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Q9JM99

- PRG4_MOUSE

UniProt

Q9JM99 - PRG4_MOUSE

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Protein

Proteoglycan 4

Gene

Prg4

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

Functioni

Plays a role in boundary lubrication within articulating joints. Prevents protein deposition onto cartilage from synovial fluid by controlling adhesion-dependent synovial growth and inhibiting the adhesion of synovial cells to the cartilage surface.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei955 – 9562Cleavage; by subtilisin-like proprotein convertase 4

GO - Molecular functioni

  1. polysaccharide binding Source: InterPro
  2. scavenger receptor activity Source: InterPro

GO - Biological processi

  1. hematopoietic stem cell proliferation Source: MGI
  2. immune response Source: InterPro
  3. negative regulation of interleukin-6 biosynthetic process Source: MGI
  4. regulation of cell proliferation Source: MGI
Complete GO annotation...

Names & Taxonomyi

Protein namesi
Recommended name:
Proteoglycan 4
Alternative name(s):
Lubricin
Megakaryocyte-stimulating factor
Superficial zone proteoglycan
Cleaved into the following chain:
Gene namesi
Name:Prg4
Synonyms:Msf, Szp
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 1

Organism-specific databases

MGIiMGI:1891344. Prg4.

Subcellular locationi

Secreted By similarity

GO - Cellular componenti

  1. extracellular space Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Disruption phenotypei

Mice are viable and fertile. In the newborn period, their joints appear normal. The aged mice exhibit abnormal protein deposits on the cartilage surface and disappearance of underlying superficial zone chondrocytes. In addition to cartilage surface changes and subsequent cartilage deterioration, intimal cells in the synovium surrounding the joint space become hyperplastic, which further contribute to joint failure.1 Publication

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi795 – 7951C → A: Not cleaved by subtilisin-like proprotein convertase. Not cleaved by subtilisin-like proprotein convertase; when associated with A-1053. 1 Publication
Mutagenesisi851 – 8533CNC → ANA: Cleaved by subtilisin-like proprotein convertase. 1 Publication
Mutagenesisi851 – 8511C → A: Cleaved by subtilisin-like proprotein convertase.
Mutagenesisi930 – 9301C → A: Cleaved by subtilisin-like proprotein convertase. 1 Publication
Mutagenesisi949 – 9557RRRRFER → ARARFEA: Not cleaved by subtilisin-like proprotein convertase 4. 1 Publication
Mutagenesisi949 – 9513RRR → ARA: Cleaved by subtilisin-like proprotein convertase 4. 1 Publication
Mutagenesisi955 – 9551R → A: Not cleaved by subtilisin-like proprotein convertase 4.
Mutagenesisi1053 – 10531C → A: Not cleaved by subtilisin-like proprotein convertase 4. Not cleaved by subtilisin-like proprotein convertase; when associated with A-795. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2424Sequence AnalysisAdd
BLAST
Chaini25 – 10541030Proteoglycan 4PRO_0000043234Add
BLAST
Chaini956 – 105499Proteoglycan 4 C-terminal partPRO_0000043235Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi30 ↔ 46AlternatePROSITE-ProRule annotation
Disulfide bondi30 ↔ 34PROSITE-ProRule annotation
Disulfide bondi34 ↔ 64AlternatePROSITE-ProRule annotation
Disulfide bondi44 ↔ 57AlternatePROSITE-ProRule annotation
Disulfide bondi44 ↔ 46PROSITE-ProRule annotation
Disulfide bondi50 ↔ 56PROSITE-ProRule annotation
Disulfide bondi57 ↔ 64PROSITE-ProRule annotation
Disulfide bondi70 ↔ 86AlternatePROSITE-ProRule annotation
Disulfide bondi70 ↔ 74PROSITE-ProRule annotation
Disulfide bondi74 ↔ 104AlternatePROSITE-ProRule annotation
Disulfide bondi84 ↔ 97AlternatePROSITE-ProRule annotation
Disulfide bondi84 ↔ 86PROSITE-ProRule annotation
Disulfide bondi90 ↔ 96PROSITE-ProRule annotation
Disulfide bondi97 ↔ 104PROSITE-ProRule annotation
Glycosylationi109 – 1091N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi795 ↔ 10531 PublicationPROSITE-ProRule annotation
Glycosylationi938 – 9381N-linked (GlcNAc...)Sequence Analysis

Post-translational modificationi

N-glycosylated.By similarity
O-glycosylated; contains glycosaminoglycan chondroitin sulfate and keratan sulfate.By similarity
The disulfide bond between Cys-795 and Cys-1053 is essential for protein cleavage.1 Publication

Keywords - PTMi

Disulfide bond, Glycoprotein, Proteoglycan

Proteomic databases

PaxDbiQ9JM99.
PRIDEiQ9JM99.

