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Protein

Ubiquitin-associated protein 1

Gene

UBAP1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Component of the ESCRT-I complex, a regulator of vesicular trafficking process. Binds to ubiquitinated cargo proteins and is required for the sorting of endocytic ubiquitinated cargos into multivesicular bodies (MVBs). Plays a role in the proteasomal degradation of ubiquitinated cell-surface proteins, such as EGFR and BST2.2 Publications

GO - Molecular functioni

  • ubiquitin binding Source: UniProtKB

GO - Biological processi

  • protein transport Source: UniProtKB-KW
  • ubiquitin-dependent protein catabolic process via the multivesicular body sorting pathway Source: UniProtKB
Complete GO annotation...

Keywords - Biological processi

Protein transport, Transport

Names & Taxonomyi

Protein namesi
Recommended name:
Ubiquitin-associated protein 1
Short name:
UBAP-1
Alternative name(s):
Nasopharyngeal carcinoma-associated gene 20 protein
Gene namesi
Name:UBAP1
ORF Names:NAG20
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 9

Organism-specific databases

HGNCiHGNC:12461. UBAP1.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: LIFEdb
  • cytosol Source: UniProtKB
  • ESCRT I complex Source: UniProtKB
  • Golgi apparatus Source: HPA
  • plasma membrane Source: HPA
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Endosome

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi17 – 193LDD → AAA: Abolishes association with the ESCRT-I complex. 1 Publication
Mutagenesisi20 – 223VPF → AAA: Abolishes association with the ESCRT-I complex. 1 Publication
Mutagenesisi37 – 371P → A: Abolishes association with the ESCRT-I complex. 1 Publication
Mutagenesisi59 – 591E → G: Abolishes association with the ESCRT-I complex. 1 Publication
Mutagenesisi404 – 4041Y → A: Strongly reduced interaction with ubiquitinated proteins. 1 Publication
Mutagenesisi472 – 4721F → A: Strongly reduced interaction with ubiquitinated proteins. 1 Publication

Organism-specific databases

PharmGKBiPA37111.

Polymorphism and mutation databases

BioMutaiUBAP1.
DMDMi67475018.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 502502Ubiquitin-associated protein 1PRO_0000211017Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei146 – 1461PhosphoserineCombined sources
Modified residuei205 – 2051PhosphoserineCombined sources
Modified residuei289 – 2891PhosphoserineCombined sources

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiQ9NZ09.
MaxQBiQ9NZ09.
PaxDbiQ9NZ09.
PeptideAtlasiQ9NZ09.
PRIDEiQ9NZ09.

PTM databases

iPTMnetiQ9NZ09.
PhosphoSiteiQ9NZ09.

Expressioni

Tissue specificityi

Ubiquitous. Highly expressed in heart, brain, placenta, lung, liver, skeletal muscle and pancreas.1 Publication

Gene expression databases

BgeeiQ9NZ09.
CleanExiHS_UBAP1.
ExpressionAtlasiQ9NZ09. baseline and differential.
GenevisibleiQ9NZ09. HS.

Organism-specific databases

HPAiHPA019804.
HPA041590.

Interactioni

Subunit structurei

Component of an ESCRT-I complex (endosomal sorting complex required for transport I) which consists of TSG101, VPS28, VPS37A and UBAP1 in a 1:1:1:1 stoechiometry. Can be a component of ESCRT-I complexes containing VPS37B, VPS37C and VPS37D (in vitro) (PubMed:22405001), but may have a preference for the ESCRT-I complex containing VPS37A (PubMed:21757351). Interacts with PTPN23. Interacts (via UBA domains) with ubiquitinated proteins.2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
PPICP458773EBI-9641159,EBI-953909

GO - Molecular functioni

  • ubiquitin binding Source: UniProtKB

Protein-protein interaction databases

BioGridi119424. 20 interactions.
DIPiDIP-47291N.
IntActiQ9NZ09. 6 interactions.
MINTiMINT-3077159.
STRINGi9606.ENSP00000441024.

