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Q9UHR4 (BI2L1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 122. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Brain-specific angiogenesis inhibitor 1-associated protein 2-like protein 1

Short name=BAI1-associated protein 2-like protein 1
Alternative name(s):
Insulin receptor tyrosine kinase substrate
Gene names
Name:BAIAP2L1
Synonyms:IRTKS
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length511 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

May function as adapter protein. Involved in the formation of clusters of actin bundles. Plays a role in the reorganization of the actin cytoskeleton in response to bacterial infection. Ref.8 Ref.13 Ref.17

Subunit structure

Interacts with RAC1. Binds to F-actin. Interacts with FASLG. Interacts (via SH3 domain) with E.coli effector protein EspF(U) (via PXXP motifs). Identified in a complex containing at least WASL, BAIAP2L1 and E.coli EspF(U). Interacts with E.coli intimin receptor Tir. Ref.8 Ref.12 Ref.13 Ref.16 Ref.17

Subcellular location

Cytoplasmcytoskeleton. Note: Recruited to actin pedestals that are formed upon infection by bacteria at bacterial attachment sites. Ref.13

Domain

The IMD domain is predicted to have a helical structure. It may induce actin bundling and filopodia formation By similarity.

Post-translational modification

Phosphorylated on tyrosine in response to insulin. Ref.8

Sequence similarities

Contains 1 IMD (IRSp53/MIM homology) domain.

Contains 1 SH3 domain.

Sequence caution

The sequence AAD20937.1 differs from that shown. Reason: Erroneous gene model prediction.

The sequence AAS07549.1 differs from that shown. Reason: Erroneous initiation.

The sequence BAB15671.1 differs from that shown. Reason: Erroneous initiation.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 511511Brain-specific angiogenesis inhibitor 1-associated protein 2-like protein 1
PRO_0000247854

Regions

Domain1 – 249249IMD
Domain339 – 40264SH3
Region483 – 51129Binds F-actin
Coiled coil115 – 15440 Potential

Amino acid modifications

Modified residue2481Phosphothreonine Ref.10 Ref.14
Modified residue2571Phosphothreonine Ref.10 Ref.14
Modified residue2611Phosphoserine Ref.7 Ref.10 Ref.14
Modified residue2811Phosphoserine Ref.10
Modified residue3311Phosphoserine Ref.10
Modified residue4121Phosphothreonine Ref.10 Ref.14
Modified residue4221Phosphoserine By similarity

Natural variations

Natural variant4601S → T.
Corresponds to variant rs2269966 [ dbSNP | Ensembl ].
VAR_033515

Experimental info

Mutagenesis1411K → E: Loss ability to induce the formation of actin clusters; when associated with K-142; R-145 and K-146. Ref.8
Mutagenesis1421K → E: Loss ability to induce the formation of actin clusters; when associated with K-141; R-145 and K-146. Ref.8
Mutagenesis1451R → E: Loss ability to induce the formation of actin clusters; when associated with K-141; K-142 and K-146. Ref.8
Mutagenesis1461K → E: Loss ability to induce the formation of actin clusters; when associated with K-141; K-142 and R-145. Ref.8
Mutagenesis488 – 51124Missing: Loss ability to induce the formation of actin clusters; induce the formation of long filopodia. Ref.8
Sequence conflict4561A → V in BAB15671. Ref.6
Sequence conflict4601S → F in BAB15671. Ref.6
Sequence conflict4641A → V in BAB15671. Ref.6
Sequence conflict4661A → V in BAB15671. Ref.6
Sequence conflict4671S → F in BAB15671. Ref.6

Secondary structure

............. 511
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q9UHR4 [UniParc].

