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Protein

TSC22 domain family protein 4

Gene

TSC22D4

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

Functioni

Transcriptional repressor.

GO - Molecular functioni

GO - Biological processi

  • negative regulation of transcription, DNA-templated Source: UniProtKB
  • 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:
TSC22 domain family protein 4
Alternative name(s):
TSC22-related-inducible leucine zipper protein 2
Tsc-22-like protein THG-1
Gene namesi
Name:TSC22D4
Synonyms:THG1, TILZ2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 7

Organism-specific databases

HGNCiHGNC:21696. TSC22D4.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA142670698.

Polymorphism and mutation databases

BioMutaiTSC22D4.
DMDMi14195254.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 395395TSC22 domain family protein 4PRO_0000219374Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei49 – 491PhosphoserineCombined sources
Modified residuei62 – 621PhosphoserineCombined sources
Modified residuei165 – 1651PhosphoserineCombined sources
Modified residuei187 – 1871PhosphoserineBy similarity
Modified residuei189 – 1891PhosphoserineBy similarity
Modified residuei211 – 2111PhosphothreonineCombined sources
Modified residuei225 – 2251PhosphoserineBy similarity
Modified residuei229 – 2291PhosphothreonineCombined sources
Modified residuei260 – 2601PhosphoserineBy similarity
Modified residuei264 – 2641PhosphoserineBy similarity
Modified residuei279 – 2791PhosphoserineCombined sources
Modified residuei370 – 3701PhosphoserineCombined sources

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiQ9Y3Q8.
MaxQBiQ9Y3Q8.
PaxDbiQ9Y3Q8.
PeptideAtlasiQ9Y3Q8.
PRIDEiQ9Y3Q8.

PTM databases

iPTMnetiQ9Y3Q8.
PhosphoSiteiQ9Y3Q8.

Expressioni

Gene expression databases

BgeeiQ9Y3Q8.
CleanExiHS_TSC22D4.
ExpressionAtlasiQ9Y3Q8. baseline and differential.
GenevisibleiQ9Y3Q8. HS.

Organism-specific databases

HPAiHPA006757.

Interactioni

Subunit structurei

Forms a homodimer or heterodimer. Can form a heterodimer with TSC22D1.

Binary interactionsi

WithEntry#Exp.IntActNotes
AIFM1O958312EBI-739485,EBI-356440
APIPQ96GX93EBI-739485,EBI-359248
CCDC146Q8IYE0-23EBI-739485,EBI-10247802
KEAP1Q141453EBI-739485,EBI-751001
LMO2P257913EBI-739485,EBI-739696
MAD2L1Q132574EBI-739485,EBI-78203
MYLIPQ8WY643EBI-739485,EBI-6952711
NRBP1Q9UHY14EBI-739485,EBI-749731
NRBP2D3DWK93EBI-739485,EBI-10176870
PCBP1Q153652EBI-739485,EBI-946095
PIH1D1Q9NWS04EBI-739485,EBI-357318
PIN1Q135264EBI-739485,EBI-714158
POLR1CO151603EBI-739485,EBI-1055079
PPLO604373EBI-739485,EBI-368321
PRKAA1Q131313EBI-739485,EBI-1181405
PRKAA2P546463EBI-739485,EBI-1383852
SMAD3P840222EBI-739485,EBI-347161
ZBTB24O431673EBI-739485,EBI-744471
ZMYND10O758005EBI-739485,EBI-747061

Protein-protein interaction databases

BioGridi123563. 79 interactions.
IntActiQ9Y3Q8. 51 interactions.
MINTiMINT-1442100.
STRINGi9606.ENSP00000300181.

Structurei

3D structure databases

ProteinModelPortaliQ9Y3Q8.
SMRiQ9Y3Q8. Positions 326-379.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni344 – 36522Leucine-zipperAdd
BLAST

Sequence similaritiesi

Belongs to the TSC-22/Dip/Bun family.Curated

Phylogenomic databases

eggNOGiKOG4797. Eukaryota.
ENOG411251N. LUCA.
GeneTreeiENSGT00530000063062.
HOGENOMiHOG000015349.
HOVERGENiHBG069048.
InParanoidiQ9Y3Q8.
OMAiCVDIYER.
OrthoDBiEOG7RZ5PT.
PhylomeDBiQ9Y3Q8.
TreeFamiTF338725.

