A0A8Q3SHH2 · A0A8Q3SHH2_HUMAN
- ProteinGolgin B1
- GeneGOLGB1
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids3101 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score1/5
Function
GO annotations
all annotations | all molecular function | virus receptor activity | dna binding | rna binding | cytoskeletal motor activity | catalytic activity | gtpase activity | structural molecule activity | transporter activity | cytoskeletal protein binding | lipid binding | cyclase activity | antioxidant activity | oxidoreductase activity | transferase activity | hydrolase activity | lyase activity | isomerase activity | ligase activity | protein tag activity | cargo receptor activity | histone binding | protein folding chaperone | translation regulator activity | nutrient reservoir activity | receptor ligand activity | molecular transducer activity | molecular adaptor activity | toxin activity | cell adhesion mediator activity | molecular function regulator activity | virus coreceptor activity | catalytic activity, acting on a protein | catalytic activity, acting on dna | catalytic activity, acting on rna | molecular carrier activity | transcription regulator activity | general transcription initiation factor activity | molecular sensor activity | molecular sequestering activity | atp-dependent activity | other molecular function | all biological process | mitotic cell cycle | cytokinesis | cytoplasmic translation | immune system process | muscle system process | circulatory system process | renal system process | respiratory system process | carbohydrate metabolic process | generation of precursor metabolites and energy | dna replication | dna repair | dna recombination | chromatin organization | dna-templated transcription | regulation of dna-templated transcription | trna metabolic process | protein folding | protein glycosylation | amino acid metabolic process | modified amino acid metabolic process | lipid metabolic process | vitamin metabolic process | sulfur compound metabolic process | intracellular protein transport | nucleocytoplasmic transport | autophagy | inflammatory response | mitochondrion organization | cytoskeleton organization | microtubule-based movement | peroxisome organization | lysosome organization | chromosome segregation | cell adhesion | establishment or maintenance of cell polarity | programmed cell death | photosynthesis | mrna metabolic process | snrna metabolic process | vesicle-mediated transport | reproductive process | digestive system process | signaling | cell differentiation | protein catabolic process | extracellular matrix organization | regulatory ncrna-mediated gene silencing | telomere organization | cell junction organization | wound healing | ribosome biogenesis | cilium organization | anatomical structure development | cell motility | nervous system process | endocrine process | protein maturation | transmembrane transport | nucleobase-containing small molecule metabolic process | hepaticobiliary system process | membrane organization | protein-containing complex assembly | cell wall organization or biogenesis | nitrogen cycle metabolic process | protein localization to plasma membrane | defense response to other organism | detoxification | meiotic nuclear division | mitotic nuclear division | mitochondrial gene expression | carbohydrate derivative metabolic process | other biological process | all cellular component | nuclear chromosome | extracellular region | extracellular space | cell wall | nucleus | nuclear envelope | nucleoplasm | chromosome | nucleolus | mitochondrion | lysosome | endosome | vacuole | peroxisome | endoplasmic reticulum | golgi apparatus | lipid droplet | microtubule organizing center | cytosol | ribosome | cytoskeleton | plasma membrane | cilium | plastid | thylakoid | external encapsulating structure | extracellular matrix | cytoplasmic vesicle | organelle | other cellular component | |||
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Aspect | Term | |
---|---|---|
Cellular Component | Golgi apparatus | |
Molecular Function | sequence-specific DNA binding | |
Biological Process | regulation of DNA-templated transcription |
Names & Taxonomy
Protein names
- Submitted names
Gene names
Organism names
- Organism
- Taxonomic lineagecellular organisms > Eukaryota (eucaryotes) > Opisthokonta > Metazoa (metazoans) > Eumetazoa > Bilateria > Deuterostomia > Chordata (chordates) > Craniata > Vertebrata (vertebrates) > Gnathostomata (jawed vertebrates) > Teleostomi > Euteleostomi (bony vertebrates) > Sarcopterygii > Dipnotetrapodomorpha > Tetrapoda (tetrapods) > Amniota (amniotes) > Mammalia (mammals) > Theria > Eutheria (placentals) > Boreoeutheria > Euarchontoglires > Primates > Haplorrhini > Simiiformes > Catarrhini > Hominoidea (apes) > Hominidae (great apes) > Homininae > Homo
Accessions
- Primary accessionA0A8Q3SHH2
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Disease & Variants
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 2,538 variants from UniProt as well as other sources including ClinVar and dbSNP.