Structurei

Secondary structure

1
502
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi383 – 3864Combined sources
Helixi390 – 40112Combined sources
Helixi406 – 41611Combined sources
Helixi420 – 43516Combined sources
Helixi440 – 44910Combined sources
Helixi454 – 46916Combined sources
Helixi474 – 48310Combined sources
Turni484 – 4863Combined sources
Helixi488 – 49811Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1WGNNMR-A381-430[»]
4AE4X-ray1.65A/B389-502[»]
ProteinModelPortaliQ9NZ09.
SMRiQ9NZ09. Positions 381-499.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9NZ09.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini17 – 6347UMAPROSITE-ProRule annotationAdd
BLAST
Domaini389 – 43042UBA 1PROSITE-ProRule annotationAdd
BLAST
Domaini451 – 49848UBA 2PROSITE-ProRule annotationAdd
BLAST

Domaini

The UMA domain mediates association with the ESCRT-I complex.2 Publications

Sequence similaritiesi

Contains 2 UBA domains.PROSITE-ProRule annotation
Contains 1 UMA domain.PROSITE-ProRule annotation

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiENOG410IG52. Eukaryota.
ENOG410ZK9H. LUCA.
GeneTreeiENSGT00390000008092.
HOGENOMiHOG000231678.
HOVERGENiHBG060426.
InParanoidiQ9NZ09.
OMAiQCVETVV.
OrthoDBiEOG75MVWG.
PhylomeDBiQ9NZ09.
TreeFamiTF329247.

Family and domain databases

InterProiIPR015940. UBA.
IPR009060. UBA-like.
IPR023340. UMA.
[Graphical view]
SUPFAMiSSF46934. SSF46934. 2 hits.
PROSITEiPS50030. UBA. 2 hits.
PS51497. UMA. 1 hit.
[Graphical view]

Sequences (4)i

Sequence statusi: Complete.

This entry describes 4 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q9NZ09-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MASKKLGADF HGTFSYLDDV PFKTGDKFKT PAKVGLPIGF SLPDCLQVVR
60 70 80 90 100
EVQYDFSLEK KTIEWAEEIK KIEEAEREAE CKIAEAEAKV NSKSGPEGDS
110 120 130 140 150
KMSFSKTHST ATMPPPINPI LASLQHNSIL TPTRVSSSAT KQKVLSPPHI
160 170 180 190 200
KADFNLADFE CEEDPFDNLE LKTIDEKEEL RNILVGTTGP IMAQLLDNNL
210 220 230 240 250
PRGGSGSVLQ DEEVLASLER ATLDFKPLHK PNGFITLPQL GNCEKMSLSS
260 270 280 290 300
KVSLPPIPAV SNIKSLSFPK LDSDDSNQKT AKLASTFHST SCLRNGTFQN
310 320 330 340 350
SLKPSTQSSA SELNGHHTLG LSALNLDSGT EMPALTSSQM PSLSVLSVCT
360 370 380 390 400
EESSPPNTGP TVTPPNFSVS QVPNMPSCPQ AYSELQMLSP SERQCVETVV
410 420 430 440 450
NMGYSYECVL RAMKKKGENI EQILDYLFAH GQLCEKGFDP LLVEEALEMH
460 470 480 490 500
QCSEEKMMEF LQLMSKFKEM GFELKDIKEV LLLHNNDQDN ALEDLMARAG

AS
Length:502
Mass (Da):55,084
Last modified:October 1, 2000 - v1
Checksum:i548457B0B2ABC0F4
GO
Isoform 2 (identifier: Q9NZ09-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     362-422: Missing.

