Q9UMX0 (UBQL1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Ubiquilin-1

Alternative name(s):
Protein linking IAP with cytoskeleton 1
Short name=PLIC-1
Short name=hPLIC-1

Gene names

Name:	UBQLN1
Synonyms:	DA41, PLIC1

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	589 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Links CD47 to the cytoskeleton. Promotes the surface expression of GABA-A receptors By similarity. Promotes the accumulation of uncleaved PSEN1 and PSEN2 by stimulating their biosynthesis. Has no effect on PSEN1 and PSEN2 degradation.
Subunit structure	Binds CD47, NBL1, GABRA1, GABRA2, GABRA3, GABRA6, GABRB1, GABRB2 and GABRB3 By similarity. Binds UBE3A, BTRC, P4HB, MTOR, PSEN1 and PSEN2. Interacts with the proteasome 19S subunit. Ref.1 Ref.3 Ref.11 Ref.12 Ref.13
Subcellular location	Cytoplasm. Nucleus.
Tissue specificity	Ubiquitous. Highly expressed throughout the brain; detected in neurons and in neuropathological lesions, such as neurofibrillary tangles and Lewy bodies. Highly expressed in heart, placenta, pancreas, lung, liver, skeletal muscle and kidney. Ref.1 Ref.11
Domain	Binds PSEN1 and PSEN2 via its UBA domain.
Post-translational modification	Phosphorylated. Ref.11
Sequence similarities	Contains 1 UBA domain. Contains 1 ubiquitin-like domain.

Ontologies

Keywords
Cellular component	Cytoplasm Nucleus Proteasome
Coding sequence diversity	Alternative splicing
PTM	Acetylation Phosphoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological process	apoptotic process Inferred from mutant phenotype Ref.12. Source: HGNC regulation of protein ubiquitination Inferred from direct assay. Source: HGNC response to hypoxia Inferred from mutant phenotype Ref.12. Source: HGNC
Cellular component	endoplasmic reticulum Inferred from direct assay Ref.12. Source: HGNC nucleus Inferred from electronic annotation. Source: UniProtKB-SubCell perinuclear region of cytoplasm Non-traceable author statement Ref.11. Source: UniProtKB proteasome complex Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	kinase binding Inferred from physical interaction Ref.11. Source: UniProtKB
Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q9UMX0-1)

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.

Isoform 2 (identifier: Q9UMX0-2)

The sequence of this isoform differs from the canonical sequence as follows:
     416-443: Missing.

Note: No experimental confirmation available.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed

Chain

2 – 589

588

Ubiquilin-1

PRO_0000211008

Regions

Domain

37 – 111

75

Ubiquitin-like

Domain

546 – 586

41

UBA

Amino acid modifications

Modified residue

2

1

N-acetylalanine Ref.14

Natural variations

Alternative sequence

416 – 443

28

Missing in isoform 2.

VSP_009787

Experimental info

Sequence conflict

25

1

A → T in AAH39294. Ref.8

Sequence conflict

41

1

V → A in BAB20436. Ref.4

Sequence conflict

61

1

F → S in BAB20436. Ref.4

Sequence conflict

91

1

L → S in BAB20436. Ref.4

Sequence conflict

125

1

S → G in CAB66578. Ref.5

Sequence conflict

202

1

P → H in AAH39294. Ref.8

Sequence conflict

537 – 538

2

NP → YS in BAB20436. Ref.4

Secondary structure

1

.

.

.

.

.

.

.

.

589

Helix Strand Turn

Details...