Genetic variation databases
PTM/Processing
Features
Showing features for modified residue (large scale data).
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Modified residue (large scale data) | 6 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 17 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 38 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 133 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 138 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 139 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 490 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 524 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 527 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 537 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 538 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 542 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 559 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 630 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 652 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 670 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 672 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 868 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 966 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1132 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1147 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1259 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 1567 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1750 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1752 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1791 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1935 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1955 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1965 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 2215 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 2588 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 2734 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 2870 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 2871 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 2877 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 2883 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 3004 | PRIDE | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue (large scale data) | 3009 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 3012 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 3015 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 3036 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 3055 | PRIDE | Phosphoserine | ||||
Sequence: S |
Structure
Family & Domains
Features
Showing features for coiled coil, region, domain, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Coiled coil | 64-99 | |||||
Sequence: LKDIIRQKDVQLQQKDEALQEERKAADNKIKKLKLH | ||||||
Region | 119-142 | Disordered | ||||
Sequence: GTVLPTEPQSEEQLSKHDKSSTEE | ||||||
Coiled coil | 246-513 | |||||
Sequence: ETEMQQKLRVLQRKLEEHEESLVGRAQVVDLLQQELTAAEQRNQILSQQLQQMEAEHNTLRNTVETEREESKILLEKMELEVAERKLSFHNLQEEMHHLLEQFEQAGQAQAELESRYSALEQKHKAEMEEKTSHILSLQKTGQELQSACDALKDQNSKLLQDKNEQAVQSAQTIQQLEDQLQQKSKEISQFLNRLPLQQHETASQTSFPDVYNEGTQAVTEENIASLQKRVVELENEKGALLLSSIELEELKAENEKLSSQITLLEAQ | ||||||
Coiled coil | 558-585 | |||||
Sequence: LSVLLLEMKEAQEEIAFLKLQLQGKRAE | ||||||
Region | 629-651 | Disordered | ||||
Sequence: SSLPAVEKEQASTEHQSRTSEEI | ||||||
Coiled coil | 678-730 | |||||
Sequence: GQCHQDELERLKSQILELELNFHKAQEIYEKNLDEKAKEISNLNQLIEEFKKN | ||||||
Coiled coil | 804-901 | |||||
Sequence: AKSKDVKIEVLQNELDDVQLQFSEQSTLIRSLQSQLQNKESEVLEGAERVRHISSKVEELSQALSQKELEITKMDQLLLEKKRDVETLQQTIEEKDQQ | ||||||
Coiled coil | 927-1025 | |||||
Sequence: IKTLKEQLNLLSRAEEAKKEQVEEDNEVSSGLKQNYDEMSPAGQISKEELQHEFDLLKKENEQRKRKLQAALINRKELLQRVSRLEEELANLKDESKKE | ||||||
Coiled coil | 1065-1120 | |||||
Sequence: ISEKEVELQHIRKDLEEKLAAEEQFQALVKQMNQTLQDKTNQIDLLQAEISENQAI | ||||||
Coiled coil | 1158-1238 | |||||
Sequence: KPELEEKILALEKEKEQLQKKLQEALTSRKAILKKAQEKERHLREELKQQKDDYNRLQEQFDEQSKENENIGDQLRQLQIQ | ||||||
Coiled coil | 1303-1330 | |||||
Sequence: VAQIKAQLKEIEAEKVELELKVSSTTSE | ||||||
Coiled coil | 1366-1406 | |||||
Sequence: AESLQQKLESSQLQIAGLEHLRELQPKLDELQKLISKKEED | ||||||
Domain | 1567-1605 | Leucine zipper homeobox-associated | ||||
Sequence: SCESLKLALEGLTEDKEKLVKEIESLKSSKIAESTEWQE | ||||||
Domain | 1728-1771 | Leucine zipper homeobox-associated | ||||
Sequence: ERVKMEYETLSKKFQSLMSEKDSLSEEVQDLKHQIEGNVSKQAN | ||||||
Compositional bias | 1746-1761 | Basic and acidic residues | ||||
Sequence: SEKDSLSEEVQDLKHQ | ||||||
Region | 1746-1828 | Disordered | ||||
Sequence: SEKDSLSEEVQDLKHQIEGNVSKQANLEATEKHDNQTNVTEEGTQSIPGETEEQDSLSMSTRPTCSESVPSAKSANPAVSKDF | ||||||
Compositional bias | 1784-1828 | Polar residues | ||||
Sequence: VTEEGTQSIPGETEEQDSLSMSTRPTCSESVPSAKSANPAVSKDF | ||||||
Coiled coil | 1834-2436 | |||||
Sequence: INNYLQQIDQLKERIAGLEEEKQKNKEFSQTLENEKNTLLSQISTKDGELKMLQEEVTKMNLLNQQIQEELSRVTKLKETAEEEKDDLEERLMNQLAELNGSIGNYCQDVTDAQIKNELLESEMKNLKKCVSELEEEKQQLVKEKTKVESEIRKEYLEKIQGAQKEPGNKSHAKELQELLKEKQQEVKQLQKDCIRYQEKISALERTVKALEFVQTESQKDLEITKENLAQAVEHRKKAQAELASFKVLLDDTQSEAARVLADNLKLKKELQSNKESVKSQMKQKDEDLERRLEQAEEKHLKEKKNMQEKLDALRREKVHLEETIGEIQVTLNKKDKEVQQLQENLDSTVTQLAAFTKSMSSLQDDRDRVIDEAKKWERKFSDAIQSKEEEIRLKEDNCSVLKDQLRQMSIHMEELKINISRLEHDKQIWESKAQTEVQLQQKVCDTLQGENKELLSQLEETRHLYHSSQNELAKLESELKSLKDQLTDLSNSLEKCKEQKGNLEGIIRQQEADIQNSKFSYEQLETDLQASRELTSRLHEEINMKEQKIISLLSGKEEAIQVAIAELRQQHDKEIKELENLLSQEEEENIVLEEENKKAVDK | ||||||
Domain | 2267-2308 | Leucine zipper homeobox-associated | ||||
Sequence: AQTEVQLQQKVCDTLQGENKELLSQLEETRHLYHSSQNELAK | ||||||
Coiled coil | 2465-2773 | |||||
