Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

O70263

- LNX1_MOUSE

UniProt

O70263 - LNX1_MOUSE

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

E3 ubiquitin-protein ligase LNX

Gene

Lnx1

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

E3 ubiquitin-protein ligase that mediates ubiquitination and subsequent proteasomal degradation of NUMB. E3 ubiquitin ligases accept ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and then directly transfers the ubiquitin to targeted substrates. Mediates ubiquitination of isoform p66 and isoform p72 of NUMB, but not that of isoform p71 or isoform p65.
Isoform 2 provides an endocytic scaffold for IGSF5/JAM4.

Pathwayi

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri45 – 8339RING-typePROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

  1. ligase activity Source: UniProtKB-KW
  2. PDZ domain binding Source: MGI
  3. ubiquitin-protein transferase activity Source: MGI
  4. zinc ion binding Source: InterPro

GO - Biological processi

  1. protein homooligomerization Source: MGI
  2. protein ubiquitination involved in ubiquitin-dependent protein catabolic process Source: MGI
  3. ubiquitin-dependent protein catabolic process Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Ligase

Keywords - Biological processi

Ubl conjugation pathway

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

UniPathwayiUPA00143.

Names & Taxonomyi

Protein namesi
Recommended name:
E3 ubiquitin-protein ligase LNX (EC:6.3.2.-)
Alternative name(s):
Ligand of Numb protein X 1
Ligand of Numb-binding protein 1
Numb-binding protein 1
Gene namesi
Name:Lnx1
Synonyms:Lnx
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 5

Organism-specific databases

MGIiMGI:1278335. Lnx1.

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi48 – 481C → A: Loss of function. 1 Publication
Mutagenesisi181 – 1811P → A: No effect on binding to NUMB protein. 1 Publication
Mutagenesisi182 – 1821G → A: Slightly affects binding to NUMB protein. 1 Publication
Mutagenesisi183 – 1831L → A: Abolishes binding to NUMB protein. 1 Publication
Mutagenesisi184 – 1841D → A: Slightly affects binding to NUMB protein. 1 Publication
Mutagenesisi185 – 1851N → A: Abolishes binding to NUMB protein. 1 Publication
Mutagenesisi186 – 1861P → A: Slightly affects binding to NUMB protein. 1 Publication
Mutagenesisi188 – 1881Y → A: Abolishes binding to NUMB protein. 1 Publication
Mutagenesisi188 – 1881Y → F: No effect on binding to NUMB protein. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 728728E3 ubiquitin-protein ligase LNXPRO_0000055914Add
BLAST

Proteomic databases

PaxDbiO70263.
PRIDEiO70263.

PTM databases

PhosphoSiteiO70263.

Expressioni

Tissue specificityi

Isoform 1 and isoform 2 are expressed in the heart. Isoform 1 is also expressed in kidney, lung and skeletal muscle while isoform 2 is also expressed in brain.1 Publication

Gene expression databases

BgeeiO70263.
CleanExiMM_LNX1.
ExpressionAtlasiO70263. baseline and differential.
GenevestigatoriO70263.

Interactioni

Subunit structurei

Interacts with CXADR. Interacts with MAGEB18 and MAGEF1 (By similarity). Interacts with the phosphotyrosine interaction domain of all isoforms of NUMB. IGSF5/JAM4 interacts with isoform 2 through the second PDZ domain, other isoforms may also interact with IGSF5/JAM4.By similarity2 Publications

Protein-protein interaction databases

BioGridi201187. 8 interactions.
IntActiO70263. 3 interactions.
MINTiMINT-253029.

Structurei

Secondary structure

1
728
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi384 – 3896Combined sources
Beta strandi398 – 4025Combined sources
Beta strandi405 – 4073Combined sources
Beta strandi409 – 4157Combined sources
Helixi420 – 4245Combined sources
Beta strandi432 – 4365Combined sources
Helixi446 – 45510Combined sources
Beta strandi456 – 46510Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3VQFX-ray1.20A381-467[»]
3VQGX-ray1.35A381-467[»]
ProteinModelPortaliO70263.
SMRiO70263. Positions 45-130, 277-722.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini278 – 36285PDZ 1PROSITE-ProRule annotationAdd
BLAST
Domaini385 – 46783PDZ 2PROSITE-ProRule annotationAdd
BLAST
Domaini508 – 59386PDZ 3PROSITE-ProRule annotationAdd
BLAST
Domaini638 – 72386PDZ 4PROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni186 – 24459Interaction with MAGEB18By similarityAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi185 – 1884NPXY motif

Domaini

The NPXY motif is required for the interaction with the PID domain of NUMB. It is however not sufficient.
The PDZ 1 domain participates in the interaction with the PID domain of NUMB, and participates in the isoform-specific ubiquitination of NUMB. The PDZ 2 domain of isoform 2 participates in the interaction with IGSF5/JAM4, other isoforms containing this domain may also interact with IGSF5/JAM4.

