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Q61464

- ZN638_MOUSE

UniProt

Q61464 - ZN638_MOUSE

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Protein

Zinc finger protein 638

Gene

Znf638

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

Functioni

Early regulator of adipogenesis that works as a transcription cofactor of CEBPs, controlling the expression of PPARG and probably of other proadipogenic genes, such as SREBF1. Binds to cytidine clusters in double-stranded DNA.1 Publication

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri1876 – 190631Matrin-typePROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

  1. DNA binding Source: UniProtKB-KW
  2. nucleotide binding Source: InterPro
  3. RNA binding Source: UniProtKB-KW
  4. zinc ion binding Source: InterPro

GO - Biological processi

  1. regulation of transcription, DNA-templated Source: UniProtKB-KW
  2. transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Activator

Keywords - Biological processi

Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding, Metal-binding, RNA-binding, Zinc

Names & Taxonomyi

Protein namesi
Recommended name:
Zinc finger protein 638
Alternative name(s):
Nuclear protein 220
Zinc finger matrin-like protein
Gene namesi
Name:Znf638
Synonyms:Np220, Zfml
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 6

Organism-specific databases

MGIiMGI:1203484. Zfml.

Subcellular locationi

Nucleus speckle 1 PublicationPROSITE-ProRule annotation

GO - Cellular componenti

  1. nucleus Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 19601960Zinc finger protein 638PRO_0000082012Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei128 – 1281PhosphoserineBy similarity
Modified residuei381 – 3811PhosphoserineBy similarity
Modified residuei418 – 4181PhosphoserineBy similarity
Modified residuei554 – 5541PhosphoserineBy similarity
Modified residuei606 – 6061PhosphoserineBy similarity
Modified residuei615 – 6151PhosphoserineBy similarity
Modified residuei1099 – 10991PhosphoserineBy similarity
Modified residuei1400 – 14001PhosphoserineBy similarity
Modified residuei1661 – 16611PhosphoserineBy similarity
Modified residuei1864 – 18641PhosphoserineBy similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ61464.
PaxDbiQ61464.
PRIDEiQ61464.

PTM databases

PhosphoSiteiQ61464.

Expressioni

Developmental stagei

In an vitro adipocyte differentiation system, induced at the protein and RNA levels shortly after exposure to the induction mixture. Levels peak before PPARG induction and rapidly decrease during later stages of differentiation.1 Publication

Gene expression databases

BgeeiQ61464.
CleanExiMM_ZFML.
ExpressionAtlasiQ61464. baseline and differential.
GenevestigatoriQ61464.

Interactioni

Subunit structurei

Interacts with FHL2 (By similarity). Interacts with CEBPA, CEBPD and CEBPG.By similarity1 Publication

Protein-protein interaction databases

BioGridi201815. 1 interaction.
IntActiQ61464. 1 interaction.
MINTiMINT-4109575.

Structurei

3D structure databases

ProteinModelPortaliQ61464.
SMRiQ61464. Positions 666-745.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini676 – 75176RRM 1PROSITE-ProRule annotationAdd
BLAST
Domaini902 – 97675RRM 2PROSITE-ProRule annotationAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi470 – 575106Arg-richAdd
BLAST
Compositional biasi1577 – 15826Poly-Lys

Sequence similaritiesi

Contains 1 matrin-type zinc finger.PROSITE-ProRule annotation
Contains 2 RRM (RNA recognition motif) domains.PROSITE-ProRule annotation

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri1876 – 190631Matrin-typePROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

Repeat, Zinc-finger

Phylogenomic databases

eggNOGiNOG45231.
GeneTreeiENSGT00770000120663.
HOGENOMiHOG000082488.
HOVERGENiHBG094186.
InParanoidiQ61464.
PhylomeDBiQ61464.

Family and domain databases

Gene3Di3.30.70.330. 3 hits.
InterProiIPR012677. Nucleotide-bd_a/b_plait.
IPR000504. RRM_dom.
IPR007087. Znf_C2H2.
IPR015880. Znf_C2H2-like.
IPR000690. Znf_C2H2_matrin.
IPR003604. Znf_U1.
[Graphical view]
SMARTiSM00360. RRM. 2 hits.
SM00355. ZnF_C2H2. 2 hits.
SM00451. ZnF_U1. 2 hits.
[Graphical view]
PROSITEiPS50102. RRM. 1 hit.
PS50171. ZF_MATRIN. 1 hit.
[Graphical view]

Sequences (6)i

Sequence statusi: Complete.

