| Gene Symbol |
RPS27A
|
| Entrez Gene |
6233
|
| Alt Symbol |
CEP80, HEL112, S27A, UBA80, UBC, UBCEP1, UBCEP80
|
| Species |
Human
|
| Gene Type |
protein-coding
|
| Description |
ribosomal protein S27a
|
| Other Description |
40S ribosomal protein S27a|epididymis luminal protein 112|ubiquitin C|ubiquitin and ribosomal protein S27a|ubiquitin carboxyl extension protein 80|ubiquitin-40S ribosomal protein S27a|ubiquitin-CEP80
|
| Swissprots |
P62979
|
| Accessions |
BAA25826 BAB79488 EAX00106 EAX00107 EAX00108 EAX00109 EAX00110 P62979 AB362574 BAF81539 AK093614 AK225079 AK225718 AK315695 BAG38058 AY952889 BC001392 AAH01392 BC042362 AAH42362 BC053371 AAH53371 BC066293 AAH66293 BF678026 BM907473 BQ276758 BQ421613 CK004647 CN344335 CR746519 DA527860 DB505702 EU794671 ACJ13725 HQ448720 ADQ33198 M10939 AAA36788 S79522 AAB21188 X63237 CAA44911 NM_001135592 NP_001129064 NM_001177413 NP_001170884 NM_002954 NP_002945
|
| Function |
Ubiquitin: Exists either covalently attached to another protein, or free (unanchored). When covalently bound, it is conjugated to target proteins via an isopeptide bond either as a monomer (monoubiquitin), a polymer linked via different Lys residues of the ubiquitin (polyubiquitin chains) or a linear polymer linked via the initiator Met of the ubiquitin (linear polyubiquitin chains). Polyubiquitin chains, when attached to a target protein, have different functions depending on the Lys residue of the ubiquitin that is linked: Lys-6-linked may be involved in DNA repair; Lys-11-linked is involved in ERAD (endoplasmic reticulum-associated degradation) and in cell-cycle regulation; Lys-29-linked is involved in lysosomal degradation; Lys-33-linked is involved in kinase modification; Lys-48-linked is involved in protein degradation via the proteasome; Lys-63-linked is involved in endocytosis, DNA-damage responses as well as in signaling processes leading to activation of the transcription fac
|
| Subcellular Location |
Ubiquitin: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
|
| Top Pathways |
Ribosome
|