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Q5JSH3 (WDR44_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 80. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
WD repeat-containing protein 44
Alternative name(s):
Rabphilin-11
Gene names
Name:WDR44
OrganismHomo sapiens (Human)
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length913 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Downstream effector for RAB11. May be involved in vesicle recycling By similarity.

Subunit structure

Interacts with the GTP-bound form of RAB11 when membrane-associated. Does not bind to other Rab and Rho small G proteins By similarity.

Subcellular location

Cytoplasmcytosol. Cytoplasmperinuclear region. Endosome membrane. Golgi apparatustrans-Golgi network. Note: Colocalized with RAB11 along microtubules oriented toward lamellipodia By similarity.

Post-translational modification

Phosphorylated upon DNA damage, probably by ATM or ATR. Ref.5 Ref.6 Ref.7 Ref.8 Ref.9 Ref.10 Ref.11 Ref.12 Ref.13

Sequence similarities

Contains 7 WD repeats.

Sequence caution

The sequence BAA92015.1 differs from that shown. Reason: Frameshift at position 792.

The sequence BAC03799.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q5JSH3-1)

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.
Isoform 2 (identifier: Q5JSH3-2)

The sequence of this isoform differs from the canonical sequence as follows:
     796-803: Missing.
Note: No experimental confirmation available.
Isoform 3 (identifier: Q5JSH3-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1-473: Missing.
     474-477: DEGM → MVNV
     884-913: IMKTDNTEVLLSADFTGAIKVFVNKRKNVS → AVAHACNPSTLGGRGRRIT
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed
Chain2 – 913912WD repeat-containing protein 44
PRO_0000262769

Regions

Repeat509 – 54840WD 1
Repeat605 – 64339WD 2
Repeat645 – 68541WD 3
Repeat690 – 72940WD 4
Repeat740 – 77940WD 5
Repeat784 – 82340WD 6
Repeat876 – 91338WD 7
Region2 – 170169Binding activity
Coiled coil119 – 18466 Potential
Compositional bias211 – 25747Pro-rich

Amino acid modifications

Modified residue21N-acetylalanine Ref.12
Modified residue51Phosphoserine Ref.5 Ref.12
Modified residue271Phosphoserine Ref.5
Modified residue501Phosphoserine Ref.6 Ref.7 Ref.11 Ref.12 Ref.13
Modified residue901Phosphoserine Ref.12
Modified residue961Phosphoserine Ref.6 Ref.9 Ref.11 Ref.12 Ref.13
Modified residue1581Phosphothreonine Ref.12
Modified residue1611Phosphoserine Ref.12
Modified residue1621Phosphoserine Ref.12
Modified residue1631Phosphothreonine Ref.12
Modified residue2191Phosphothreonine Ref.11
Modified residue2621Phosphoserine Ref.5 Ref.7 Ref.11
Modified residue2711Phosphothreonine Ref.7
Modified residue3441Phosphoserine By similarity
Modified residue3491Phosphothreonine By similarity
Modified residue4031Phosphoserine Ref.5 Ref.11 Ref.12 Ref.13
Modified residue4701Phosphoserine Ref.10 Ref.11
Modified residue4711Phosphoserine Ref.10 Ref.11
Modified residue4721Phosphoserine Ref.10 Ref.11
Modified residue5611Phosphoserine Ref.8 Ref.10 Ref.12
Modified residue5631Phosphoserine Ref.12
Modified residue5651Phosphoserine Ref.8 Ref.12
Modified residue5681Phosphoserine Ref.8
Modified residue7831Phosphotyrosine Ref.7
Modified residue7991Phosphothreonine Ref.7
Modified residue8001Phosphotyrosine Ref.7

Natural variations

Alternative sequence1 – 473473Missing in isoform 3.
VSP_021807
Alternative sequence474 – 4774DEGM → MVNV in isoform 3.
VSP_021808
Alternative sequence796 – 8038Missing in isoform 2.
VSP_021809
Alternative sequence884 – 91330IMKTD…RKNVS → AVAHACNPSTLGGRGRRIT in isoform 3.
VSP_021810
Natural variant2891A → T. Ref.2
Corresponds to variant rs17271416 [ dbSNP | Ensembl ].
VAR_029538
Natural variant2961T → A. Ref.4
Corresponds to variant rs17855531 [ dbSNP | Ensembl ].
VAR_029539

Experimental info

Sequence conflict891L → P in CAD97788. Ref.2
Sequence conflict961S → G in CAL38210. Ref.2
Sequence conflict1941S → P in AAH28697. Ref.4
Sequence conflict2061V → A in CAL38662. Ref.2
Sequence conflict2501P → L in CAL38662. Ref.2
Sequence conflict3311A → P in CAD98010. Ref.2
Sequence conflict3801G → D in CAL38210. Ref.2
Sequence conflict4731D → N in CAL38662. Ref.2
Sequence conflict5341V → A in CAD97788. Ref.2
Sequence conflict5391A → L in CAD97788. Ref.2
Sequence conflict5861E → G in CAD97788. Ref.2
Sequence conflict6131L → P in CAL38662. Ref.2
Sequence conflict649 – 6502Missing in BAA92015. Ref.1
Sequence conflict7401K → R in CAL38210. Ref.2
Sequence conflict7401K → R in CAL38662. Ref.2
Sequence conflict8581L → S in CAL38662. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified February 15, 2005. Version 1.
Checksum: 8E43761C542DD6B9

