRLPMKKNNNLYSWDDFMELGRSIPDTQLEQVIESQKANQCAVLIYTSGTTGIPKGVMLSHDNITWIAGAVTKDFKLTDKHETVVSYLPLSHIAAQMMDIWVPIKIGALTYFAQADALKGTLVSTLKEVKPTVFIGVPQIWEKIHEMVKKNSAKSMGLKKKAFVWARNIGFKVNSKKMLGKYNTPVSYRMAKTLVFSKVKTSLGLDHCHSFISGTAPLNQETAEFFLSLDIPIGELYGLSESSGPHTISNQNNYRLLSCGKILTGCKNMLFQQNKDGIGEICLWGRHIFMGYLESETETTEAIDDEGWLHSGDLGQLDGLGFLYVTGHIKEILITAGGENVPPIPVETLVKKKIPIISNAMLVGDKLKFLSMLLTLKCEMNQMSGEPLDKLNFEAINFCRGLGSQASTVTEIVKQQDPLVYKAIQQGINAVNQEAMNNAQRIEKWVILEKDFSIYGGELGPMMKLKRHFVAQKYKKQIDHMYH
Protein: MAGUK p55 subfamily member 4 (Amyotrophic lateral sclerosis 2 chromosomal region candidate gene 5 protein) (Discs large homolog 6) (Q96JB8)
Organism: Homo sapiens (Human)
Function: May play a role in retinal photoreceptors development.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:15914641}. Note=Detected at the outer limiting membrane (OLM) and in the outer plexiform layer (OPL) of the retina. At the OLM, detected apical to the adherens junction (AJ).
Interaction partners:
- Protein PALS1
- Rhodopsin kinase GRK7
- Inositol 1,4,5-trisphosphate-gated calcium channel ITPR2
- Recoverin
- Rhodopsin kinase GRK1
Sequence:
MIQSDKGADPPDKKDMKLSTATNPQNGLSQILRLVLQELSLFYGRDVNGVCLLYDLLHSPWLQALLKIYDCLQEFKEKKLVPATPHAQVLSYEVVELLRETPTSPEIQELRQMLQAPHFKALLSAHDTIAQKDFEPLLPPLPDNIPESEEAMRIVCLVKNQQPLGATIKRHEMTGDILVARIIHGGLAERSGLLYAGDKLVEVNGVSVEGLDPEQVIHILAMSRGTIMFKVVPVSDPPVNSQQMVYVRAMTEYWPQEDPDIPCMDAGLPFQKGDILQIVDQNDALWWQARKISDPATCAGLVPSNHLLKRKQREFWWSQPYQPHTCLKSTLSISMEEEDDMKIDEKCVEADEETFESEELSEDKEEFVGYGQKFFIAGFRRSMRLCRRKSHLSPLHASVCCTGSCYSAVGAPYEEVVRYQRRPSDKYRLIVLMGPSGVGVNELRRQLIEFNPSHFQSAVPHTTRTKKSYEMNGREYHYVSKETFENLIYSHRMLEYGEYKGHLYGTSVDAVQTVLVEGKICVMDLEPQDIQGVRTHELKPYVIFIKPSNMRCMKQSRKNAKVITDYYVDMKFKDEDLQEMENLAQRMETQFGQFFDHVIVNDSLHDACAQLLSAIQKAQEEPQWVPATWISSDTESQ
Protein: LLGL scribble cell polarity complex component 1 (Lethal(2) giant larvae protein homolog 1 isoform X2) (E7FD67)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}. Endomembrane system {ECO:0000256|ARBA:ARBA00004308}.
