wanglab/gogpt-training-data huggingface dataset:
Protein: DnaJ homolog subfamily A member 3, mitochondrial (DnaJ protein Tid-1) (hTid-1) (Hepatocellular carcinoma-associated antigen 57) (Tumorous imaginal discs protein Tid56 homolog) (Q96EY1)
Organism: Homo sapiens (Human)
Function: Modulates apoptotic signal transduction or effector structures within the mitochondrial matrix. Affect cytochrome C release from the mitochondria and caspase 3 activation, but not caspase 8 activation. Isoform 1 increases apoptosis triggered by both TNF and the DNA-damaging agent mytomycin C; in sharp contrast, isoform 2 suppresses apoptosis. Can modulate IFN-gamma-mediated transcriptional activity. Isoform 2 may play a role in neuromuscular junction development as an effector of the MUSK signaling pathway.
Subcellular location: Mitochondrion matrix. Cytoplasm, cytosol {ECO:0000250}. Postsynaptic cell membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Note=Recruited to the postsynaptic cell membrane of the neuromuscular junction through interaction with MUSK. {ECO:0000250}.
Interaction partners:
- Stress-70 protein, mitochondrial
- Heat shock cognate 71 kDa protein
- Heat shock 70 kDa protein 1A
- Heat shock 70 kDa protein 4
- Endoplasmic reticulum chaperone BiP
- GrpE protein homolog 1, mitochondrial
- GrpE protein homolog 2, mitochondrial
- Heat shock 70 kDa protein 1-like
- ATP-dependent Clp protease proteolytic subunit, mitochondrial
- Interferon gamma receptor 2
Sequence:
MAARCSTRWLLVVVGTPRLPAISGRGARPPREGVVGAWLSRKLSVPAFASSLTSCGPRALLTLRPGVSLTGTKHNPFICTASFHTSAPLAKEDYYQILGVPRNASQKEIKKAYYQLAKKYHPDTNKDDPKAKEKFSQLAEAYEVLSDEVKRKQYDAYGSAGFDPGASGSQHSYWKGGPTVDPEELFRKIFGEFSSSSFGDFQTVFDQPQEYFMELTFNQAAKGVNKEFTVNIMDTCERCNGKGNEPGTKVQHCHYCGGSGMETINTGPFVMRSTCRRCGGRGSIIISPCVVCRGAGQAKQKKRVMIPVPAGVEDGQTVRMPVGKREIFITFRVQKSPVFRRDGADIHSDLFISIAQALLGGTARAQGLYETINVTIPPGTQTDQKIRMGGKGIPRINSYGYGDHYIHIKIRVPKRLTSRQQSLILSYAEDETDVEGTVNGVTLTSSGGSTMDSSAGSKARREAGEDEEGFLSKLKKMFTS
Protein: FERM, ARHGEF and pleckstrin domain-containing protein 1 (FERM, RhoGEF and pleckstrin domain-containing protein 1) (F1LYQ8)
Organism: Rattus norvegicus (Rat)
Function: May play a role in semaphorin signaling (By similarity). Functions as guanine nucleotide exchange factor for RAC1. Plays a role in the assembly and disassembly of dendritic filopodia, the formation of dendritic spines, regulation of dendrite length and ultimately the formation of synapses.
Subcellular location: Cell membrane {ECO:0000269|PubMed:23209303}; Peripheral membrane protein {ECO:0000269|PubMed:23209303}; Cytoplasmic side {ECO:0000269|PubMed:23209303}. Synapse {ECO:0000250}. Synapse, synaptosome {ECO:0000269|PubMed:23209303}. Cytoplasm, cytosol {ECO:0000269|PubMed:23209303}. Cell projection, filopodium {ECO:0000269|PubMed:23209303}. Cell projection, dendrite {ECO:0000269|PubMed:23209303}. Cell projection, dendritic spine {ECO:0000269|PubMed:23209303}. Note=Recruited to the cell membrane via interaction with CADM1.