This entry describes 6 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q61464-1) [UniParc]FASTAAdd to Basket

Also known as: Alpha

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
MSRPRFNPRG TFPLQRPRAP NPPGMRPPGP FVRPGSMGLP RFYPAGRARG
60 70 80 90 100
IPHRFPGHGS YQNMGPQRMN VQVTQHRTDP RLTKEKLDFP EAQQKKGKPH
110 120 130 140 150
GSRWDDESHI TPPVEVKQSS VTQVTEQSPK VQSRYTKESA SSILASFGLS
160 170 180 190 200
NEDLEELSRY PDEQLTPENM PLILRDIRMR KMSRRLPNLP SHSRNKETLS
210 220 230 240 250
NETVSSNVID YGHASKYGYT EDPLEVRIYD PEIPTDEVKN EFQPQQSISA
260 270 280 290 300
TVSTPNVICN SVFPGGDMFR QMDFPGESSS QSFFPVESGT KMSGLHISGQ
310 320 330 340 350
SVLEPVKSIS QSISQTVSQT TSQSLNPPSM NQVPFTFELD AVLRQQERIS
360 370 380 390 400
QKSVISSADA HGGPTESKKD YQSEADLPIR SPFGIVKASW LPKFTQAGAQ
410 420 430 440 450
KMKRLPTPSM MNDYYAASPR IFPHLCSLCN VECSHLKDWI QHQNTSTHIE
460 470 480 490 500
SCRQLRQQYP DWNPEILPSR RNESNRKENE TPRRRSHSPS PRHSRRSSSG
510 520 530 540 550
HRIRRSRSPV RYIYRPRSRS PRICHRFISK YRSRSRSRSR SRSPYRSRNL
560 570 580 590 600
LRRSPKSYRS ASPERTSRKS VRSDRKKALE DGGQRSVHGT EVTKQKHTET
610 620 630 640 650
VDKGLSPAQK PKLASGTKPS AKSLSSVKSD SHLGAYSAHK SENLEDDTLP
660 670 680 690 700
EGKQESGKSA LAQRKPQKDQ SLSSNSILLV SELPEDGFTE EDIRKAFLPF
710 720 730 740 750
GKISDVLLVP CRNEAYLEME LRKAVTSIMK YIETMPLVIK GKSVKVCVPG
760 770 780 790 800
KKKPQNKEMK KKPSDIKKSS ASALKKETDA SKTMETVSSS SSAKSGQIKS
810 820 830 840 850
STVKVNKCAG KSAGSVKSVV TVAAKGKASI KTAKSGKKSL EAKKSGNIKN
860 870 880 890 900
KDSNKPVTVP ANSEIKASSE DKATGKSAEE SPSGTLEATE KEPVNKESEE
910 920 930 940 950
MSVVFISNLP NKGYSTEEIY NLAKPFGALK DILVLSSHKK AYIEINKKSA
960 970 980 990 1000
DSMVKFYTCF PISMDGNQLS ISMAPEHVDL KDEEALFTTL IQENDPEANI
1010 1020 1030 1040 1050
DKIYNRFVHL DNLPEDGLQC VLCVGHQFGK VDRYMFMSNK NKVILQLESP
1060 1070 1080 1090 1100
ESALSMYNFL KQNPQNIGEH VLTCTLSPKT DSEVQRKNDL ELGKGSTFSP
1110 1120 1130 1140 1150
DLKNSPVDES EVQTAADSSS VKPSEVEEET TSNIGTETSV HQEELGKEEP
1160 1170 1180 1190 1200
KQALCESDFA IQTLELEAQG AEVSIEIPLV ASTPANIELF SENIDESALN
1210 1220 1230 1240 1250
QQMYTSDFEK EEAEVTNPET ELAVSDSVFI EERNIKGIIE DSPSETEDIF
1260 1270 1280 1290 1300
SGIVQPMVDA IAEVDKHETV SEVLPSACNV TQAPGSYIED EKVVSKKDIA
1310 1320 1330 1340 1350
EKVILDEKEE DEFNVKETRM DLQVKTEKAE KNEAIIFKEK LEKIIAAIRE
1360 1370 1380 1390 1400
KPIESSVIKA DPTKGLDQTS KPDETGKSSV LTVSNVYSSK SSIKATVVSS
1410 1420 1430 1440 1450
PKAKSTPSKT ESHSTFPKPV LREQIKADKK VSAKEFGLLK NTRSGLAESN
1460 1470 1480 1490 1500
SKSKPTQIGV NRGCSGRISA LQCKDSKVDY KDITKQSQET ETKPPIMKRD
1510 1520 1530 1540 1550
DSNNKALALQ NTKNSKSTTD RSSKSKEEPL FTFNLDEFVT VDEVIEEVNP
1560 1570 1580 1590 1600
SQAKQNPLKG KRKEALKISP SPELNLKKKK GKTSVPHSVE GELSFVTLDE
1610 1620 1630 1640 1650
IGEEEDATVQ ALVTVDEVID EEELNMEEMV KNSNSLLTLD ELIDQDDCIP
1660 1670 1680 1690 1700
HSGPKDVTVL SMAEEQDLQQ ERLVTVDEIG EVEESADITF ATLNAKRDKR
1710 1720 1730 1740 1750
DSIGFISSQM PEDPSTLVTV DEIQDDSSDF HLMTLDEVTE EDENSLADFN
1760 1770 1780 1790 1800
NLKEELNFVT VDEVGDEEDG DNDSKVELAR GKIEHHTDKK GNRKRRAVDP
1810 1820 1830 1840 1850
KKSKLDSFSQ VGPGSETVTQ KDLKTMPERH LAAKTPMKRV RLGKSSPSQK
1860 1870 1880 1890 1900
VAEPTKGEEA FQMSEGVDDA ELKDSEPDEK RRKTQDSSVG KSMTSDVPGD
1910 1920 1930 1940 1950
LDFLVPKAGF FCPICSLFYS GEKAMANHCK STRHKQNTEK FMAKQRKEKE
1960
QNETEERSSR
Length:1,960
Mass (Da):218,134
Last modified:July 19, 2005 - v2
Checksum:i27DF6740BFE410ED
GO
Isoform 2 (identifier: Q61464-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     810-832: Missing.
     1147-1200: KEEPKQALCE...SENIDESALN → PGSETVTQKD...GEEAFQMSEG
     1201-1832: Missing.
     1833-1866: Missing.

