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Protein

WD repeat-containing protein 44

Gene

WDR44

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

Functioni

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

GO - Biological processi

Complete GO annotation...

Enzyme and pathway databases

SignaLinkiQ5JSH3.

Names & Taxonomyi

Protein namesi
Recommended name:
WD repeat-containing protein 44
Alternative name(s):
Rabphilin-11
Gene namesi
Name:WDR44
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome X

Organism-specific databases

HGNCiHGNC:30512. WDR44.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Endosome, Golgi apparatus, Membrane

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA128394668.

Polymorphism and mutation databases

BioMutaiWDR44.
DMDMi74762196.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedCombined sources
Chaini2 – 913912WD repeat-containing protein 44PRO_0000262769Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanineCombined sources
Modified residuei3 – 31PhosphoserineCombined sources
Modified residuei11 – 111PhosphotyrosineCombined sources
Modified residuei27 – 271PhosphoserineCombined sources
Modified residuei50 – 501PhosphoserineCombined sources
Modified residuei66 – 661PhosphoserineCombined sources
Modified residuei71 – 711PhosphoserineCombined sources
Modified residuei81 – 811PhosphoserineCombined sources
Modified residuei96 – 961PhosphoserineCombined sources
Modified residuei126 – 1261PhosphoserineCombined sources
Modified residuei158 – 1581PhosphothreonineCombined sources
Modified residuei219 – 2191PhosphothreonineCombined sources
Modified residuei262 – 2621PhosphoserineCombined sources
Modified residuei271 – 2711PhosphothreonineCombined sources
Modified residuei342 – 3421PhosphoserineCombined sources
Modified residuei344 – 3441PhosphoserineCombined sources
Modified residuei349 – 3491PhosphothreonineCombined sources
Modified residuei403 – 4031PhosphoserineCombined sources
Modified residuei470 – 4701PhosphoserineCombined sources
Modified residuei471 – 4711PhosphoserineCombined sources
Modified residuei472 – 4721PhosphoserineCombined sources
Modified residuei479 – 4791PhosphotyrosineBy similarity
Modified residuei561 – 5611PhosphoserineCombined sources
Modified residuei565 – 5651PhosphoserineCombined sources

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiQ5JSH3.
MaxQBiQ5JSH3.
PaxDbiQ5JSH3.
PeptideAtlasiQ5JSH3.
PRIDEiQ5JSH3.

PTM databases

iPTMnetiQ5JSH3.
PhosphoSiteiQ5JSH3.

Expressioni

Gene expression databases

BgeeiQ5JSH3.
CleanExiHS_WDR44.
ExpressionAtlasiQ5JSH3. baseline and differential.
GenevisibleiQ5JSH3. HS.

Organism-specific databases

HPAiHPA038084.
HPA046719.

Interactioni

Subunit structurei

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

Protein-protein interaction databases

BioGridi120014. 35 interactions.
IntActiQ5JSH3. 4 interactions.
MINTiMINT-4650026.
STRINGi9606.ENSP00000254029.

Structurei

3D structure databases

ProteinModelPortaliQ5JSH3.
SMRiQ5JSH3. Positions 506-865.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati509 – 54840WD 1Add
BLAST
Repeati605 – 64339WD 2Add
BLAST
Repeati645 – 68541WD 3Add
BLAST
Repeati690 – 72940WD 4Add
BLAST
Repeati740 – 77940WD 5Add
BLAST
Repeati784 – 82340WD 6Add
BLAST
Repeati876 – 91338WD 7Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni2 – 170169Binding activityAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili119 – 18466Sequence analysisAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi211 – 25747Pro-richAdd
BLAST

Sequence similaritiesi

Contains 7 WD repeats.PROSITE-ProRule annotation

Keywords - Domaini

Coiled coil, Repeat, WD repeat

Phylogenomic databases

eggNOGiKOG0283. Eukaryota.
ENOG410XQPJ. LUCA.
GeneTreeiENSGT00530000063479.
HOGENOMiHOG000267152.
HOVERGENiHBG080376.
InParanoidiQ5JSH3.
OMAiKTDHTEV.
OrthoDBiEOG7W6WK0.
PhylomeDBiQ5JSH3.
TreeFamiTF329226.

