UBA2 | ENSG00000126261 | NCBI 10054

Details for: UBA2

Gene ID: 10054

Symbol: UBA2

Ensembl ID: ENSG00000126261

Description: ubiquitin like modifier activating enzyme 2

Associated with

Metabolism of proteins
(R-HSA-392499)
Post-translational protein modification
(R-HSA-597592)
Processing and activation of sumo
(R-HSA-3215018)
Sumo is conjugated to e1 (uba2:sae1)
(R-HSA-3065676)
Sumo is transferred from e1 to e2 (ube2i, ubc9)
(R-HSA-3065678)
Sumoylation
(R-HSA-2990846)
Atp binding
(GO:0005524)
Cytoplasm
(GO:0005737)
Magnesium ion binding
(GO:0000287)
Nucleoplasm
(GO:0005654)
Positive regulation of protein sumoylation
(GO:0033235)
Protein binding
(GO:0005515)
Protein heterodimerization activity
(GO:0046982)
Protein sumoylation
(GO:0016925)
Small protein activating enzyme binding
(GO:0044388)
Sumo activating enzyme activity
(GO:0019948)
Sumo activating enzyme complex
(GO:0031510)
Sumo binding
(GO:0032183)
Transferase activity
(GO:0016740)
Ubiquitin-like protein conjugating enzyme binding
(GO:0044390)

Other Information

Proteins

SUMO-activating enzyme subunit 2

Genular Protein ID: 680463697

Symbol: SAE2_HUMAN

Name: SUMO-activating enzyme subunit 2

UniProtKB Accession Codes:

Q9UBT2 B3KWB9 O95605 Q59H87 Q6IBP6 Q9NTJ1 Q9UED2

Database IDs:

Citations:

PubMed ID: 9920803

Title: In vitro SUMO-1 modification requires two enzymatic steps, E1 and E2.

PubMed ID: 9920803

DOI: 10.1006/bbrc.1998.9995

PubMed ID: 10217437

Title: Molecular cloning and characterization of human AOS1 and UBA2, components of the sentrin-activating enzyme complex.

PubMed ID: 10217437

DOI: 10.1016/s0014-5793(99)00367-1

PubMed ID: 10187858

Title: Identification of the enzyme required for activation of the small ubiquitin-like protein SUMO-1.

PubMed ID: 10187858

DOI: 10.1074/jbc.274.15.10618

PubMed ID: 11230166

Title: Towards a catalog of human genes and proteins: sequencing and analysis of 500 novel complete protein coding human cDNAs.

PubMed ID: 11230166

DOI: 10.1101/gr.gr1547r

PubMed ID: 14702039

Title: Complete sequencing and characterization of 21,243 full-length human cDNAs.

PubMed ID: 14702039

DOI: 10.1038/ng1285

PubMed ID: 15057824

Title: The DNA sequence and biology of human chromosome 19.

PubMed ID: 15057824

DOI: 10.1038/nature02399

PubMed ID: 15489334

Title: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).

PubMed ID: 15489334

DOI: 10.1101/gr.2596504

PubMed ID: 9853615

Title: Selection system for genes encoding nuclear-targeted proteins.

PubMed ID: 9853615

DOI: 10.1038/4315

PubMed ID: 11481243

Title: Expression and regulation of the mammalian SUMO-1 E1 enzyme.

PubMed ID: 11481243

DOI: 10.1096/fj.00-0818fje

PubMed ID: 11451954

Title: Polymeric chains of SUMO-2 and SUMO-3 are conjugated to protein substrates by SAE1/SAE2 and Ubc9.

PubMed ID: 11451954

DOI: 10.1074/jbc.m104214200

PubMed ID: 16620772

Title: A general approach for investigating enzymatic pathways and substrates for ubiquitin-like modifiers.

PubMed ID: 16620772

DOI: 10.1016/j.abb.2006.03.002

PubMed ID: 18669648

Title: A quantitative atlas of mitotic phosphorylation.

PubMed ID: 18669648

DOI: 10.1073/pnas.0805139105

PubMed ID: 19413330

Title: Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach.