Sequence: MSSLQNDRDRIVGDYQQLEERHLSIILEKDQLIQEAAAENNKLKEEIRGLRSHMDDLNSENAKLDAELIQYREDLNQVITIKDSQQKQLLEVQLQQNKELENKYAKLEEKLKESEEANEDLRRSFNALQEEKQDLSKEIESLKVSISQLTRQVTALQEEGTLGLYHAQLKVKEEEVHRLSALFSSSQKRIAELEEELVCVQKEAAKKVGEIEDKLKKELKHLHHDAGIMRNETETAEERVAELARDLVEMEQKLLMVTKENKGLTAQIQSFGRSMSSLQNSRDHANEELDELKRKYDASLKELAQLKEQ | ||||||
Domain | 2576-2618 | Leucine zipper homeobox-associated | ||||
Sequence: KESEEANEDLRRSFNALQEEKQDLSKEIESLKVSISQLTRQVT | ||||||
Coiled coil | 2802-2843 | |||||
Sequence: LEKLNQQLLSKDEQLLHLSSQLEDSYNQVQSFSKAMASLQNE | ||||||
Region | 2855-2875 | Disordered | ||||
Sequence: RKSEEGKQRSAAQPSTSPAEV | ||||||
Coiled coil | 2875-2993 | |||||
Sequence: VQSLKKAMSSLQNDRDRLLKELKNLQQQYLQINQEITELHPLKAQLQEYQDKTKAFQIMQEELRQENLSWQHELHQLRMEKSSWEIHERRMKEQYLMAISDKDQQLSHLQNLIRELRSS | ||||||
Region | 2997-3020 | Disordered | ||||
Sequence: TQPLKVQYQRQASPETSASPDGSQ | ||||||
Coiled coil | 3033-3067 | |||||
Sequence: LNDSLKEIHQKELRIQQLNSNFSQLLEEKNTLSIQ |
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusFragment
- Length3,101
- Mass (Da)358,087
- Last updated2022-10-12 v1
- Checksum147743967E76C0D5
Computationally mapped potential isoform sequences
There are 26 potential isoforms mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
Q14789 | GOGB1_HUMAN | GOLGB1 | 3259 | ||
C9J8Q0 | C9J8Q0_HUMAN | GOLGB1 | 3102 | ||
E7EU81 | E7EU81_HUMAN | GOLGB1 | 3223 | ||
F8WF12 | F8WF12_HUMAN | GOLGB1 | 39 | ||
A0A8J9C4H3 | A0A8J9C4H3_HUMAN | GOLGB1 | 3264 | ||
H0Y867 | H0Y867_HUMAN | GOLGB1 | 3027 | ||
H7C5I7 | H7C5I7_HUMAN | GOLGB1 | 2865 | ||
A0A8Q3WLR7 | A0A8Q3WLR7_HUMAN | GOLGB1 | 101 | ||
A0A8Q3WKE2 | A0A8Q3WKE2_HUMAN | GOLGB1 | 2791 | ||
A0A8Q3WKA7 | A0A8Q3WKA7_HUMAN | GOLGB1 | 3066 | ||
A0A8Q3WKB4 | A0A8Q3WKB4_HUMAN | GOLGB1 | 40 | ||
A0A8Q3WK91 | A0A8Q3WK91_HUMAN | GOLGB1 | 431 | ||
A0A8Q3WK92 | A0A8Q3WK92_HUMAN | GOLGB1 | 3068 | ||
A0A8Q3WLG1 | A0A8Q3WLG1_HUMAN | GOLGB1 | 177 | ||
A0A8Q3WLC9 | A0A8Q3WLC9_HUMAN | GOLGB1 | 2867 | ||
A0A8Q3WKV5 | A0A8Q3WKV5_HUMAN | GOLGB1 | 387 | ||
A0A8Q3SHQ4 | A0A8Q3SHQ4_HUMAN | GOLGB1 | 3003 | ||
A0A8Q3SHQ5 | A0A8Q3SHQ5_HUMAN | GOLGB1 | 2870 | ||
A0A8Q3SHQ9 | A0A8Q3SHQ9_HUMAN | GOLGB1 | 2648 | ||
A0A8Q3SHR7 | A0A8Q3SHR7_HUMAN | GOLGB1 | 198 | ||
A0A8Q3SHI6 | A0A8Q3SHI6_HUMAN | GOLGB1 | 479 | ||
A0A8Q3SHI9 | A0A8Q3SHI9_HUMAN | GOLGB1 | 2959 | ||
A0A8Q3SHM0 | A0A8Q3SHM0_HUMAN | GOLGB1 | 2735 | ||
A0A8Q3SHM5 | A0A8Q3SHM5_HUMAN | GOLGB1 | 94 | ||
A0A8Q3SHP0 | A0A8Q3SHP0_HUMAN | GOLGB1 | 2966 | ||
A0A8Q3SHH5 | A0A8Q3SHH5_HUMAN | GOLGB1 | 2657 |
Features
Showing features for compositional bias, non-terminal residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 1746-1761 | Basic and acidic residues | ||||
Sequence: SEKDSLSEEVQDLKHQ | ||||||
Compositional bias | 1784-1828 | Polar residues | ||||
Sequence: VTEEGTQSIPGETEEQDSLSMSTRPTCSESVPSAKSANPAVSKDF | ||||||
Non-terminal residue | 3101 | |||||
Sequence: A |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AC119736 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AC133750 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. |