Interaction partners:
- Cell division control protein 42 homolog
Sequence:
MGEIEQKPTPASRLGAPENSGISTLERGQKPPPTPSGKLMTVKIQMLDDTQEAFEVPQRAPGKVLFDAVCNHLNLVEGDYFGLEFPDHRKIVVWLDLLKPIVKQIRRPKHVLVKFVVKFFPPDHTQLQEELTRYLFALQVKQDLAQGRLTCNDTSAALLISHIVQSEIGDFDEALDREHLAKNKYVPQQDALEDKIVEFHHSHIGQTPAESDFQLLEVARRLEMYGIRLHPAKDREGTKINLAVANTGILVFQGFTKINAFNWAKVRKLSFKRKRFLIKLRPDVNSSYQDTLEFLMAGRDFCKSFWKICVEHHAFFRLFEEPKPKPKPVLFSRGSSFRFSGRTQKQVLDYVKEGGHKKVQFERKHSKIHSTRSLVSQPTAPNSEVPKQSPQSASLTFGEGTESPSAQSCQQAKETKVCTLEPGPRQSPALSKSPSGSKAADGTAAAAPPEEEDEEEGGKDGIRPSNPQPPQPSTGSLTGSPHLSELSINSQGGAAPANVTLSPNLSPDNKQASPLISPLLNDQACPRTDDEEEGRRKRFPTDKAYYIAKEVSTTERTYLKDLEVIASWFQSTVSKEDSMPEALKSLIFPNFEPLHKFHTNFLKEIEQRLALWEGRSNAHIRGDYQRIGDVMLKNIQGMKHLAAHLWKHSEALEALETSIKGSRRLEHFCRDFELQKVCYLPLNTFLLRPLHRLMHYKQVLERLCKHHPPNHADFRDCRAALAEITEMVAQLHGTMIKMENFQKLHELKKDLIGIDNLVIPGREFIRLGSLSKLSGKGLQQRMFFLFNDVLLYTSRGLTASNQFKVHGQLPLYGMTIEESEEEWGVPHCLTLRGQRQSIIVAASSRSEMEKWLEDIQMAIDLAEKSNGPTPELLASSPPDNKSPDEATAADQESEDDLSASRTSLERQAPHRGNTMVHVCWHRSTSVSMVDFSIAVENQLSGNLLRKFKNSNGWQKLWVVFTNFCLFFYKSHQDSHPLASLPLLGYSLTIPSESENIHKDYVFKLHFKSHVYYFRAESEYTFERWMEVIRSATSSASRAHSLSHKESHLY
Protein: Membrane protein FAM174A (Hepatitis C virus NS5A-transactivated protein 6) (HCV NS5A-transactivated protein 6) (Transmembrane protein 157) (Q8TBP5)
Organism: Homo sapiens (Human)
Subcellular location: Membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}.
Interaction partners:
Sequence:
MKASQCCCCLSHLLASVLLLLLLPELSGPLAVLLQAAEAAPGLGPPDPRPRTLPPLPPGPTPAQQPGRGLAEAAGPRGSEGGNGSNPVAGLETDDHGGKAGEGSVGGGLAVSPNPGDKPMTQRALTVLMVVSGAVLVYFVVRTVRMRRRNRKTRRYGVLDTNIENMELTPLEQDDEDDDNTLFDANHPRR
Protein: Zinc finger protein JACKDAW (ID1-like zinc finger protein 3) (Protein indeterminate-domain 10) (Q700D2)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Transcription factor that, together with BIB, regulates tissue boundaries and asymmetric cell division by a rapid up-regulation of 'SCARECROW' (SCR), thus controlling the nuclear localization of 'SHORT-ROOT' (SHR) and restricting its action. Binds DNA via its zinc fingers. Recognizes and binds to SCL3 promoter sequence 5'-AGACAA-3' to promotes its expression when in complex with RGA. Confines CYCD6 expression to the cortex-endodermis initial/daughter (CEI/CEID) tissues. Required for radial patterning and stem cell maintenance. Counteracted by 'MAGPIE' (MGP). Binds to the SCR and MGP promoter sequences. Controls position-dependent signals that regulate epidermal-cell-type patterning.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00768, ECO:0000269|PubMed:17785527, ECO:0000269|PubMed:24821766, ECO:0000269|PubMed:25829440}.
Interaction partners:
- Protein SHORT-ROOT
- Scarecrow-like protein 3
- Protein SCARECROW
- Transcription factor WER
- Homeobox-leucine zipper protein GLABRA 2
- WUSCHEL-related homeobox 5
- Putative cyclin-D6-1
- Transcription factor GLABRA 3
- CLAVATA3/ESR
- Transcription factor EGL1
Sequence:
MQMIPGDPFSISSSMGGFVHQETHLHHLQQQIPDLNPNSNPNPNAKPNSSSAKKKRNQPGTPDPDADVIALSPTTLMATNRFVCEICNKGFQRDQNLQLHRRGHNLPWKLKQRSKQEVIKKKVYICPIKTCVHHDASRALGDLTGIKKHYSRKHGEKKWKCEKCSKKYAVQSDWKAHAKTCGTREYKCDCGTLFSRKDSFITHRAFCDALTEEGARMSSLSNNNPVISTTNLNFGNESNVMNNPNLPHGFVHRGVHHPDINAAISQFGLGFGHDLSAMHAQGLSEMVQMASTGNHHLFPSSSSSLPDFSGHHQFQIPMTSTNPSLTLSSSSTSQQTSASLQHQTLKDSSFSPLFSSSSENKQNKPLSPMSATALLQKAAQMGSTRSNSSTAPSFFAGPTMTSSSATASPPPRSSSPMMIQQQLNNFNTNVLRENHNRAPPPLSGVSTSSVDNNPFQSNRSGLNPAQQMGLTRDFLGVSNEHHPHQTGRRPFLPQELARFAPLG
Protein: Serpin-Z2 (ArathZ2) (Q9ZQR6)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Probable serine protease inhibitor.
