wanglab/gogpt-training-data huggingface dataset:
Protein: Inner centromere protein (P53352)
Organism: Gallus gallus (Chicken)
Function: Component of the chromosomal passenger complex (CPC), a complex that acts as a key regulator of mitosis. The CPC complex has essential functions at the centromere in ensuring correct chromosome alignment and segregation and is required for chromatin-induced microtubule stabilization and spindle assembly. Acts as a scaffold regulating CPC localization and activity. The C-terminus associates with AURKB, the N-terminus associated with BIRC5/survivin and CDCA8/borealin tethers the CPC to the inner centromere, and the microtubule binding activity within the central SAH domain directs AURKB toward substrates near microtubules. The flexibility of the SAH domain is proposed to allow AURKB to follow substrates on dynamic microtubules while ensuring CPC docking to static chromatin. Activates AURKB.
Subcellular location: Nucleus {ECO:0000269|PubMed:8408220}. Chromosome, centromere {ECO:0000269|PubMed:8408220}. Chromosome {ECO:0000269|PubMed:8408220}. Cytoplasm, cytoskeleton, spindle {ECO:0000269|PubMed:8408220}. Midbody {ECO:0000250|UniProtKB:Q9NQS7}. Chromosome, centromere, kinetochore {ECO:0000250|UniProtKB:Q9NQS7}. Note=Is restricted to the nucleus in interphase, remains tightly bound to the chromosomes until early metaphase, and during late metaphase gets concentrated in linear arrays that transect the metaphase plate between the chromosomes (PubMed:8408220). As anaphase begins to move to the spindle midzone where it is intimately associated with the bundled microtubules (PubMed:8408220). Later in anaphase gets closely associated with the cell cortex, and by telophase is concentrated at each side of the midbody in the intercellular bridge, with which it is discarded after (PubMed:8408220). {ECO:0000269|PubMed:8408220}.
Interaction partners:
- Borealin
- Aurora kinase A
- Baculoviral IAP repeat containing 5
- Borealin-2
- Serine/threonine-protein kinase PLK
- BUB1 N-terminal domain-containing protein.
- Kinetochore protein NDC80 homolog
- Nbl1_Borealin_N domain-containing protein.
- BUB1 mitotic checkpoint serine/threonine kinase
- Cell division cycle protein 20 homolog
Sequence:
MAVATGLARLPVVCNQRLAELLRQVDDVDLLWLEEIHEEAARMFGSHYSDQPELMPKTPSQKNRKRRKRPSALRGESLELGRRRLSRRRTNNLKAVSSKRDSQRLQNKEDTEGLGTEAQELSSQTVSRRLTRSQVAAPADRSEVLPEHLRERVVPVVEISVCDRISAEFQFQKCASERAENHSASLPPSSDDKSPKESSAAESQPLPAASELIVPHTPEAKGAGKNKSAFKKTANVADTTVVLSEKELGLEEVDDSAQVQKHNERDDKEPSQRTTDSPETPTGSRLSRRSVRRSLMGKPSTIRRTSLAEKYSLARKRESTIRKSIARTVIKRKAPQKLSVSSSSVNGSGSEEVPEDEETVVNAGPPPVPQTPPKLDFQGLRMSLRSQTVNRNEQQQETSNNECDLSKSEKTQEPPQSARRKTSYKRAVDQRYDTQQAEDGGLSPLRKKTPSPPCPASKVVRPFKTFLHTVEKNQLLMTPSSVGRNGVIKSFIKYNTPLQHDPKEKERQKLQALRKKEEAEQLRKQKVEEEKKRRQEEAKLRREERLRKVLQARERAEQLEEERKRRIEQKLALFDEKTEKAREERLAEEKIKKRAAAKKMEEAEARRRQDEEARKQKALQQEEEERRHKELMQKKKEEEQERARKIAEQRQAEQEREKQLAAEREQERKKEQERKKEEERIQAEKQREQQEKAARLQKEVLAAKEQLQKEMEKKEKEEQLLAEMKRQEQEQKKLPEEQKAKDVAQTQHLENKENSPACNSYQMTPQYHKDPKPPKINPNNYGMDLNSDDSTDDESQPRKPIPAWASGNQLSQAVIRQYYNPPNVDALFGTIVSPKLEDIFYKSKPRYFKRTSSAVWNSPPFPGAKSVLGLPYSLKKY