PubMed ID: 19413330

DOI: 10.1021/ac9004309

PubMed ID: 19443651

Title: Conformational transition associated with E1-E2 interaction in small ubiquitin-like modifications.

PubMed ID: 19443651

DOI: 10.1074/jbc.m109.000257

PubMed ID: 19608861

Title: Lysine acetylation targets protein complexes and co-regulates major cellular functions.

PubMed ID: 19608861

DOI: 10.1126/science.1175371

PubMed ID: 20068231

Title: Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis.

PubMed ID: 20068231

DOI: 10.1126/scisignal.2000475

PubMed ID: 21269460

Title: Initial characterization of the human central proteome.

PubMed ID: 21269460

DOI: 10.1186/1752-0509-5-17

PubMed ID: 22403398

Title: Small ubiquitin-like modifier (SUMO) modification of E1 Cys domain inhibits E1 Cys domain enzymatic activity.

PubMed ID: 22403398

DOI: 10.1074/jbc.m112.353789

PubMed ID: 23095757

Title: Sumoylation of SAE2 C terminus regulates SAE nuclear localization.

PubMed ID: 23095757

DOI: 10.1074/jbc.m112.420877

PubMed ID: 23186163

Title: Toward a comprehensive characterization of a human cancer cell phosphoproteome.

PubMed ID: 23186163

DOI: 10.1021/pr300630k

PubMed ID: 24275569

Title: An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome.

PubMed ID: 24275569

DOI: 10.1016/j.jprot.2013.11.014

PubMed ID: 25114211

Title: Mapping of SUMO sites and analysis of SUMOylation changes induced by external stimuli.

PubMed ID: 25114211

DOI: 10.1073/pnas.1413825111

PubMed ID: 25772364

Title: SUMO-2 orchestrates chromatin modifiers in response to DNA damage.

PubMed ID: 25772364

DOI: 10.1016/j.celrep.2015.02.033

PubMed ID: 28110515

Title: Missense variant in UBA2 associated with aplasia cutis congenita, duane anomaly, hip dysplasia and other anomalies: A possible new disorder involving the SUMOylation pathway.

PubMed ID: 28110515

DOI: 10.1002/ajmg.a.38078

PubMed ID: 28112733

Title: Site-specific mapping of the human SUMO proteome reveals co-modification with phosphorylation.

PubMed ID: 28112733

DOI: 10.1038/nsmb.3366

PubMed ID: 15660128

Title: Structures of the SUMO E1 provide mechanistic insights into SUMO activation and E2 recruitment to E1.

PubMed ID: 15660128

DOI: 10.1038/sj.emboj.7600552

PubMed ID: 17643372

Title: The intrinsic affinity between E2 and the Cys domain of E1 in ubiquitin-like modifications.

PubMed ID: 17643372

DOI: 10.1016/j.molcel.2007.05.023

PubMed ID: 20164921

Title: Active site remodelling accompanies thioester bond formation in the SUMO E1.

PubMed ID: 20164921

DOI: 10.1038/nature08765

PubMed ID: 34040189

Title: UBA2 variants underlie a recognizable syndrome with variable aplasia cutis congenita and ectrodactyly.

PubMed ID: 34040189

DOI: 10.1038/s41436-021-01182-1

Sequence Information:

Length: 640
Mass: 71224
Checksum: C12D15293BBF90EB
Sequence:

MALSRGLPRE LAEAVAGGRV LVVGAGGIGC ELLKNLVLTG FSHIDLIDLD TIDVSNLNRQ 
FLFQKKHVGR SKAQVAKESV LQFYPKANIV AYHDSIMNPD YNVEFFRQFI LVMNALDNRA 
ARNHVNRMCL AADVPLIESG TAGYLGQVTT IKKGVTECYE CHPKPTQRTF PGCTIRNTPS 
EPIHCIVWAK YLFNQLFGEE DADQEVSPDR ADPEAAWEPT EAEARARASN EDGDIKRIST 
KEWAKSTGYD PVKLFTKLFK DDIRYLLTMD KLWRKRKPPV PLDWAEVQSQ GEETNASDQQ 
NEPQLGLKDQ QVLDVKSYAR LFSKSIETLR VHLAEKGDGA ELIWDKDDPS AMDFVTSAAN 
LRMHIFSMNM KSRFDIKSMA GNIIPAIATT NAVIAGLIVL EGLKILSGKI DQCRTIFLNK 
QPNPRKKLLV PCALDPPNPN CYVCASKPEV TVRLNVHKVT VLTLQDKIVK EKFAMVAPDV 
QIEDGKGTIL ISSEEGETEA NNHKKLSEFG IRNGSRLQAD DFLQDYTLLI NILHSEDLGK 
DVEFEVVGDA PEKVGPKQAE DAAKSITNGS DDGAQPSTST AQEQDDVLIV DSDEEDSSNN 
ADVSEEERSR KRKLDEKENL SAKRSRIEQK EELDDVIALD