Interaction partners:
- Quinoprotein amine dehydrogenase, beta chain-like RIC1-like guanyl-nucleotide exchange factor
- Quinoprotein amine dehydrogenase, beta chain-like RIC1-like guanyl-nucleotide exchange factor
- Metacaspase-9
Sequence:
MDSKRKNQELSTSETADPSLSKTNKKQKIDMQEAMKNQNEVSLLLVGKVISAVAKNSNCVFSPASINAVLTVTAANTDNKTLRSFILSFLKSSSTEETNAIFHELASVVFKDGSETGGPKIAAVNGVWMEQSLSCNPDWEDLFLNFFKASFAKVDFRHKAEEVRLDVNTWASRHTNDLIKEILPRGSVTSLTNWIYGNALYFKGAWEKAFDKSMTRDKPFHLLNGKSVSVPFMRSYEKQFIEAYDGFKVLRLPYRQGRDDTNREFSMYLYLPDKKGELDNLLERITSNPGFLDSHIPEYRVDVGDFRIPKFKIEFGFEASSVFNDFELNVSLHQKALIEIDEEGTEAAAATTVVVVTGSCLWEPKKKIDFVADHPFLFLIREDKTGTLLFAGQIFDPSELSSALDRA
Protein: Parathyroid hormone (PTH) (Parathormone) (Parathyrin) (P01270)
Organism: Homo sapiens (Human)
Function: PTH elevates calcium level by dissolving the salts in bone and preventing their renal excretion. Stimulates [1-14C]-2-deoxy-D-glucose (2DG) transport and glycogen synthesis in osteoblastic cells.
Subcellular location: Secreted.
Interaction partners:
- Parathyroid hormone/parathyroid hormone-related peptide receptor
- Parathyroid hormone-related protein
- Parathyroid hormone 2 receptor
- Fibroblast growth factor 23
- Guanine nucleotide-binding protein G
- Tuberoinfundibular peptide of 39 residues
- Extracellular calcium-sensing receptor
- 25-hydroxyvitamin D-1 alpha hydroxylase, mitochondrial
- Osteocalcin
- Pro-glucagon
Sequence:
MIPAKDMAKVMIVMLAICFLTKSDGKSVKKRSVSEIQLMHNLGKHLNSMERVEWLRKKLQDVHNFVALGAPLAPRDAGSQRPRKKEDNVLVESHEKSLGEADKADVNVLTKAKSQ
Protein: HTH-type transcriptional regulator UlaR (P0A9W0)
Organism: Escherichia coli (strain K12)
Function: Represses ulaG and the ulaABCDEF operon. Two ulaR binding sites have been identified in each promoter. Full activity requires simultaneous interaction of UlaR with both divergent promoters and seems to be dependent on repressor-mediated DNA loop formation, which is helped by the action of integration host factor.
Subcellular location: Cytoplasm {ECO:0000305}.