Interaction partners:
Sequence:
MMKFRFRRQGNDPHREKIKQDLFAFNKTVEHGFPNQPSALAYDPKLQLMAIGTKSGAIKIYGAPGVEMTGLHKDTAAVTQIHFLCGQGRILSLLDDNTIHLWEIVQRENRSHLLEVHSFNLPGRPGIESTSATRVTVMLLNLSCNLLALGTEGGGVHFLELPTLTLLNKSLFQDEIMQSVPEEYKCGKSLGPVESLQEHPKDSDKILIGYSRGLVVLWDLSSRHVDNLFLGKQQLESLVWERSGNSFVSSHSDGGYMVWAVSSSNPCTHDPVSSTIPYGPFPCKAVNKILWRTTESGAPLVLFSGGMPRASYGDRHCLTILQDSSHVTLDFTSRVIDFFTIHCTDTEKDFDEPSALVVLLEEELVVIDLQMPGWPTVPAPYLAPLHSSAITCSCHISNVPPKLWERVISAGQQQCPLQNYENWPICGGKNLAPDPKQKELLLTGHEDGTVRFWDASGVSLKPLYKLSTASIFQTDCEHNDSLTQAGEEEWPPFRKVGCFDPYSDDPRLGIQKISLCKYSGKLVVAGTAGQVIVMVLGDEKSDHMIDVATVDLLQDREGFTWKGHDRLPPKSGSVVFAPGFQPVVLVQCLPPAAVTAVTLHAEWNLIAFGTSHGFGLFDYHRRSPVLARCTLHPNDSLAMEGPLSRVKSLKKSLRQSFRRIRKSRVSGKKRVVVNSPTSKVQEANAHLADHDAEVTPVQRRIEPRSADDSLSGVVRCLCFADTFLRDGTHHGPTMWAGTNSGSVYAYALDVPSQEKFSEQSVEALLGKEIQLMHRAPVVSIAVLDGRGNPLPEPYEVSRDLAKAPDMQGSHSVLIASEEQFKVFMLPKVSAKTKFKLTAHEGCRVRKVALANFTSVSSEDYSENALVCLTNMGDIHMFSVPALRPQVRYDCVRKEDISGIASCVFTKTGQGFYLISPSEYERFSLSARVITEPLCGVDVERPHDVSAHSSSTTLPPQANGTHKSQAESKSAETEDLLEEMRSVLSSPILDSPNSSADITLDTTGDLTVEDVKDFLMTVDEAENNFRNITEEDGRSAGILIN
Protein: Nuclear receptor subfamily 0 group B member 2 (Orphan nuclear receptor SHP) (Small heterodimer partner) (Q62227)
Organism: Mus musculus (Mouse)
Function: Transcriptional regulator that acts as a negative regulator of receptor-dependent signaling pathways. Specifically inhibits transactivation of the nuclear receptor with which it interacts. Inhibits transcriptional activity of NEUROD1 on E-box-containing promoter by interfering with the coactivation function of the p300/CBP-mediated transcription complex for NEUROD1 (By similarity). Essential component of the liver circadian clock which via its interaction with NR1D1 and RORG regulates NPAS2-mediated hepatic lipid metabolism. Regulates the circadian expression of cytochrome P450 (CYP) enzymes. Represses: NR5A2 and HNF4A to down-regulate CYP2C38, NFLI3 to up-regulate CYP2A5, BHLHE41/HNF1A axis to up-regulate CYP1A2, CYP2E1 and CYP3A11, and NR1D1 to up-regulate CYP2B10, CYP4A10 and CYP4A14.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:Q15466}. Nucleus {ECO:0000250|UniProtKB:Q15466}. Note=Colocalizes with NEUROD1 in the nucleus. {ECO:0000250|UniProtKB:Q15466}.
Interaction partners:
- Nuclear receptor subfamily 5 group A member 2
- Hepatocyte nuclear factor 4-alpha
- Bile acid receptor
- Steroidogenic factor 1
- Cytochrome P450 7A1
- Oxysterols receptor LXR-alpha
- Peroxisome proliferator-activated receptor alpha
- Peroxisome proliferator-activated receptor gamma
- Nuclear receptor subfamily 1 group I member 2
- 7-alpha-hydroxycholest-4-en-3-one 12-alpha-hydroxylase
Sequence:
MSSGQSGVCPCQGSAGRPTILYALLSPSPRTRPVAPASHSHCLCQQQRPVRLCAPHRTCREALDVLAKTVAFLRNLPSFCHLPHEDQRRLLECCWGPLFLLGLAQDAVTFEVAEAPVPSILKKILLEEASSGTQGAQPSDRPQPSLAAVQWLQRCLESFWSLELGPKEYAYLKGTILFNPDVPGLRASCHIAHLQQEAHWALCEVLEPWYPASQGRLARILLMASTLKNIPGTLLVDLFFRPIMGDVDITELLEDMLLLR
Protein: Signal transducer CD24 (Lymphocyte antigen 52) (Ly-52) (M1/69-J11D heat stable antigen) (HSA) (Nectadrin) (R13-Ag) (X62 heat stable antigen) (CD antigen CD24) (P24807)
Organism: Mus musculus (Mouse)
Function: May have a pivotal role in cell differentiation of different cell types. May have a specific role in early thymocyte development. Signaling could be triggered by the binding of a lectin-like ligand to the CD24 carbohydrates, and transduced by the release of second messengers derived from the GPI-anchor. Modulates B-cell activation responses (By similarity). In association with SIGLEC10 may be involved in the selective suppression of the immune response to danger-associated molecular patterns (DAMPs) such as HMGB1, HSP70 and HSP90. Plays a role in the control of autoimmunity.