Note: Derived from EST data. No experimental confirmation available.
Show »
Length:441
Mass (Da):48,247
Checksum:i001566AEC2898859
GO
Isoform 3 (identifier: Q9NZ09-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-53: MASKKLGADF...DCLQVVREVQ → MSGAVRGRRR...LLRSWVQIFM

Note: No experimental confirmation available.
Show »
Length:538
Mass (Da):58,982
Checksum:iC88D72AB978B9358
GO
Isoform 4 (identifier: Q9NZ09-4) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-11: MASKKLGADFH → MSGAVRGRRR...LLRRRQQRHS

Note: No experimental confirmation available.
Show »
Length:566
Mass (Da):61,845
Checksum:i66126A6497B8BC94
GO

Sequence cautioni

The sequence BAC11162.1 differs from that shown. Reason: Erroneous initiation. Curated
The sequence BAH12084.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti81 – 811C → R in CAG38582 (Ref. 4) Curated
Sequence conflicti187 – 1871T → N in BAH14025 (PubMed:14702039).Curated
Sequence conflicti331 – 3311E → D in BAC11176 (PubMed:14702039).Curated
Sequence conflicti398 – 3981T → M in BAH12084 (PubMed:14702039).Curated
Sequence conflicti403 – 4031G → C in BAC11323 (PubMed:14702039).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti357 – 3571N → K.1 Publication
Corresponds to variant rs16935457 [ dbSNP | Ensembl ].
VAR_034577

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 5353MASKK…VREVQ → MSGAVRGRRREVGLQHGGCG TGGGYGDGLARSGQSWRWWR SLSLGAVGSSAGTEPGRPAG ASTFRLLRRRQQRHSGSKWL LRSWVQIFM in isoform 3. 1 PublicationVSP_046866Add
BLAST
Alternative sequencei1 – 1111MASKKLGADFH → MSGAVRGRRREVGLQHGGCG TGGGYGDGLARSGQSWRWWR SLSLGAVGSSAGTEPGRPAG ASTFRLLRRRQQRHS in isoform 4. 1 PublicationVSP_046867Add
BLAST
Alternative sequencei362 – 42261Missing in isoform 2. CuratedVSP_013650Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF222043 mRNA. Translation: AAF37827.2.
AL136733 mRNA. Translation: CAB66667.1.
AK074724 mRNA. Translation: BAC11162.1. Different initiation.
AK074745 mRNA. Translation: BAC11176.1.
AK074812 mRNA. Translation: BAC11224.1.
AK074969 mRNA. Translation: BAC11323.1.
AK074995 mRNA. Translation: BAC11342.1.
AK295482 mRNA. Translation: BAH12084.1. Different initiation.
AK303711 mRNA. Translation: BAH14025.1.
CR533551 mRNA. Translation: CAG38582.1.
AK223235 mRNA. Translation: BAD96955.1.
AL353662 Genomic DNA. Translation: CAI15914.1.
AL353662 Genomic DNA. Translation: CAI15915.1.
CH471071 Genomic DNA. Translation: EAW58467.1.
CH471071 Genomic DNA. Translation: EAW58468.1.
CH471071 Genomic DNA. Translation: EAW58469.1.
CH471071 Genomic DNA. Translation: EAW58470.1.
BC020950 mRNA. Translation: AAH20950.1.
BC098141 mRNA. Translation: AAH98141.1.
BC098316 mRNA. Translation: AAH98316.1.
BC099726 mRNA. Translation: AAH99726.1.
BC100668 mRNA. Translation: AAI00669.1.
CCDSiCCDS55303.1. [Q9NZ09-4]
CCDS6550.1. [Q9NZ09-1]
RefSeqiNP_001164672.1. NM_001171201.1. [Q9NZ09-4]
NP_001164673.1. NM_001171202.1. [Q9NZ09-3]
NP_001164674.1. NM_001171203.2. [Q9NZ09-1]
NP_001164675.1. NM_001171204.2. [Q9NZ09-1]
NP_057609.2. NM_016525.4. [Q9NZ09-1]
XP_006716842.1. XM_006716779.2. [Q9NZ09-1]
XP_011516201.1. XM_011517899.1. [Q9NZ09-1]
UniGeneiHs.268963.