Interaction partners:
- Probable L-ascorbate-6-phosphate lactonase UlaG
- Ascorbate-specific PTS system EIIB component
- Ascorbate-specific PTS system EIIC component
- Deoxyribose operon repressor
- L-ribulose-5-phosphate 4-epimerase UlaF
- Ascorbate-specific PTS system EIIA component
- Peptidyl-lysine N-acetyltransferase PatZ
- 3-keto-L-gulonate-6-phosphate decarboxylase UlaD
- Putative sgc region transcriptional regulator
- L-ribulose-5-phosphate 3-epimerase UlaE
Sequence:
MTEAQRHQILLEMLAQLGFVTVEKVVERLGISPATARRDINKLDESGKLKKVRNGAEAITQQRPRWTPMNLHQAQNHDEKVRIAKAASQLVNPGESVVINCGSTAFLLGREMCGKPVQIITNYLPLANYLIDQEHDSVIIMGGQYNKSQSITLSPQGSENSLYAGHWMFTSGKGLTAEGLYKTDMLTAMAEQKMLSVVGKLVVLVDSSKIGERAGMLFSRADQIDMLITGKNANPEILQQLEAQGVSILRV
Protein: Spastin (A0A2R8Y7K2)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
XACRNGHLQSESGAVPKRKDPLTHTSNSLPRSKTVMKTGSAGLSGHHRAPSYSGLSMVSGVKQGSGPAPTTHKGTPKTNRTNKPSTPTTATRKKKDLKNFRNVDSNLANLIMNEIVDNGTAVKFDDIAGQDLAKQALQEIVILPSLRPELFTGLRAPARGLLLFGPPGNGKTMLAKAVAAESNATFFNISAASLTSKYVQSAGDDRVLVMGATNRPQELDEAVLRRFIKRVYVSLPNEETRLLLLKNLLCKQGSPLTQKELAQLARMTDGYSGSDLTALAKDAALGPIRELKPEQVKNMSASEMRNIRLSDFTESLKKIKRSVSPQTLEAYIRWNKDFGDTTV
Protein: Rubrerythrin-1 (Rr 1) (NADH peroxidase) (NPXase) (Npx) (EC 1.11.1.1) (Q97FZ9)
Organism: Clostridium acetobutylicum (strain ATCC 824 / DSM 792 / JCM 1419 / IAM 19013 / LMG 5710 / NBRC 13948 / NRRL B-527 / VKM B-1787 / 2291 / W)
Function: Functions as the terminal component of an NADH peroxidase (NADH:H(2)O(2) oxidoreductase) when using NADH:rubredoxin oxidoreductase (NROR) as the electron transport intermediary from NADH to RubY.
Interaction partners:
- Predicted S-adenosylmethionine-dependent methyltransferase
- Rubredoxin
- Desulfoferrodoxin
- 6-carboxy-5,6,7,8-tetrahydropterin synthase
- 6-carboxy-5,6,7,8-tetrahydropterin synthase
Sequence:
MKSLKGTKTAENLMKAFAGESQARNRYTFYSNTAKKEGYVQISNIFLETAENERMHAKRFFKFLSEGLDDEAVEINGASYPTTLGDTKKNLIAAAKGENEEWTDLYPSFAKTAEDEGFKGVAAAFRLIAAVEKEHEKRYNALLKNIEENKVFEKDEVKFWKCIKCGYIFEGKTAPKVCPACLHPQAYFEILSENY
Protein: Myelin-associated neurite-outgrowth inhibitor (Mani) (p20) (A1KXE4)
Organism: Homo sapiens (Human)
Function: Inhibitor of neuronal axonal outgrowth. Acts as a negative regulator of CDC42 and STAT3 and a positive regulator of STMN2. Positive regulator of CDC27.
Subcellular location: Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:D4AEP3}. Cell membrane {ECO:0000250|UniProtKB:Q80XQ8}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q80XQ8}. Cell projection, axon {ECO:0000250|UniProtKB:Q80XQ8}. Note=Expressed in neuronal cell bodies and axonal fibers. {ECO:0000250|UniProtKB:Q80XQ8}.
Interaction partners:
Sequence:
MNPVYSPGSSGVPYANAKGIGYPAGFPMGYAAAAPAYSPNMYPGANPTFQTGYTPGTPYKVSCSPTSGAVPPYSSSPNPYQTAVYPVRSAYPQQSPYAQQGTYYTQPLYAAPPHVIHHTTVVQPNGMPATVYPAPIPPPRGNGVTMGMVAGTTMAMSAGTLLTAHSPTPVAPHPVTVPTYRAPGTPTYSYVPPQW
Protein: Olfactory receptor (Q8VGX9)
Organism: Mus musculus (Mouse)
Subcellular location: Cell membrane {ECO:0000256|RuleBase:RU363047}; Multi-pass membrane protein {ECO:0000256|RuleBase:RU363047}. Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
Sequence:
MSNTISQTMESPNHTDLDPSIFFLLGIPGLEQFHMWLSLPVCCLGTATIVGNITILVVVATEPTLHRPVYLFLCMLSTIDLAASFSTVPKLLAILWCGAGHISASACLTQMFFIHAFCMMESTVLLAMAFDRYVAICHPLRYSTILTDTIIARIGVVAMMRGSLLMLPCPFLIGRLSFCQSHVIPHTYCEHMAVVKLACGDTRPNRVYGLTAALLVIGVDLFCIGLSYALIAQAVFRLSSQEARSKALGTCGSHVCVILISYTPALFSFFTHRFGHHVPLHIHILLANVYLLFPPALNPVVYGVKTREIRERVAKVFQWGQGTRLKISK
Protein: Sec24c protein (Q8R2V9)
Organism: Mus musculus (Mouse)
Subcellular location: Cytoplasmic vesicle, COPII-coated vesicle membrane {ECO:0000256|ARBA:ARBA00004299}; Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004299}; Cytoplasmic side {ECO:0000256|ARBA:ARBA00004299}. Endoplasmic reticulum membrane {ECO:0000256|ARBA:ARBA00004397}; Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004397}; Cytoplasmic side {ECO:0000256|ARBA:ARBA00004397}.