Family and domain databases

InterProiIPR000580. TSC-22_Dip_Bun.
[Graphical view]
PANTHERiPTHR12348. PTHR12348. 1 hit.
PfamiPF01166. TSC22. 1 hit.
[Graphical view]
ProDomiPD007152. TSC-22_Dip_Bun. 1 hit.
[Graphical view] [Entries sharing at least one domain]
PROSITEiPS01289. TSC22. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q9Y3Q8-1) [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
MSGGKKKSSF QITSVTTDYE GPGSPGASDP PTPQPPTGPP PRLPNGEPSP
60 70 80 90 100
DPGGKGTPRN GSPPPGAPSS RFRVVKLPHG LGEPYRRGRW TCVDVYERDL
110 120 130 140 150
EPHSFGGLLE GIRGASGGAG GRSLDSRLEL ASLGLGAPTP PSGLSQGPTS
160 170 180 190 200
WLRPPPTSPG PQARSFTGGL GQLVVPSKAK AEKPPLSASS PQQRPPEPET
210 220 230 240 250
GESAGTSRAA TPLPSLRVEA EAGGSGARTP PLSRRKAVDM RLRMELGAPE
260 270 280 290 300
EMGQVPPLDS RPSSPALYFT HDASLVHKSP DPFGAVAAQK FSLAHSMLAI
310 320 330 340 350
SGHLDSDDDS GSGSLVGIDN KIEQAMDLVK SHLMFAVREE VEVLKEQIRE
360 370 380 390
LAERNAALEQ ENGLLRALAS PEQLAQLPSS GVPRLGPPAP NGPSV
Length:395
Mass (Da):41,026
Last modified:June 1, 2001 - v2
Checksum:iDA08B5617C9BB151
GO
Isoform 2 (identifier: Q9Y3Q8-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-239: Missing.

Note: No experimental confirmation available.
Show »
Length:156
Mass (Da):16,685
Checksum:iF240ECD884DDFFF6
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti355 – 3562NA → KR in CAB43491 (PubMed:10488076).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti329 – 3291V → M in a breast cancer sample; somatic mutation. 1 Publication
VAR_036284

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 239239Missing in isoform 2. 1 PublicationVSP_056245Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ133115 mRNA. Translation: CAB43491.1.
AK297702 mRNA. Translation: BAG60060.1.
AC092849 Genomic DNA. No translation available.
CH236956 Genomic DNA. Translation: EAL23831.1.
CH471091 Genomic DNA. Translation: EAW76527.1.
CH471091 Genomic DNA. Translation: EAW76528.1.
CH471091 Genomic DNA. Translation: EAW76529.1.
CH471091 Genomic DNA. Translation: EAW76531.1.
BC001486 mRNA. Translation: AAH01486.1.
BC001966 mRNA. Translation: AAH01966.1.
BC002972 mRNA. Translation: AAH02972.1.
BC010406 mRNA. Translation: AAH10406.1.
CCDSiCCDS5695.1. [Q9Y3Q8-1]
RefSeqiNP_001289972.1. NM_001303043.1. [Q9Y3Q8-1]
NP_112197.1. NM_030935.4. [Q9Y3Q8-1]
UniGeneiHs.469798.

Genome annotation databases

EnsembliENST00000300181; ENSP00000300181; ENSG00000166925. [Q9Y3Q8-1]
ENST00000393991; ENSP00000377560; ENSG00000166925. [Q9Y3Q8-2]
GeneIDi81628.
KEGGihsa:81628.
UCSCiuc003uva.3. human. [Q9Y3Q8-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ133115 mRNA. Translation: CAB43491.1.
AK297702 mRNA. Translation: BAG60060.1.
AC092849 Genomic DNA. No translation available.
CH236956 Genomic DNA. Translation: EAL23831.1.
CH471091 Genomic DNA. Translation: EAW76527.1.
CH471091 Genomic DNA. Translation: EAW76528.1.
CH471091 Genomic DNA. Translation: EAW76529.1.
CH471091 Genomic DNA. Translation: EAW76531.1.
BC001486 mRNA. Translation: AAH01486.1.
BC001966 mRNA. Translation: AAH01966.1.
BC002972 mRNA. Translation: AAH02972.1.
BC010406 mRNA. Translation: AAH10406.1.
CCDSiCCDS5695.1. [Q9Y3Q8-1]
RefSeqiNP_001289972.1. NM_001303043.1. [Q9Y3Q8-1]
NP_112197.1. NM_030935.4. [Q9Y3Q8-1]
UniGeneiHs.469798.

3D structure databases

ProteinModelPortaliQ9Y3Q8.
SMRiQ9Y3Q8. Positions 326-379.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi123563. 79 interactions.
IntActiQ9Y3Q8. 51 interactions.
MINTiMINT-1442100.
STRINGi9606.ENSP00000300181.

PTM databases

iPTMnetiQ9Y3Q8.
PhosphoSiteiQ9Y3Q8.

Polymorphism and mutation databases

BioMutaiTSC22D4.
DMDMi14195254.

Proteomic databases

EPDiQ9Y3Q8.
MaxQBiQ9Y3Q8.
PaxDbiQ9Y3Q8.
PeptideAtlasiQ9Y3Q8.
PRIDEiQ9Y3Q8.