Family and domain databases

Gene3Di2.130.10.10. 2 hits.
InterProiIPR020472. G-protein_beta_WD-40_rep.
IPR015943. WD40/YVTN_repeat-like_dom.
IPR001680. WD40_repeat.
IPR017986. WD40_repeat_dom.
[Graphical view]
PfamiPF00400. WD40. 4 hits.
[Graphical view]
PRINTSiPR00320. GPROTEINBRPT.
SMARTiSM00320. WD40. 6 hits.
[Graphical view]
SUPFAMiSSF50978. SSF50978. 2 hits.
PROSITEiPS50082. WD_REPEATS_2. 4 hits.
PS50294. WD_REPEATS_REGION. 1 hit.
[Graphical view]

Sequences (4)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 4 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q5JSH3-1) [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
MASESDTEEF YDAPEDVHLG GGYPVGSPGK VGLSTFKETE NTAYKVGNES
60 70 80 90 100
PVQELKQDVS KKIIESIIEE SQKVLQLEDD SLDSKGKELS DQATASPIVA
110 120 130 140 150
RTDLSNIPGL LAIDQVLPEE SQKAESQNTF EETELELKKC FPSDETCEKP
160 170 180 190 200
VDETTKLTQT SSTEQLNVLE TETEVLNKEA VEVKGGGDVL EPVSSDSLST
210 220 230 240 250
KDFAAVEEVA PAKPPRHLTP EPDIVASTKK PVPARPPPPT NFPPPRPPPP
260 270 280 290 300
SRPAPPPRKR KSELEFETLK TPDIDVPKEN ITSDSLLTAS MASESTVKDS
310 320 330 340 350
QPSLDLASAT SGDKIVTAQE NGKAPDGQTV AGEVMGPQRP RSNSGRELTD
360 370 380 390 400
EEILASVMIK NLDTGEEIPL SLAEEKLPTG INPLTLHIMR RTKEYVSNDA
410 420 430 440 450
AQSDDEEKLQ SQPTDTDGGR LKQKTTQLKK FLGKSVKRAK HLAEEYGERA
460 470 480 490 500
INKVKSVRDE VFHTDQDDPS SSDDEGMPYT RPVKFKAAHG FKGPYDFDQI
510 520 530 540 550
KVVQDLSGEH MGAVWTMKFS HCGRLLASAG QDNVVRIWAL KNAFDYFNNM
560 570 580 590 600
RMKYNTEGRV SPSPSQESLS SSKSDTDTGV CSGTDEDPDD KNAPFRQRPF
610 620 630 640 650
CKYKGHTADL LDLSWSKNYF LLSSSMDKTV RLWHISRREC LCCFQHIDFV
660 670 680 690 700
TAIAFHPRDD RYFLSGSLDG KLRLWNIPDK KVALWNEVDG QTKLITAANF
710 720 730 740 750
CQNGKYAVIG TYDGRCIFYD TEHLKYHTQI HVRSTRGRNK VGRKITGIEP
760 770 780 790 800
LPGENKILVT SNDSRIRLYD LRDLSLSMKY KGYVNSSSQI KASFSHDFTY
810 820 830 840 850
LVSGSEDKYV YIWSTYHDLS KFTSVRRDRN DFWEGIKAHN AVVTSAIFAP
860 870 880 890 900
NPSLMLSLDV QSEKSEGNEK SEDAEVLDAT PSGIMKTDNT EVLLSADFTG
910
AIKVFVNKRK NVS
Length:913
Mass (Da):101,366
Last modified:February 15, 2005 - v1
Checksum:i8E43761C542DD6B9
GO
Isoform 2 (identifier: Q5JSH3-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     796-803: Missing.

Note: No experimental confirmation available.
Show »
Length:905
Mass (Da):100,403
Checksum:i81A8AAA300D4FE9F
GO
Isoform 3 (identifier: Q5JSH3-3) [UniParc]FASTAAdd to basket

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.
Show »
Length:429
Mass (Da):48,565
Checksum:iB6AA91342F478464
GO
Isoform 4 (identifier: Q5JSH3-4) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     37-61: Missing.
     659-722: Missing.