Interaction partners:
Sequence:
DDRKLINTDKEKTLFQPQTGTYQTLAKECVAQGCCVDLFLFPNQYVDVATLSVVPQLTGGSVYKYACFQVENDQERFLSDLRRDVQKVVGFDAVMRVRTSTGIRAVDFFGAFYMSNTTDVELAGLDGDKTVTVEFKHDDRLNEENGALLQCALLYTSCAGQRRLRIHNLALNCCTQLADLYRNCETDTLINYMAKFAYRAVLNSPVKTVRDTLITQCAQILACYRKNCASPSSAGQLILPECMKLLPVYLNCVLKSDVLQPGAEVTTDDRAYVRQLVSSMDVAETNVFFYPRLLPLTKSPLDSTAEPPAVRASEERLSSGDIYLLENGLNLFVWVGASVQQGVVQSLFNVSSFSQITSGLSVLPVLDNPLSKKVRGLIDSLRAQRMRYMKLIVVKQEDKLEMLFKHFLVEDKSLSGGASYVDFLCHMHKEIRQLLS
Protein: At4g37295 (Q8LCF5)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- PAMP-induced secreted peptide 2
- Precursor of CEP16
- Transmembrane protein
- At2g23270
- F28L1.2 protein
- Protein CASPARIAN STRIP INTEGRITY FACTOR 1
- Protein CASPARIAN STRIP INTEGRITY FACTOR 2
- Protein IDA
- Precursor of CEP1
- Protein IDA-LIKE 2
Sequence:
MRPVGLIFTVMFLVSAFSESRTADCRVLLGGSTEEIDQSKIHGVDLRSEDLLGVVIHGYKKLRWLSSAGERMHTMASGPSRRGAGH
Protein: Negative regulator of sporulation PMD1 (P32634)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Negatively regulates early sporulation-specific genes. Seems to exert its function by positively regulating the Ras/cAMP pathway. Required for growth under alkaline conditions. Acts synergetically with MDS3.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:14562095}.
Interaction partners:
Sequence:
MTVLQPPSSVCYPLNLPIVPNPNLDEATRKKLTLECRTGAAVELARSGVFVHGGLTLPLNLTIINSLQLQKELILYFGKQKDRNADFKTLADWISPEIFFLDLISRTWQRINTTIDTTSENELNNGLSFKERLFHSMCFTESNIYIFGGLMVSPHNGYELIATNELWKLDLKTKCWSLISENPQITRRFNHSMHVLNENNENQDTKLIIVGGLDNMDIPVKKIDIFNLRTSLWESESKSDENPASKGSSKILVNIDGMPISLSHDSNFSVLIENNQAEIPTLALYYPQREANTSRRGTDDGSFSTYAHDLDDKSKLPKHHHHHHGDLKYFESDDADENAVKTLMSPIVILPLLGNSQGARMTSNPTQNNKENSILQVPFHLQYPSGNYFNYNIVVIGFYPDPQPSNLHCFIYNIASGKWIRVNIACTECSISMHRFWKLLIWKSHHQALLLGTRTDDFCSPSVQKFDHILSFSLPMLNGYNKLVNTKHTRTNNGIANSHNLNVNLSLYDHLPYSNSSTIEHTNPYTVTQGYSLDDSGIPRLTSTATSQFENYSRYITVPLEMESTSSIFPPYAMVLGKDALEIFGKTLSDFEFITADGDSIGVPVYLLRKRWGRYFDSLLSNGYANTSFNYEFNGDTSNIISFSPHTASKTTKFGNSSQSSNGSLEKYFSKNGNSKSNSNTSLKKPHSVDFTSSTSSPKQRAISHNKLSPSEPILCADEEDSRSNTLKQHATGDTGLKETGTSNKRPISTTCSSTGMVFRVPFQDMKNSKLGLSEQSGRSTRASSVSPPPVYKKSTNDGNDSNCTLSNTPLVYRRASTVGTTTNSSVDDGFSSIRRASHPLQSYIIAKSSPSSISKASPAEKAFSRRKSSALRFIASPNQSRQTSFASTASTASVVSSTSGRRRNSNQISHLGSSASLPNSPILPVLNIPLPPQEKIPLEPLPPVPKAPSRRSSSLAEYVQFGRDSPVASRRSSHSTRKSSSSDARRISNSSLLRNTLDSQLLSNSYGSDIPYEASIQEYGMNNGRDEEEDGDNQDYGCISPSNIRPIFSTINAININGNFKEGEFFSSKSYINNEKSRRLSYISNPESVESTNSNNNAIIELEPLLTPRSLYMPWSTASVRAFAEFFYTAQINGKWLLAPVTLDLLIMAKIYEIPILYELITEVLYKIISKKEEGLSVTCEALLNLFQQKVSRYCNENEGKIRKQLDSSESYQDTLEIKRSLANIDNGYVDSYLLRNTSMAQSIHYTDDSNGETEIDMHHTGISSIGSLANRAVPTVFAGGPRDSHNSIGSIAFPSNSGVQNIRRSVSLFSPATKKKSSLSRETDPLDTSDQFTDDVPDSGPVSRQQNFPRRSSSFTETVPTEPTRYNYQNLDSSKSNRASDDKEEQNEQATLQDISNFDKYKVETLQKRNSNDGKDLDRTNDPLKNRGTEIPQNSSNLETDPFIRDSFDSDSGSSFRSDSDDLDSQLGILPFTKMNKKLQEQTSQEFDDSIDPLYKIGSSTPGSSRLHGSFSKYIRPNSQREDGSEYVNISSLENMVSPNALPPVDYVMKSIYRTSVLVNDSNLMTRTKEAIELSKVLKKLKKKVLQDISQMDDEMRETGKPIFARGSSSPTLSRQHSDVATPLKQQENTRPALKFASSSPISEGFRKSSIKFSQAPSTQISPRTSVTDFTASQQRRQHMNKRFSTQTTHSTSALFMNPAFMPSAVNTGRKESEGHCEDRSATANRTNRKEDATTNDNDNIAPFPFFGKRR