Protein: GM32356p (Q8IH21)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MMMHSRNRSWTLTLLALGVVLSTSAEDVPRSNRIAVPGEPLYYLMADAGPVVTPNEALKRTNRSLLKWWDDLFPRNNNNCCNNNNNNLLYPTAPLLPAPAVPNNCNGLQLQDLDPFKQMKLFKKLPELFPTASPCGQCGGGCGQNNYVAPAPQSPSYGGDGYGVLPNGGYTKPDTEYNGPGDGDAGYVAPAAPAYEAPAPPAPAYEAPAPPAPVYEAPAPAAPAYEAPAPAAPAYEAPAPAAPAYETPATDYSAPAPPAPAYEPPASSYTQGYSQPAQPSYVGAPPAQIVYQPIIYLSTPLASKSSTSQVEYDDQKYVTPTAPPSPPPPAPVYEAPSQSCYQPAAPPAPNYATPSCQTPIRLSLIDQPYRVAPELFEEYNYRLALASQNIL
Protein: TIM2 protein (Q9NAX2)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MSILLADIDATCAALGYSDGQKYQAEPDAAEGLKHLIWILRRDLDNHEYRRHLGRSKVLQTDLVYMLPDYVHHEELSDLLIRLLVILTNPTLLLYREGAPKDNHGRKVFMELIDILQGYKAAFAKDKVWSALFEKLKQALEIAFAIRSEEQNLLIERILVLVRNVLQVPANPEAECRADNDASLHDQVIWALHQTGMLDLVLFVISSPDEEQFHLHGLEIVCLLFREQSAESLADASLQRSLSEKQRDQQELLAARRRERARRQARPPPGRHSRFGGTYVIRNMKSVSDRDVICHQALERVSSIDFDREKQQQKRSHRHIQEEAQVTRRSAFTVRLCLREYCIEVLRSAYNTLVRQVRRVLERNAGSSSHDDSYLLWAIRFFMEFNRLSGLQLQLVSESLSVQCFHWVLTRMQHDMDMIVSDKKQARLWAKRLHVALLTFRELLQSLLALQKLKDDNNARALFDMLLNNVCYVLEYRETVLHLLMNYNEAHSTKVFLRDVVETANVFIKMMERFCQDSVVVQDKKRGGGASRKKKQAATKSKPPAAPQPTEEELSSKWAELATEVCSLLSTELEMPEDEQPLPFDAASEKSIDDQREDCMIRINKLLRSEKLDQAIALLRAAREVWPENEVFGAISAAPEDELLLLREIFMSNITTVESEDKENEKDQKQDEYEDEDDDLDNEEYEEQDNGLTEKTFKFDDFARRLLNPKIVRACTLVLSDWADIPTRSLKAAVTILHRIAYGCKCAGMLFQAKLFRIFQQVFSVERDVHQEELRRLAIFVVRKFVEVAPTNPKIYAELLFYKGIREANELESGYCDAYEAGTKGAWTEEQESELRFLFEENQRNPETDKDVIDWILDNLVDKTRNRRTVLKKLKELGLLFKAPTKRSTKSAQSGKNVWQPEEDDELRSLYDQHRIEPDCLERLVNEFAERRSKQQIIKRMLQIHLIADKSEILPAKKGRGKDKPKKDVEMEGEGDEFDFAEEPMFEDQGYKKPKSKPKKVQKRQMVRTPLDVGTIRALIGQVDSEKYQSAIEWLQECLQDASEDTEEAVEDDDGVPLLPLMENQKNAMEDGDFQKVLVALGMQPPISGMEAYWRIPIYLNSADLILRSKILAGEEVDAEPEDEAADDEDGEEAEESDEEEDFLEKHSRQRKENIATQQQRKLDSLMFNQSDDETEQRAPPKAKDKPKASEKKAKRKVKGKAKESKDCNDDGTDKAELEKPNTDDLFNQLRAKRATKIKLSDMALNESTNAAQEADDDAFNFNSEDYRARLLELEDEEQNSKDADENGGDKENITNKSLQRARRVNVIDSDSDNDDDGALPADKTNKRPRSDDDGDSGHMDANAEEDSDEEANFLARKKPAKVDGEPAKRRRLAIIDDDDEDDF
Protein: Palmitoyltransferase ZDHHC7 (EC 2.3.1.225) (Acyltransferase ZDHHC7) (EC 2.3.1.-) (Zinc finger DHHC domain-containing protein 7) (Q6DHI1)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: Golgi-localized palmitoyltransferase that catalyzes the addition of palmitate onto various protein substrates and therefore functions in several unrelated biological processes (Probable). Has no stringent fatty acid selectivity and in addition to palmitate can also transfer onto target proteins myristate from tetradecanoyl-CoA and stearate from octadecanoyl-CoA (Probable).