Subcellular location: Cell membrane; Lipid-anchor, GPI-anchor.
Interaction partners:
- Sialic acid-binding Ig-like lectin 10
- P-selectin
- High mobility group protein B1
- Neural cell adhesion molecule L1
- Epithelial cell adhesion molecule
- CD44 antigen
- Prominin-1
- E-selectin
- Platelet endothelial cell adhesion molecule
- Heat shock 70 kDa protein 1B
Sequence:
MGRAMVARLGLGLLLLALLLPTQIYCNQTSVAPFPGNQNISASPNPSNATTRGGGSSLQSTAGLLALSLSLLHLYC
Protein: Zinc finger protein 536 (O15090)
Organism: Homo sapiens (Human)
Function: Transcriptional repressor that negatively regulates neuron differentiation by repressing retinoic acid-induced gene transcription. Binds and interrupts RARA from binding to retinoic acid response elements (RARE) composed of tandem 5'-AGGTCA-3' sites known as DR1-DR5. Recognizes and binds 2 copies of the core DNA sequence 5'-CCCCCA-3'.
Subcellular location: Nucleus {ECO:0000269|PubMed:19398580}.
Interaction partners:
Sequence:
MEEASLCLGVSSAEPEAEPHLSGPVLNGQYAMSQKLHQITSQLSHAFPELHPRPNPEEKPPASLEEKAHVPMSGQPMGSQMALLANQLGREVDTSLNGRVDLQQFLNGQNLGIMSQMSDIEDDARKNRKYPCPLCGKRFRFNSILSLHMRTHTGEKPFKCPYCDHRAAQKGNLKIHLRTHKLGNLGKGRGRVREENRLLHELEERAILRDKQLKGSLLQPRPDLKPPPHAQQAPLAACTLALQANHSVPDVAHPVPSPKPASVQEDAVAPAAGFRCTFCKGKFKKREELDRHIRILHKPYKCTLCDFAASQEEELISHVEKAHITAESAQGQGPNGGGEQSANEFRCEVCGQVFSQAWFLKGHMRKHKDSFEHCCQICGRRFKEPWFLKNHMKVHLNKLSVKNKSPSDPEVPVPMGGMSQEAHANLYSRYLSCLQSGFMTPDKAGLSEPSQLYGKGELPMKEKEALGKLLSPISSMAHGVPEGDKHSLLGCLNLVPPLKSSCIERLQAAAKAAEMDPVNSYQAWQLMARGMAMEHGFLSKEHPLQRNHEDTLANAGVLFDKEKREYVLVGADGSKQKMPADLVHSTKVGSQRDLPSKLDPLESSRDFLSHGLNQTLEYNLQGPGNMKEKPTECPDCGRVFRTYHQVVVHSRVHKRDRKGEEDGLHVGLDERRGSGSDQESQSVSRSTTPGSSNVTEESGVGGGLSQTGSAQEDSPHPSSPSSSDIGEEAGRSAGVQQPALLRDRSLGSAMKDCPYCGKTFRTSHHLKVHLRIHTGEKPYKCPHCDYAGTQSASLKYHLERHHRERQNGAGPLSGQPPNQDHKDEMSSKASLFIRPDILRGAFKGLPGIDFRGGPASQQWTSGVLSSGDHSGQATGMSSEVPSDALKGTDLPSKSTHFSEIGRAYQSIVSNGVNFQGSLQAFMDSFVLSSLKKEKDMKDKALADPPSMKVHGVDGGEEKPSGKSSQRKSEKSQYEPLDLSVRPDAASLPGSSVTVQDSIAWHGCLFCAFTTSSMELMALHLQANHLGKAKRKDNTIGVTVNCKDQAREASKMALLPSLQSNKDLGLSNMISSLDSASEKMAQGQLKETLGEQKSGAWTGHVDPAFCNFPSDFYKQFGVYPGMVGSGASSSCPNKEPDGKAHSEEDVPILIPETTSKNTTDDLSDIASSEDMDSSKGENNDEEDVETEPEMMTKPLSALSKDSSSDGGDSLQPTGTSQPVQGLVSPLSQAPEKQWHSQGLLQAQDPLAGLPKPERGPQSLDKPMNMLSVLRAYSSDGLAAFNGLASSTANSGCIKRPDLCGK
Protein: C-C chemokine receptor type 5 (C-C CKR-5) (CC-CKR-5) (CCR-5) (MIP-1 alpha receptor) (CD antigen CD195) (P51682)
Organism: Mus musculus (Mouse)
Function: Receptor for a number of inflammatory CC-chemokines including CCL3/MIP-1-alpha, CCL4/MIP-1-beta and RANTES and subsequently transduces a signal by increasing the intracellular calcium ion level. May play a role in the control of granulocytic lineage proliferation or differentiation. Participates in T-lymphocyte migration to the infection site by acting as a chemotactic receptor.
