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Q9UQR0

- SCML2_HUMAN

UniProt

Q9UQR0 - SCML2_HUMAN

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Protein

Sex comb on midleg-like protein 2

Gene
SCML2
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 4 out of 5 - Experimental evidence at protein leveli

Functioni

Putative Polycomb group (PcG) protein. PcG proteins act by forming multiprotein complexes, which are required to maintain the transcriptionally repressive state of homeotic genes throughout development By similarity.

GO - Molecular functioni

  1. DNA binding Source: ProtInc
  2. sequence-specific DNA binding transcription factor activity Source: ProtInc

GO - Biological processi

  1. anatomical structure morphogenesis Source: ProtInc
  2. transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Repressor

Keywords - Biological processi

Transcription, Transcription regulation

Names & Taxonomyi

Protein namesi
Recommended name:
Sex comb on midleg-like protein 2
Gene namesi
Name:SCML2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome X

Organism-specific databases

HGNCiHGNC:10581. SCML2.

Subcellular locationi

Nucleus Inferred

GO - Cellular componenti

  1. nucleus Source: UniProtKB
  2. PcG protein complex Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA34999.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 700700Sex comb on midleg-like protein 2PRO_0000097628Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei256 – 2561Phosphoserine1 Publication
Modified residuei267 – 2671Phosphoserine1 Publication
Modified residuei299 – 2991Phosphoserine1 Publication
Modified residuei300 – 3001Phosphoserine1 Publication
Modified residuei305 – 3051Phosphothreonine1 Publication
Modified residuei499 – 4991Phosphoserine4 Publications
Modified residuei503 – 5031Phosphothreonine2 Publications
Modified residuei511 – 5111Phosphoserine4 Publications
Modified residuei583 – 5831Phosphoserine1 Publication
Modified residuei590 – 5901Phosphoserine4 Publications
Modified residuei594 – 5941Phosphoserine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ9UQR0.
PaxDbiQ9UQR0.
PeptideAtlasiQ9UQR0.
PRIDEiQ9UQR0.

PTM databases

PhosphoSiteiQ9UQR0.

Expressioni

Tissue specificityi

Highly expressed in placenta, thymus and testis. Detected at lower levels in brain, liver, skeletal muscle, pancreas and ovary.1 Publication

Gene expression databases

ArrayExpressiQ9UQR0.
BgeeiQ9UQR0.
CleanExiHS_SCML2.
GenevestigatoriQ9UQR0.

Organism-specific databases

HPAiHPA001662.

Interactioni

Protein-protein interaction databases

BioGridi115661. 6 interactions.
DIPiDIP-53760N.
IntActiQ9UQR0. 2 interactions.
STRINGi9606.ENSP00000251900.

Structurei

Secondary structure

1
700
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi35 – 428
Helixi49 – 513
Beta strandi52 – 543
Beta strandi68 – 736
Beta strandi76 – 8914
Beta strandi92 – 976
Beta strandi102 – 1043
Beta strandi106 – 1094
Beta strandi115 – 1173
Helixi120 – 1234
Helixi138 – 1403
Helixi141 – 1499
Helixi157 – 1593
Beta strandi177 – 1815
Beta strandi189 – 19810
Beta strandi201 – 2066
Helixi211 – 2133
Beta strandi215 – 2184
Helixi229 – 2335
Beta strandi356 – 3594
Beta strandi369 – 3713
Helixi373 – 3786
Beta strandi383 – 3875
Helixi388 – 40215
Helixi406 – 4094
Beta strandi422 – 4276
Beta strandi430 – 4356
Helixi442 – 45514

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1OI1X-ray1.78A24-243[»]
2BIVX-ray1.70A/B/C1-243[»]
2MEMNMR-A354-468[»]
2VYTX-ray1.90A/B24-243[»]
4EDUX-ray2.58A29-243[»]
ProteinModelPortaliQ9UQR0.
SMRiQ9UQR0. Positions 5-269, 628-694.

Miscellaneous databases

EvolutionaryTraceiQ9UQR0.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati33 – 13199MBT 1Add
BLAST
Repeati139 – 240102MBT 2Add
BLAST
Domaini631 – 70070SAMAdd
BLAST

Sequence similaritiesi

Belongs to the SCM family.
Contains 2 MBT repeats.

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiNOG315447.
HOGENOMiHOG000236280.
HOVERGENiHBG056406.
InParanoidiQ9UQR0.
KOiK11465.
OMAiTSKIVMS.
OrthoDBiEOG73BVC2.
PhylomeDBiQ9UQR0.
TreeFamiTF106488.