PTM databases

PhosphoSiteiQ9JM99.

Expressioni

Tissue specificityi

Highly expressed in cartilage, bone and liver and weakly expressed in heart, brain and muscle. Expressed in the surface chondrocytes and in synovial intimal cells. Isoform B is expressed in bone, small intestine, muscle, testis, heart, liver and lung. Isoform C and isoform D are widely expressed.2 Publications

Developmental stagei

First detected at the forming joint surface from E15.5, after cavitation has begun. At later stages of morphogenesis, strong expression is observed in cartilage surface cells (superficial zone chondocytes) and in the newly forming synovium.1 Publication

Gene expression databases

BgeeiQ9JM99.
ExpressionAtlasiQ9JM99. baseline and differential.
GenevestigatoriQ9JM99.

Interactioni

Subunit structurei

Homodimer; disulfide-linked.1 Publication

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini26 – 6944SMB 1PROSITE-ProRule annotationAdd
BLAST
Domaini66 – 10843SMB 2PROSITE-ProRule annotationAdd
BLAST
Repeati317 – 32481; approximate
Repeati325 – 33282; approximate
Repeati333 – 34083; approximate
Repeati349 – 35684; approximate
Repeati357 – 36485
Repeati365 – 37176; approximate
Repeati372 – 37987
Repeati380 – 38788
Repeati388 – 39589
Repeati396 – 403810
Repeati404 – 411811
Repeati412 – 418712; approximate
Repeati419 – 426813
Repeati427 – 434814
Repeati435 – 442815
Repeati443 – 450816; approximate
Repeati451 – 458817
Repeati459 – 466818
Repeati467 – 474819
Repeati475 – 482820
Repeati483 – 490821
Repeati491 – 498822
Repeati499 – 506823
Repeati507 – 514824
Repeati515 – 522825
Repeati523 – 530826
Repeati531 – 538827
Repeati539 – 546828
Repeati547 – 554829
Repeati555 – 562830
Repeati563 – 570831
Repeati571 – 578832
Repeati579 – 586833
Repeati587 – 594834
Repeati595 – 602835
Repeati603 – 610836
Repeati611 – 618837
Repeati797 – 84044Hemopexin 1Add
BLAST
Repeati841 – 88848Hemopexin 2Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni317 – 61830237 X 8 AA repeats of K-X-P-X-P-T-T-XAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi157 – 18428Ser-richAdd
BLAST
Compositional biasi350 – 606257Glu-richAdd
BLAST
Compositional biasi659 – 69941Lys-richAdd
BLAST

Sequence similaritiesi

Contains 2 hemopexin repeats.Curated
Contains 2 SMB (somatomedin-B) domains.Curated

Keywords - Domaini

Repeat, Signal

Phylogenomic databases

eggNOGiNOG12793.
GeneTreeiENSGT00530000063751.
HOGENOMiHOG000115691.
HOVERGENiHBG101613.
InParanoidiQ9JM99.
OrthoDBiEOG7HMS1H.

Family and domain databases

Gene3Di2.110.10.10. 2 hits.
InterProiIPR000585. Hemopexin-like_dom.
IPR018487. Hemopexin-like_repeat.
IPR018486. Hemopexin_CS.
IPR020436. Somatomedin_B_chordata.
IPR001212. Somatomedin_B_dom.
[Graphical view]
PfamiPF00045. Hemopexin. 1 hit.
PF01033. Somatomedin_B. 2 hits.
[Graphical view]
PRINTSiPR00022. SOMATOMEDINB.
SMARTiSM00120. HX. 2 hits.
SM00201. SO. 2 hits.
[Graphical view]
SUPFAMiSSF50923. SSF50923. 2 hits.
PROSITEiPS00024. HEMOPEXIN. 1 hit.
PS51642. HEMOPEXIN_2. 2 hits.
PS00524. SMB_1. 2 hits.
PS50958. SMB_2. 2 hits.
[Graphical view]

Sequences (5)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 5 isoformsi produced by alternative splicing. Align