The gene details are incomplete or unavailable at the moment.

Database document:

This is a preview of the gene's schema. Only a few entries are kept for 'singleCellExpressions,' 'mRNAExpressions,' and other large data arrays for visualization purposes. You can zoom in with the mouse wheel for a closer view, and the text will adjust automatically if necessary. For the full schema, download it here.

Details for: UBA2

Associated with

Other Information

In vitro SUMO-1 modification requires two enzymatic steps, E1 and E2. PubMed ID: 9920803

Molecular cloning and characterization of human AOS1 and UBA2, components of the sentrin-activating enzyme complex. PubMed ID: 10217437

Identification of the enzyme required for activation of the small ubiquitin-like protein SUMO-1. PubMed ID: 10187858

Towards a catalog of human genes and proteins: sequencing and analysis of 500 novel complete protein coding human cDNAs. PubMed ID: 11230166

Complete sequencing and characterization of 21,243 full-length human cDNAs. PubMed ID: 14702039

The DNA sequence and biology of human chromosome 19. PubMed ID: 15057824

The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). PubMed ID: 15489334

Selection system for genes encoding nuclear-targeted proteins. PubMed ID: 9853615

Expression and regulation of the mammalian SUMO-1 E1 enzyme. PubMed ID: 11481243

Polymeric chains of SUMO-2 and SUMO-3 are conjugated to protein substrates by SAE1/SAE2 and Ubc9. PubMed ID: 11451954

A general approach for investigating enzymatic pathways and substrates for ubiquitin-like modifiers. PubMed ID: 16620772

A quantitative atlas of mitotic phosphorylation. PubMed ID: 18669648

Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach. PubMed ID: 19413330

Conformational transition associated with E1-E2 interaction in small ubiquitin-like modifications. PubMed ID: 19443651

Lysine acetylation targets protein complexes and co-regulates major cellular functions. PubMed ID: 19608861

Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis. PubMed ID: 20068231

Initial characterization of the human central proteome. PubMed ID: 21269460

Small ubiquitin-like modifier (SUMO) modification of E1 Cys domain inhibits E1 Cys domain enzymatic activity. PubMed ID: 22403398

Sumoylation of SAE2 C terminus regulates SAE nuclear localization. PubMed ID: 23095757

Toward a comprehensive characterization of a human cancer cell phosphoproteome. PubMed ID: 23186163

An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome. PubMed ID: 24275569

Mapping of SUMO sites and analysis of SUMOylation changes induced by external stimuli. PubMed ID: 25114211

SUMO-2 orchestrates chromatin modifiers in response to DNA damage. PubMed ID: 25772364

Missense variant in UBA2 associated with aplasia cutis congenita, duane anomaly, hip dysplasia and other anomalies: A possible new disorder involving the SUMOylation pathway. PubMed ID: 28110515

Site-specific mapping of the human SUMO proteome reveals co-modification with phosphorylation. PubMed ID: 28112733

Structures of the SUMO E1 provide mechanistic insights into SUMO activation and E2 recruitment to E1. PubMed ID: 15660128

The intrinsic affinity between E2 and the Cys domain of E1 in ubiquitin-like modifications. PubMed ID: 17643372

Active site remodelling accompanies thioester bond formation in the SUMO E1. PubMed ID: 20164921

UBA2 variants underlie a recognizable syndrome with variable aplasia cutis congenita and ectrodactyly. PubMed ID: 34040189