FASTA913101,366
        10         20         30         40         50         60 
MASESDTEEF YDAPEDVHLG GGYPVGSPGK VGLSTFKETE NTAYKVGNES PVQELKQDVS 

        70         80         90        100        110        120 
KKIIESIIEE SQKVLQLEDD SLDSKGKELS DQATASPIVA RTDLSNIPGL LAIDQVLPEE 

       130        140        150        160        170        180 
SQKAESQNTF EETELELKKC FPSDETCEKP VDETTKLTQT SSTEQLNVLE TETEVLNKEA 

       190        200        210        220        230        240 
VEVKGGGDVL EPVSSDSLST KDFAAVEEVA PAKPPRHLTP EPDIVASTKK PVPARPPPPT 

       250        260        270        280        290        300 
NFPPPRPPPP SRPAPPPRKR KSELEFETLK TPDIDVPKEN ITSDSLLTAS MASESTVKDS 

       310        320        330        340        350        360 
QPSLDLASAT SGDKIVTAQE NGKAPDGQTV AGEVMGPQRP RSNSGRELTD EEILASVMIK 

       370        380        390        400        410        420 
NLDTGEEIPL SLAEEKLPTG INPLTLHIMR RTKEYVSNDA AQSDDEEKLQ SQPTDTDGGR 

       430        440        450        460        470        480 
LKQKTTQLKK FLGKSVKRAK HLAEEYGERA INKVKSVRDE VFHTDQDDPS SSDDEGMPYT 

       490        500        510        520        530        540 
RPVKFKAAHG FKGPYDFDQI KVVQDLSGEH MGAVWTMKFS HCGRLLASAG QDNVVRIWAL 

       550        560        570        580        590        600 
KNAFDYFNNM RMKYNTEGRV SPSPSQESLS SSKSDTDTGV CSGTDEDPDD KNAPFRQRPF 

       610        620        630        640        650        660 
CKYKGHTADL LDLSWSKNYF LLSSSMDKTV RLWHISRREC LCCFQHIDFV TAIAFHPRDD 

       670        680        690        700        710        720 
RYFLSGSLDG KLRLWNIPDK KVALWNEVDG QTKLITAANF CQNGKYAVIG TYDGRCIFYD 

       730        740        750        760        770        780 
TEHLKYHTQI HVRSTRGRNK VGRKITGIEP LPGENKILVT SNDSRIRLYD LRDLSLSMKY 

       790        800        810        820        830        840 
KGYVNSSSQI KASFSHDFTY LVSGSEDKYV YIWSTYHDLS KFTSVRRDRN DFWEGIKAHN 

       850        860        870        880        890        900 
AVVTSAIFAP NPSLMLSLDV QSEKSEGNEK SEDAEVLDAT PSGIMKTDNT EVLLSADFTG 

       910 
AIKVFVNKRK NVS 

« Hide

Isoform 2 [UniParc].

Checksum: 81A8AAA300D4FE9F
Show »

FASTA905100,403
Isoform 3 [UniParc].

Checksum: B6AA91342F478464
Show »