Isoform A (identifier: Q9JM99-1) [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
MGWKILPVCL SLLLPVVLIQ QVSSQDLSSC AGRCGEGYSR DATCNCDYNC
60 70 80 90 100
QHYMECCPDF KRVCSPELSC KGRCFESFAR GRECDCDSQC KQYGKCCADY
110 120 130 140 150
DSFCEEVHNS TSPSSKTAPT PAGASDTIKS TTKRSPKSPT TRTIKVVESE
160 170 180 190 200
ELTEEHSDSE NQESSSSSSS SSSTIRKIKS SKNSANRELQ KNPNVKDNKK
210 220 230 240 250
NTPKKKPNPE PPAVDEAGSG LDNGEFKLTP PPPDPPTTPH SKVATSPKTT
260 270 280 290 300
AAKPVTPKPS LAPNSETSKE ASLASNKETT VETKETTATN KQSSASKKKT
310 320 330 340 350
TSVKETRSAE KTSDKDVEPT STTPKNSAPT TTKKPVTTTK ESKFLPLPQE
360 370 380 390 400
PEPTTAKEPP PTTKKPEPTT RKEPEPTTPK EPEPTTPKEP EPTTPKEPEP
410 420 430 440 450
TTPKEPPPTT KKPEPTTPKE PGPTTPKEPE PTTTKEPEPT TTKEPESTTR
460 470 480 490 500
KEPEPTTPKE PEPTTPKEPE PTTLKEPEPT TPKEPEPTTP KEPEPTTPKE
510 520 530 540 550
PEPTTPKEPE PTTPKEPEPT TPKEPEPTTP KEPEPTTPKE PEPTTPKKPE
560 570 580 590 600
PTTPKEPVPT TPKEPEPTTP KEPEPTTPKE PEPTTRKEPE PTTPKEPEPT
610 620 630 640 650
TPKEPEPTTP KKPEPTTTSP KTTTLKATTL APKVTAPAEE IQNKPEETTP
660 670 680 690 700
ASEDSDDSKT TLKPQKPTKA PKPTKKPTKA PKKPTSTKKP KTPKTRKPKT
710 720 730 740 750
TPSPLKTTSA TPELNTTPLE VMLPTTTIPK QTPNPETAEV NPDHEDADGG
760 770 780 790 800
EGEKPLIPGP PVLFPTAIPG TDLLAGRLNQ GININPMLSD ETNLCNGKPV
810 820 830 840 850
DGLTTLRNGT LVAFRGHYFW MLNPFRPPSP PRRITEVWGI PSPIDTVFTR
860 870 880 890 900
CNCEGKTFFF KDSQYWRFTN DVVDPGYPKQ IVKGFGGLTG KIVAALSIAK
910 920 930 940 950
YKDRPESVYF FKRGGNIQQY TYKQEPMKKC TGRRPAINYS VYGEAAQVRR
960 970 980 990 1000
RRFERAVGPF QTHTFRIHYS VPMRVSYQDK GFLHNEVKVS TMWRGFPNVV
1010 1020 1030 1040 1050
TSAITLPNIR KPDGYDYYAF SKDQYYNIDV PTRTARAITT RSGQTLSKIW

YNCP
Length:1,054
Mass (Da):115,996
Last modified:December 6, 2005 - v2
Checksum:i13312FB7070DF2A4
GO
Isoform B (identifier: Q9JM99-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     26-66: Missing.

Show »
Length:1,013
Mass (Da):111,425
Checksum:i49334633D98BD1E4
GO
Isoform C (identifier: Q9JM99-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     107-194: Missing.

Show »
Length:966
Mass (Da):106,637
Checksum:i123569A1FABFC5BD
GO
Isoform D (identifier: Q9JM99-4) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     26-66: Missing.
     107-194: Missing.

Show »
Length:925
Mass (Da):102,066
Checksum:i1CD5556F5467CD48
GO
Isoform E (identifier: Q9JM99-5) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     107-194: Missing.
     224-766: Missing.

Note: No experimental confirmation available.

Show »
Length:423
Mass (Da):47,989
Checksum:iEBC6B86287506E4C
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti65 – 662SP → TT in BAE28900. (PubMed:16141072)Curated
Sequence conflicti703 – 7031S → A in BAA92310. (PubMed:11124536)Curated
Sequence conflicti780 – 7801Q → R in BAA92310. (PubMed:11124536)Curated
Sequence conflicti788 – 7881L → P in BAA92310. (PubMed:11124536)Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei26 – 6641Missing in isoform B and isoform D. CuratedVSP_016471Add
BLAST
Alternative sequencei107 – 19488Missing in isoform C, isoform D and isoform E. 1 PublicationVSP_016472Add
BLAST
Alternative sequencei224 – 766543Missing in isoform E. 1 PublicationVSP_016473Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB034730 mRNA. Translation: BAA92310.1.
AK132597 mRNA. Translation: BAE21253.1.
AK149469 mRNA. Translation: BAE28900.1.
CCDSiCCDS48391.1. [Q9JM99-5]
RefSeqiNP_001103616.1. NM_001110146.1.
UniGeneiMm.174256.
Mm.329131.