Turn

543 – 547

5

Helix

548 – 556

9

Helix

562 – 572

11

Helix

576 – 583

8

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified March 1, 2002. Version 2. Checksum: 8B4756B6113B7025	FASTA	589	62,519
	10 20 30 40 50 60 MAESGESGGP PGSQDSAAGA EGAGAPAAAA SAEPKIMKVT VKTPKEKEEF AVPENSSVQQ 70 80 90 100 110 120 FKEEISKRFK SHTDQLVLIF AGKILKDQDT LSQHGIHDGL TVHLVIKTQN RPQDHSAQQT 130 140 150 160 170 180 NTAGSNVTTS STPNSNSTSG SATSNPFGLG GLGGLAGLSS LGLNTTNFSE LQSQMQRQLL 190 200 210 220 230 240 SNPEMMVQIM ENPFVQSMLS NPDLMRQLIM ANPQMQQLIQ RNPEISHMLN NPDIMRQTLE 250 260 270 280 290 300 LARNPAMMQE MMRNQDRALS NLESIPGGYN ALRRMYTDIQ EPMLSAAQEQ FGGNPFASLV 310 320 330 340 350 360 SNTSSGEGSQ PSRTENRDPL PNPWAPQTSQ SSSASSGTAS TVGGTTGSTA SGTSGQSTTA 370 380 390 400 410 420 PNLVPGVGAS MFNTPGMQSL LQQITENPQL MQNMLSAPYM RSMMQSLSQN PDLAAQMMLN 430 440 450 460 470 480 NPLFAGNPQL QEQMRQQLPT FLQQMQNPDT LSAMSNPRAM QALLQIQQGL QTLATEAPGL 490 500 510 520 530 540 IPGFTPGLGA LGSTGGSSGT NGSNATPSEN TSPTAGTTEP GHQQFIQQML QALAGVNPQL 550 560 570 580 QNPEVRFQQQ LEQLSAMGFL NREANLQALI ATGGDINAAI ERLLGSQPS
	Isoform 2 [UniParc]. Checksum: 1E0BC42EC5BA4DA6	FASTA	561	59,220
	10 20 30 40 50 60 MAESGESGGP PGSQDSAAGA EGAGAPAAAA SAEPKIMKVT VKTPKEKEEF AVPENSSVQQ 70 80 90 100 110 120 FKEEISKRFK SHTDQLVLIF AGKILKDQDT LSQHGIHDGL TVHLVIKTQN RPQDHSAQQT 130 140 150 160 170 180 NTAGSNVTTS STPNSNSTSG SATSNPFGLG GLGGLAGLSS LGLNTTNFSE LQSQMQRQLL 190 200 210 220 230 240 SNPEMMVQIM ENPFVQSMLS NPDLMRQLIM ANPQMQQLIQ RNPEISHMLN NPDIMRQTLE 250 260 270 280 290 300 LARNPAMMQE MMRNQDRALS NLESIPGGYN ALRRMYTDIQ EPMLSAAQEQ FGGNPFASLV 310 320 330 340 350 360 SNTSSGEGSQ PSRTENRDPL PNPWAPQTSQ SSSASSGTAS TVGGTTGSTA SGTSGQSTTA 370 380 390 400 410 420 PNLVPGVGAS MFNTPGMQSL LQQITENPQL MQNMLSAPYM RSMMQSLSQN PDLAAQMQNP 430 440 450 460 470 480 DTLSAMSNPR AMQALLQIQQ GLQTLATEAP GLIPGFTPGL GALGSTGGSS GTNGSNATPS 490 500 510 520 530 540 ENTSPTAGTT EPGHQQFIQQ MLQALAGVNP QLQNPEVRFQ QQLEQLSAMG FLNREANLQA 550 560 LIATGGDINA AIERLLGSQP S

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Identification of ubiquilin, a novel presenilin interactor that increases presenilin protein accumulation." Mah A.L., Perry G., Smith M.A., Monteiro M.J. J. Cell Biol. 151:847-862(2000) [PubMed: 11076969] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), INTERACTION WITH PSEN1 AND PSEN2, TISSUE SPECIFICITY. Tissue: Brain.
[2]	Mah A.L., Monteiro M.J. Submitted (JAN-2002) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[3]	"The hPLIC proteins may provide a link between the ubiquitination machinery and the proteasome." Kleijnen M.F., Shih A.H., Zhou P., Kumar S., Soccio R.E., Kedersha N.L., Gill G., Howley P.M. Mol. Cell 6:409-419(2000) [PubMed: 10983987] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), INTERACTION WITH UBE3A; BTRC AND THE PROTEASOME. Tissue: B-cell.
[4]	"Molecular cloning and expression analysis of the human DA41 gene and its mapping to chromosome 9q21.2-q21.3." Hanaoka E., Ozaki T., Ohira M., Nakamura Y., Suzuki M., Takahashi E., Moriya H., Nakagawara A., Sakiyama S. J. Hum. Genet. 45:188-191(2000) [PubMed: 10807547] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). Tissue: Lung.
[5]	"Towards a catalog of human genes and proteins: sequencing and analysis of 500 novel complete protein coding human cDNAs." Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S., Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H., Lauber J., Duesterhoeft A., Beyer A., Koehrer K., Strack N., Mewes H.-W., Ottenwaelder B., Obermaier B. , Tampe J., Heubner D., Wambutt R., Korn B., Klein M., Poustka A. Genome Res. 11:422-435(2001) [PubMed: 11230166] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). Tissue: Brain.
[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: 15164053] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases 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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2). Tissue: Brain and Muscle.
[9]	"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: 14702039] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-316. Tissue: Embryo.
[10]	Lubec G., Chen W.-Q., Sun Y. Submitted (DEC-2008) to UniProtKB Cited for: PROTEIN SEQUENCE OF 71-83; 207-236; 244-253 AND 547-582, MASS SPECTROMETRY. Tissue: Fetal brain cortex.
[11]	"Characterization of ubiquilin 1, an mTOR-interacting protein." Wu S., Mikhailov A., Kallo-Hosein H., Hara K., Yonezawa K., Avruch J. Biochim. Biophys. Acta 1542:41-56(2002) [PubMed: 11853878] [Abstract] Cited for: PHOSPHORYLATION, INTERACTION WITH MTOR, TISSUE SPECIFICITY.
[12]	"Role of ubiquilin associated with protein-disulfide isomerase in the endoplasmic reticulum in stress-induced apoptotic cell death." Ko H.S., Uehara T., Nomura Y. J. Biol. Chem. 277:35386-35392(2002) [PubMed: 12095988] [Abstract] Cited for: INTERACTION WITH P4HB.
[13]	"Mass spectrometric characterization of the affinity-purified human 26S proteasome complex." Wang X., Chen C.-F., Baker P.R., Chen P.-L., Kaiser P., Huang L. Biochemistry 46:3553-3565(2007) [PubMed: 17323924] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], INTERACTION WITH PROTEASOME. Tissue: Embryonic kidney.
[14]	"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach." Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S. Anal. Chem. 81:4493-4501(2009) [PubMed: 19413330] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, MASS SPECTROMETRY. Tissue: Embryonic kidney.
[15]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed: 21269460] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AF176069 mRNA. Translation: AAD49751.3.
AF293384 mRNA. Translation: AAG02473.1.
AB035275 mRNA. Translation: BAB20436.1.
AL136643 mRNA. Translation: CAB66578.1.
AL354920 Genomic DNA. Translation: CAI15100.1.
AL354920 Genomic DNA. Translation: CAI15101.1.
CH471089 Genomic DNA. Translation: EAW62659.1.
CH471089 Genomic DNA. Translation: EAW62661.1.
BC010066 mRNA. Translation: AAH10066.1.
BC039294 mRNA. Translation: AAH39294.1.
AK074535 mRNA. No translation available.