Family and domain databases

Gene3Di1.10.150.50. 1 hit.
InterProiIPR021987. DUF3588.
IPR004092. Mbt.
IPR001660. SAM.
IPR013761. SAM/pointed.
IPR021129. SAM_type1.
[Graphical view]
PfamiPF12140. DUF3588. 1 hit.
PF02820. MBT. 2 hits.
PF00536. SAM_1. 1 hit.
[Graphical view]
SMARTiSM00561. MBT. 2 hits.
SM00454. SAM. 1 hit.
[Graphical view]
SUPFAMiSSF47769. SSF47769. 1 hit.
PROSITEiPS51079. MBT. 2 hits.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q9UQR0-1) [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

MGQTVNEDSM DVKKENQEKT PQSSTSSVQR DDFHWEEYLK ETGSISAPSE    50
CFRQSQIPPV NDFKVGMKLE ARDPRNATSV CIATVIGITG ARLRLRLDGS 100
DNRNDFWRLV DSPDIQPVGT CEKEGDLLQP PLGYQMNTSS WPMFLLKTLN 150
GSEMASATLF KKEPPKPPLN NFKVGMKLEA IDKKNPYLIC PATIGDVKGD 200
EVHITFDGWS GAFDYWCKYD SRDIFPAGWC RLTGDVLQPP GTSVPIVKNI 250
AKTESSPSEA SQHSMQSPQK TTLILPTQQV RRSSRIKPPG PTAVPKRSSS 300
VKNITPRKKG PNSGKKEKPL PVICSTSAAS LKSLTRDRGM LYKDVASGPC 350
KIVMSTVCVY VNKHGNFGPH LDPKRIQQLP DHFGPGPVNV VLRRIVQACV 400
DCALETKTVF GYLKPDNRGG EVITASFDGE THSIQLPPVN SASFALRFLE 450
NFCHSLQCDN LLSSQPFSSS RGHTHSSAEH DKNQSAKEDV TERQSTKRSP 500
QQTVPYVVPL SPKLPKTKEY ASEGEPLFAG GSAIPKEENL SEDSKSSSLN 550
SGNYLNPACR NPMYIHTSVS QDFSRSVPGT TSSPLVGDIS PKSSPHEVKF 600
QMQRKSEAPS YIAVPDPSVL KQGFSKDPST WSVDEVIQFM KHTDPQISGP 650
LADLFRQHEI DGKALFLLKS DVMMKYMGLK LGPALKLCYY IEKLKEGKYS 700
Length:700
Mass (Da):77,257
Last modified:May 1, 2000 - v1
Checksum:i05E086D4928DEE73
GO
Isoform 2 (identifier: Q9UQR0-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-562: Missing.

Note: No experimental confirmation available.

Show »
Length:138
Mass (Da):15,471
Checksum:iA1FBA9624DF36ABE
GO

Sequence cautioni

The sequence AAH51913.1 differs from that shown. Reason: Erroneous initiation.

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 562562Missing in isoform 2. VSP_010277Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
Y18004 mRNA. Translation: CAB38943.1.
AL833937 mRNA. Translation: CAD38792.1.
AL096763, AL031007, Z93023 Genomic DNA. Translation: CAI42221.1.
AL031007, AL096763, Z93023 Genomic DNA. Translation: CAI43048.1.
Z93023, AL031007, AL096763 Genomic DNA. Translation: CAI43176.1.
BC040497 mRNA. No translation available.
CH471074 Genomic DNA. Translation: EAW98937.1.
BC051913 mRNA. Translation: AAH51913.1. Different initiation.
BC064617 mRNA. Translation: AAH64617.1.
CCDSiCCDS14185.1. [Q9UQR0-1]
RefSeqiNP_006080.1. NM_006089.2. [Q9UQR0-1]
UniGeneiHs.495774.

Genome annotation databases

EnsembliENST00000251900; ENSP00000251900; ENSG00000102098. [Q9UQR0-1]
GeneIDi10389.
KEGGihsa:10389.
UCSCiuc004cyl.2. human. [Q9UQR0-1]