FASTA42948,565

References

[1]"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: 14702039] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 190-913 (ISOFORM 1).
Tissue: Teratocarcinoma and Tongue.
[2]"The full-ORF clone resource of the German cDNA consortium."
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I.
BMC Genomics 8:399-399(2007) [PubMed: 17974005] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2), VARIANT THR-289.
Tissue: Colon endothelium and Endometrial tumor.
[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. expand/collapse author list , 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: 15772651] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]"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: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), VARIANT ALA-296.
Tissue: Testis.
[5]"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: 17081983] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-5; SER-27; SER-262 AND SER-403, MASS SPECTROMETRY.
Tissue: Cervix carcinoma.
[6]"A probability-based approach for high-throughput protein phosphorylation analysis and site localization."
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.
Nat. Biotechnol. 24:1285-1292(2006) [PubMed: 16964243] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-50 AND SER-96, MASS SPECTROMETRY.
Tissue: Cervix carcinoma.
[7]"Global proteomic profiling of phosphopeptides using electron transfer dissociation tandem mass spectrometry."
Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A.
Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007) [PubMed: 17287340] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-50; SER-262; THR-271; TYR-783; THR-799 AND TYR-800, MASS SPECTROMETRY.
Tissue: Embryonic kidney.
[8]"ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage."
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.
Science 316:1160-1166(2007) [PubMed: 17525332] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-561; SER-565 AND SER-568, MASS SPECTROMETRY.
Tissue: Embryonic kidney.
[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: 18220336] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-96, MASS SPECTROMETRY.
Tissue: Cervix carcinoma.
[10]"Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
Mol. Cell 31:438-448(2008) [PubMed: 18691976] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-470; SER-471; SER-472 AND SER-561, MASS SPECTROMETRY.
Tissue: Cervix carcinoma.
[11]"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: 18669648] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-50; SER-96; THR-219; SER-262; SER-403; SER-470; SER-471 AND SER-472, MASS SPECTROMETRY.
Tissue: Cervix carcinoma.
[12]"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: 19413330] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-5; SER-50; SER-90; SER-96; THR-158; SER-161; SER-162; THR-163; SER-403; SER-561; SER-563 AND SER-565, MASS SPECTROMETRY.
Tissue: Embryonic kidney.
[13]"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: 19690332] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-50; SER-96 AND SER-403, MASS SPECTROMETRY.
Tissue: Leukemic T-cell.
[14]"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: 21269460] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AK001978 mRNA. Translation: BAA92015.1. Sequence problems.
AK092077 mRNA. Translation: BAC03799.1. Different initiation.
AK127556 mRNA. Translation: BAC87033.1.
AM393332 mRNA. Translation: CAL38210.1.
AM393787 mRNA. Translation: CAL38662.1.
BX537578 mRNA. Translation: CAD97788.1.
BX538087 mRNA. Translation: CAD98010.1.
AL391474, AL391803, AL391830 Genomic DNA. Translation: CAI41402.1.
AL391474, AL391803, AL391830 Genomic DNA. Translation: CAI41403.1.
AL391803, AL391474, AL391830 Genomic DNA. Translation: CAI41482.1.
AL391803, AL391474, AL391830 Genomic DNA. Translation: CAI41483.1.
AL391830, AL391474, AL391803 Genomic DNA. Translation: CAI41512.1.
AL391830, AL391474, AL391803 Genomic DNA. Translation: CAI41513.1.
BC028697 mRNA. Translation: AAH28697.3.
IPIIPI00444371.
IPI00807730.
IPI00872729.
RefSeqNP_001171894.1. NM_001184965.1.
NP_001171895.1. NM_001184966.1.
NP_061918.3. NM_019045.4.
UniGeneHs.98510.

3D structure databases

HSSPHSSP built from PDB template 1R5M based on UniProtKB P38262.
ProteinModelPortalQ5JSH3.
SMRQ5JSH3. Positions 494-814.
ModBaseSearch...

Protein-protein interaction databases

IntActQ5JSH3. 1 interaction.
STRINGQ5JSH3.

PTM databases

PhosphoSiteQ5JSH3.

Polymorphism databases

DMDM74762196.

Proteomic databases

PRIDEQ5JSH3.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000254029; ENSP00000254029; ENSG00000131725.
GeneID54521.
KEGGhsa:54521.
NMPDRfig|9606.3.peg.33281.
UCSCuc004eqn.1. human.
uc004eqo.1. human.

Organism-specific databases

CTD54521.
GeneCardsGC0XP117480.
H-InvDBHIX0017006.
HGNCHGNC:30512. WDR44.
HPAHPA038084.
neXtProtNX_Q5JSH3.
PharmGKBPA128394668.
GenAtlasSearch...

Phylogenomic databases

eggNOGprNOG17842.
GeneTreeENSGT00530000063479.
HOVERGENHBG080376.
InParanoidQ5JSH3.
OMADHTEVLL.
OrthoDBEOG4K6G3H.
PhylomeDBQ5JSH3.

Gene expression databases

ArrayExpressQ5JSH3.
BgeeQ5JSH3.
CleanExHS_WDR44.
GenevestigatorQ5JSH3.
GermOnlineENSG00000131725. Homo sapiens.

Family and domain databases

InterProIPR020472. G-protein_beta_WD-40_rep.
IPR015943. WD40/YVTN_repeat-like_dom.
IPR001680. WD40_repeat.
IPR011046. WD40_repeat-like_dom.
IPR017986. WD40_repeat_dom.
[Graphical view]
Gene3DG3DSA:2.130.10.10. WD40/YVTN_repeat-like. 3 hits.
PfamPF00400. WD40. 4 hits.
[Graphical view]
PRINTSPR00320. GPROTEINBRPT.
SMARTSM00320. WD40. 6 hits.
[Graphical view]
SUPFAMSSF50978. WD40_like. 1 hit.
PROSITEPS00678. WD_REPEATS_1. False negative.
PS50082. WD_REPEATS_2. 4 hits.
PS50294. WD_REPEATS_REGION. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio56920.

Entry information

Entry nameWDR44_HUMAN
AccessionPrimary (citable) accession number: Q5JSH3
Secondary accession number(s): Q0JS52 expand/collapse secondary AC list , Q0JTF3, Q5JSH2, Q6ZSC1, Q7Z365, Q7Z3P6, Q8NAU8, Q8NHU5, Q9NUV4
Entry history
Integrated into UniProtKB/Swiss-Prot: November 28, 2006
Last sequence update: February 15, 2005
Last modified: January 25, 2012
This is version 80 of the entry and version 1 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.

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