Subcellular location: Golgi apparatus membrane {ECO:0000250|UniProtKB:Q91WU6}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Estrogen receptor 2b
- Estrogen receptor
Sequence:
MQSSGQRLRDVEQHQPLLSGGEEEVTAGRVWFIQDSCGMVCAFMTWSLVMYAEFVVNFVMLLPSKNFWYTLINGVAFNFLAVLALTSHLRTMLTDPGAVPKGNATKEYMESLQLKPGEVIYKCPKCCSIKPERAHHCSICKRCIRKMDHHCPWVNNCVGENNQRFFVLFTMYIASISLHALCLSGFHFFTCVKVQWNECSDFSPPVAVMLLIFLCLEALLFLTFTAVMFGTQIHSICNDETEIERLKNEKPTWERRVRWDGMKAVFGGPPSLLWFNPFAGLRLRMLMVRARRSGAEFSV
Protein: Heat shock transcription factor 4 (A0A8I6AKB5)
Organism: Rattus norvegicus (Rat)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MQEAPAALPTEPGPSPVPAFLGKLWALVGDPGTDHLIRWSPSGTSFLVSDQSRFAKEVLPQYFKHSNMASFVRQLNMYGFRKVVSIEQGGLLRPERDHVEFQHPSFVRGCEQLLERVRRKVPALRGDDTRWRPEDLGRLLGEVQALRGVQESTEARLQELRQQNEILWREVVTLRQSHSQQHRVIGKLIQCLFGPLQTGPSSTGAKRKLSLMLDEGSACSASAKFNACPVSGALLQDPYFIQSPLPETTVGLSPHRARGPIISDIPEDCPSPEGHRLSPSSAGRRGTLGLDRGNRSPESLLPPVLLRPPPETVEPMDALGPSLHGREWTLMDLDMELSLMQPLAPERAEAELTVKDLTSSGVGKDHTLGTPLMLDVQADLEGAALSVPGALTLYNATESNASYLDPGASPSSP
Protein: Alginate biosynthesis protein AlgA [Includes: Mannose-6-phosphate isomerase (EC 5.3.1.8) (Phosphohexomutase) (Phosphomannose isomerase) (PMI); Mannose-1-phosphate guanylyltransferase (EC 2.7.7.13) (GDP-mannose pyrophosphorylase) (GMP) (GMPP) (GTP--mannose-1-phosphate guanylyltransferase)] (P07874)
Organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Function: Produces a precursor for alginate polymerization. The alginate layer provides a protective barrier against host immune defenses and antibiotics.
Interaction partners:
- GDP-mannose 6-dehydrogenase
- Phosphomannomutase/phosphoglucomutase
- Probable alginate O-acetylase AlgJ
- Alginate lyase
- Alginate production protein AlgE
- Mannuronan synthase
- Mannuronan C5-epimerase
- Alginate biosynthesis protein AlgF
- Mannuronan synthase
- Probable alginate O-acetylase AlgI
Sequence:
MIPVILSGGSGSRLWPLSRKQYPKQFLALTGDDTLFQQTIKRLAFDGMQAPLLVCNKEHRFIVQEQLEAQNLASQAILLEPFGRNTAPAVAIAAMKLVAEGRDELLLILPADHVIEDQRAFQQALALATNAAEKGEMVLFGIPASRPETGYGYIRASADAQLPEGVSRVQSFVEKPDEARAREFVAAGGYYWNSGMFLFRASRYLEELKKHDADIYDTCLLALERSQHDGDLVNIDAATFECCPDNSIDYAVMEKTSRACVVPLSAGWNDVGSWSSIWDVHAKDANGNVTKGDVLVHDSHNCLVHGNGKLVSVIGLEDIVVVETKDAMMIAHKDRVQDVKHVVKDLDAQGRSETQNHCEVYRPWGSYDSVDMGGRFQVKHITVKPGARLSLQMHHHRAEHWIVVSGTAQVTCDDKTFLLTENQSTYIPIASVHRLANPGKIPLEIIEVQSGSYLGEDDIERLEDVYGRTAEPALQVVAGSR
Protein: Synaptosomal-associated protein 29 (SNAP-29) (Golgi SNARE of 32 kDa) (Gs32) (Soluble 29 kDa NSF attachment protein) (Vesicle-membrane fusion protein SNAP-29) (Q9ERB0)
Organism: Mus musculus (Mouse)
Function: SNAREs, soluble N-ethylmaleimide-sensitive factor-attachment protein receptors, are essential proteins for fusion of cellular membranes. SNAREs localized on opposing membranes assemble to form a trans-SNARE complex, an extended, parallel four alpha-helical bundle that drives membrane fusion. SNAP29 is a SNARE involved in autophagy through the direct control of autophagosome membrane fusion with the lysososome membrane. Also plays a role in ciliogenesis by regulating membrane fusions.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:O95721}. Golgi apparatus membrane {ECO:0000250|UniProtKB:Q9Z2P6}; Peripheral membrane protein {ECO:0000305}. Cytoplasmic vesicle, autophagosome membrane {ECO:0000269|PubMed:27628032}; Peripheral membrane protein {ECO:0000305}. Cell projection, cilium membrane {ECO:0000250|UniProtKB:O95721}; Peripheral membrane protein {ECO:0000305}. Note=Appears to be mostly membrane-bound, probably via interaction with syntaxins, but a significant portion is cytoplasmic. Localizes to the ciliary pocket from where the cilium protrudes. {ECO:0000250|UniProtKB:O95721}.