Genome annotation databases

EnsembliENST00000297661; ENSP00000297661; ENSG00000165006. [Q9NZ09-1]
ENST00000359544; ENSP00000352541; ENSG00000165006. [Q9NZ09-1]
ENST00000379186; ENSP00000368484; ENSG00000165006. [Q9NZ09-2]
ENST00000625521; ENSP00000486574; ENSG00000165006. [Q9NZ09-4]
GeneIDi51271.
KEGGihsa:51271.
UCSCiuc003ztx.4. human. [Q9NZ09-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF222043 mRNA. Translation: AAF37827.2.
AL136733 mRNA. Translation: CAB66667.1.
AK074724 mRNA. Translation: BAC11162.1. Different initiation.
AK074745 mRNA. Translation: BAC11176.1.
AK074812 mRNA. Translation: BAC11224.1.
AK074969 mRNA. Translation: BAC11323.1.
AK074995 mRNA. Translation: BAC11342.1.
AK295482 mRNA. Translation: BAH12084.1. Different initiation.
AK303711 mRNA. Translation: BAH14025.1.
CR533551 mRNA. Translation: CAG38582.1.
AK223235 mRNA. Translation: BAD96955.1.
AL353662 Genomic DNA. Translation: CAI15914.1.
AL353662 Genomic DNA. Translation: CAI15915.1.
CH471071 Genomic DNA. Translation: EAW58467.1.
CH471071 Genomic DNA. Translation: EAW58468.1.
CH471071 Genomic DNA. Translation: EAW58469.1.
CH471071 Genomic DNA. Translation: EAW58470.1.
BC020950 mRNA. Translation: AAH20950.1.
BC098141 mRNA. Translation: AAH98141.1.
BC098316 mRNA. Translation: AAH98316.1.
BC099726 mRNA. Translation: AAH99726.1.
BC100668 mRNA. Translation: AAI00669.1.
CCDSiCCDS55303.1. [Q9NZ09-4]
CCDS6550.1. [Q9NZ09-1]
RefSeqiNP_001164672.1. NM_001171201.1. [Q9NZ09-4]
NP_001164673.1. NM_001171202.1. [Q9NZ09-3]
NP_001164674.1. NM_001171203.2. [Q9NZ09-1]
NP_001164675.1. NM_001171204.2. [Q9NZ09-1]
NP_057609.2. NM_016525.4. [Q9NZ09-1]
XP_006716842.1. XM_006716779.2. [Q9NZ09-1]
XP_011516201.1. XM_011517899.1. [Q9NZ09-1]
UniGeneiHs.268963.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1WGNNMR-A381-430[»]
4AE4X-ray1.65A/B389-502[»]
ProteinModelPortaliQ9NZ09.
SMRiQ9NZ09. Positions 381-499.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi119424. 20 interactions.
DIPiDIP-47291N.
IntActiQ9NZ09. 6 interactions.
MINTiMINT-3077159.
STRINGi9606.ENSP00000441024.

PTM databases

iPTMnetiQ9NZ09.
PhosphoSiteiQ9NZ09.

Polymorphism and mutation databases

BioMutaiUBAP1.
DMDMi67475018.

Proteomic databases

EPDiQ9NZ09.
MaxQBiQ9NZ09.
PaxDbiQ9NZ09.
PeptideAtlasiQ9NZ09.
PRIDEiQ9NZ09.

Protocols and materials databases

DNASUi51271.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000297661; ENSP00000297661; ENSG00000165006. [Q9NZ09-1]
ENST00000359544; ENSP00000352541; ENSG00000165006. [Q9NZ09-1]
ENST00000379186; ENSP00000368484; ENSG00000165006. [Q9NZ09-2]
ENST00000625521; ENSP00000486574; ENSG00000165006. [Q9NZ09-4]
GeneIDi51271.
KEGGihsa:51271.
UCSCiuc003ztx.4. human. [Q9NZ09-1]

Organism-specific databases

CTDi51271.
GeneCardsiUBAP1.
HGNCiHGNC:12461. UBAP1.
HPAiHPA019804.
HPA041590.
MIMi609787. gene.
neXtProtiNX_Q9NZ09.
PharmGKBiPA37111.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiENOG410IG52. Eukaryota.
ENOG410ZK9H. LUCA.
GeneTreeiENSGT00390000008092.
HOGENOMiHOG000231678.
HOVERGENiHBG060426.
InParanoidiQ9NZ09.
OMAiQCVETVV.
OrthoDBiEOG75MVWG.
PhylomeDBiQ9NZ09.
TreeFamiTF329247.