Last modified March 1, 2004. Version 2.
Checksum: C2304C4444B02F02

FASTA51156,883
        10         20         30         40         50         60 
MSRGPEEVNR LTESTYRNVM EQFNPGLRNL INLGKNYEKA VNAMILAGKA YYDGVAKIGE 

        70         80         90        100        110        120 
IATGSPVSTE LGHVLIEISS THKKLNESLD ENFKKFHKEI IHELEKKIEL DVKYMNATLK 

       130        140        150        160        170        180 
RYQTEHKNKL ESLEKSQAEL KKIRRKSQGS RNALKYEHKE IEYVETVTSR QSEIQKFIAD 

       190        200        210        220        230        240 
GCKEALLEEK RRFCFLVDKH CGFANHIHYY HLQSAELLNS KLPRWQETCV DAIKVPEKIM 

       250        260        270        280        290        300 
NMIEEIKTPA STPVSGTPQA SPMIERSNVV RKDYDTLSKC SPKMPPAPSG RAYTSPLIDM 

       310        320        330        340        350        360 
FNNPATAAPN SQRVNNSTGT SEDPSLQRSV SVATGLNMMK KQKVKTIFPH TAGSNKTLLS 

       370        380        390        400        410        420 
FAQGDVITLL IPEEKDGWLY GEHDVSKARG WFPSSYTKLL EENETEAVTV PTPSPTPVRS 

       430        440        450        460        470        480 
ISTVNLSENS SVVIPPPDYL ECLSMGAAAD RRADSARTTS TFKAPASKPE TAAPNDANGT 

       490        500        510 
AKPPFLSGEN PFATVKLRPT VTNDRSAPII R 

« Hide

References

« Hide 'large scale' references
[1]"Gene expression profiling in the human hypothalamus-pituitary-adrenal axis and full-length cDNA cloning."
Hu R.-M., Han Z.-G., Song H.-D., Peng Y.-D., Huang Q.-H., Ren S.-X., Gu Y.-J., Huang C.-H., Li Y.-B., Jiang C.-L., Fu G., Zhang Q.-H., Gu B.-W., Dai M., Mao Y.-F., Gao G.-F., Rong R., Ye M. expand/collapse author list , Zhou J., Xu S.-H., Gu J., Shi J.-X., Jin W.-R., Zhang C.-K., Wu T.-M., Huang G.-Y., Chen Z., Chen M.-D., Chen J.-L.
Proc. Natl. Acad. Sci. U.S.A. 97:9543-9548(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Adrenal gland.
[2]"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. expand/collapse author list , 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].
[3]"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. expand/collapse author list , 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].
[4]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
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].
Tissue: Placenta.
[6]"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. expand/collapse author list , 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] OF 317-511.
Tissue: Lung.
[7]"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-261, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[8]"Characterisation of IRTKS, a novel IRSp53/MIM family actin regulator with distinct filament bundling properties."
Millard T.H., Dawson J., Machesky L.M.
J. Cell Sci. 120:1663-1672(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH RAC1 AND F-ACTIN, PHOSPHORYLATION, MUTAGENESIS OF LYS-141; LYS-142; ARG-145; LYS-146 AND 488-GLY--ARG-511.
[9]"Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis."
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III
J. Proteome Res. 7:1346-1351(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[10]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-248; THR-257; SER-261; SER-281; SER-331 AND THR-412, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[11]"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].
[12]"Identification of SH3 domain interaction partners of human FasL (CD178) by phage display screening."
Voss M., Lettau M., Janssen O.
BMC Immunol. 10:53-53(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH FASLG.
[13]"Insulin receptor tyrosine kinase substrate links the E. coli O157:H7 actin assembly effectors Tir and EspF(U) during pedestal formation."
Vingadassalom D., Kazlauskas A., Skehan B., Cheng H.C., Magoun L., Robbins D., Rosen M.K., Saksela K., Leong J.M.
Proc. Natl. Acad. Sci. U.S.A. 106:6754-6759(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH E.COLI EFFECTOR PROTEIN ESPF(U), IDENTIFICATION IN A COMPLEX WITH WASL AND E.COLI EFFECTOR PROTEIN ESPF(U), INTERACTION WITH E.COLI INTIMIN RECEPTOR TIR, SUBCELLULAR LOCATION.
[14]"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 THR-248; THR-257; SER-261 AND THR-412, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[15]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[16]"Recognition of tandem PxxP motifs as a unique Src homology 3-binding mode triggers pathogen-driven actin assembly."
Aitio O., Hellman M., Kazlauskas A., Vingadassalom D.F., Leong J.M., Saksela K., Permi P.
Proc. Natl. Acad. Sci. U.S.A. 107:21743-21748(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 339-402 IN COMPLEX WITH E.COLI EFFECTOR PROTEIN ESPF(U), SUBUNIT.
[17]"Enterohaemorrhagic Escherichia coli exploits a tryptophan switch to hijack host f-actin assembly."
Aitio O., Hellman M., Skehan B., Kesti T., Leong J.M., Saksela K., Permi P.
Structure 20:1692-1703(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 339-402 IN COMPLEX WITH WASL AND E.COLI ESPF(U), FUNCTION, IDENTIFICATION IN A COMPLEX WITH WASL AND E.COLI ESPF(U).
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF119666 mRNA. Translation: AAF17223.2.
AC004841 Genomic DNA. Translation: AAD20937.1. Sequence problems.
AC093169 Genomic DNA. No translation available.
AC093799 Genomic DNA. Translation: AAS07549.1. Different initiation.
AC093799 Genomic DNA. Translation: AAS07550.1.
CH236956 Genomic DNA. Translation: EAL23890.1.
CH471091 Genomic DNA. Translation: EAW76706.1.
BC013888 mRNA. Translation: AAH13888.1.
AK027142 mRNA. Translation: BAB15671.1. Different initiation.
CCDSCCDS34687.1.
RefSeqNP_061330.2. NM_018842.4.
UniGeneHs.656063.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2KXCNMR-A339-402[»]
2LNHNMR-B339-402[»]
ProteinModelPortalQ9UHR4.
SMRQ9UHR4. Positions 6-227, 339-402.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid121017. 13 interactions.
DIPDIP-53820N.
IntActQ9UHR4. 5 interactions.
MINTMINT-5006683.
STRING9606.ENSP00000005260.