Interaction partners:
- Vesicle-associated membrane protein 7
- Vesicle-associated membrane protein 8
- Syntaxin-17
- Beclin 1-associated autophagy-related key regulator
- Syntaxin-7
- Syntaxin-6
- Synaptobrevin homolog YKT6
- Syntaxin-3
- Syntaxin-4
- Synaptosomal-associated protein 23
Sequence:
MSGYPKSYNPFDDDVEEEDTRPAPWKDVRDLPDGPDAPIDRQQYLRQEVLRRAEATAASTSRSLSLMYESEKIGVASSEELVRQRGVLEHTEKMVDKMDQDLKMSQKHINSIKSVFGGFINYFKSKPVEPPPEQNGSIVSQPNSRLKEAINTSKDQENKYQASHPNLRRLQDAELDSVPKEPSSTVNTEVYPKNSTLRTYHQKIDSNLDELSVGLGHLKDIALGMQTEIEEQDDILDRLTTKVDKLDVNIKSTEKKVRQL
Protein: Harmonin (Usher syndrome 1C) (Q29RC0)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Cell projection {ECO:0000256|ARBA:ARBA00004316}.
Interaction partners:
- Cadherin-related 23.
- Usher syndrome 1Gb
- Myosin VIIAa
- Cadherin-related 23
- Protocadherin-15
- Protocadherin-related 15b.
- Myosin VIIAb
- Usher syndrome 2A
- Adhesion G-protein coupled receptor V1
- Clarin 1
Sequence:
MERKVAREFRHKVELLIDNEAEKDYLYDVLRMYHQSMDLPVLVGDLKLVINEPKRLPLFDAIRPLIPLKHQVQYDQLTPKRSRKLKEVRLDRTHPEGLGLSVRGGLEFGSGLFISQIVKDGQAGNVGLQVGDEIVRINGYSISSCIHEEVINLIKTKKTVSLKVRHVGMIPVKSSSDEPLKWQFVDQFVSESGEKSNSIAGLASIGGNEIKEKKVFLSLVGTKGMGISISSGPTKKPGIYVSNVKPGSLSAEVGLQVGDQIVEVNGVEFTNLSHQEAVRVLKSSRSLTITVLTGAGSELFMTDEERLAVEARHELDRQELMHQKKVALETNKIVKEQQEKERQRKMEISQKAAEEEERYRKEMERIEAAEKKHHKEWEDDWGSKEKKKSVSPAASPSPPPPTRLAPSPKPKTSTADSYEEETGEGFQKYVDDFDPHSMFTAEQIAGRDVRLLRIKKEGKLDLAIEGGIDSPLGKIVVSSIYEGGAADKHGGVVSGDEIMAVNGKILTDVTLAEGQTSMAQAWNSGGDWIDLVIAVSPPKEYEDEVTFF
Protein: Bifunctional heparan sulfate N-deacetylase/N-sulfotransferase 3 (EC 2.8.2.8) (Glucosaminyl N-deacetylase/N-sulfotransferase 3) (NDST-3) (N-heparan sulfate sulfotransferase 3) (N-HSST 3) [Includes: Heparan sulfate N-deacetylase 3 (EC 3.-.-.-); Heparan sulfate N-sulfotransferase 3 (EC 2.8.2.-)] (Q9EQH7)
Organism: Mus musculus (Mouse)
Function: Essential bifunctional enzyme that catalyzes both the N-deacetylation and the N-sulfation of glucosamine (GlcNAc) of the glycosaminoglycan in heparan sulfate. Modifies the GlcNAc-GlcA disaccharide repeating sugar backbone to make N-sulfated heparosan, a prerequisite substrate for later modifications in heparin biosynthesis. Has high deacetylase activity but low sulfotransferase activity.