Miscellaneous databases

ChiTaRSiUBAP1. human.
EvolutionaryTraceiQ9NZ09.
GeneWikiiUBAP1.
GenomeRNAii51271.
PROiQ9NZ09.
SOURCEiSearch...

Gene expression databases

BgeeiQ9NZ09.
CleanExiHS_UBAP1.
ExpressionAtlasiQ9NZ09. baseline and differential.
GenevisibleiQ9NZ09. HS.

Family and domain databases

InterProiIPR015940. UBA.
IPR009060. UBA-like.
IPR023340. UMA.
[Graphical view]
SUPFAMiSSF46934. SSF46934. 2 hits.
PROSITEiPS50030. UBA. 2 hits.
PS51497. UMA. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Isolation and characterization of a novel cDNA, UBAP1, derived from the tumor suppressor locus in human chromosome 9p21-22."
    Qian J., Yang J., Zhang X., Zhang B., Wang J., Zhou M., Tang K., Li W., Zeng Z., Zhao X., Shen S., Li G.
    J. Cancer Res. Clin. Oncol. 127:613-618(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Testis.
  3. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 4), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 11-502 (ISOFORM 3).
    Tissue: Hippocampus and Kidney.
  4. "Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
    Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
    Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
  5. Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.
    Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), VARIANT LYS-357.
    Tissue: Stomach.
  6. "DNA sequence and analysis of human chromosome 9."
    Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S., Bagguley C.L.
    , Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A., Frankland J.A., French L., Fricker D.G., Garner P., Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S., Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E., Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D., Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E., Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K., Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M., Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J., Dunham I.
    Nature 429:369-374(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] (ISOFORMS 1 AND 2).
  7. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  8. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Colon.
  9. "UBAP1 is a component of an endosome-specific ESCRT-I complex that is essential for MVB sorting."
    Stefani F., Zhang L., Taylor S., Donovan J., Rollinson S., Doyotte A., Brownhill K., Bennion J., Pickering-Brown S., Woodman P.
    Curr. Biol. 21:1245-1250(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH PTPN23, IDENTIFICATION IN ESCRT-I COMPLEX, SUBUNIT, SUBCELLULAR LOCATION, DOMAIN, MUTAGENESIS OF PRO-37; GLU-59; TYR-404 AND PHE-472.
  10. "Toward a comprehensive characterization of a human cancer cell phosphoproteome."
    Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., Mohammed S.
    J. Proteome Res. 12:260-271(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-205 AND SER-289, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma and Erythroleukemia.
  11. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-146, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  12. "Solution structure of UBA domain of human ubiquitin associated protein 1 (UBAP1)."
    RIKEN structural genomics initiative (RSGI)
    Submitted (NOV-2004) to the PDB data bank
    Cited for: STRUCTURE BY NMR OF 381-430.
  13. Cited for: X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS) OF 389-502, FUNCTION, IDENTIFICATION IN ESCRT-I COMPLEX, SUBUNIT, DOMAIN, MUTAGENESIS OF 17-LEU--ASP-19 AND 20-VAL--PHE-22.

Entry informationi

Entry nameiUBAP1_HUMAN
AccessioniPrimary (citable) accession number: Q9NZ09
Secondary accession number(s): B7Z348
, B7Z8N9, D3DRL7, F5GXE2, F5H0J8, Q4V759, Q53FP7, Q5T7B3, Q6FI75, Q8NC52, Q8NCG6, Q8NCH9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 10, 2005
Last sequence update: October 1, 2000
Last modified: July 6, 2016
This is version 139 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 9
    Human chromosome 9: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.