Note: No experimental confirmation available.
Show »
Length:824
Mass (Da):91,272
Checksum:i015DB327476F0083
GO

Sequence cautioni

The sequence BAA92015.1 differs from that shown. Reason: Frameshift at position 792. Curated
The sequence BAC03799.1 differs from that shown. Reason: Erroneous initiation. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti89 – 891L → P in CAD97788 (PubMed:17974005).Curated
Sequence conflicti96 – 961S → G in CAL38210 (PubMed:17974005).Curated
Sequence conflicti194 – 1941S → P in AAH28697 (PubMed:15489334).Curated
Sequence conflicti206 – 2061V → A in CAL38662 (PubMed:17974005).Curated
Sequence conflicti250 – 2501P → L in CAL38662 (PubMed:17974005).Curated
Sequence conflicti276 – 2761V → A in BAG61611 (PubMed:14702039).Curated
Sequence conflicti331 – 3311A → P in CAD98010 (PubMed:17974005).Curated
Sequence conflicti380 – 3801G → D in CAL38210 (PubMed:17974005).Curated
Sequence conflicti473 – 4731D → N in CAL38662 (PubMed:17974005).Curated
Sequence conflicti534 – 5341V → A in CAD97788 (PubMed:17974005).Curated
Sequence conflicti539 – 5391A → L in CAD97788 (PubMed:17974005).Curated
Sequence conflicti547 – 5471F → L in BAG61611 (PubMed:14702039).Curated
Sequence conflicti586 – 5861E → G in CAD97788 (PubMed:17974005).Curated
Sequence conflicti613 – 6131L → P in CAL38662 (PubMed:17974005).Curated
Sequence conflicti649 – 6502Missing in BAA92015 (PubMed:14702039).Curated
Sequence conflicti740 – 7401K → R in CAL38210 (PubMed:17974005).Curated
Sequence conflicti740 – 7401K → R in CAL38662 (PubMed:17974005).Curated
Sequence conflicti858 – 8581L → S in CAL38662 (PubMed:17974005).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti289 – 2891A → T.1 Publication
Corresponds to variant rs17271416 [ dbSNP | Ensembl ].
VAR_029538
Natural varianti296 – 2961T → A.1 Publication
Corresponds to variant rs17855531 [ dbSNP | Ensembl ].
VAR_029539

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 473473Missing in isoform 3. 1 PublicationVSP_021807Add
BLAST
Alternative sequencei37 – 6125Missing in isoform 4. 1 PublicationVSP_046637Add
BLAST
Alternative sequencei474 – 4774DEGM → MVNV in isoform 3. 1 PublicationVSP_021808
Alternative sequencei659 – 72264Missing in isoform 4. 1 PublicationVSP_046638Add
BLAST
Alternative sequencei796 – 8038Missing in isoform 2. 1 PublicationVSP_021809
Alternative sequencei884 – 91330IMKTD…RKNVS → AVAHACNPSTLGGRGRRIT in isoform 3. 1 PublicationVSP_021810Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK001978 mRNA. Translation: BAA92015.1. Sequence problems.
AK092077 mRNA. Translation: BAC03799.1. Different initiation.
AK127556 mRNA. Translation: BAC87033.1.
AK299711 mRNA. Translation: BAG61611.1.
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.
CCDSiCCDS14572.1. [Q5JSH3-1]
CCDS55482.1. [Q5JSH3-2]
CCDS55483.1. [Q5JSH3-4]
RefSeqiNP_001171894.1. NM_001184965.1. [Q5JSH3-2]
NP_001171895.1. NM_001184966.1. [Q5JSH3-4]
NP_061918.3. NM_019045.4. [Q5JSH3-1]
UniGeneiHs.98510.

Genome annotation databases

EnsembliENST00000254029; ENSP00000254029; ENSG00000131725. [Q5JSH3-1]
ENST00000371822; ENSP00000360887; ENSG00000131725. [Q5JSH3-4]
ENST00000371825; ENSP00000360890; ENSG00000131725. [Q5JSH3-2]
GeneIDi54521.
KEGGihsa:54521.
UCSCiuc004eqn.4. human. [Q5JSH3-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK001978 mRNA. Translation: BAA92015.1. Sequence problems.
AK092077 mRNA. Translation: BAC03799.1. Different initiation.
AK127556 mRNA. Translation: BAC87033.1.
AK299711 mRNA. Translation: BAG61611.1.
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.
CCDSiCCDS14572.1. [Q5JSH3-1]
CCDS55482.1. [Q5JSH3-2]
CCDS55483.1. [Q5JSH3-4]
RefSeqiNP_001171894.1. NM_001184965.1. [Q5JSH3-2]
NP_001171895.1. NM_001184966.1. [Q5JSH3-4]
NP_061918.3. NM_019045.4. [Q5JSH3-1]
UniGeneiHs.98510.

3D structure databases

ProteinModelPortaliQ5JSH3.
SMRiQ5JSH3. Positions 506-865.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi120014. 35 interactions.
IntActiQ5JSH3. 4 interactions.
MINTiMINT-4650026.
STRINGi9606.ENSP00000254029.