PTM databases

PhosphoSiteQ9UHR4.

Polymorphism databases

DMDM74735022.

Proteomic databases

MaxQBQ9UHR4.
PaxDbQ9UHR4.
PeptideAtlasQ9UHR4.
PRIDEQ9UHR4.

Protocols and materials databases

DNASU55971.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000005260; ENSP00000005260; ENSG00000006453.
GeneID55971.
KEGGhsa:55971.
UCSCuc003upj.3. human.

Organism-specific databases

CTD55971.
GeneCardsGC07M097920.
H-InvDBHIX0167837.
HGNCHGNC:21649. BAIAP2L1.
HPAHPA019484.
HPA021257.
HPA023874.
HPA029503.
MIM611877. gene.
neXtProtNX_Q9UHR4.
PharmGKBPA142672562.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG71665.
HOVERGENHBG054462.
InParanoidQ9UHR4.
OMAYRNVMEQ.
OrthoDBEOG7N0C3W.
PhylomeDBQ9UHR4.
TreeFamTF325648.

Gene expression databases

BgeeQ9UHR4.
CleanExHS_BAIAP2L1.
GenevestigatorQ9UHR4.

Family and domain databases

InterProIPR027681. BAIAP2.
IPR013606. IRSp53/MIM_homology_IMD.
IPR001452. SH3_domain.
[Graphical view]
PANTHERPTHR14206. PTHR14206. 1 hit.
PfamPF08397. IMD. 1 hit.
PF14604. SH3_9. 1 hit.
[Graphical view]
SMARTSM00326. SH3. 1 hit.
[Graphical view]
SUPFAMSSF50044. SSF50044. 1 hit.
PROSITEPS51338. IMD. 1 hit.
PS50002. SH3. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSBAIAP2L1. human.
GeneWikiBAIAP2L1.
GenomeRNAi55971.
NextBio61407.
PROQ9UHR4.
SOURCESearch...

Entry information

Entry nameBI2L1_HUMAN
AccessionPrimary (citable) accession number: Q9UHR4
Secondary accession number(s): A4D268 expand/collapse secondary AC list , Q75L21, Q75L22, Q96CV4, Q9H5F5, Q9Y2M8
Entry history
Integrated into UniProtKB/Swiss-Prot: July 25, 2006
Last sequence update: March 1, 2004
Last modified: July 9, 2014
This is version 122 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 7

Human chromosome 7: entries, gene names and cross-references to MIM