Subcellular location: Cell membrane; Multi-pass membrane protein.
Interaction partners:
- C-C motif chemokine 3
- C-C motif chemokine 2
- C-C motif chemokine 4
- T-cell surface glycoprotein CD4
- C-C motif chemokine 5
- C-C motif chemokine 8
- C-X-C motif chemokine 9
- C-X-C motif chemokine 10
- Eotaxin
- Stromal cell-derived factor 1
Sequence:
MDFQGSVPTYSYDIDYGMSAPCQKINVKQIAAQLLPPLYSLVFIFGFVGNMMVFLILISCKKLKSVTDIYLLNLAISDLLFLLTLPFWAHYAANEWVFGNIMCKVFTGLYHIGYFGGIFFIILLTIDRYLAIVHAVFALKVRTVNFGVITSVVTWAVAVFASLPEIIFTRSQKEGFHYTCSPHFPHTQYHFWKSFQTLKMVILSLILPLLVMVICYSGILHTLFRCRNEKKRHRAVRLIFAIMIVYFLFWTPYNIVLLLTTFQEFFGLNNCSSSNRLDQAMQATETLGMTHCCLNPVIYAFVGEKFRSYLSVFFRKHMVKRFCKRCSIFQQDNPDRASSVYTRSTGEHEVSTGL
Protein: WW domain-binding protein 2 (WBP-2) (P97765)
Organism: Mus musculus (Mouse)
Function: Acts as transcriptional coactivator of estrogen and progesterone receptors (ESR1 and PGR) upon hormone activation. In presence of estrogen, binds to ESR1-responsive promoters. Required for YAP1 coactivation function on PGR activity. Synergizes with WBP2 in enhancing PGR activity (By similarity). Modulates expression of post-synaptic scaffolding proteins via regulation of ESR1, ESR2 and PGR.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:Q969T9}. Nucleus {ECO:0000250|UniProtKB:Q969T9}. Note=Translocates from cytoplasm to nucleus when phosphorylated. {ECO:0000250|UniProtKB:Q969T9}.
Interaction partners:
- Transcriptional coactivator YAP1
- WW domain-containing transcription regulator protein 1
- NEDD4-like E3 ubiquitin-protein ligase WWP2
- Cytochrome c1, heme protein, mitochondrial
- E3 ubiquitin-protein ligase NEDD4
- Cytochrome b-c1 complex subunit 7
- Cytochrome b-c1 complex subunit Rieske, mitochondrial
Sequence:
MALNKNHSEGGGVIVNNTESILMSYDHVELTFNDMKNVPEAFKGTKKGTVYLTPYRVIFLSKGKDAMQSFMMPFYLMKDCEIKQPVFGANFIKGIVKAEAGGGWEGSASYKLTFTAGGAIEFGQRMLQVASQASRGEVPNGAYGYPYMPSGAYVFPPPVANGMYPCPPGYPYPPPPPEFYPGPPMMDGAMGYVQPPPPPYPGPMEPPVSGPSAPATPAAEAKAAEAAASAYYNPGNPHNVYMPTSQPPPPPYYPPEDKKTQ
Protein: Vacuolar morphogenesis protein 6 (Vacuolar protein sorting-associated protein 39) (O13955)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Required for vacuolar assembly. Acts as component of the HOPS complex that acts during the docking stage of vacuole fusion. HOPS is required for vacuolar SNARE complex assembly. It remains bound to SNARE complexes after vacuole fusion (By similarity).
Subcellular location: Vacuole membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}.