Subcellular location: Golgi apparatus membrane {ECO:0000250}; Single-pass type II membrane protein {ECO:0000250}.
Interaction partners:
- Heparan sulfate 2-O-sulfotransferase 1
- D-glucuronyl C5-epimerase
Sequence:
MSFIMKPHRHFQRTLILLATFCMVSIIISAYYLYSGYKQESEVSGRASEVDCGDLQHIPSRLMEVRRTMISDASRTDPTVLVFVESQYSSLGQDIIMMLESIRFHYHTEIAPGKGDLPALTDNVKGKYVLIIYENILKYINMDSWNRSLLDKYCIEYGVGIIGFHKTSEKNLQSFQFRGFPFSISGNLAVKDCCINPHSPLLRVTKSSKLDRGSLPGTDWTVFQINHSTYQPVIFAKVKTPENLSPPISKHAFYATIIHDLGLHDGIQRVLFGNNLNFWLHKLIFIDAISFLSGKRLTLSLDRYILVDIDDIFVGKEGTRMNTNDVKALLDTQNLLRTQITNFTFNLGFSGKFYHTGTEEEDEGDDCLLGSVDEFWWFPHMWSHMQPHLFHNESSLIEQMILNKKFALEHGIPTDMGYAVSPHHSGVYPVHVQLYEAWKKVWNIKITSTEEYPHLKPARYRRGFIHKNIMVLPRQTCGLFTHTIFYKEYPGGPRELDKSIHGGELFFTVVLNPISIFMTHLSNYGNDRLGLYTFVNLANFVQTWTNLRLQTLPPAQLAHKYFELFPDQKDPLWQNPCDDKRHRDIWSKEKTCDRLPKFLVIGPQKTGTTALCLFLIMHPSILSNSPSPKSFEEVQFFNRNNYHRGIDWYMDFFPVPSNVTTDFLFEKSANYFHSEDAPKRAASLVPKAKIITILIDPSDRAYSWYQHQRSHEDPAALKFSFYEVISAGPNAPWELRTLQKRCLVPGWYANHIERWLVYFPPFQLLIIDGQHLRTTPATVMDEVQKFLGVSPHYNYSEALTFDSHKGFWCQLLEEGKTKCLGKSKGRKYPPMDSDSRAFLSSYYRDHNVELSKLLHRLGQPLPSWLRQELQKVR
Protein: DDB1- and CUL4-associated factor 12 (Centrosome-related protein TCC52) (Testis cancer centrosome-related protein) (WD repeat-containing protein 40A) (Q5T6F0)
Organism: Homo sapiens (Human)
Function: Substrate-recognition component of a DCX (DDB1-CUL4-X-box) E3 ubiquitin-protein ligase complex of the DesCEND (destruction via C-end degrons) pathway, which recognizes a C-degron located at the extreme C terminus of target proteins, leading to their ubiquitination and degradation. The C-degron recognized by the DesCEND pathway is usually a motif of less than ten residues and can be present in full-length proteins, truncated proteins or proteolytically cleaved forms. The DCX(DCAF12) complex specifically recognizes proteins with a diglutamate (Glu-Glu) at the C-terminus, such as MAGEA3, MAGEA6 and CCT5, leading to their ubiquitination and degradation. Ubiquitination of MAGEA3, MAGEA6 by DCX(DCAF12) complex is required for starvation-induced autophagy. Also directly recognizes the C-terminal glutamate-leucine (Glu-Leu) degron as an alternative degron in proteins such as MOV10, leading to their ubiquitination and degradation. Controls the protein level of MOV10 during spermatogenesis and in T cells, especially after their activation.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:18957058, ECO:0000269|PubMed:34065512}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000269|PubMed:18957058}. Nucleus {ECO:0000269|PubMed:34065512}.