Note: No experimental confirmation available.

Show »
Length:1,271
Mass (Da):142,198
Checksum:i342F546EFC525823
GO
Isoform 3 (identifier: Q61464-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     438-454: DWIQHQNTSTHIESCRQ → VSVFKRLLYNDAQCPGF
     456-1960: Missing.

Note: No experimental confirmation available.

Show »
Length:455
Mass (Da):50,951
Checksum:i5B605A1F5153B1C3
GO
Isoform 4 (identifier: Q61464-4) [UniParc]FASTAAdd to Basket

Also known as: Beta

The sequence of this isoform differs from the canonical sequence as follows:
     1833-1866: Missing.

Show »
Length:1,926
Mass (Da):214,460
Checksum:i3B2F3A7AF4580259
GO
Isoform 5 (identifier: Q61464-5) [UniParc]FASTAAdd to Basket

Also known as: Gamma

The sequence of this isoform differs from the canonical sequence as follows:
     1147-1832: Missing.

Show »
Length:1,274
Mass (Da):142,134
Checksum:i344E096A235A8168
GO
Isoform 6 (identifier: Q61464-7) [UniParc]FASTAAdd to Basket

Also known as: Delta

The sequence of this isoform differs from the canonical sequence as follows:
     1147-1866: Missing.

Show »
Length:1,240
Mass (Da):138,461
Checksum:iF2BF9C3AA2F2883B
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti32 – 321V → L in AAH76615. (PubMed:15489334)Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei438 – 45417DWIQH…ESCRQ → VSVFKRLLYNDAQCPGF in isoform 3. 1 PublicationVSP_014807Add
BLAST
Alternative sequencei456 – 19601505Missing in isoform 3. 1 PublicationVSP_014808Add
BLAST
Alternative sequencei810 – 83223Missing in isoform 2. 1 PublicationVSP_014809Add
BLAST
Alternative sequencei1147 – 1866720Missing in isoform 6. 1 PublicationVSP_014810Add
BLAST
Alternative sequencei1147 – 1832686Missing in isoform 5. 1 PublicationVSP_014811Add
BLAST
Alternative sequencei1147 – 120054KEEPK…ESALN → PGSETVTQKDLKTMPERHLA AKTPMKRVRIGKSSPSQKVA EPTKGEEAFQMSEG in isoform 2. 1 PublicationVSP_014812Add
BLAST
Alternative sequencei1201 – 1832632Missing in isoform 2. 1 PublicationVSP_014813Add
BLAST
Alternative sequencei1833 – 186634Missing in isoform 2 and isoform 4. 2 PublicationsVSP_014814Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D83033 mRNA. Translation: BAA11749.1.
AK043029 mRNA. Translation: BAC31439.1.
BC076615 mRNA. Translation: AAH76615.1.
CCDSiCCDS20288.1. [Q61464-4]
CCDS51823.1. [Q61464-2]
PIRiJC4842.
RefSeqiNP_001159843.1. NM_001166371.1. [Q61464-2]
NP_032743.2. NM_008717.3.
UniGeneiMm.132392.