Interaction partners:
- Vacuolar membrane protein pep3
- Vacuolar protein sorting-associated protein 41
- Vacuolar protein sorting-associated protein 33
- Probable vacuolar protein sorting-associated protein 16 homolog
- Vacuolar protein sorting-associated protein 8
- E3 ubiquitin-protein ligase pep5
- Vacuolar protein sorting-associated protein 3
- Ypt/Rab-type GTPase ypt7
- Synaptobrevin homolog ykt6
- Vesicle transport v-SNARE protein vti1
Sequence:
MHRAFSLYRVLELSKARVECVFELGGLVYVSNSNGDLDSYKIYNNEEEEAADFVMEHVDVYPNFTKKPITKVVSCATQDIFYALSDSQVYVYQISTFKKLFSFGAHCQNMCLYGDELIVLSSKKNLEIYEIQKNSKPNLTKTISLNDRPRSLAWVSPTMILVSLSNDFCAVNTETSRISSLNLAWQQSSSLGLGISYIGMSIKSNKLHITRISDDEVLLSKDSQGLLVNLKSLQVSRNPLRWPTVPQAVIYNSPYIITLHNQYIYIWNKETYAMIQQIGISNIYSTFSCHKNTFFTSNSYVWILTPEDFSNQIEALLNTENLNEAISVLSQITVSQFPKRDYYLRITKREKALRSFSSGDYDLAMRLFSEISESPSTVLGLFPGLLDNNYSDAISILSMAPSQNESIESNVLFPGNHSNSQTDLRNGDAVSTVANNKRLRSLSTYLTDSRRKANRFLSYDEEHYFLQKKNLFLNADGTLVAKEKLEKIAVQIDTTLFLIYMISSPALVGSLLRLPNRCETSVVETNLLSAKMYRELVEYYYGKSLHEAALDLLTKLCDEPTDTLSLKGKSNTTSKYEPILSYLEKLSPELDHLIFKYSRVPLSEDPQNSIVIFIDENSEASTISKGVVLKYLETISYKVSIIYLEKLLLDNKFNDTVFPTRLALLYLKRILELEETTDFKNQEVFKQTIEKLEDYLTNSKQYDANVVLQEINSQDEFLSTVSIILYRRLSRHQDALDVYLKILNDWEGALSYCNSVYSIDGETEPYYMLLAEISKNYKSGSLNILDFITKYSSRLDLNRVFPLLPKNISMKSYHSLFSSQFRQLFEELSNKETQSKLYQKRLEDLNEELTKVRSEKVVITREKTCLFCHKRLGKSVISIFPDGSVVHYGCAKKYVSSNHLPYEAY
Protein: Uncharacterized protein C6B1.03c (O43067)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus {ECO:0000269|PubMed:16823372}.
Interaction partners:
Sequence:
MGKNNPFVHSNANFPPLQTHNFEDIPEKGYTIFSSPRIDVFNEERPHSGINLNQYQHHEDDAELQSNNPFLNKDSGVDLLKLHSRSNSRIYEAKPKRVIKPKIAIIECNEMAENPPFWNQNKAFERKVSSKESFNMLGYDKIDKLDSSNSYLGDFGVHHDGPFDPCSKHRNLDAATSPIAAFSSQSEANSLPAFLLPNNSKGVEKSEENEDGVTDNDSSNVNSSTNESPNPTDINVCSNDDATDNTENNLKKKASFIYRLRKHLKRNSIETE
Protein: Glucose-induced degradation protein 4 homolog (Vacuolar import and degradation protein 24 homolog) (Q8IVV7)
Organism: Homo sapiens (Human)
Function: Substrate-recognition subunit of the CTLH E3 ubiquitin-protein ligase complex that selectively accepts ubiquitin from UBE2H and mediates ubiquitination and subsequent proteasomal degradation of the transcription factor HBP1 (Probable). Binds proteins and peptides with a Pro/N-degron consisting of an unmodified N-terminal Pro followed by a small residue, and has the highest affinity for the peptide Pro-Gly-Leu-Trp. Binds peptides with an N-terminal sequence of the type Pro-[Ala,Gly]-[Leu,Met,Gln,Ser,Tyr]-[Glu,Gly,His,Ser,Val,Trp,Tyr]. Does not bind peptides with an acetylated N-terminal Pro residue.
Interaction partners:
- Armadillo repeat-containing protein 8
- Glucose-induced degradation protein 8 homolog
- E3 ubiquitin-protein transferase RMND5A
- Ran-binding protein 9
- Ran-binding protein 10
- WD repeat-containing protein 26
- Muskelin
- E3 ubiquitin-protein transferase MAEA
- E3 ubiquitin-protein transferase RMND5B
- Fructose-1,6-bisphosphatase 1
Sequence:
MCARGQVGRGTQLRTGRPCSQVPGSRWRPERLLRRQRAGGRPSRPHPARARPGLSLPATLLGSRAAAAVPLPLPPALAPGDPAMPVRTECPPPAGASAASAASLIPPPPINTQQPGVATSLLYSGSKFRGHQKSKGNSYDVEVVLQHVDTGNSYLCGYLKIKGLTEEYPTLTTFFEGEIISKKHPFLTRKWDADEDVDRKHWGKFLAFYQYAKSFNSDDFDYEELKNGDYVFMRWKEQFLVPDHTIKDISGASFAGFYYICFQKSAASIEGYYYHRSSEWYQSLNLTHVPEHSAPIYEFR
Protein: D-glucuronyl C5-epimerase (EC 5.1.3.17) (Heparan sulfate C5-epimerase) (Hsepi) (Heparin sulfate C5-epimerase) (Heparin/heparan sulfate:glucuronic acid C5-epimerase) (Heparosan-N-sulfate-glucuronate 5-epimerase) (Q9EPS3)
Organism: Mus musculus (Mouse)
Function: Converts D-glucuronic acid residues adjacent to N-sulfate sugar residues to L-iduronic acid residues, both in maturing heparan sulfate (HS) and heparin chains. This is important for further modifications that determine the specificity of interactions between these glycosaminoglycans and proteins.