Genome annotation databases

EnsembliENSMUST00000006171; ENSMUSP00000006171; ENSMUSG00000006014.
ENSMUST00000162367; ENSMUSP00000125551; ENSMUSG00000006014.
GeneIDi96875.
KEGGimmu:96875.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB034730 mRNA. Translation: BAA92310.1 .
AK132597 mRNA. Translation: BAE21253.1 .
AK149469 mRNA. Translation: BAE28900.1 .
CCDSi CCDS48391.1. [Q9JM99-5 ]
RefSeqi NP_001103616.1. NM_001110146.1.
UniGenei Mm.174256.
Mm.329131.

3D structure databases

ModBasei Search...
MobiDBi Search...

PTM databases

PhosphoSitei Q9JM99.

Proteomic databases

PaxDbi Q9JM99.
PRIDEi Q9JM99.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000006171 ; ENSMUSP00000006171 ; ENSMUSG00000006014 .
ENSMUST00000162367 ; ENSMUSP00000125551 ; ENSMUSG00000006014 .
GeneIDi 96875.
KEGGi mmu:96875.

Organism-specific databases

CTDi 10216.
MGIi MGI:1891344. Prg4.

Phylogenomic databases

eggNOGi NOG12793.
GeneTreei ENSGT00530000063751.
HOGENOMi HOG000115691.
HOVERGENi HBG101613.
InParanoidi Q9JM99.
OrthoDBi EOG7HMS1H.

Miscellaneous databases

NextBioi 352339.
PROi Q9JM99.
SOURCEi Search...

Gene expression databases

Bgeei Q9JM99.
ExpressionAtlasi Q9JM99. baseline and differential.
Genevestigatori Q9JM99.

Family and domain databases

Gene3Di 2.110.10.10. 2 hits.
InterProi IPR000585. Hemopexin-like_dom.
IPR018487. Hemopexin-like_repeat.
IPR018486. Hemopexin_CS.
IPR020436. Somatomedin_B_chordata.
IPR001212. Somatomedin_B_dom.
[Graphical view ]
Pfami PF00045. Hemopexin. 1 hit.
PF01033. Somatomedin_B. 2 hits.
[Graphical view ]
PRINTSi PR00022. SOMATOMEDINB.
SMARTi SM00120. HX. 2 hits.
SM00201. SO. 2 hits.
[Graphical view ]
SUPFAMi SSF50923. SSF50923. 2 hits.
PROSITEi PS00024. HEMOPEXIN. 1 hit.
PS51642. HEMOPEXIN_2. 2 hits.
PS00524. SMB_1. 2 hits.
PS50958. SMB_2. 2 hits.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Isolation, characterization and mapping of the mouse and human PRG4 (proteoglycan 4) genes."
    Ikegawa S., Sano M., Koshizuka Y., Nakamura Y.
    Cytogenet. Cell Genet. 90:291-297(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A), TISSUE SPECIFICITY, IDENTIFICATION OF ISOFORMS B; C AND D.
  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 E), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 572-1054.
    Strain: C57BL/6J.
    Tissue: Head and Liver.
  3. "The secreted glycoprotein lubricin protects cartilage surfaces and inhibits synovial cell overgrowth."
    Rhee D.K., Marcelino J., Baker M., Gong Y., Smits P., Lefebvre V., Jay G.D., Stewart M., Wang H., Warman M.L., Carpten J.D.
    J. Clin. Invest. 115:622-631(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, DISRUPTION PHENOTYPE.
  4. "Consequences of disease-causing mutations on lubricin protein synthesis, secretion, and post-translational processing."
    Rhee D.K., Marcelino J., Al-Mayouf S., Schelling D.K., Bartels C.F., Cui Y., Laxer R., Goldbach-Mansky R., Warman M.L.
    J. Biol. Chem. 280:31325-31332(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEOLYTIC PROCESSING, DISULFIDE BOND, MUTAGENESIS OF 949-ARG--ARG-955; 949-ARG--ARG-951; CYS-795; 851-CYS--CYS-853; CYS-930 AND CYS-1053.

Entry informationi

Entry nameiPRG4_MOUSE
AccessioniPrimary (citable) accession number: Q9JM99
Secondary accession number(s): Q3UEL1, Q3V198
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 6, 2005
Last sequence update: December 6, 2005
Last modified: October 29, 2014
This is version 98 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Miscellaneous

Different forms varying in molecular weight have been observed. Such forms are possibly due to different levels of glycosylation and protein cleavage.

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3