IPI

IPI00071180.
IPI00099550.

RefSeq

NP_038466.2. NM_013438.4.
NP_444295.1. NM_053067.2.

UniGene

Hs.9589.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2JY5	NMR	-	A	541-586	[»]
2JY6	NMR	-	B	541-586	[»]
2KLC	NMR	-	A	34-112	[»]

ProteinModelPortal

Q9UMX0.

SMR

Q9UMX0. Positions 1-112, 537-586.

ModBase

Search...

Protein-protein interaction databases

IntAct

Q9UMX0. 38 interactions.

MINT

MINT-150317.

STRING

Q9UMX0.

PTM databases

PhosphoSite

Q9UMX0.

Polymorphism databases

DMDM

48475013.

2D gel databases

REPRODUCTION-2DPAGE

IPI00071180.

Proteomic databases

PRIDE

Q9UMX0.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000376395; ENSP00000365576; ENSG00000135018.

GeneID

29979.

KEGG

hsa:29979.

UCSC

uc004amv.1. human.
uc004amw.1. human.

Organism-specific databases

CTD

29979.

GeneCards

GC09M086274.

H-InvDB

HIX0008127.

HGNC

HGNC:12508. UBQLN1.

HPA

CAB037256.

MIM

605046. gene.

neXtProt

NX_Q9UMX0.

PharmGKB

PA37155.

GenAtlas

Search...

Phylogenomic databases

GeneTree

ENSGT00390000005720.

HOGENOM

HBG560425.

HOVERGEN

HBG064537.

InParanoid

Q9UMX0.

OMA

NRSQDHS.

OrthoDB

EOG48KRBD.

PhylomeDB

Q9UMX0.

Gene expression databases

ArrayExpress

Q9UMX0.

Bgee

Q9UMX0.

CleanEx

HS_UBQLN1.

Genevestigator

Q9UMX0.

GermOnline

ENSG00000135018. Homo sapiens.

Family and domain databases

InterPro

IPR016024. ARM-type_fold.
IPR006636. STI1_HS-bd.
IPR009060. UBA-like.
IPR000449. UBA/transl_elong_EF1B_N.
IPR015940. UBA/transl_elong_EF1B_N_euk.
IPR015496. Ubiquilin.
IPR000626. Ubiquitin.
IPR019955. Ubiquitin_supergroup.
[Graphical view]

KO

K04523.

PANTHER

PTHR10677. Ubiquilin. 1 hit.

Pfam

PF00627. UBA. 1 hit.
PF00240. ubiquitin. 1 hit.
[Graphical view]

SMART

SM00727. STI1. 4 hits.
SM00165. UBA. 1 hit.
SM00213. UBQ. 1 hit.
[Graphical view]

SUPFAM

SSF48371. ARM-type_fold. 1 hit.
SSF46934. UBA_like. 1 hit.

PROSITE

PS50030. UBA. 1 hit.
PS00299. UBIQUITIN_1. False negative.
PS50053. UBIQUITIN_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

NextBio

52732.

SOURCE

Search...

Entry information

Entry name

UBQL1_HUMAN

Accession

Primary (citable) accession number: Q9UMX0
Secondary accession number(s): Q5T6J5 , Q5T6J9, Q8IXS9, Q8N2Q3, Q9H0T8, Q9H3R4, Q9HAZ5

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 29, 2004
Last sequence update:	March 1, 2002
Last modified:	January 25, 2012
This is version 109 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.