Subcellular location: Golgi apparatus membrane {ECO:0000269|PubMed:11279150}; Single-pass type II membrane protein {ECO:0000269|PubMed:11279150}.
Interaction partners:
- Heparan sulfate 2-O-sulfotransferase 1
- Heparan-sulfate 6-O-sulfotransferase 1
- Heparan sulfate glucosamine 3-O-sulfotransferase 1
- Bifunctional heparan sulfate N-deacetylase/N-sulfotransferase 1
- Exostosin-1
- Bifunctional heparan sulfate N-deacetylase/N-sulfotransferase 2
- Heparan-sulfate 6-O-sulfotransferase 2
- Heparan-sulfate 6-O-sulfotransferase 3
- Syndecan-1
- Bifunctional heparan sulfate N-deacetylase/N-sulfotransferase 3
Sequence:
MRCLAARVNYKTLIIICALFTLVTVLLWNKCSSDKAIQFPRHLSSGFRVDGLEKRSAASESNHYANHIAKQQSEEAFPQEQQKAPPVVGGFNSNGGSKVLGLKYEEIDCLINDEHTIKGRREGNEVFLPFTWVEKYFDVYGKVVQYDGYDRFEFSHSYSKVYAQRSPYHPDGVFMSFEGYNVEVRDRVKCISGVEGVPLSTQWGPQGYFYPIQIAQYGLSHYSKNLTEKPPHIEVYETAEDRDRNIRPNEWTVPKGCFMASVADKSRSTNVKQFIAPETSEGVSLQLGNTKDFIISFDLKLLTNGSVSVVLETTEKNQLFTVHYVSNTQLIAFRDRDIYYGIGPRTSWSTVTRDLVTDLRKGVGLSNTKAVKPTKIMPKKVVRLIAKGKGFLDNITISTTAHMAAFFAASDWLVRNQDEKGGWPIMVTRKLGEGFKSLEPGWYSAMAQGQAISTLVRAYLLTKDYVFLSSALRATAPYKFPSEQHGVKAVFMNKHDWYEEYPTTPSSFVLNGFMYSLIGLYDLKETAGETLGKEARSLYERGMESLKAMLPLYDTGSGTIYDLRHFMLGIAPNLARWDYHTTHINQLQLLSTIDESPIFKEFVKRWKSYLKGSRAKHN
Protein: Cold shock-like protein CspLB (CspB) (P0A358)
Organism: Listeria innocua serovar 6a (strain ATCC BAA-680 / CLIP 11262)
Subcellular location: Cytoplasm {ECO:0000250}.
Interaction partners:
Sequence:
MQTGTVKWFNSEKGFGFIEVEGGDDVFVHFSAIEGEGFKTLDEGQSVEFEIVEGQRGPQAEKVTKL
Protein: Protein phosphatase 1 regulatory subunit 14D (Gastrointestinal and brain-specific PP1-inhibitory protein 1) (GBPI-1) (Q9NXH3)
Organism: Homo sapiens (Human)
Function: Inhibitor of PPP1CA. Has inhibitory activity only when phosphorylated, creating a molecular switch for regulating the phosphorylation status of PPP1CA substrates and smooth muscle contraction.
Subcellular location: Cytoplasm {ECO:0000305}.
Interaction partners:
- Protein phosphatase 1 regulatory subunit 14C
- Protein phosphatase 1 regulatory subunit 14B
- Protein phosphatase 1 regulatory subunit 14A
Sequence:
MLSSSPASCTSPSPDGENPCKKVHWASGRRRTSSTDSESKSHPDSSKIPRSRRPSRLTVKYDRGQLQRWLEMEQWVDAQVQELFQDQATPSEPEIDLEALMDLSTEEQKTQLEAILGNCPRPTEAFISELLSQLKKLRRLSRPQK
Protein: BLOC-3 complex member HPS1 (Hermansky-Pudlak syndrome 1 protein) (Q92902)
Organism: Homo sapiens (Human)
Function: Component of the BLOC-3 complex, a complex that acts as a guanine exchange factor (GEF) for RAB32 and RAB38, promotes the exchange of GDP to GTP, converting them from an inactive GDP-bound form into an active GTP-bound form. The BLOC-3 complex plays an important role in the control of melanin production and melanosome biogenesis and promotes the membrane localization of RAB32 and RAB38.