Sequence similaritiesi

Contains 4 PDZ (DHR) domains.PROSITE-ProRule annotation
Contains 1 RING-type zinc finger.PROSITE-ProRule annotation

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri45 – 8339RING-typePROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

Repeat, Zinc-finger

Phylogenomic databases

eggNOGiNOG236845.
GeneTreeiENSGT00760000119017.
HOGENOMiHOG000261605.
HOVERGENiHBG039539.
InParanoidiO70263.
KOiK10692.
OMAiVFPRLYH.
OrthoDBiEOG75F4CJ.
PhylomeDBiO70263.
TreeFamiTF330709.

Family and domain databases

Gene3Di2.30.42.10. 4 hits.
3.30.40.10. 1 hit.
InterProiIPR001478. PDZ.
IPR018957. Znf_C3HC4_RING-type.
IPR001841. Znf_RING.
IPR013083. Znf_RING/FYVE/PHD.
IPR017907. Znf_RING_CS.
[Graphical view]
PfamiPF00595. PDZ. 4 hits.
PF00097. zf-C3HC4. 1 hit.
[Graphical view]
SMARTiSM00228. PDZ. 4 hits.
SM00184. RING. 1 hit.
[Graphical view]
SUPFAMiSSF50156. SSF50156. 4 hits.
PROSITEiPS50106. PDZ. 4 hits.
PS00518. ZF_RING_1. 1 hit.
PS50089. ZF_RING_2. 1 hit.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: O70263-1) [UniParc]FASTAAdd to Basket

Also known as: LNX, LNXp80

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
MNQPDLADDP DPSPEPLCIV CGQNHSPEEN HFYTYTEDVD DDLICHICLQ
60 70 80 90 100
ALLDPLDTPC GHTYCTLCLT NFLVEKDFCP VDRKPVVLQH CKKSSILVNK
110 120 130 140 150
LLNKLLVTCP FTEHCTEVLQ RCDLQHHFQT SCKGASHYGL TKDRKRRSQD
160 170 180 190 200
GCPDGCASLM ATTLSPEVSA AATISLMTDE PGLDNPAYVS SVEDGEPVAN
210 220 230 240 250
SSDSGRSNRT RARPFERSTM RSRSFKKINR ALSALRRTKS GSVVANHVDQ
260 270 280 290 300
GRDNSENTTV PEVFPRLFHL IPDGEITSIK INRADPSESL SIRLVGGSET
310 320 330 340 350
PLVHIIIQHI YRDGVIARDG RLLPGDIILK VNGMDISNVP HNYAVRLLRQ
360 370 380 390 400
PCQVLRLTVL REQKFRSRSN AHVPDSYGPR DDSFHVILNK SSPEEQLGIK
410 420 430 440 450
LVRRVDEPGV FIFNVLNGGV ADRHGQLEEN DRVLAINGHD LRFGSPESAA
460 470 480 490 500
HLIQASERRV HLVVSRQVRQ SSPDIFQEAG WISNGQQSPG PGERNTASKP
510 520 530 540 550
AATCHEKVVS VWKDPSESLG MTVGGGASHR EWDLPIYVIS VEPGGVISRD
560 570 580 590 600
GRIKTGDILL NVNGIELTEV SRTEAVAILK SAPSSVVLKA LEVKEQEAQE
610 620 630 640 650
DCSPAALDSN HNVTPPGDWS PSWVMWLELP QYLCNCKDVI LRRNTAGSLG
660 670 680 690 700
FCIVGGYEEY SGNKPFFIKS IVEGTPAYND GRIRCGDILL AVNGRSTSGM
710 720
IHACLARMLK ELKGRITLTI ASWPGTFL
Length:728
Mass (Da):80,157
Last modified:August 1, 1998 - v1
Checksum:iE2914BD364C0CEC4
GO
Isoform 2 (identifier: O70263-2) [UniParc]FASTAAdd to Basket