Protein: Conserved oligomeric Golgi complex subunit 4 (COG complex subunit 4) (Component of oligomeric Golgi complex 4) (Protein SEC38) (Q06096)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Acts as essential component of the peripheral membrane COG complex that is involved in intra-Golgi protein trafficking. COG is located at the cis-Golgi, and regulates tethering of retrograde intra-Golgi vesicles and possibly a number of other membrane trafficking events. Possesses ATPase activity.
Subcellular location: Golgi apparatus membrane {ECO:0000250|UniProtKB:Q9H9E3}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q9H9E3}; Cytoplasmic side {ECO:0000250|UniProtKB:Q9H9E3}.
Interaction partners:
- Conserved oligomeric Golgi complex subunit 8
- Conserved oligomeric Golgi complex subunit 6
- Conserved oligomeric Golgi complex subunit 3
- Conserved oligomeric Golgi complex subunit 2
- Conserved oligomeric Golgi complex subunit 1
- Conserved oligomeric Golgi complex subunit 5
- Conserved oligomeric Golgi complex subunit 7
- Protein SLY1
- Integral membrane protein SED5
- Vacuolar protein sorting-associated protein 53
Sequence:
MEGQKSNASWESSIIEGQLSKNLARYTLLLDKLSTLSQIDKLSEVIANDYAKQSKQLNAFVQQSQSSLNKESRKLELQRTNLTTTLTQFHETVATISSSNARAKAIHDDIETVDQERALVNKTLQFVKDVRTLKNNISLAHSALETKDYLVAATAINEIRSLPDKKLIVSEFAKKVVPSSEIPEEPAILIKNWCKELTSLFQEQFMEATRTQDIKELTLMFKMFPMIGQDVLGLDLYSKYVCDIIADESRKIMSNSMENSTKFQGFFSQVLLHLFKIVSTIINDHSKVIATCYGKKHMVHVMEKVEKEADLQASLILDIFMETRKIERTIHDINEWEHSQKNEDVNIDSNQSDIETDGETEKSSIISIHDLALLIMEFSQILQNWSMYSRFYSVKWNEFSDLHPHVLQPPPPIADGKFALKLKQDKVFDEFQVFVLNHLQRSFRNSISLEELPSLNDLITAVPLNDHDNISYPVTSVLDDLILLVRKNLISVVNTGQFKLLASFLNELVKFFQNRFLVKFMQNKFKLLQSKLASNVSLKRYIPKGEEQSATSRSVSPPANKFSPLSRFTFRGAAASALTNIQSNLQAVVAEDEDSILALHHYLIYLNTLYLSKVYVHRLLSIEILEDDSQRILRDNFPFDNDAAQLQNLIINSEKLVLEQTDKLSKWAVKYLFQNILQNRVRNLLGTVFVNSASSNSSTSNQKNVSRDYSAGSNQKNYITSIEDFEDLSQINSFNSKWNQLIIPYKNILHNEAYAELLSVIVDYIVTTLEQRIWTLEFNELGVTKLDRELSLFIGNMCGLNYNLREKFLKLTQIVLLLGLDDDNFDLTTGDIKDDFNGTFDWVINSQERIKARNMKIDRTQ
Protein: Gem-associated protein 6 (Gemin-6) (SIP2) (Q8WXD5)
Organism: Homo sapiens (Human)
Function: The SMN complex catalyzes the assembly of small nuclear ribonucleoproteins (snRNPs), the building blocks of the spliceosome, and thereby plays an important role in the splicing of cellular pre-mRNAs. Most spliceosomal snRNPs contain a common set of Sm proteins SNRPB, SNRPD1, SNRPD2, SNRPD3, SNRPE, SNRPF and SNRPG that assemble in a heptameric protein ring on the Sm site of the small nuclear RNA to form the core snRNP (Sm core). In the cytosol, the Sm proteins SNRPD1, SNRPD2, SNRPE, SNRPF and SNRPG are trapped in an inactive 6S pICln-Sm complex by the chaperone CLNS1A that controls the assembly of the core snRNP. To assemble core snRNPs, the SMN complex accepts the trapped 5Sm proteins from CLNS1A forming an intermediate. Binding of snRNA inside 5Sm triggers eviction of the SMN complex, thereby allowing binding of SNRPD3 and SNRPB to complete assembly of the core snRNP.