Interaction partners:
- BLOC-3 complex member HPS4
- BLOC-2 complex member HPS3
- BLOC-2 complex member HPS6
- Biogenesis of lysosome-related organelles complex 1 subunit 6
- BLOC-2 complex member HPS5
- Biogenesis of lysosome-related organelles complex 1 subunit 3
- Biogenesis of lysosome-related organelles complex 1 subunit 1
- Dysbindin
- Biogenesis of lysosome-related organelles complex 1 subunit 2
- SNARE-associated protein Snapin
Sequence:
MKCVLVATEGAEVLFYWTDQEFEESLRLKFGQSENEEEELPALEDQLSTLLAPVIISSMTMLEKLSDTYTCFSTENGNFLYVLHLFGECLFIAINGDHTESEGDLRRKLYVLKYLFEVHFGLVTVDGHLIRKELRPPDLAQRVQLWEHFQSLLWTYSRLREQEQCFAVEALERLIHPQLCELCIEALERHVIQAVNTSPERGGEEALHAFLLVHSKLLAFYSSHSASSLRPADLLALILLVQDLYPSESTAEDDIQPSPRRARSSQNIPVQQAWSPHSTGPTGGSSAETETDSFSLPEEYFTPAPSPGDQSSGSTIWLEGGTPPMDALQIAEDTLQTLVPHCPVPSGPRRIFLDANVKESYCPLVPHTMYCLPLWQGINLVLLTRSPSAPLALVLSQLMDGFSMLEKKLKEGPEPGASLRSQPLVGDLRQRMDKFVKNRGAQEIQSTWLEFKAKAFSKSEPGSSWELLQACGKLKRQLCAIYRLNFLTTAPSRGGPHLPQHLQDQVQRLMREKLTDWKDFLLVKSRRNITMVSYLEDFPGLVHFIYVDRTTGQMVAPSLNCSQKTSSELGKGPLAAFVKTKVWSLIQLARRYLQKGYTTLLFQEGDFYCSYFLWFENDMGYKLQMIEVPVLSDDSVPIGMLGGDYYRKLLRYYSKNRPTEAVRCYELLALHLSVIPTDLLVQQAGQLARRLWEASRIPLL
Protein: GTP-binding nuclear protein Ran (J3KQE5)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|RuleBase:RU363057}.
Interaction partners:
Sequence:
RRRRLRLRRLNCASAIFPASVGRARRRFWKLVLVGDGGTGKTTFVKRHLTGEFEKKYVATLGVEVHPLVFHTNRGPIKFNVWDTAGQEKFGGLRDGYYIQAQCAIIMFDVTSRVTYKNVPNWHRDLVRVCENIPIVLCGNKVDIKDRKVKAKSIVFHRKKNLQYYDISAKSNYNFEKPFLWLARKLIGDPNLEFVAMPALAPPEVVMDPALAAQYEHDLEVAQTTALPDEDDDL
Protein: Leucine-rich repeat-containing protein ODA7 (Q382D9)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MTEMTKDVLIAACKKNGGYAAPRLNDQLFLQCRGFLRIENLEEYVNLKVLWLEQNAISDFYGIETLQQLVSLFVQNNTISSLDTLPPLNGLRVLNISHNYLTSLSGIAAGCPQLETLQASHNRIGSLKECCSLWDLKDTLTSVDLSFNKIEIGEGDMGPVEFFGQLPNVSVIYFHGNPGSHGMKGYRRSMILHLPQLKYLDERPVFTEERRVVEAWGSGGEAAEGREREAIRKEKKDHLQSCVKVLYDRMEENREVRDRLTKQWEERRAVEMEWWKEERRKQRTQVSELEGSEELSRNLLTAAEEEEYATIVKDFRVGGDAIRASEVERRKAYEQQQAVEAVRAAALREIEEEEEKEGEATVEGSERAVFLSDEDMLQEVEEEIFKVLGSVEKDPYVGRTSLKMGRAVGAATSRLCGDQSKRKSRNGIWEKFYSWEKRIE
Protein: Ectodermal, isoform F (X2JAX9)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Uncharacterized protein, isoform C
- FI03362p
- LD17368p
- Kazal-like domain-containing protein
Sequence:
MKFVILLCVLSALLLQIEASPLQRLSRSERAVSRQQTVNNEVAPAVAPASDDDDDDDDEDDDDEPDLGDLIDDDDVLLISGLSDDDEEEDDDEDEEDDTPQGQAAPAATASDDDEEEDDDDDDYLDRLFDDILGDDEDEDDDDETPAATAQQSAVAAAPAQTLDEVAPAAASSVSAGISDGVDLPAESGNAAEVLAAGNAADESVSAAVAPAQNAAASSSNNEGIAGDDDEEADDDDDDDDDDIIGDDIIEARREARDLKNNVIDMSTDAFQARHNHFIDAIFSRINRIVSENYDPYVVNLTGRSVLPNAASGSNVKAANKKQSTSSKVGGHKKLKNTRSEPRSVNSNQEAREAAVKLQEQLTQLQSELAIKAVEKRPSPTSPATESESDSGSPKAETRTVSGSKTGQKKSSNKQNTKKASGLKSGNYNQPAGASKAGASSAGAVEKLQKAEGRLSGLASLKRVGNVKVISDAEGRNSTIKAKFTLGPLVLRVEKSFKKGSVRSVKSATARTNEMMGRIKFSVLDDRATLMSIKVQQPKQVEVESKDNHDRTREFVWRRTPKIAKLVNEKLKLAAESLFAPQGVEVVRL
Protein: Spindle pole body component (Q389Z9)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Cytoplasm, cytoskeleton, microtubule organizing center {ECO:0000256|RuleBase:RU363050}.