Also known as: LNX-B, LNXp70

The sequence of this isoform differs from the canonical sequence as follows:
     1-131: MNQPDLADDP...CDLQHHFQTS → MKALLLLVLPWLSPANYIDNVGNLHFLYSEL

Show »
Length:628
Mass (Da):68,790
Checksum:iF4CC529ED9D33D55
GO
Isoform 3 (identifier: O70263-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-131: MNQPDLADDP...CDLQHHFQTS → MKALLLLVLPWLSPANYIDNVGNLHFLYSEL
     332-357: NGMDISNVPHNYAVRLLRQPCQVLRL → PMRRELVTIGYKIVSCRLCVAHNLSP
     358-728: Missing.

Note: No experimental conformation available.

Show »
Length:257
Mass (Da):28,202
Checksum:iADCE0552F3BAA28D
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti258 – 2581T → N in BAC31789. (PubMed:16141072)Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 131131MNQPD…HFQTS → MKALLLLVLPWLSPANYIDN VGNLHFLYSEL in isoform 2 and isoform 3. 3 PublicationsVSP_005734Add
BLAST
Alternative sequencei332 – 35726NGMDI…QVLRL → PMRRELVTIGYKIVSCRLCV AHNLSP in isoform 3. 1 PublicationVSP_012588Add
BLAST
Alternative sequencei358 – 728371Missing in isoform 3. 1 PublicationVSP_012589Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF034745 mRNA. Translation: AAC40075.1.
AF034746 mRNA. Translation: AAC40076.1.
AK044127 mRNA. Translation: BAC31789.1.
BC040367 mRNA. Translation: AAH40367.1.
CCDSiCCDS19347.1. [O70263-2]
CCDS51524.1. [O70263-1]
PIRiT09457.
T09458.
RefSeqiNP_001153049.1. NM_001159577.1. [O70263-1]
NP_001153050.1. NM_001159578.1.
NP_001153051.1. NM_001159579.1. [O70263-2]
NP_001153052.1. NM_001159580.1.
NP_034857.3. NM_010727.4. [O70263-2]
XP_006504317.1. XM_006504254.1. [O70263-1]
UniGeneiMm.440403.

Genome annotation databases

EnsembliENSMUST00000039744; ENSMUSP00000040098; ENSMUSG00000029228. [O70263-2]
ENSMUST00000087161; ENSMUSP00000084405; ENSMUSG00000029228. [O70263-1]
ENSMUST00000117388; ENSMUSP00000113035; ENSMUSG00000029228. [O70263-1]
ENSMUST00000117525; ENSMUSP00000113837; ENSMUSG00000029228. [O70263-2]
GeneIDi16924.
KEGGimmu:16924.
UCSCiuc008xtr.2. mouse. [O70263-1]
uc008xtu.2. mouse. [O70263-3]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF034745 mRNA. Translation: AAC40075.1 .
AF034746 mRNA. Translation: AAC40076.1 .
AK044127 mRNA. Translation: BAC31789.1 .
BC040367 mRNA. Translation: AAH40367.1 .
CCDSi CCDS19347.1. [O70263-2 ]
CCDS51524.1. [O70263-1 ]
PIRi T09457.
T09458.
RefSeqi NP_001153049.1. NM_001159577.1. [O70263-1 ]
NP_001153050.1. NM_001159578.1.
NP_001153051.1. NM_001159579.1. [O70263-2 ]
NP_001153052.1. NM_001159580.1.
NP_034857.3. NM_010727.4. [O70263-2 ]
XP_006504317.1. XM_006504254.1. [O70263-1 ]
UniGenei Mm.440403.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
3VQF X-ray 1.20 A 381-467 [» ]
3VQG X-ray 1.35 A 381-467 [» ]
ProteinModelPortali O70263.
SMRi O70263. Positions 45-130, 277-722.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 201187. 8 interactions.
IntActi O70263. 3 interactions.
MINTi MINT-253029.

PTM databases

PhosphoSitei O70263.