Interaction partners:
- DNA damage-binding protein 1
- Cullin-4A
- DDB1- and CUL4-associated factor 4
- Cullin-4B
- DDB1- and CUL4-associated factor 5
- DDB1- and CUL4-associated factor 6
- DDB1- and CUL4-associated factor 11
- DNA damage-binding protein 2
- DDB1- and CUL4-associated factor 10
- DDB1- and CUL4-associated factor 8
Sequence:
MARKVVSRKRKAPASPGAGSDAQGPQFGWDHSLHKRKRLPPVKRSLVYYLKNREVRLQNETSYSRVLHGYAAQQLPSLLKEREFHLGTLNKVFASQWLNHRQVVCGTKCNTLFVVDVQTSQITKIPILKDREPGGVTQQGCGIHAIELNPSRTLLATGGDNPNSLAIYRLPTLDPVCVGDDGHKDWIFSIAWISDTMAVSGSRDGSMGLWEVTDDVLTKSDARHNVSRVPVYAHITHKALKDIPKEDTNPDNCKVRALAFNNKNKELGAVSLDGYFHLWKAENTLSKLLSTKLPYCRENVCLAYGSEWSVYAVGSQAHVSFLDPRQPSYNVKSVCSRERGSGIRSVSFYEHIITVGTGQGSLLFYDIRAQRFLEERLSACYGSKPRLAGENLKLTTGKGWLNHDETWRNYFSDIDFFPNAVYTHCYDSSGTKLFVAGGPLPSGLHGNYAGLWS
Protein: Cd155 (Poliovirus receptor) (Q91WP1)
Organism: Mus musculus (Mouse)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004479}.
Interaction partners:
Sequence:
MAQLARATRSPLSWLLLLFCYALRKAGGDIRVLVPYNSTGVLGGSTTLHCSLTSNENVTITQITWMKKDSGGSHALVAVFHPKKGPNIKEPERVKFLAAQQDLRNASLAISNLSVEDEGIYECQIATFPRGSRSTNAWLKVQARPKNTAEALEPSPTLILQDVAKCISANGHPPGRISWPSNVNGSHREMKEPGSQPGTTTVTSYLSMVPSRQADGKNITCTVEHESLQELDQLLVTLSQPYPPENVSISGYDGNWYVGLTNLTLTCEAHSKPAPDMAGYNWSTTTGDFPNSVKRQGNMLLISTVEDGLNNTVIVCEVTNALGSGQGQVHIIVKEKPENMQQNTRLHLGYIFLIVFVLAVVIIIAALYTIRRCRHGRALQSNPSERENVQYSSVNGDCRLNMEPNSTR
Protein: Apelin receptor (Angiotensin receptor-like 1) (G-protein coupled receptor APJ) (G-protein coupled receptor HG11) (P35414)
Organism: Homo sapiens (Human)
Function: Receptor for apelin receptor early endogenous ligand (APELA) and apelin (APLN) hormones coupled to G proteins that inhibit adenylate cyclase activity. Plays a key role in early development such as gastrulation, blood vessels formation and heart morphogenesis by acting as a receptor for APELA hormone (By similarity). May promote angioblast migration toward the embryonic midline, i.e. the position of the future vessel formation, during vasculogenesis (By similarity). Promotes sinus venosus (SV)-derived endothelial cells migration into the developing heart to promote coronary blood vessel development (By similarity). Also plays a role in various processes in adults such as regulation of blood vessel formation, blood pressure, heart contractility and heart failure.
Subcellular location: Cell membrane {ECO:0000269|PubMed:25639753, ECO:0000269|PubMed:35817871, ECO:0000269|PubMed:38428423}. Note=After exposure to apelin (APLN), internalized from the cell surface into an endosomal recycling compartment, from where it is recycled to the cell membrane (By similarity). After exposure to apelin receptor early endogenous ligand (APELA), internalized from the cell surface into an endosomal recycling compartment, from where it is recycled to the cell membrane (PubMed:25639753). {ECO:0000250|UniProtKB:Q9JHG3, ECO:0000269|PubMed:25639753}.