PTM databases

iPTMnetiQ5JSH3.
PhosphoSiteiQ5JSH3.

Polymorphism and mutation databases

BioMutaiWDR44.
DMDMi74762196.

Proteomic databases

EPDiQ5JSH3.
MaxQBiQ5JSH3.
PaxDbiQ5JSH3.
PeptideAtlasiQ5JSH3.
PRIDEiQ5JSH3.

Protocols and materials databases

DNASUi54521.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000254029; ENSP00000254029; ENSG00000131725. [Q5JSH3-1]
ENST00000371822; ENSP00000360887; ENSG00000131725. [Q5JSH3-4]
ENST00000371825; ENSP00000360890; ENSG00000131725. [Q5JSH3-2]
GeneIDi54521.
KEGGihsa:54521.
UCSCiuc004eqn.4. human. [Q5JSH3-1]

Organism-specific databases

CTDi54521.
GeneCardsiWDR44.
H-InvDBHIX0017006.
HGNCiHGNC:30512. WDR44.
HPAiHPA038084.
HPA046719.
neXtProtiNX_Q5JSH3.
PharmGKBiPA128394668.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG0283. Eukaryota.
ENOG410XQPJ. LUCA.
GeneTreeiENSGT00530000063479.
HOGENOMiHOG000267152.
HOVERGENiHBG080376.
InParanoidiQ5JSH3.
OMAiKTDHTEV.
OrthoDBiEOG7W6WK0.
PhylomeDBiQ5JSH3.
TreeFamiTF329226.

Enzyme and pathway databases

SignaLinkiQ5JSH3.

Miscellaneous databases

GeneWikiiWDR44.
GenomeRNAii54521.
PROiQ5JSH3.

Gene expression databases

BgeeiQ5JSH3.
CleanExiHS_WDR44.
ExpressionAtlasiQ5JSH3. baseline and differential.
GenevisibleiQ5JSH3. HS.

Family and domain databases

Gene3Di2.130.10.10. 2 hits.
InterProiIPR020472. G-protein_beta_WD-40_rep.
IPR015943. WD40/YVTN_repeat-like_dom.
IPR001680. WD40_repeat.
IPR017986. WD40_repeat_dom.
[Graphical view]
PfamiPF00400. WD40. 4 hits.
[Graphical view]
PRINTSiPR00320. GPROTEINBRPT.
SMARTiSM00320. WD40. 6 hits.
[Graphical view]
SUPFAMiSSF50978. SSF50978. 2 hits.
PROSITEiPS50082. WD_REPEATS_2. 4 hits.
PS50294. WD_REPEATS_REGION. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  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.
    , 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] (ISOFORMS 3 AND 4), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 190-913 (ISOFORM 1).
    Tissue: Brain, Teratocarcinoma and Tongue.
  2. 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.
    , 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. "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), 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] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-11; SER-27; SER-262 AND SER-403, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    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] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-50 AND SER-96, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  7. "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.
  8. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-96; THR-219; SER-262; SER-403; SER-470; SER-471 AND SER-472, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  9. "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: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS], IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  10. "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-96 AND SER-403, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  11. "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: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-3; SER-27; SER-50; SER-96; THR-219; SER-262; SER-342 AND SER-403, CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS], IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  12. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  13. "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-50; SER-262; THR-271; SER-403; SER-561 AND SER-565, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  14. "Toward a comprehensive characterization of a human cancer cell phosphoproteome."
    Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., Mohammed S.
    J. Proteome Res. 12:260-271(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-50; SER-66; SER-71; SER-81; SER-96; SER-126; THR-158; THR-219; SER-262; SER-344; SER-403 AND SER-561, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma and Erythroleukemia.
  15. "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 SER-27; SER-96; THR-349; SER-403 AND SER-561, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.

Entry informationi

Entry nameiWDR44_HUMAN
AccessioniPrimary (citable) accession number: Q5JSH3
Secondary accession number(s): B4DSE9
, F8W913, Q0JS52, Q0JTF3, Q5JSH2, Q6ZSC1, Q7Z365, Q7Z3P6, Q8NAU8, Q8NHU5, Q9NUV4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 28, 2006
Last sequence update: February 15, 2005
Last modified: July 6, 2016
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

Complete proteome, Reference proteome

Documents

  1. Human chromosome X
    Human chromosome X: 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. 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.