Genome annotation databases

EnsembliENSMUST00000113835; ENSMUSP00000109466; ENSMUSG00000030016. [Q61464-2]
GeneIDi18139.
KEGGimmu:18139.
UCSCiuc009coo.2. mouse. [Q61464-3]
uc009coq.2. mouse. [Q61464-2]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D83033 mRNA. Translation: BAA11749.1 .
AK043029 mRNA. Translation: BAC31439.1 .
BC076615 mRNA. Translation: AAH76615.1 .
CCDSi CCDS20288.1. [Q61464-4 ]
CCDS51823.1. [Q61464-2 ]
PIRi JC4842.
RefSeqi NP_001159843.1. NM_001166371.1. [Q61464-2 ]
NP_032743.2. NM_008717.3.
UniGenei Mm.132392.

3D structure databases

ProteinModelPortali Q61464.
SMRi Q61464. Positions 666-745.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 201815. 1 interaction.
IntActi Q61464. 1 interaction.
MINTi MINT-4109575.

PTM databases

PhosphoSitei Q61464.

Proteomic databases

MaxQBi Q61464.
PaxDbi Q61464.
PRIDEi Q61464.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000113835 ; ENSMUSP00000109466 ; ENSMUSG00000030016 . [Q61464-2 ]
GeneIDi 18139.
KEGGi mmu:18139.
UCSCi uc009coo.2. mouse. [Q61464-3 ]
uc009coq.2. mouse. [Q61464-2 ]

Organism-specific databases

CTDi 18139.
MGIi MGI:1203484. Zfml.

Phylogenomic databases

eggNOGi NOG45231.
GeneTreei ENSGT00770000120663.
HOGENOMi HOG000082488.
HOVERGENi HBG094186.
InParanoidi Q61464.
PhylomeDBi Q61464.

Miscellaneous databases

NextBioi 293380.
PROi Q61464.
SOURCEi Search...

Gene expression databases

Bgeei Q61464.
CleanExi MM_ZFML.
ExpressionAtlasi Q61464. baseline and differential.
Genevestigatori Q61464.

Family and domain databases

Gene3Di 3.30.70.330. 3 hits.
InterProi IPR012677. Nucleotide-bd_a/b_plait.
IPR000504. RRM_dom.
IPR007087. Znf_C2H2.
IPR015880. Znf_C2H2-like.
IPR000690. Znf_C2H2_matrin.
IPR003604. Znf_U1.
[Graphical view ]
SMARTi SM00360. RRM. 2 hits.
SM00355. ZnF_C2H2. 2 hits.
SM00451. ZnF_U1. 2 hits.
[Graphical view ]
PROSITEi PS50102. RRM. 1 hit.
PS50171. ZF_MATRIN. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "A family of novel DNA-binding nuclear proteins having polypyrimidine tract-binding motif and arginine/serine-rich motif."
    Matsushima Y., Ohshima M., Sonoda M., Kitagawa Y.
    Biochem. Biophys. Res. Commun. 223:427-433(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 4; 5 AND 6).
    Tissue: Heart.
  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 3).
    Strain: C57BL/6J.
    Tissue: Cerebellum.
  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 2).
    Strain: C57BL/6.
    Tissue: Head.
  4. Lubec G., Kang S.U.
    Submitted (APR-2007) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 761-768; 873-891; 1395-1404; 1506-1513 AND 1874-1881, IDENTIFICATION BY MASS SPECTROMETRY.
    Strain: C57BL/6.
    Tissue: Brain.
  5. "Regulation of adipocyte differentiation by the zinc finger protein ZNF638."
    Meruvu S., Hugendubler L., Mueller E.
    J. Biol. Chem. 286:26516-26523(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH CEBPA; CEBPD AND CEBPG, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE.

Entry informationi

Entry nameiZN638_MOUSE
AccessioniPrimary (citable) accession number: Q61464
Secondary accession number(s): Q6DFV9, Q8C941
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 19, 2005
Last sequence update: July 19, 2005
Last modified: November 26, 2014
This is version 112 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, 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