Subcellular location: Nucleus, nucleoplasm {ECO:0000269|PubMed:11748230}. Nucleus, gem {ECO:0000269|PubMed:11748230}. Cytoplasm {ECO:0000269|PubMed:11748230}. Note=Found both in the nucleoplasm and in nuclear bodies called gems (Gemini of Cajal bodies) that are often in proximity to Cajal (coiled) bodies. Also found in the cytoplasm.
Interaction partners:
- Gem-associated protein 8
- Serine-threonine kinase receptor-associated protein
- Gem-associated protein 5
- Gem-associated protein 7
- Gem-associated protein 2
- Probable ATP-dependent RNA helicase DDX20
- Gem-associated protein 4
- Survival motor neuron protein
- Small nuclear ribonucleoprotein E
- Small nuclear ribonucleoprotein-associated proteins B and B'
Sequence:
MSEWMKKGPLEWQDYIYKEVRVTASEKNEYKGWVLTTDPVSANIVLVNFLEDGSMSVTGIMGHAVQTVETMNEGDHRVREKLMHLFTSGDCKAYSPEDLEERKNSLKKWLEKNHIPITEQGDAPRTLCVAGVLTIDPPYGPENCSSSNEIILSRVQDLIEGHLTASQ
Protein: Cannabinoid receptor 2 (CB-2) (CB2) (rCB2) (Q9QZN9)
Organism: Rattus norvegicus (Rat)
Function: Heterotrimeric G protein-coupled receptor for endocannabinoid 2-arachidonoylglycerol mediating inhibition of adenylate cyclase. May function in inflammatory response, nociceptive transmission and bone homeostasis (By similarity).
Subcellular location: Cell membrane {ECO:0000269|PubMed:18286196}; Multi-pass membrane protein {ECO:0000269|PubMed:18286196}. Cell projection, dendrite {ECO:0000269|PubMed:18286196}. Perikaryon {ECO:0000269|PubMed:18286196}. Note=Localizes to apical dendrite of pyramidal neurons.
Interaction partners:
- Cannabinoid receptor 1
- G protein-coupled receptor 55
- Fatty-acid amide hydrolase 1
- Transient receptor potential cation channel subfamily V member 1
- Monoglyceride lipase
- Corticosteroid-binding globulin
- N-acyl-phosphatidylethanolamine-hydrolyzing phospholipase D
Sequence:
MAGCRELELTNGSNGGLEFNPMKEYMILSDAQQIAVAVLCTLMGLLSALENVAVLYLILSSQRLRRKPSYLFIGSLAGADFLASVIFACNFVIFHVFHGVDSRNIFLLKIGSVTMTFTASVGSLLLTAVDRYLCLCYPPTYKALVTRGRALVALGVMWVLSALISYLPLMGWTCCPSPCSELFPLIPNDYLLGWLLFIAILFSGIIYTYGYVLWKAHQHVASLAEHQDRQVPGIARMRLDVRLAKTLGLVMAVLLICWFPALALMGHSLVTTLSDKVKEAFAFCSMLCLVNSMINPIIYALRSGEIRSAAQHCLTGWKKYLQGLGSEGKEEAPKSSVTETEAEVKTTTGPGSRTPGCSNC
Protein: Ribonuclease P/MRP protein subunit POP5 (Q9DB28)
Organism: Mus musculus (Mouse)
Function: Component of ribonuclease P, a protein complex that generates mature tRNA molecules by cleaving their 5'-ends. Also a component of the MRP ribonuclease complex, which cleaves pre-rRNA sequences.