Polymorphism databases

DMDMi47117338.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
Y18004 mRNA. Translation: CAB38943.1 .
AL833937 mRNA. Translation: CAD38792.1 .
AL096763 , AL031007 , Z93023 Genomic DNA. Translation: CAI42221.1 .
AL031007 , AL096763 , Z93023 Genomic DNA. Translation: CAI43048.1 .
Z93023 , AL031007 , AL096763 Genomic DNA. Translation: CAI43176.1 .
BC040497 mRNA. No translation available.
CH471074 Genomic DNA. Translation: EAW98937.1 .
BC051913 mRNA. Translation: AAH51913.1 . Different initiation.
BC064617 mRNA. Translation: AAH64617.1 .
CCDSi CCDS14185.1. [Q9UQR0-1 ]
RefSeqi NP_006080.1. NM_006089.2. [Q9UQR0-1 ]
UniGenei Hs.495774.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1OI1 X-ray 1.78 A 24-243 [» ]
2BIV X-ray 1.70 A/B/C 1-243 [» ]
2MEM NMR - A 354-468 [» ]
2VYT X-ray 1.90 A/B 24-243 [» ]
4EDU X-ray 2.58 A 29-243 [» ]
ProteinModelPortali Q9UQR0.
SMRi Q9UQR0. Positions 5-269, 628-694.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 115661. 6 interactions.
DIPi DIP-53760N.
IntActi Q9UQR0. 2 interactions.
STRINGi 9606.ENSP00000251900.

PTM databases

PhosphoSitei Q9UQR0.

Polymorphism databases

DMDMi 47117338.

Proteomic databases

MaxQBi Q9UQR0.
PaxDbi Q9UQR0.
PeptideAtlasi Q9UQR0.
PRIDEi Q9UQR0.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000251900 ; ENSP00000251900 ; ENSG00000102098 . [Q9UQR0-1 ]
GeneIDi 10389.
KEGGi hsa:10389.
UCSCi uc004cyl.2. human. [Q9UQR0-1 ]

Organism-specific databases

CTDi 10389.
GeneCardsi GC0XM018167.
HGNCi HGNC:10581. SCML2.
HPAi HPA001662.
MIMi 300208. gene.
neXtProti NX_Q9UQR0.
PharmGKBi PA34999.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG315447.
HOGENOMi HOG000236280.
HOVERGENi HBG056406.
InParanoidi Q9UQR0.
KOi K11465.
OMAi TSKIVMS.
OrthoDBi EOG73BVC2.
PhylomeDBi Q9UQR0.
TreeFami TF106488.

Miscellaneous databases

EvolutionaryTracei Q9UQR0.
GenomeRNAii 10389.
NextBioi 39356.
PROi Q9UQR0.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q9UQR0.
Bgeei Q9UQR0.
CleanExi HS_SCML2.
Genevestigatori Q9UQR0.

Family and domain databases

Gene3Di 1.10.150.50. 1 hit.
InterProi IPR021987. DUF3588.
IPR004092. Mbt.
IPR001660. SAM.
IPR013761. SAM/pointed.
IPR021129. SAM_type1.
[Graphical view ]
Pfami PF12140. DUF3588. 1 hit.
PF02820. MBT. 2 hits.
PF00536. SAM_1. 1 hit.
[Graphical view ]
SMARTi SM00561. MBT. 2 hits.
SM00454. SAM. 1 hit.
[Graphical view ]
SUPFAMi SSF47769. SSF47769. 1 hit.
PROSITEi PS51079. MBT. 2 hits.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Identification of SCML2, a second human gene homologous to the Drosophila Sex comb on midleg (Scm): a new gene cluster on Xp22."
    Montini E., Buchner G., Spalluto C., Andolfi G., Caruso A., de Dunnen J.T., Trump D., Rocchi M., Ballabio A., Franco B.
    Genomics 58:65-72(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
    Tissue: Testis.
  3. "The DNA sequence of the human X chromosome."
    Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D., Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.
    , Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S., Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S., Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D., Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H., McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K., Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D., Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R., Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A., Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F., Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S., Rogers J., Bentley D.R.
    Nature 434:325-337(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "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 1).
    Tissue: Testis and Uterus.
  6. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic kidney.
  7. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-256; SER-267; SER-299; SER-300; THR-305; SER-499; THR-503; SER-511; SER-583; SER-590 AND SER-594, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  8. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  9. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
    Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
    Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-499; SER-511 AND SER-590, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  10. "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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-499; THR-503; SER-511 AND SER-590, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  11. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  12. "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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-499; SER-511 AND SER-590, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  13. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  14. "Crystal structure of the malignant brain tumor (MBT) repeats in sex comb on midleg-like 2 (SCML2)."
    Sathyamurthy A., Allen M.D., Murzin A.G., Bycroft M.
    J. Biol. Chem. 278:46968-46973(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.78 ANGSTROMS) OF 33-243.

Entry informationi

Entry nameiSCML2_HUMAN
AccessioniPrimary (citable) accession number: Q9UQR0
Secondary accession number(s): Q5JXE6
, Q86U98, Q8IWD0, Q8NDP2, Q9UGC5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 10, 2004
Last sequence update: May 1, 2000
Last modified: July 9, 2014
This is version 122 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome X
    Human chromosome X: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  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

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