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Q9UMX0 (UBQL1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 130. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length589 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence 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

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

The UBA domain mediates binding to PSEN1 and PSEN2. It also binds ubiquitin with micromolar affinity, independently of polyubiquitin linkage type.

Post-translational modification

Phosphorylated. Ref.11

Sequence similarities

Contains 1 UBA domain.

Contains 1 ubiquitin-like domain.

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 keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.14
Chain2 – 589588Ubiquilin-1
PRO_0000211008

Regions

Domain37 – 11175Ubiquitin-like
Domain546 – 58641UBA

Amino acid modifications

Modified residue21N-acetylalanine Ref.14 Ref.15 Ref.17 Ref.18

Natural variations

Alternative sequence416 – 44328Missing in isoform 2.
VSP_009787

Experimental info

Sequence conflict251A → T in AAH39294. Ref.8
Sequence conflict411V → A in BAB20436. Ref.4
Sequence conflict611F → S in BAB20436. Ref.4
Sequence conflict911L → S in BAB20436. Ref.4
Sequence conflict1251S → G in CAB66578. Ref.5
Sequence conflict2021P → H in AAH39294. Ref.8
Sequence conflict537 – 5382NP → YS in BAB20436. Ref.4

Secondary structure

....................... 589
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified March 1, 2002. Version 2.
Checksum: 8B4756B6113B7025

FASTA58962,519
        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 

« Hide

Isoform 2 [UniParc].

Checksum: 1E0BC42EC5BA4DA6
Show »

FASTA56159,220

References

« Hide '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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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. expand/collapse author list , Tampe J., Heubner D., Wambutt R., Korn B., Klein M., Poustka A.
Genome Res. 11:422-435(2001) [PubMed] [Europe PMC] [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. expand/collapse author list , 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].
[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. expand/collapse author list , 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] [Europe PMC] [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. expand/collapse author list , 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] 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, IDENTIFICATION BY 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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
[15]"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[16]"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] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[17]"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[18]"Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[19]"Affinity makes the difference: nonselective interaction of the UBA domain of Ubiquilin-1 with monomeric ubiquitin and polyubiquitin chains."
Zhang D., Raasi S., Fushman D.
J. Mol. Biol. 377:162-180(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 541-586 ALONE AND IN COMPLEX WITH UBIQUITIN.
+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.
RefSeqNP_038466.2. NM_013438.4.
NP_444295.1. NM_053067.2.
UniGeneHs.9589.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2JY5NMR-A541-586[»]
2JY6NMR-B541-586[»]
2KLCNMR-A34-112[»]
ProteinModelPortalQ9UMX0.
SMRQ9UMX0. Positions 1-112, 537-586.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid119007. 327 interactions.
DIPDIP-41629N.
IntActQ9UMX0. 49 interactions.
MINTMINT-150317.
STRING9606.ENSP00000365576.

PTM databases

PhosphoSiteQ9UMX0.

Polymorphism databases

DMDM48475013.

2D gel databases

REPRODUCTION-2DPAGEIPI00071180.

Proteomic databases

PaxDbQ9UMX0.
PRIDEQ9UMX0.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000257468; ENSP00000257468; ENSG00000135018. [Q9UMX0-2]
ENST00000376395; ENSP00000365576; ENSG00000135018. [Q9UMX0-1]
GeneID29979.
KEGGhsa:29979.
UCSCuc004amv.3. human. [Q9UMX0-1]
uc004amw.3. human. [Q9UMX0-2]

Organism-specific databases

CTD29979.
GeneCardsGC09M086274.
HGNCHGNC:12508. UBQLN1.
HPACAB037256.
HPA054143.
MIM605046. gene.
neXtProtNX_Q9UMX0.
PharmGKBPA37155.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG5272.
HOVERGENHBG064537.
InParanoidQ9UMX0.
KOK04523.
OMARSQDHSA.
OrthoDBEOG7HF1J8.
PhylomeDBQ9UMX0.
TreeFamTF314412.

Gene expression databases

ArrayExpressQ9UMX0.
BgeeQ9UMX0.
CleanExHS_UBQLN1.
GenevestigatorQ9UMX0.

Family and domain databases

InterProIPR006636. STI1_HS-bd.
IPR009060. UBA-like.
IPR015940. UBA/transl_elong_EF1B_N_euk.
IPR000449. UBA/Ts_N.
IPR015496. Ubiquilin.
IPR000626. Ubiquitin-like.
IPR028799. UBQLN1.
[Graphical view]
PANTHERPTHR10677. PTHR10677. 1 hit.
PTHR10677:SF8. PTHR10677:SF8. 1 hit.
PfamPF00627. UBA. 1 hit.
PF00240. ubiquitin. 1 hit.
[Graphical view]
SMARTSM00727. STI1. 4 hits.
SM00165. UBA. 1 hit.
SM00213. UBQ. 1 hit.
[Graphical view]
SUPFAMSSF46934. SSF46934. 1 hit.
PROSITEPS50030. UBA. 1 hit.
PS50053. UBIQUITIN_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSUBQLN1. human.
EvolutionaryTraceQ9UMX0.
GeneWikiUBQLN1.
GenomeRNAi29979.
NextBio52732.
PROQ9UMX0.
SOURCESearch...

Entry information

Entry nameUBQL1_HUMAN
AccessionPrimary (citable) accession number: Q9UMX0
Secondary accession number(s): Q5T6J5 expand/collapse secondary AC list , Q5T6J9, Q8IXS9, Q8N2Q3, Q9H0T8, Q9H3R4, Q9HAZ5
Entry history
Integrated into UniProtKB/Swiss-Prot: March 29, 2004
Last sequence update: March 1, 2002
Last modified: April 16, 2014
This is version 130 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 9

Human chromosome 9: entries, gene names and cross-references to MIM