Interaction partners:
- Apelin
- Apelin receptor early endogenous ligand
- Guanine nucleotide-binding protein subunit beta-4
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein subunit beta-5
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein subunit alpha-13
- Guanine nucleotide-binding protein G
Sequence:
MEEGGDFDNYYGADNQSECEYTDWKSSGALIPAIYMLVFLLGTTGNGLVLWTVFRSSREKRRSADIFIASLAVADLTFVVTLPLWATYTYRDYDWPFGTFFCKLSSYLIFVNMYASVFCLTGLSFDRYLAIVRPVANARLRLRVSGAVATAVLWVLAALLAMPVMVLRTTGDLENTTKVQCYMDYSMVATVSSEWAWEVGLGVSSTTVGFVVPFTIMLTCYFFIAQTIAGHFRKERIEGLRKRRRLLSIIVVLVVTFALCWMPYHLVKTLYMLGSLLHWPCDFDLFLMNIFPYCTCISYVNSCLNPFLYAFFDPRFRQACTSMLCCGQSRCAGTSHSSSGEKSASYSSGHSQGPGPNMGKGGEQMHEKSIPYSQETLVVD
Protein: Neuron-specific calcium-binding protein hippocalcin (Calcium-binding protein BDR-2) (P84074)
Organism: Homo sapiens (Human)
Function: Calcium-binding protein that may play a role in the regulation of voltage-dependent calcium channels. May also play a role in cyclic-nucleotide-mediated signaling through the regulation of adenylate and guanylate cyclases (By similarity).
Subcellular location: Cytoplasm, cytosol {ECO:0000250|UniProtKB:P84076, ECO:0000269|PubMed:28398555}. Membrane {ECO:0000250|UniProtKB:P84076}; Peripheral membrane protein {ECO:0000250|UniProtKB:P84076}. Note=Association with membranes is calcium-dependent (By similarity). Enriched in the perinuclear region, probably at the trans Golgi network in response to calcium (PubMed:28398555). {ECO:0000250|UniProtKB:P84076, ECO:0000269|PubMed:28398555}.
Interaction partners:
- Voltage-gated potassium channel KCNC1
- Arylsulfatase A
- Torsin-1A
- THAP domain-containing protein 1
- A-type voltage-gated potassium channel KCND3
- AP-2 complex subunit beta
Sequence:
MGKQNSKLRPEMLQDLRENTEFSELELQEWYKGFLKDCPTGILNVDEFKKIYANFFPYGDASKFAEHVFRTFDTNSDGTIDFREFIIALSVTSRGRLEQKLMWAFSMYDLDGNGYISREEMLEIVQAIYKMVSSVMKMPEDESTPEKRTEKIFRQMDTNNDGKLSLEEFIRGAKSDPSIVRLLQCDPSSASQF
Protein: High affinity cGMP-specific 3',5'-cyclic phosphodiesterase 9A (EC 3.1.4.35) (O70628)
Organism: Mus musculus (Mouse)
Function: Specifically hydrolyzes the second messenger cGMP, which is a key regulator of many important physiological processes. Highly specific: compared to other members of the cyclic nucleotide phosphodiesterase family, has the highest affinity and selectivity for cGMP. Specifically regulates natriuretic-peptide-dependent cGMP signaling in heart, acting as a regulator of cardiac hypertrophy in myocytes and muscle. Does not regulate nitric oxide-dependent cGMP in heart. Additional experiments are required to confirm whether its ability to hydrolyze natriuretic-peptide-dependent cGMP is specific to heart or is a general feature of the protein (Probable). In brain, involved in cognitive function, such as learning and long-term memory.
Subcellular location: Cell projection, ruffle membrane {ECO:0000250|UniProtKB:O76083}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:O76083}. Golgi apparatus {ECO:0000250|UniProtKB:O76083}. Endoplasmic reticulum {ECO:0000250|UniProtKB:O76083}. Cell membrane, sarcolemma {ECO:0000250|UniProtKB:O76083}.
Interaction partners:
- Adenine phosphoribosyltransferase
- Hypoxanthine-guanine phosphoribosyltransferase
- Guanylate kinase
- Inosine triphosphate pyrophosphatase
- GMP synthase
- Guanylate cyclase soluble subunit alpha-2
- Guanylate cyclase soluble subunit alpha-1
- Guanylate cyclase soluble subunit beta-1
- Atrial natriuretic peptide receptor 1
- Atrial natriuretic peptide receptor 2
Sequence:
MGAGSSSYRPKAIYLDIDGRIQKVVFSKYCNSSDIMDLFCIATGLPRNTTISLLTTDDAMVSIDPTMPANSERTPYKVRPVAVKQVSEREELIQGVLAQVAEQFSRAFKINELKAEVANHLAVLEKRVELEGLKVVEIEKCKSDIKKMREELAARNSRTNCPCKYSFLDNKKLTPRRDVPTYPKYLLSPETIEALRKPTFDVWLWEPNEMLSCLEHMYHDLGLVRDFSINPITLRRWLLCVHDNYRNNPFHNFRHCFCVTQMMYSMVWLCGLQEKFSQMDILVLMTAAICHDLDHPGYNNTYQINARTELAVRYNDISPLENHHCAIAFQILARPECNIFASVPPEGFRQIRQGMITLILATDMARHAEIMDSFKEKMENFDYSNEEHLTLLKMILIKCCDISNEVRPMEVAEPWVDCLLEEYFMQSDREKSEGLPVAPFMDRDKVTKATAQIGFIKFVLIPMFETVTKLFPVVEETMLRPLWESREHYEELKQLDDAMKELQKKTESLTSGAPENTTEKNRDAKDSEGHSPPN
Protein: Protein farnesyltransferase subunit beta (FTase-beta) (EC 2.5.1.58) (CAAX farnesyltransferase subunit beta) (Ras proteins prenyltransferase subunit beta) (Q8K2I1)
Organism: Mus musculus (Mouse)
Function: Essential subunit of the farnesyltransferase complex. Catalyzes the transfer of a farnesyl moiety from farnesyl diphosphate to a cysteine at the fourth position from the C-terminus of several proteins having the C-terminal sequence Cys-aliphatic-aliphatic-X.