Subcellular location: Nucleus, nucleolus {ECO:0000250|UniProtKB:Q969H6}.
Interaction partners:
- Ribonuclease P protein subunit p29
- Ribonuclease P protein subunit p30
- Processing of 1, ribonuclease P/MRP family
- Ribonuclease P protein subunit p21
- Ribonuclease P protein subunit p25
- Ribonuclease P protein subunit p38
- Ribonuclease P protein subunit p40
- Ribonuclease P protein subunit p25-like protein
- H/ACA ribonucleoprotein complex subunit 2
- Ribonuclease P protein subunit p20
Sequence:
MVRFKHRYLLCELVSEDARCRLSLDDRVLGGLVRDTIARVHGAFGAAACSVGFAVRYLNAYTGVVLLRCRKDFYQLVWSALPFITYLENKGHRYPCFFNTLHVGGTIRTCQKFLIQYNRRQLLILLQNCTDEGEREAIKKSVSRSCLLDREPVEELSDSAGEEVAEAME
Protein: Lysosomal cobalamin transporter ABCD4 (EC 7.6.2.8) (ATP-binding cassette sub-family D member 4) (PMP70-related protein) (P70R) (Peroxisomal membrane protein 1-like) (PXMP1-L) (Peroxisomal membrane protein 69) (PMP69) (O89016)
Organism: Mus musculus (Mouse)
Function: Lysosomal membrane protein that transports cobalamin (Vitamin B12) from the lysosomal lumen to the cytosol in an ATP-dependent manner. Targeted by LMBRD1 lysosomal chaperone from the endoplasmic reticulum to the lysosomal membrane. Then forms a complex with lysosomal chaperone LMBRD1 and cytosolic MMACHC to transport cobalamin across the lysosomal membrane.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:O14678}; Multi-pass membrane protein {ECO:0000255}. Lysosome membrane {ECO:0000250|UniProtKB:O14678}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Lysosomal cobalamin transport escort protein LMBD1
- DNA repair protein RAD51 homolog 1
Sequence:
MAVPGPTARAGARPRLDLQLVQRFVRIQKVFFPSWSSQNVLMFMTLLCVTLLEQLVIYQVGLIPSQYYGVLGNKDLDGFKALTLLAVTLIVLNSTLKSFDQFTCNLLYVSWRKDLTEHLHHLYFRARVYYTLNVLRDDIDNPDQRISQDVERFCRQLSSVTSKLIISPFTLTYYTYQCFQSTGWLGPVSIFGYFIVGTMVNKTLMGPIVTKLVQQEKLEGDFRFKHMQIRVNAEPAAFYRAGLVEHMRTDRRLQRLLQTQRELMSRELWLYIGINTFDYLGSILSYVVIAIPIFSGVYGDLSPTELSTLVSKNAFVCIYLISCFTQLIDLSTTLSDVAGYTHRIGELQEALLDMSRKSQDCEALGESEWDLDKTPGCPTTEPSDTAFLLDRVSILAPSSDKPLIKDLSLKICEGQSLLITGNTGTGKTSLLRVLGGLWEGMKGSVQMLADFGPHGVLFLPQKPFFTDGTLREQVIYPLKEIYPDSGSADDERIVRFLELAGLSSLVARTGGLDQQVDWNWYDVLSPGEMQRLSFARLFYLQPKYAVLDEATSALTEEAESELYRIGQQLGMTFISVGHRPSLEKFHSWVLRLHGGGSWELTRIKLE
Protein: HIP1 protein (Q8VHU1)
Organism: Rattus norvegicus (Rat)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
Sequence:
PRAGDTGVKLEVNERILGSCTSLMQAIKVLVVASKDLQKEIVESGRGTASPKEFYAKNSRWTEGLISASKAVGWGATIMVDAADLVVQGKGKFEELMVCSHEIAASTAQLVAASKVKANKGSLNLTQLQQASRGVNQATAAVVASTISGKSQIEETDSMDFSSMTLTQIKRQEMDSQVRVLELENDLQKERQKLGELRKKHYELAGVAEGWEEGTEASPSAVQEAVPDKE