Interaction partners:
- Spindle pole body component
- Gamma-tubulin complex subunit, putative
- Gamma tubulin complex component protein N-terminal domain-containing protein
- Tubulin gamma chain
- Tubulin delta chain
Sequence:
MTTHLWANFVTSLESRGISFQHVQHASDRSAVISAAGFGDPISVAILETEWMKRCAPTSTQHASPVGVSDKGAFAPPPPLQAPQTAAATVSSPTRLAPQFSDHTKLEDVPEEIQDRVITAEVLAAAVGNGGSLLQASRDGFVVSRYVPVSMRGLCKTIVPIADSFVALRKVERAEYMGKSLVAMALGEAVSEICTSYAHEIANLQRWSQKKAMPLMGVVSEVLRAGHHIVRLRQVLPTDSILEEEGTLSMAGWRLLNHIHEQAEKHSGSREDDELLNLLLRRASVPYLRVLHRWVHEGVVEDPYGEFFISDASLPTGAASTTTAAPVSAVAGMKKSAVRRIFPPCGGGGDDYGETGMDDAHAFERRFSMNKNMVPNFILTNTKMAKIVFYTGKYCCLLREYNGALPSFGELSNQILIWSGVDELHRRIEESYEIASGEVLQLFLGPQVDLLGHLTSLKSYFLHQRSDWLIDFLDSAEELLLKSPFQVKAHSVRVLLQAAIARCCGKDLYHTLIGCSFSGTTVAQDIINSHERQNDESPQRASTNGRRSATRIETRCCIELLQLEADLKWPLTMVIDPPVLEQFNIVFRLFTWLKTCERDVTTSWTGDTDLDPHYQRAYIIKHQLIQFIRQFQFYAAHFVVEPLWGRMMNRICQADSIFAVNSALKDFFKGIELGLVLSSATRFRSLARILEIASVFSETGRPGAAQGLSEQRLQEILQDVETQFLKALSELASPVGADYPQLVPLLTWIDFSGYYDRNGVYRVLYSASAATEPVSSSATDRRKR
Protein: HCG1 protein (Zinc finger protein 165) (Q53Z40)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus {ECO:0000256|PROSITE-ProRule:PRU00187}.
Interaction partners:
Sequence:
MATEPKKAAAQNSPEDEGLLIVKIEEEEFIHGQDTCLQRSELLKQELCRQLFRQFCYQDSPGPREALSRLRELCCQWLKPEIHTKEQILELLVLEQFLTILPGDLQAWVHEHYPESGEEAVTILEDLERGTDEAVLQVQAHEHGQEIFQKKVSPPGPALNVKLQPVETKAHFDSSEPQLLWDCDNESENSRSMPKLEIFEKIESQRIISGRISGYISEASGESQDICKSAGRVKRQWEKESGESQRLSSAQDEGFGKILTHKNTVRGEIISHDGCERRLNLNSNEFTHQKSCKHGTCDQSFKWNSDFINHQIIYAGEKNHQYGKSFKSPKLAKHAAVFSGDKTHQCNECGKAFRHSSKLARHQRIHTGERCYECNECGKSFAESSDLTRHRRIHTGERPFGCKECGRAFNLNSHLIRHQRIHTREKPYECSECGKTFRVSSHLIRHFRIHTGEKPYECSECGRAFSQSSNLSQHQRIHMRENLLM