Interaction partners:
- Protein farnesyltransferase/geranylgeranyltransferase type-1 subunit alpha
- CAAX prenyl protease 2
- CAAX prenyl protease 1 homolog
- Geranylgeranyl pyrophosphate synthase
- All trans-polyprenyl-diphosphate synthase PDSS1
- Farnesyl pyrophosphate synthase
- Dehydrodolichyl diphosphate synthase complex subunit Dhdds
- Dehydrodolichyl diphosphate synthase complex subunit Nus1
- All trans-polyprenyl-diphosphate synthase PDSS2
- Protein Churchill
Sequence:
MASSSSFTYYCPPSSSPVWSEPLYSLRPEHVRERLQDDSVETVTSIEQAKVEEKIQEVFSSYKFNHLVPRLILQREKHFHYLKRGLRQLTDAYECLDASRPWLCYWILHSLELLDEPIPQIVATDVCQFLELCQSPDGGFGGGPGQYPHLAPTYAAVNALCIIGTEEAYNVINREKLLQYLYSLKQPDGSFLMHVGGEVDVRSAYCAASVASLTNIITPDLFEGTAEWIARCQNWEGGIGGVPGMEAHGGYTFCGLAALVILKKERSLNLKSLLQWVTSRQMRFEGGFQGRCNKLVDGCYSFWQAGLLPLLHRALHAQGDPALSMSHWMFHQQALQEYILMCCQCPAGGLLDKPGKSRDFYHTCYCLSGLSIAQHFGSGAMLHDMVMGVPENVLQPTHPVYNIGPEKVIQATTHFLQKPVPGFEECEDEVTSDPATD
Protein: C-C motif chemokine 4 (G-26 T-lymphocyte-secreted protein) (HC21) (Lymphocyte activation gene 1 protein) (LAG-1) (MIP-1-beta(1-69)) (Macrophage inflammatory protein 1-beta) (MIP-1-beta) (PAT 744) (Protein H400) (SIS-gamma) (Small-inducible cytokine A4) (T-cell activation protein 2) (ACT-2) [Cleaved into: MIP-1-beta(3-69)] (P13236)
Organism: Homo sapiens (Human)
Function: Monokine with inflammatory and chemokinetic properties. Binds to CCR5. One of the major HIV-suppressive factors produced by CD8+ T-cells. Recombinant MIP-1-beta induces a dose-dependent inhibition of different strains of HIV-1, HIV-2, and simian immunodeficiency virus (SIV). The processed form MIP-1-beta(3-69) retains the abilities to induce down-modulation of surface expression of the chemokine receptor CCR5 and to inhibit the CCR5-mediated entry of HIV-1 in T-cells. MIP-1-beta(3-69) is also a ligand for CCR1 and CCR2 isoform B.
Subcellular location: Secreted.
Interaction partners:
- C-C chemokine receptor type 2
- C-C chemokine receptor type 5
- C-C chemokine receptor type 1
- C-C chemokine receptor type 3
- C-C motif chemokine 3
- C-C chemokine receptor type 7
- C-X-C chemokine receptor type 4
- C-X-C chemokine receptor type 3
- Interleukin-8
- C-C chemokine receptor type 8
Sequence:
MKLCVTVLSLLMLVAAFCSPALSAPMGSDPPTACCFSYTARKLPRNFVVDYYETSSLCSQPAVVFQTKRSKQVCADPSESWVQEYVYDLELN