Protocols and materials databases

DNASUi81628.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000300181; ENSP00000300181; ENSG00000166925. [Q9Y3Q8-1]
ENST00000393991; ENSP00000377560; ENSG00000166925. [Q9Y3Q8-2]
GeneIDi81628.
KEGGihsa:81628.
UCSCiuc003uva.3. human. [Q9Y3Q8-1]

Organism-specific databases

CTDi81628.
GeneCardsiTSC22D4.
HGNCiHGNC:21696. TSC22D4.
HPAiHPA006757.
MIMi611914. gene.
neXtProtiNX_Q9Y3Q8.
PharmGKBiPA142670698.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG4797. Eukaryota.
ENOG411251N. LUCA.
GeneTreeiENSGT00530000063062.
HOGENOMiHOG000015349.
HOVERGENiHBG069048.
InParanoidiQ9Y3Q8.
OMAiCVDIYER.
OrthoDBiEOG7RZ5PT.
PhylomeDBiQ9Y3Q8.
TreeFamiTF338725.

Miscellaneous databases

GenomeRNAii81628.
NextBioi35464977.
PROiQ9Y3Q8.
SOURCEiSearch...

Gene expression databases

BgeeiQ9Y3Q8.
CleanExiHS_TSC22D4.
ExpressionAtlasiQ9Y3Q8. baseline and differential.
GenevisibleiQ9Y3Q8. HS.

Family and domain databases

InterProiIPR000580. TSC-22_Dip_Bun.
[Graphical view]
PANTHERiPTHR12348. PTHR12348. 1 hit.
PfamiPF01166. TSC22. 1 hit.
[Graphical view]
ProDomiPD007152. TSC-22_Dip_Bun. 1 hit.
[Graphical view] [Entries sharing at least one domain]
PROSITEiPS01289. TSC22. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Transforming growth factor-beta-stimulated clone-22 is a member of a family of leucine zipper proteins that can homo- and heterodimerize and has transcriptional repressor activity."
    Kester H.A., Blanchetot C., den Hertog J., van der Saag P.T., van der Burg B.
    J. Biol. Chem. 274:27439-27447(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  2. "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.
    , 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] (ISOFORM 2).
    Tissue: Lung.
  3. "The DNA sequence of human chromosome 7."
    Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H., Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A., Delehaunty K.D., Miner T.L.
    , Nash W.E., Cordes M., Du H., Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C., Latreille P., Miller N., Johnson D., Murray J., Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E., Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H., Wilson R.K.
    Nature 424:157-164(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. "Human chromosome 7: DNA sequence and biology."
    Scherer S.W., Cheung J., MacDonald J.R., Osborne L.R., Nakabayashi K., Herbrick J.-A., Carson A.R., Parker-Katiraee L., Skaug J., Khaja R., Zhang J., Hudek A.K., Li M., Haddad M., Duggan G.E., Fernandez B.A., Kanematsu E., Gentles S.
    , Christopoulos C.C., Choufani S., Kwasnicka D., Zheng X.H., Lai Z., Nusskern D.R., Zhang Q., Gu Z., Lu F., Zeesman S., Nowaczyk M.J., Teshima I., Chitayat D., Shuman C., Weksberg R., Zackai E.H., Grebe T.A., Cox S.R., Kirkpatrick S.J., Rahman N., Friedman J.M., Heng H.H.Q., Pelicci P.G., Lo-Coco F., Belloni E., Shaffer L.G., Pober B., Morton C.C., Gusella J.F., Bruns G.A.P., Korf B.R., Quade B.J., Ligon A.H., Ferguson H., Higgins A.W., Leach N.T., Herrick S.R., Lemyre E., Farra C.G., Kim H.-G., Summers A.M., Gripp K.W., Roberts W., Szatmari P., Winsor E.J.T., Grzeschik K.-H., Teebi A., Minassian B.A., Kere J., Armengol L., Pujana M.A., Estivill X., Wilson M.D., Koop B.F., Tosi S., Moore G.E., Boright A.P., Zlotorynski E., Kerem B., Kroisel P.M., Petek E., Oscier D.G., Mould S.J., Doehner H., Doehner K., Rommens J.M., Vincent J.B., Venter J.C., Li P.W., Mural R.J., Adams M.D., Tsui L.-C.
    Science 300:767-772(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. "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: Cervix, Lung and Skin.
  7. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-62; THR-211 AND SER-279, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Platelet.
  8. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-62; THR-211 AND SER-370, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  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-49 AND SER-279, 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-165; SER-279 AND SER-370, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  11. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  12. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-229 AND SER-279, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  13. Cited for: VARIANT [LARGE SCALE ANALYSIS] MET-329.

Entry informationi

Entry nameiT22D4_HUMAN
AccessioniPrimary (citable) accession number: Q9Y3Q8
Secondary accession number(s): A4D2C3, A8MWR6, D6W5V9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 1, 2001
Last sequence update: June 1, 2001
Last modified: May 11, 2016
This is version 141 of the entry and version 2 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

Complete proteome, Reference proteome

Documents

  1. Human chromosome 7
    Human chromosome 7: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.