Proteomic databases

PaxDbi O70263.
PRIDEi O70263.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000039744 ; ENSMUSP00000040098 ; ENSMUSG00000029228 . [O70263-2 ]
ENSMUST00000087161 ; ENSMUSP00000084405 ; ENSMUSG00000029228 . [O70263-1 ]
ENSMUST00000117388 ; ENSMUSP00000113035 ; ENSMUSG00000029228 . [O70263-1 ]
ENSMUST00000117525 ; ENSMUSP00000113837 ; ENSMUSG00000029228 . [O70263-2 ]
GeneIDi 16924.
KEGGi mmu:16924.
UCSCi uc008xtr.2. mouse. [O70263-1 ]
uc008xtu.2. mouse. [O70263-3 ]

Organism-specific databases

CTDi 84708.
MGIi MGI:1278335. Lnx1.

Phylogenomic databases

eggNOGi NOG236845.
GeneTreei ENSGT00760000119017.
HOGENOMi HOG000261605.
HOVERGENi HBG039539.
InParanoidi O70263.
KOi K10692.
OMAi VFPRLYH.
OrthoDBi EOG75F4CJ.
PhylomeDBi O70263.
TreeFami TF330709.

Enzyme and pathway databases

UniPathwayi UPA00143 .

Miscellaneous databases

ChiTaRSi Lnx1. mouse.
NextBioi 290980.
PROi O70263.
SOURCEi Search...

Gene expression databases

Bgeei O70263.
CleanExi MM_LNX1.
ExpressionAtlasi O70263. baseline and differential.
Genevestigatori O70263.

Family and domain databases

Gene3Di 2.30.42.10. 4 hits.
3.30.40.10. 1 hit.
InterProi IPR001478. PDZ.
IPR018957. Znf_C3HC4_RING-type.
IPR001841. Znf_RING.
IPR013083. Znf_RING/FYVE/PHD.
IPR017907. Znf_RING_CS.
[Graphical view ]
Pfami PF00595. PDZ. 4 hits.
PF00097. zf-C3HC4. 1 hit.
[Graphical view ]
SMARTi SM00228. PDZ. 4 hits.
SM00184. RING. 1 hit.
[Graphical view ]
SUPFAMi SSF50156. SSF50156. 4 hits.
PROSITEi PS50106. PDZ. 4 hits.
PS00518. ZF_RING_1. 1 hit.
PS50089. ZF_RING_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "The mammalian numb phosphotyrosine-binding domain. Characterization of binding specificity and identification of a novel PDZ domain-containing numb binding protein, LNX."
    Dho S.E., Jacob S., Wolting C.D., French M.B., Rohrschneider L.R., McGlade C.J.
    J. Biol. Chem. 273:9179-9187(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), FUNCTION, TISSUE SPECIFICITY, MUTAGENESIS OF PRO-181; GLY-182; LEU-183; ASP-184; ASN-185; PRO-186 AND TYR-188.
    Tissue: Brain and Embryo.
  2. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
    Strain: C57BL/6J.
    Tissue: Brain cortex.
  3. "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 3).
    Tissue: Eye.
  4. "LNX functions as a RING type E3 ubiquitin ligase that targets the cell fate determinant Numb for ubiquitin-dependent degradation."
    Nie J., McGill M.A., Dermer M., Dho S.E., Wolting C.D., McGlade C.J.
    EMBO J. 21:93-102(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DOMAIN NPXY MOTIF, MUTAGENESIS OF CYS-48.
  5. "A novel PTB-PDZ domain interaction mediates isoform-specific ubiquitylation of mammalian Numb."
    Nie J., Li S.S.-C., McGlade C.J.
    J. Biol. Chem. 279:20807-20815(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DOMAINS PDZ, INTERACTION WITH NUMB.
  6. "Ligand-of-Numb protein X is an endocytic scaffold for junctional adhesion molecule 4."
    Kansaku A., Hirabayashi S., Mori H., Fujiwara N., Kawata A., Ikeda M., Rokukawa C., Kurihara H., Hata Y.
    Oncogene 25:5071-5084(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH IGSF5.

Entry informationi

Entry nameiLNX1_MOUSE
AccessioniPrimary (citable) accession number: O70263
Secondary accession number(s): O70264, Q8BRI8, Q8CFR3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 28, 2003
Last sequence update: August 1, 1998
Last modified: November 26, 2014
This is version 127 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3